|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-208 |
8.94e-128 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 358.35 E-value: 8.94e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 6 QLTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFYLA 85
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 86 HHAGVKPELSPWENLRFYQKIQGLAlDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTA 165
Cdd:PRK13538 81 HQPGIKTELTALENLRFYQRLHGPG-DDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1419237541 166 IDKKGVSDLIVHIEKHCENGGMVIFTSHQ--AAESHKVKILSLDQ 208
Cdd:PRK13538 160 IDKQGVARLEALLAQHAEQGGMVILTTHQdlPVASDKVRKLRLGQ 204
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-210 |
7.92e-102 |
|
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: 292.85 E-value: 7.92e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 6 QLTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFYLA 85
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 86 HHAGVKPELSPWENLRFYQKIQGLALDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTA 165
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1419237541 166 IDKKGVSDLIVHIEKHCENGGMVIFTSHQAAESHKVKILSLDQFK 210
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGDFK 206
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-206 |
4.26e-87 |
|
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: 255.36 E-value: 4.26e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFYLAH 86
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 HAGVKPELSPWENLRFYQKIQGLAldDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAI 166
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGA--QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1419237541 167 DKKGVSDLIVHIEKHCENGGMVIFTSHQAAESHKVKILSL 206
Cdd:TIGR01189 159 DKAGVALLAGLLRAHLARGGIVLLTTHQDLGLVEARELRL 198
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
7-194 |
4.82e-79 |
|
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: 235.08 E-value: 4.82e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFYLAH 86
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 HAGVKPELSPWENLRFYQKIQGlaldDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAI 166
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHS----DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*...
gi 1419237541 167 DKKGVSDLIVHIEKHCENGGMVIFTSHQ 194
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-210 |
8.93e-59 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 183.54 E-value: 8.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 5 NQLTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDipiQKQRDEYYSELF-Y 83
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEAChY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 84 LAHHAGVKPELSPWENLRFYQKIQG---LALDDealwyALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILD 160
Cdd:PRK13539 78 LGHRNAMKPALTVAENLEFWAAFLGgeeLDIAA-----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1419237541 161 EPFTAIDKKGVSDLIVHIEKHCENGGMVIFTSHQAAESHKVKILSLDQFK 210
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQGGIVIAATHIPLGLPGARELDLGPFA 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-164 |
6.16e-37 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 126.22 E-value: 6.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 22 FENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYS-ELFYLAHHAGVKPELSPWENL 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRkEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1419237541 101 RFYQKIQGL---ALDDEALWyALDKVGLIGREELACSY----LSAGQQRRVALAKLWLIKQKLWILDEPFT 164
Cdd:pfam00005 81 RLGLLLKGLskrEKDARAEE-ALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-194 |
7.29e-36 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 125.06 E-value: 7.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFYLAH 86
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 HAGVKPELSPWENLRFYQKIQGLALDDEALWYALDKVGLIgreELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAI 166
Cdd:PRK13540 82 RSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLI---DYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180
....*....|....*....|....*...
gi 1419237541 167 DKKGVSDLIVHIEKHCENGGMVIFTSHQ 194
Cdd:PRK13540 159 DELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
7-195 |
1.62e-35 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 124.58 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQkqRDEYYSELFYLAH 86
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT--RGDRSRFMAYLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 HAGVKPELSPWENLRFYQKIQGLAlDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAI 166
Cdd:PRK13543 90 LPGLKADLSTLENLHFLCGLHGRR-AKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
170 180
....*....|....*....|....*....
gi 1419237541 167 DKKGVSDLIVHIEKHCENGGMVIFTSHQA 195
Cdd:PRK13543 169 DLEGITLVNRMISAHLRGGGAALVTTHGA 197
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-197 |
3.32e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 121.71 E-value: 3.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFYLAH 86
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 HAGVKPELSPWENLRFYQKIQGL--ALDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFT 164
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLprKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190
....*....|....*....|....*....|...
gi 1419237541 165 AIDKKGVSDLIVHIEKHCENGGMVIFTSHQAAE 197
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEE 193
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-197 |
9.23e-34 |
|
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: 120.73 E-value: 9.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFYLAH 86
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 HAGVKPELSPWENLRFYQKIQGLALDDEALWYA--LDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFT 164
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEelIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190
....*....|....*....|....*....|...
gi 1419237541 165 AIDKKGVSDLIVHIEKHCENGGMVIFTSHQAAE 197
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQE 194
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-193 |
2.32e-30 |
|
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: 109.79 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFYLAH 86
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 HAGVKPELSPWENLRfyqkiqglalddealwyaldkvgligreelacsyLSAGQQRRVALAKLWLIKQKLWILDEPFTAI 166
Cdd:cd03230 81 EPSLYENLTVRENLK----------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180
....*....|....*....|....*..
gi 1419237541 167 DKKGVSDLIVHIEKHCENGGMVIFTSH 193
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSH 153
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-194 |
1.50e-28 |
|
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: 106.40 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 15 ERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRdeyyseLFYLAHHAGV---K 91
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS------LKELRRKVGLvfqN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 92 PE-----LSPWENLRFYQKIQGLALDD--EALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFT 164
Cdd:cd03225 84 PDdqffgPTVEEEVAFGLENLGLPEEEieERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190
....*....|....*....|....*....|
gi 1419237541 165 AIDKKGVSDLIVHIEKHCENGGMVIFTSHQ 194
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAEGKTIIIVTHD 193
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
17-194 |
2.40e-28 |
|
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: 106.26 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 17 GENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQrdeyysELFYLAHHAGV---KPE 93
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKK------NLRELRRKVGLvfqNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 94 ---LSP--WENLRFYQKIQGLALD--DEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAI 166
Cdd:COG1122 86 dqlFAPtvEEDVAFGPENLGLPREeiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGL 165
|
170 180
....*....|....*....|....*...
gi 1419237541 167 DKKGVSDLIVHIEKHCENGGMVIFTSHQ 194
Cdd:COG1122 166 DPRGRRELLELLKRLNKEGKTVIIVTHD 193
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-201 |
2.48e-28 |
|
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: 104.25 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 8 TITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKqrdeyyselfylahh 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 88 agvkpelSPWENLRfyqkiqglalddealwyalDKVGLIGReelacsyLSAGQQRRVALAKLWLIKQKLWILDEPFTAID 167
Cdd:cd00267 66 -------LPLEELR-------------------RRIGYVPQ-------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190
....*....|....*....|....*....|....
gi 1419237541 168 KKGVSDLIVHIEKHCENGGMVIFTSHQAAESHKV 201
Cdd:cd00267 113 PASRERLLELLRELAEEGRTVIIVTHDPELAELA 146
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-208 |
1.13e-27 |
|
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: 104.15 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 9 ITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRdeyySELFYLAHHA 88
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER----KRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 89 GVKPE--LSPWE--NLRFYQKIQGL----ALDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILD 160
Cdd:cd03235 78 SIDRDfpISVRDvvLMGLYGHKGLFrrlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1419237541 161 EPFTAIDKKGVSDLIVHIEKHCENGGMVIFTSH--QAAESHKVKILSLDQ 208
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTHdlGLVLEYFDRVLLLNR 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-167 |
5.84e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 103.25 E-value: 5.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 1 MTHTN-QLTITNL----ACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRD 75
Cdd:COG1116 1 MSAAApALELRGVskrfPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 76 EYyselfylahhaGV---KPELSPW----ENLRFYQKIQGLALD---DEALWYaLDKVGLIGREElacSY---LSAGQQR 142
Cdd:COG1116 81 DR-----------GVvfqEPALLPWltvlDNVALGLELRGVPKAerrERAREL-LELVGLAGFED---AYphqLSGGMRQ 145
|
170 180
....*....|....*....|....*
gi 1419237541 143 RVALAKLWLIKQKLWILDEPFTAID 167
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALD 170
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-167 |
5.94e-25 |
|
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: 96.88 E-value: 5.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIeGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFYLAH 86
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 HAGVKPELSPWENLRFYQKIQGLA--LDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFT 164
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPskEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
...
gi 1419237541 165 AID 167
Cdd:cd03264 160 GLD 162
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-197 |
8.80e-25 |
|
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: 96.43 E-value: 8.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQK----QRDeyyseLF 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvppeRRN-----IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 83 YLAHHAGVKPELSPWENLRFYQKIQGLALDDE---ALWyALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWIL 159
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLRGVPKAEIrarVRE-LLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1419237541 160 DEPFTAIDKKGVSDLIVHIEKHCENGGM-VIFTSHQAAE 197
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGItTIYVTHDQEE 193
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
16-205 |
1.82e-24 |
|
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: 96.00 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 16 RGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRdeyyselfylaHHAGV---KP 92
Cdd:cd03293 14 GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----------PDRGYvfqQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 93 ELSPW----ENLRFYQKIQGLAlDDEALWYA---LDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTA 165
Cdd:cd03293 83 ALLPWltvlDNVALGLELQGVP-KAEARERAeelLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1419237541 166 ID---KKGVSDLIVHIEKhcENGGMVIFTSHQAAE----SHKVKILS 205
Cdd:cd03293 162 LDaltREQLQEELLDIWR--ETGKTVLLVTHDIDEavflADRVVVLS 206
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-194 |
3.45e-24 |
|
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: 95.04 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQkqrDEYYSELFYLAH 86
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 HAGVKPELSPWENLRFYQKIQGLALDDEALW--YALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFT 164
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRidEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190
....*....|....*....|....*....|
gi 1419237541 165 AIDKKGVSDLIVHIEKHCENGGMVIFTSHQ 194
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-207 |
4.63e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 91.47 E-value: 4.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 37 IEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYyseLFYLAHHAGVKPELSPWENLRFYQKIQGLAlddEAL 116
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY---CTYIGHNLGLKLEMTVFENLKFWSEIYNSA---ETL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 117 WYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSDLIVHIEKHCENGGMVIFTSHQAA 196
Cdd:PRK13541 105 YAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHLES 184
|
170
....*....|.
gi 1419237541 197 ESHKVKILSLD 207
Cdd:PRK13541 185 SIKSAQILQLD 195
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
15-201 |
1.36e-22 |
|
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: 91.01 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 15 ERGENRLF--ENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDeyySEL-FYLAHHAGVK 91
Cdd:cd03255 11 GGGGEKVQalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSE---KELaAFRRRHIGFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 92 -------PELSPWENLRFYQKIQGLALDDEALW--YALDKVGLIGREELACSYLSAGQQRRVALAKLwLIKQ-KLWILDE 161
Cdd:cd03255 88 fqsfnllPDLTALENVELPLLLAGVPKKERRERaeELLERVGLGDRLNHYPSELSGGQQQRVAIARA-LANDpKIILADE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1419237541 162 PFTAIDKKGVSDLIVHIEKHCENGGM-VIFTSHQ---AAESHKV 201
Cdd:cd03255 167 PTGNLDSETGKEVMELLRELNKEAGTtIVVVTHDpelAEYADRI 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-197 |
1.94e-22 |
|
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: 89.55 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSE---LFY 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrrIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 84 LAHHAGVKPELSPWENLRFyqkiqglalddealwyaldkvgligreelacsYLSAGQQRRVALAKLWLIKQKLWILDEPF 163
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL--------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190
....*....|....*....|....*....|....*
gi 1419237541 164 TAIDKKGVSDLIVHIEKHCENGGM-VIFTSHQAAE 197
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQLGItVVLVTHDLDE 163
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
27-198 |
2.11e-22 |
|
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: 90.50 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 27 FSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFYLAHHAGVKPELSPWENLRFYQKI 106
Cdd:cd03266 26 FTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTGLYDRLTARENLEYFAGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 107 QGLALDdeALWYALDKV-GLIGREELA---CSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSDLIVHIEKHC 182
Cdd:cd03266 106 YGLKGD--ELTARLEELaDRLGMEELLdrrVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLR 183
|
170
....*....|....*...
gi 1419237541 183 ENGGMVIFTSH--QAAES 198
Cdd:cd03266 184 ALGKCILFSTHimQEVER 201
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-194 |
2.90e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 90.20 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLfeNCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQK----QRDeyYSELF 82
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlppaERP--VSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 83 Y---LAHHagvkpeLSPWENLrfyqkiqGLALDD---------EALWYALDKVGLIGREELACSYLSAGQQRRVALAKLW 150
Cdd:COG3840 78 QennLFPH------LTVAQNI-------GLGLRPglkltaeqrAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1419237541 151 LIKQKLWILDEPFTAID---KKGVSDLIVHIekHCENGGMVIFTSHQ 194
Cdd:COG3840 145 VRKRPILLLDEPFSALDpalRQEMLDLVDEL--CRERGLTVLMVTHD 189
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-201 |
7.53e-22 |
|
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: 88.81 E-value: 7.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRdEYYSELFYLAH 86
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 HAGVKPELSPWENLRFYQKIQGLalDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAI 166
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGI--RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1419237541 167 DKKGVSDLIVHIEKHCENGGMVIFTSHQAAESHKV 201
Cdd:cd03268 158 DPDGIKELRELILSLRDQGITVLISSHLLSEIQKV 192
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-169 |
8.88e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 91.31 E-value: 8.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQK----QRD------E 76
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlppeKRNvgmvfqD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 77 YysELFylahhagvkPELSPWENLRFYQKIQGLALDD--EALWYALDKVGLigrEELACSY---LSAGQQRRVALAKLWL 151
Cdd:COG3842 86 Y--ALF---------PHLTVAENVAFGLRMRGVPKAEirARVAELLELVGL---EGLADRYphqLSGGQQQRVALARALA 151
|
170
....*....|....*...
gi 1419237541 152 IKQKLWILDEPFTAIDKK 169
Cdd:COG3842 152 PEPRVLLLDEPLSALDAK 169
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
16-208 |
2.87e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.42 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 16 RGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDeyySELFYLAHHAGV----- 90
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKR---REIPYLRRRIGVvfqdf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 91 K--PELSPWENLRFYQKIQGLALDD--EALWYALDKVGLIGREELACSYLSAGQQRRVALAKLwLIKQ-KLWILDEPFTA 165
Cdd:COG2884 89 RllPDRTVYENVALPLRVTGKSRKEirRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARA-LVNRpELLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1419237541 166 IDKKGVSDLIVHIEKHCENGGMVIFTSHQAA--ESHKVKILSLDQ 208
Cdd:COG2884 168 LDPETSWEIMELLEEINRRGTTVLIATHDLElvDRMPKRVLELED 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
26-210 |
4.59e-21 |
|
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: 86.79 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 26 NFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFYLAHHAGVKPELSPWENLRFYQK 105
Cdd:cd03263 22 SLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQFDALFDELTVREHLRFYAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 106 IQGL---ALDDEALWYaLDKVGLIGREELACSYLSAGQQRRVALAkLWLIKQ-KLWILDEPFTAID---KKGVSDLIVHI 178
Cdd:cd03263 102 LKGLpksEIKEEVELL-LRVLGLTDKANKRARTLSGGMKRKLSLA-IALIGGpSVLLLDEPTSGLDpasRRAIWDLILEV 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 1419237541 179 EKHCEnggmVIFTSHQAAE----SHKVKILSLDQFK 210
Cdd:cd03263 180 RKGRS----IILTTHSMDEaealCDRIAIMSDGKLR 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
24-197 |
6.25e-21 |
|
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: 86.91 E-value: 6.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 24 NCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQK----QRD-----EYYSeLFylahhagvkPEL 94
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpphKRPvntvfQNYA-LF---------PHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 95 SPWENLRFYQKIQGLALDD--EALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVS 172
Cdd:cd03300 88 TVFENIAFGLRLKKLPKAEikERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRK 167
|
170 180
....*....|....*....|....*.
gi 1419237541 173 DLIVHIEK-HCENGGMVIFTSHQAAE 197
Cdd:cd03300 168 DMQLELKRlQKELGITFVFVTHDQEE 193
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-167 |
7.13e-21 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 86.78 E-value: 7.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGE----NRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRD-EYYSE- 80
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRRv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 81 --LF---YLAHHagvkPELSPWENLRFYQKIQGLALDDEALWYALDKVGLigREELACSY---LSAGQQRRVALAKLWLI 152
Cdd:COG1124 82 qmVFqdpYASLH----PRHTVDRILAEPLRIHGLPDREERIAELLEQVGL--PPSFLDRYphqLSGGQRQRVAIARALIL 155
|
170
....*....|....*
gi 1419237541 153 KQKLWILDEPFTAID 167
Cdd:COG1124 156 EPELLLLDEPTSALD 170
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-167 |
2.36e-20 |
|
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: 85.31 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENR-LFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDeyySELFYLA 85
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKG---KALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 86 HHAG-------VKPELSPWENL---RFYQK--IQGLA-----LDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAK 148
Cdd:cd03256 78 RQIGmifqqfnLIERLSVLENVlsgRLGRRstWRSLFglfpkEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170
....*....|....*....
gi 1419237541 149 LWLIKQKLWILDEPFTAID 167
Cdd:cd03256 158 ALMQQPKLILADEPVASLD 176
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-193 |
3.62e-20 |
|
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: 83.64 E-value: 3.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 8 TITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQK-QRDEyyselfyLAH 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKE-------LAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 HAGVKPElspwenlrfyqkiqglalddealwyALDKVGLigrEELA---CSYLSAGQQRRVALAKLwLIKQ-KLWILDEP 162
Cdd:cd03214 74 KIAYVPQ-------------------------ALELLGL---AHLAdrpFNELSGGERQRVLLARA-LAQEpPILLLDEP 124
|
170 180 190
....*....|....*....|....*....|..
gi 1419237541 163 FTAIDKKGVSDLIVHIEKHCENGGM-VIFTSH 193
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKtVVMVLH 156
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-169 |
6.11e-20 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 86.24 E-value: 6.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 6 QLTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEG--YVLWNDI---PIQKqRDeyYSE 80
Cdd:TIGR03265 4 YLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGtiYQGGRDItrlPPQK-RD--YGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 81 LF--YlahhaGVKPELSPWENLRFYQKIQGLALD--DEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKL 156
Cdd:TIGR03265 81 VFqsY-----ALFPNLTVADNIAYGLKNRGMGRAevAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGL 155
|
170
....*....|...
gi 1419237541 157 WILDEPFTAIDKK 169
Cdd:TIGR03265 156 LLLDEPLSALDAR 168
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-194 |
2.15e-19 |
|
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: 85.42 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 16 RGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQK-QRDEYYSELFYLAHHAGVkPEL 94
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWVPQHPFL-FAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 95 SPWENLRFYQKIQglalDDEALWYALDKVGL--------------IGReelACSYLSAGQQRRVALAKLWLIKQKLWILD 160
Cdd:TIGR02857 411 TIAENIRLARPDA----SDAEIREALERAGLdefvaalpqgldtpIGE---GGAGLSGGQAQRLALARAFLRDAPLLLLD 483
|
170 180 190
....*....|....*....|....*....|....
gi 1419237541 161 EPFTAIDKKGVSDLIVHIEKHCEnGGMVIFTSHQ 194
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHR 516
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-200 |
2.71e-19 |
|
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: 82.03 E-value: 2.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 11 NLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFYLAHHAGV 90
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 91 KPELSPWENLRFYQKIQGL--ALDDEALWYALDKVGLI-GREELACSYlSAGQQRRVALAKLWLIKQKLWILDEPFTAID 167
Cdd:cd03265 85 DDELTGWENLYIHARLYGVpgAERRERIDELLDFVGLLeAADRLVKTY-SGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190
....*....|....*....|....*....|....
gi 1419237541 168 KKGVSDLIVHIEKHCENGGMVIF-TSHQAAESHK 200
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEFGMTILlTTHYMEEAEQ 197
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-167 |
3.73e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.00 E-value: 3.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 1 MTHTNQLTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWN-----DIPIQkQRD 75
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgedvtHRSIQ-QRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 76 -----EYYSeLFylahhagvkPELSPWENLRFYQKIQGLALDD--EALWYALDKVGLIGREELACSYLSAGQQRRVALAK 148
Cdd:PRK11432 80 icmvfQSYA-LF---------PHMSLGENVGYGLKMLGVPKEErkQRVKEALELVDLAGFEDRYVDQISGGQQQRVALAR 149
|
170
....*....|....*....
gi 1419237541 149 LWLIKQKLWILDEPFTAID 167
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLD 168
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-193 |
5.97e-19 |
|
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: 81.40 E-value: 5.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNL----ACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEyysELF 82
Cdd:cd03257 2 LEVKNLsvsfPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRR---LRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 83 YLAHHAGVKPE-----LSP--------WENLRFYQKIQGLALDDEALWYALDKVGLigREELACSY---LSAGQQRRVAL 146
Cdd:cd03257 79 IRRKEIQMVFQdpmssLNPrmtigeqiAEPLRIHGKLSKKEARKEAVLLLLVGVGL--PEEVLNRYpheLSGGQRQRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1419237541 147 AKLWLIKQKLWILDEPFTAID---KKGVSDLIVHIEKhcENGGMVIFTSH 193
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDvsvQAQILDLLKKLQE--ELGLTLLFITH 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-193 |
1.20e-18 |
|
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: 83.34 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 21 LFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIqKQRDeyyseLFYLAHHAGVKP---EL--- 94
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL-RQID-----PASLRRQIGVVLqdvFLfsg 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 95 SPWENLRFYQKiqglALDDEALWYALDKVGL---IgrEELACSY----------LSAGQQRRVALAKLWLIKQKLWILDE 161
Cdd:COG2274 564 TIRENITLGDP----DATDEEIIEAARLAGLhdfI--EALPMGYdtvvgeggsnLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190
....*....|....*....|....*....|...
gi 1419237541 162 PFTAIDKKGVSDLIVHIEKHCenGGM-VIFTSH 193
Cdd:COG2274 638 ATSALDAETEAIILENLRRLL--KGRtVIIIAH 668
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-193 |
1.41e-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: 79.99 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 16 RGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPI-QKQRdeyYSELFYLAHHagVKPEL 94
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkAKER---RKSIGYVMQD--VDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 95 ---SPWENLRFYQKIqgLALDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKG- 170
Cdd:cd03226 85 ftdSVREELLLGLKE--LDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNm 162
|
170 180
....*....|....*....|....*
gi 1419237541 171 --VSDLIVHIEKhceNGGMVIFTSH 193
Cdd:cd03226 163 erVGELIRELAA---QGKAVIVITH 184
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
24-193 |
1.73e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 80.09 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 24 NCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPI----QKQRDEYYSEL-------FYLAhhagvkP 92
Cdd:COG1136 26 GVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsERELARLRRRHigfvfqfFNLL------P 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 93 ELSPWENLRFYQKIQGL--ALDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLwLIKQ-KLWILDEPFTAIDKK 169
Cdd:COG1136 100 ELTALENVALPLLLAGVsrKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARA-LVNRpKLILADEPTGNLDSK 178
|
170 180
....*....|....*....|....*..
gi 1419237541 170 ---GVSDLIVHIekHCENGGMVIFTSH 193
Cdd:COG1136 179 tgeEVLELLREL--NRELGTTIVMVTH 203
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-198 |
2.75e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.11 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEyYSELFYLAh 86
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED-TRLMFQDA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 hagvkpELSPW----ENLrfyqkiqGLALD----DEALwYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWI 158
Cdd:PRK11247 91 ------RLLPWkkviDNV-------GLGLKgqwrDAAL-QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1419237541 159 LDEPFTAID---KKGVSDLIVHIEKhcENGGMVIFTSHQAAES 198
Cdd:PRK11247 157 LDEPLGALDaltRIEMQDLIESLWQ--QHGFTVLLVTHDVSEA 197
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-168 |
7.65e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 78.29 E-value: 7.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMP---AEGYVLWND-----IPIQKQR---- 74
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGrrltaLPAEQRRigil 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 75 --DEYyseLFylahhagvkPELSPWENLRFY--QKIQGLALDDEALwYALDKVGLIGREELACSYLSAGQQRRVALAKLW 150
Cdd:COG4136 82 fqDDL---LF---------PHLSVGENLAFAlpPTIGRAQRRARVE-QALEEAGLAGFADRDPATLSGGQRARVALLRAL 148
|
170
....*....|....*...
gi 1419237541 151 LIKQKLWILDEPFTAIDK 168
Cdd:COG4136 149 LAEPRALLLDEPFSKLDA 166
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
24-197 |
8.96e-18 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 79.22 E-value: 8.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 24 NCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSEL--------FylaHHAGVKPELS 95
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkismvF---QSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 96 PWENLRFYQKIQGLALDD--EALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAID---KKG 170
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEreERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDpliRRE 198
|
170 180
....*....|....*....|....*..
gi 1419237541 171 VSDLIVHIEKhcENGGMVIFTSHQAAE 197
Cdd:cd03294 199 MQDELLRLQA--ELQKTIVFITHDLDE 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-211 |
1.29e-17 |
|
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: 77.93 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 9 ITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQK-QRDEYYSE------L 81
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlSEAELYRLrrrmgmL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 82 FylaHHAGVKPELSPWENLRFY---------QKIQGLALDdealwyALDKVGLIGREELACSYLSAGQQRRVALAKLWLI 152
Cdd:cd03261 83 F---QSGALFDSLTVFENVAFPlrehtrlseEEIREIVLE------KLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1419237541 153 KQKLWILDEPFTAIDKKG---VSDLIVHIekHCENGGMVIFTSHQAAESHKV--KILSLDQFKL 211
Cdd:cd03261 154 DPELLLYDEPTAGLDPIAsgvIDDLIRSL--KKELGLTSIMVTHDLDTAFAIadRIAVLYDGKI 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-193 |
2.24e-17 |
|
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: 79.56 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACE-----RGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEyysEL 81
Cdd:COG1123 261 LEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR---SL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 82 FYLAHHAGV---KPE--LSPW--------ENLRFYQKIQGLALDDEALWyALDKVGLigREELACSY---LSAGQQRRVA 145
Cdd:COG1123 338 RELRRRVQMvfqDPYssLNPRmtvgdiiaEPLRLHGLLSRAERRERVAE-LLERVGL--PPDLADRYpheLSGGQRQRVA 414
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1419237541 146 LAKLWLIKQKLWILDEPFTAIDKKGVSDLIVHIEKHCENGGM-VIFTSH 193
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLtYLFISH 463
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
24-211 |
3.92e-17 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 76.29 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 24 NCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDeyySELFYLAHHAGVK-------PELSP 96
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRG---RAIPYLRRKIGVVfqdfrllPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 97 WENLRFYQKIQGLALDD--EALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSDL 174
Cdd:cd03292 96 YENVAFALEVTGVPPREirKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1419237541 175 IVHIEKHCENGGMVIFTSHQAA--ESHKVKILSLDQFKL 211
Cdd:cd03292 176 MNLLKKINKAGTTVVVATHAKElvDTTRHRVIALERGKL 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-201 |
4.01e-17 |
|
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: 76.61 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWND-----IPIQKQrdeyysEL 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdVPVQER------NV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 82 FYLAHHAGVKPELSPWENLRFYQKIQ-GLALDDEALWYA-----LDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQK 155
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKpRSERPPEAEIRAkvhelLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1419237541 156 LWILDEPFTAIDKKGVSDLIVHIEK-HCENGGMVIFTSHQAAESHKV 201
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRlHDELHVTTVFVTHDQEEALEV 203
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-201 |
5.13e-17 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 75.99 E-value: 5.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 28 SVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWN--DIPIQKQRDEYYSELF-------YLAHHAGVKPELSPWE 98
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvDVTAAPPADRPVSMLFqennlfaHLTVEQNVGLGLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 99 NLRfyqkiqglALDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAID---KKGVSDLI 175
Cdd:cd03298 100 KLT--------AEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalRAEMLDLV 171
|
170 180
....*....|....*....|....*.
gi 1419237541 176 VHIekHCENGGMVIFTSHQAAESHKV 201
Cdd:cd03298 172 LDL--HAETKMTVLMVTHQPEDAKRL 195
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-194 |
5.98e-17 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 76.57 E-value: 5.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 6 QLTITNLACERGENR-LFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEyysELFYL 84
Cdd:TIGR02315 1 MLEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGK---KLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 85 AHHAG-------VKPELSPWENL--------RFYQKIQGLALDDE---ALwYALDKVGLIGREELACSYLSAGQQRRVAL 146
Cdd:TIGR02315 78 RRRIGmifqhynLIERLTVLENVlhgrlgykPTWRSLLGRFSEEDkerAL-SALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1419237541 147 AKLWLIKQKLWILDEPFTAIDKKG---VSDLIVHIEKhcENGGMVIFTSHQ 194
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTskqVMDYLKRINK--EDGITVIINLHQ 205
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-193 |
6.82e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 77.49 E-value: 6.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWND------IPIQKQRdeyyse 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlftnLPPRERR------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 81 LFYLAHHAGVKPELSPWENLRFYQKIQGLALDD-----EALwyaLDKVGLigrEELACSY---LSAGQQRRVALAKLWLI 152
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEirarvEEL---LELVQL---EGLADRYpsqLSGGQRQRVALARALAV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1419237541 153 KQKLWILDEPFTAID---KKGVSDLIVHIekHCENGGMVIFTSH 193
Cdd:COG1118 151 EPEVLLLDEPFGALDakvRKELRRWLRRL--HDELGGTTVFVTH 192
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-196 |
7.28e-17 |
|
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: 75.68 E-value: 7.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGL-----AMPAEGYVLWNDipiqkqRDEYYSEL 81
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDG------KDIYDLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 82 FYLAHHAGV-----KP---ELSPWENLRFYQKIQGL----ALDDEALWyALDKVGLIGRE--ELACSYLSAGQQRRVALA 147
Cdd:cd03260 75 DVLELRRRVgmvfqKPnpfPGSIYDNVAYGLRLHGIklkeELDERVEE-ALRKAALWDEVkdRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1419237541 148 KLWLIKQKLWILDEPFTAID---KKGVSDLIVHIEKHCenggMVIFTSH---QAA 196
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDpisTAKIEELIAELKKEY----TIVIVTHnmqQAA 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-201 |
1.53e-16 |
|
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: 75.02 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEyysELFYLAH 86
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEK---ELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 HAGVkpeL----------SPWENLRFY---------QKIQGLALddealwYALDKVGLIGREELACSYLSAGQQRRVALA 147
Cdd:COG1127 83 RIGM---LfqggalfdslTVFENVAFPlrehtdlseAEIRELVL------EKLELVGLPGAADKMPSELSGGMRKRVALA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1419237541 148 KLWLIKQKLWILDEPFTAID---KKGVSDLIVHIekHCENGGMVIFTSHQAAESHKV 201
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDpitSAVIDELIREL--RDELGLTSVVVTHDLDSAFAI 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-197 |
1.68e-16 |
|
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: 74.64 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 24 NCNFsVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYV-----LWND------IPIQKQRdeyyseLFYLAHHAGVKP 92
Cdd:cd03297 16 KIDF-DLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtVLFDsrkkinLPPQQRK------IGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 93 ELSPWENLRFYQKIQGLALDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVS 172
Cdd:cd03297 89 HLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180
....*....|....*....|....*.
gi 1419237541 173 DLIVHIEK-HCENGGMVIFTSHQAAE 197
Cdd:cd03297 169 QLLPELKQiKKNLNIPVIFVTHDLSE 194
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-167 |
7.61e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 73.65 E-value: 7.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 1 MTHTNQLTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWN--DIPiQKQRDEYY 78
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDgeNIP-AMSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 79 ------SELFylaHHAGVKPELSPWEN----LRFYQKIQGLALDDEALwYALDKVGLIGREELACSYLSAGQQRRVALAK 148
Cdd:PRK11831 81 tvrkrmSMLF---QSGALFTDMNVFDNvaypLREHTQLPAPLLHSTVM-MKLEAVGLRGAAKLMPSELSGGMARRAALAR 156
|
170
....*....|....*....
gi 1419237541 149 LWLIKQKLWILDEPFTAID 167
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQD 175
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-197 |
7.67e-16 |
|
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: 73.35 E-value: 7.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSEL--FYL 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgiGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 85 AHHAGVKPELSPWENLRFYQKIQGL--ALDDEALWYALDKVGLigrEELA---CSYLSAGQQRRVALAKLWLIKQKLWIL 159
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLskKEREEKLEELLEEFHI---THLRkskASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1419237541 160 DEPFTAIDKKGVSDlIVHIEKHCENGGM-VIFTSHQAAE 197
Cdd:cd03218 158 DEPFAGVDPIAVQD-IQKIIKILKDRGIgVLITDHNVRE 195
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-194 |
9.96e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 73.99 E-value: 9.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 24 NCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQkqrDEYYSELFYLahhagvkPE-------LSP 96
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIGYL-------PEerglypkMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 97 WENLRFYQKIQGLALDD--EALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSDL 174
Cdd:COG4152 89 GEQLVYLARLKGLSKAEakRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELL 168
|
170 180
....*....|....*....|
gi 1419237541 175 IVHIEKHCENGGMVIFTSHQ 194
Cdd:COG4152 169 KDVIRELAAKGTTVIFSSHQ 188
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-194 |
1.12e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.08 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 5 NQLTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDE-------- 76
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvad 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 77 ------YYSELFYLAHHAGVKPELSPWENLrFYQKIQGLALD-----DEALWYaLDKVGLIGREELAC-SYLSAGQQRRV 144
Cdd:PRK10619 84 knqlrlLRTRLTMVFQHFNLWSHMTVLENV-MEAPIQVLGLSkqearERAVKY-LAKVGIDERAQGKYpVHLSGGQQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1419237541 145 ALAKLWLIKQKLWILDEPFTAIDKKGVSDLIVHIEKHCENGGMVIFTSHQ 194
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-193 |
1.19e-15 |
|
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: 71.31 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 24 NCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKqrdeyyselfylahhagvkpeLSPWENLRF- 102
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF---------------------ASPRDARRAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 103 ----YQkiqglalddealwyaldkvgligreelacsyLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSDLIVHI 178
Cdd:cd03216 77 iamvYQ-------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI 125
|
170
....*....|....*
gi 1419237541 179 EKHCENGGMVIFTSH 193
Cdd:cd03216 126 RRLRAQGVAVIFISH 140
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-196 |
1.26e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.46 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 5 NQLTITNLACERGENR-LFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGL--------AMPAEGYVLWndIPiqkQRD 75
Cdd:COG4178 361 GALALEDLTLRTPDGRpLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwpygsgriARPAGARVLF--LP---QRP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 76 eyyselfYLahhagvkpelsPWENLR---FYQKIQGlALDDEALWYALDKVGL---IGR--EELACSY-LSAGQQRRVAL 146
Cdd:COG4178 436 -------YL-----------PLGTLRealLYPATAE-AFSDAELREALEAVGLghlAERldEEADWDQvLSLGEQQRLAF 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1419237541 147 AKLWLIKQKLWILDEPFTAIDKKGVSDLIVHIEKHCEnGGMVIFTSHQAA 196
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLREELP-GTTVISVGHRST 545
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-193 |
1.83e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.16 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 18 ENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRdeyySELFYLAHHAGV---KPEL 94
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKK----VKLSDIRKKVGLvfqYPEY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 95 SPWENlRFYQKI----QGLALDDEAL----WYALDKVGLiGREELACSY---LSAGQQRRVALAKLWLIKQKLWILDEPF 163
Cdd:PRK13637 95 QLFEE-TIEKDIafgpINLGLSEEEIenrvKRAMNIVGL-DYEDYKDKSpfeLSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190
....*....|....*....|....*....|.
gi 1419237541 164 TAIDKKGVSDLIVHIEK-HCENGGMVIFTSH 193
Cdd:PRK13637 173 AGLDPKGRDEILNKIKElHKEYNMTIILVSH 203
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-194 |
2.13e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 71.04 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 20 RLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPA--EGYVLWNDIPIQKqrDEYYSELFYLAHHAGVKPELSPW 97
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDK--RSFRKIIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 98 ENLRFYQKIQGlalddealwyaldkvgligreelacsyLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSDLIVH 177
Cdd:cd03213 101 ETLMFAAKLRG---------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153
|
170
....*....|....*..
gi 1419237541 178 IEKHCENGGMVIFTSHQ 194
Cdd:cd03213 154 LRRLADTGRTIICSIHQ 170
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-193 |
3.16e-15 |
|
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: 69.40 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDipiqkqrdeyYSELFYLAH 86
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS----------TVKIGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 hagvkpelspwenlrfyqkiqglalddealwyaldkvgligreelacsyLSAGQQRRVALAKLWLIKQKLWILDEPFTAI 166
Cdd:cd03221 71 -------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
170 180
....*....|....*....|....*..
gi 1419237541 167 DKKGVSDLIVHIEKHcenGGMVIFTSH 193
Cdd:cd03221 102 DLESIEALEEALKEY---PGTVILVSH 125
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
17-193 |
6.29e-15 |
|
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: 69.55 E-value: 6.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 17 GENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRdeyyselfylahhagvkpelsp 96
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 97 WENLRfyQKIQGLALDDEALwyaldkVGLIgreelACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKG---VSD 173
Cdd:cd03246 71 PNELG--DHVGYLPQDDELF------SGSI-----AENILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGeraLNQ 137
|
170 180
....*....|....*....|
gi 1419237541 174 LIVHIEKhceNGGMVIFTSH 193
Cdd:cd03246 138 AIAALKA---AGATRIVIAH 154
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-191 |
6.84e-15 |
|
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: 70.25 E-value: 6.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQR---DEYYSELFY 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKkniNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 84 LAHHAGVKPELSPWENLRFYQ-KIQGLAlDDEALWYA---LDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWIL 159
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPiKVKGMS-KAEAEERAlelLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1419237541 160 DEPFTAIDK---KGVSDLIVHIEKhcENGGMVIFT 191
Cdd:cd03262 160 DEPTSALDPelvGEVLDVMKDLAE--EGMTMVVVT 192
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-198 |
6.97e-15 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 70.57 E-value: 6.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 23 ENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEyysELFYLAHHAgvkpeLSPWENLRf 102
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD---RMVVFQNYS-----LLPWLTVR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 103 yQKIqGLALD-----------DEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGV 171
Cdd:TIGR01184 73 -ENI-ALAVDrvlpdlskserRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180
....*....|....*....|....*...
gi 1419237541 172 SDLIVHIEKHC-ENGGMVIFTSHQAAES 198
Cdd:TIGR01184 151 GNLQEELMQIWeEHRVTVLMVTHDVDEA 178
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-207 |
9.99e-15 |
|
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: 68.72 E-value: 9.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 19 NRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLampaegyvlWndiP-----IQKQRDEyysELFYLAHhagvKPE 93
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL---------W---PwgsgrIGMPEGE---DLLFLPQ----RPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 94 LSPwENLRfyqkiqglalddEALWYALDKVgligreelacsyLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSD 173
Cdd:cd03223 75 LPL-GTLR------------EQLIYPWDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180 190
....*....|....*....|....*....|....*
gi 1419237541 174 LIVHIEKHCENggmVIFTSHQAA-ESHKVKILSLD 207
Cdd:cd03223 130 LYQLLKELGIT---VISVGHRPSlWKFHDRVLDLD 161
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
16-197 |
1.02e-14 |
|
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: 70.50 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 16 RGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVL---------WN--DIpiqKQRDEYYS-ELfy 83
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerrggEDvwEL---RKRIGLVSpAL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 84 lahHAGVKPELSPWE--------NLRFYQKIQglALDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLwLIKQ- 154
Cdd:COG1119 88 ---QLRFPRDETVLDvvlsgffdSIGLYREPT--DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARA-LVKDp 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1419237541 155 KLWILDEPFTAIDKKGVSDLIVHIEKHCENGGM-VIFTSHQAAE 197
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPtLVLVTHHVEE 205
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-198 |
1.02e-14 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 71.37 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 39 GHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQkQRDEYYSELFYLAHHAGVKPELSPWENLRFYQKIQGL--ALDDEAL 116
Cdd:TIGR01187 3 GPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-NVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVprAEIKPRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 117 WYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKgVSDLIVHIEK--HCENGGMVIFTSHQ 194
Cdd:TIGR01187 82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKK-LRDQMQLELKtiQEQLGITFVFVTHD 160
|
....
gi 1419237541 195 AAES 198
Cdd:TIGR01187 161 QEEA 164
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-194 |
2.23e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 69.83 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 16 RGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFYLAHHAGVKPELS 95
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 96 PwenlRFYQKIQ----GLALDDEALWYALDK-VGLIGREEL---ACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAID 167
Cdd:PRK13652 94 P----TVEQDIAfgpiNLGLDEETVAHRVSSaLHMLGLEELrdrVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180
....*....|....*....|....*...
gi 1419237541 168 KKGVSDLIVHIEKHCENGGM-VIFTSHQ 194
Cdd:PRK13652 170 PQGVKELIDFLNDLPETYGMtVIFSTHQ 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-197 |
2.55e-14 |
|
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: 70.70 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACE--RGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPA---EGYVLWNDIPIQKQRDEyysel 81
Cdd:COG1123 5 LEVRDLSVRypGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEA----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 82 fYLAHHAGVKPE-----LSPW---ENLRFYQKIQGL---ALDDEALWyALDKVGLIGREELACSYLSAGQQRRVALAKLW 150
Cdd:COG1123 80 -LRGRRIGMVFQdpmtqLNPVtvgDQIAEALENLGLsraEARARVLE-LLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1419237541 151 LIKQKLWILDEPFTAIDKKGVSDLIVHIEKHCENGGM-VIFTSHQAAE 197
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTtVLLITHDLGV 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
17-193 |
2.71e-14 |
|
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: 67.79 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 17 GENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQK-QRDEYYSELFYLAHHagvkPEL- 94
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAYVPQD----PFLf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 95 --SPWENLrfyqkiqglalddealwyaldkvgligreelacsyLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVS 172
Cdd:cd03228 89 sgTIRENI-----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180
....*....|....*....|.
gi 1419237541 173 DLIVHIEKHCEnGGMVIFTSH 193
Cdd:cd03228 134 LILEALRALAK-GKTVIVIAH 153
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-204 |
3.07e-14 |
|
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: 68.90 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLfENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWN--DI---PIQKQRDEYYSEL 81
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkDItnlPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 82 FYLAHHAGVKPELSPWENLRFYQKIQglalDDEALwyaLDKVGLIGREELACSY---LSAGQQRRVALAKLWLIKQKLWI 158
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKE----IERKV---LEIAEMLGIDHLLNRKpetLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1419237541 159 LDEPFTAIDKKGVSDLIVHIEK-HCENGGMVIFTSHQAAE----SHKVKIL 204
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKiRKEFGVTVLHVTHDFEEawalADKVAIM 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-162 |
3.35e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 9 ITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEG--------------------------- 61
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGevsipkglrigylpqeppldddltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 62 YVLWNDIPIQKQRDEYyselfylaHHAGVKPElSPWENLRFYQKIQGlALDDEALWYA-------LDKVGLIGRE-ELAC 133
Cdd:COG0488 81 TVLDGDAELRALEAEL--------EELEAKLA-EPDEDLERLAELQE-EFEALGGWEAearaeeiLSGLGFPEEDlDRPV 150
|
170 180
....*....|....*....|....*....
gi 1419237541 134 SYLSAGQQRRVALAKLWLIKQKLWILDEP 162
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-204 |
3.78e-14 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 69.00 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 17 GENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIpiqKQRDEyySELFYLAHHAGV---KPE 93
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGL---DTLDE--ENLWEIRKKVGMvfqNPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 94 -------------LSPwENLRF-----YQKIQglalddealwYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQK 155
Cdd:TIGR04520 88 nqfvgatveddvaFGL-ENLGVpreemRKRVD----------EALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1419237541 156 LWILDEPFTAIDKKGVSDLIVHIEK-HCENGGMVIFTSH---QAAESHKVKIL 204
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKlNKEEGITVISITHdmeEAVLADRVIVM 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-167 |
5.57e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 68.64 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPI-QKQRDEyyselfyLA 85
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLaDWSPAE-------LA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 86 HHAGVKPE-----------------LSPWENLRfyqkiqglALDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAK 148
Cdd:PRK13548 76 RRRAVLPQhsslsfpftveevvamgRAPHGLSR--------AEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLAR 147
|
170 180
....*....|....*....|....*
gi 1419237541 149 ----LWLI--KQKLWILDEPFTAID 167
Cdd:PRK13548 148 vlaqLWEPdgPPRWLLLDEPTSALD 172
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-167 |
6.40e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.19 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRdeyySELFYLAH 86
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 HAGVKPELSPWENLRFYQKIQGLALDD--EALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFT 164
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQrlEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
...
gi 1419237541 165 AID 167
Cdd:PRK11248 158 ALD 160
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
17-169 |
8.30e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 68.82 E-value: 8.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 17 GENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWN-----DIPIQkQRD-----EYYSeLFylah 86
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgqditHVPAE-NRHvntvfQSYA-LF---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 hagvkPELSPWENLRFYQKIQGLALDD--EALWYALDKVGLigrEELA---CSYLSAGQQRRVALAKLWLIKQKLWILDE 161
Cdd:PRK09452 99 -----PHMTVFENVAFGLRMQKTPAAEitPRVMEALRMVQL---EEFAqrkPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
....*...
gi 1419237541 162 PFTAIDKK 169
Cdd:PRK09452 171 SLSALDYK 178
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-198 |
1.29e-13 |
|
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: 69.27 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 14 CERGENRLFENC--------NFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFYLA 85
Cdd:TIGR01257 930 CVKNLVKIFEPSgrpavdrlNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 86 HHAGVKPELSPWENLRFYQKIQGLALDDEALWYA--LDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPF 163
Cdd:TIGR01257 1010 QHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEamLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190
....*....|....*....|....*....|....*...
gi 1419237541 164 TAID---KKGVSDLIVHIekhcENGGMVIFTSHQAAES 198
Cdd:TIGR01257 1090 SGVDpysRRSIWDLLLKY----RSGRTIIMSTHHMDEA 1123
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-162 |
2.71e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.78 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNdipiQKQRDEYYSElfylaH 86
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----ETVKIGYFDQ-----H 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 HAGVKPELSPWENLRfyqkiQGLALDDEAlwYALDKVG--LIGREEL--ACSYLSAGQQRRVALAKLWLIKQKLWILDEP 162
Cdd:COG0488 387 QEELDPDKTVLDELR-----DGAPGGTEQ--EVRGYLGrfLFSGDDAfkPVGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
23-201 |
3.64e-13 |
|
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: 66.17 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 23 ENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIqKQRDEyySELF----YLAHHAGVKPELSPWE 98
Cdd:cd03295 18 NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI-REQDP--VELRrkigYVIQQIGLFPHMTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 99 NLRFYQKIQGL------ALDDEALwyALdkVGLiGREELACSY---LSAGQQRRVALAKLWLIKQKLWILDEPFTAID-- 167
Cdd:cd03295 95 NIALVPKLLKWpkekirERADELL--AL--VGL-DPAEFADRYpheLSGGQQQRVGVARALAADPPLLLMDEPFGALDpi 169
|
170 180 190
....*....|....*....|....*....|....*
gi 1419237541 168 -KKGVSDLIVHIEKhcENGGMVIFTSHQAAESHKV 201
Cdd:cd03295 170 tRDQLQEEFKRLQQ--ELGKTIVFVTHDIDEAFRL 202
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-206 |
5.25e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.51 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 1 MTHTNQLTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYY-S 79
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYrQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 80 ELFYLAHhagvKPEL---SPWENLRFYQKIQGLALDDEALWYALDKVGLigREEL---ACSYLSAGQQRRVALAKLWLIK 153
Cdd:PRK10247 82 QVSYCAQ----TPTLfgdTVYDNLIFPWQIRNQQPDPAIFLDDLERFAL--PDTIltkNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1419237541 154 QKLWILDEPFTAID---KKGVSDLIVHIEKhcENGGMVIFTSHQAAE-SHKVKILSL 206
Cdd:PRK10247 156 PKVLLLDEITSALDesnKHNVNEIIHRYVR--EQNIAVLWVTHDKDEiNHADKVITL 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
39-193 |
5.64e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.80 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 39 GHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQkqrdeyYSELFYLAHHAGVKPELSPWENLRFYQKIQ----------G 108
Cdd:PRK13638 34 GANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD------YSKRGLLALRQQVATVFQDPEQQIFYTDIDsdiafslrnlG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 109 LALD------DEALwyALDKVGLIGREELACsyLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSDLIVHIEKHC 182
Cdd:PRK13638 108 VPEAeitrrvDEAL--TLVDAQHFRHQPIQC--LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIV 183
|
170
....*....|.
gi 1419237541 183 ENGGMVIFTSH 193
Cdd:PRK13638 184 AQGNHVIISSH 194
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-169 |
7.32e-13 |
|
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: 64.58 E-value: 7.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLW-----NDIPiQKQRD-----E 76
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIggrdvTDLP-PKDRDiamvfQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 77 YYSeLFylahhagvkPELSPWENLRFYQKIQGL---ALDDEALWYAldkvGLIGREELACSY---LSAGQQRRVALAKLW 150
Cdd:cd03301 80 NYA-LY---------PHMTVYDNIAFGLKLRKVpkdEIDERVREVA----ELLQIEHLLDRKpkqLSGGQRQRVALGRAI 145
|
170
....*....|....*....
gi 1419237541 151 LIKQKLWILDEPFTAIDKK 169
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAK 164
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-211 |
7.47e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.90 E-value: 7.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 17 GENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLW--NDIPIQKQRDEYYSE----LFYLAHHagV 90
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsgHDITRLKNREVPFLRrqigMIFQDHH--L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 91 KPELSPWENLRFYQKIQGLALDD--EALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDK 168
Cdd:PRK10908 91 LMDRTVYDNVAIPLIIAGASGDDirRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1419237541 169 KGVSDLIVHIEKHCENGGMVIFTSHQAA--ESHKVKILSLDQFKL 211
Cdd:PRK10908 171 ALSEGILRLFEEFNRVGVTVLMATHDIGliSRRSYRMLTLSDGHL 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-191 |
8.81e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.16 E-value: 8.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQR--DEYYSELFYL 84
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 85 AHHAG-------VKPELSPWENLrfyqkIQGLAL-----DDEALWYA---LDKVGLIGREELACSYLSAGQQRRVALAKL 149
Cdd:PRK11264 84 RQHVGfvfqnfnLFPHRTVLENI-----IEGPVIvkgepKEEATARArelLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1419237541 150 WLIKQKLWILDEPFTAIDKKGVSDLIVHIEKHC-ENGGMVIFT 191
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIVT 201
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-201 |
1.20e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 64.73 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 17 GENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQ---------KQRDEYYSELFYLAhh 87
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkvderliRQEAGMVFQQFYLF-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 88 agvkPELSPWENLRF-YQKIQGLALDD-EALWYAL-DKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFT 164
Cdd:PRK09493 90 ----PHLTALENVMFgPLRVRGASKEEaEKQARELlAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 1419237541 165 AIDKKGVSDLIVHIEKHCENG-GMVIFTsHQAAESHKV 201
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLAEEGmTMVIVT-HEIGFAEKV 202
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
24-204 |
1.25e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 64.77 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 24 NCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQrdeyysELFYLAHHAGVKPElSPwENlRFY 103
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDD------NFEKLRKHIGIVFQ-NP-DN-QFV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 104 QKI----QGLALDDEALWY---------ALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKG 170
Cdd:PRK13648 98 GSIvkydVAFGLENHAVPYdemhrrvseALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 1419237541 171 VSDLIVHIEKHCENGGMVIFT-SH---QAAESHKVKIL 204
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNITIISiTHdlsEAMEADHVIVM 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
7-201 |
1.79e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.14 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWN--DIPIQKQRDEYYSELFYL 84
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdeDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 85 AHHAGVKPELSPWENLRFYQKIQglalDDEALWYALDKVGLIgREELACSY--------LSAGQQRRVALAKLWLIKQKL 156
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIR----DDLSAEQREDRANEL-MEEFHIEHlrdsmgqsLSGGERRRVEIARALAANPKF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1419237541 157 WILDEPFTAIDKKGVSDlIVHIEKHCENGGM-VIFTSHQAAESHKV 201
Cdd:PRK10895 159 ILLDEPFAGVDPISVID-IKRIIEHLRDSGLgVLITDHNVRETLAV 203
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-197 |
1.85e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 64.37 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 18 ENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGyvlwnDIPIQKQRdeyYSE--LFYLAHHAGV---KP 92
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESG-----QIIIDGDL---LTEenVWDIRHKIGMvfqNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 93 E-----LSPWENLRFYQKIQGLALDD--EALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTA 165
Cdd:PRK13650 91 DnqfvgATVEDDVAFGLENKGIPHEEmkERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190
....*....|....*....|....*....|...
gi 1419237541 166 IDKKGVSDLIVHIEKHCENGGM-VIFTSHQAAE 197
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDYQMtVISITHDLDE 203
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-193 |
2.60e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.94 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 26 NFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRdeyySELFYLAHHAGV---KPE---LSPW-- 97
Cdd:PRK13639 22 NFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK----KSLLEVRKTVGIvfqNPDdqlFAPTve 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 98 ENLRFYQKIQGLALDD--EALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSDLI 175
Cdd:PRK13639 98 EDVAFGPLNLGLSKEEveKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIM 177
|
170
....*....|....*...
gi 1419237541 176 VHIEKHCENGGMVIFTSH 193
Cdd:PRK13639 178 KLLYDLNKEGITIIISTH 195
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-204 |
3.09e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 63.88 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 24 NCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIP--------IQKQ-----------------RDEYy 78
Cdd:PRK13635 25 DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdVRRQvgmvfqnpdnqfvgatvQDDV- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 79 seLFYLahhagvkpelspwENlrfyqkiQGLALDD--EALWYALDKVGL---IGREElacSYLSAGQQRRVALAKLWLIK 153
Cdd:PRK13635 104 --AFGL-------------EN-------IGVPREEmvERVDQALRQVGMedfLNREP---HRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1419237541 154 QKLWILDEPFTAIDKKGVSDLIVHIEKHCENGGM-VIFTSH---QAAESHKVKIL 204
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGItVLSITHdldEAAQADRVIVM 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-201 |
3.54e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 64.28 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 23 ENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSE-----LFYLAHHAGVKPELSPW 97
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkkIAMVFQSFALMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 98 ENLRFYQKIQGLALdDEALWYALDKVGLIGREELACSY---LSAGQQRRVALAKLWLIKQKLWILDEPFTAID---KKGV 171
Cdd:PRK10070 125 DNTAFGMELAGINA-EERREKALDALRQVGLENYAHSYpdeLSGGMRQRVGLARALAINPDILLMDEAFSALDpliRTEM 203
|
170 180 190
....*....|....*....|....*....|.
gi 1419237541 172 SDLIVHIE-KHCENggmVIFTSHQAAESHKV 201
Cdd:PRK10070 204 QDELVKLQaKHQRT---IVFISHDLDEAMRI 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-167 |
4.51e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.09 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFylah 86
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRV---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 hAGVKPELSPWENLRFYQKIQ------------GLALDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQ 154
Cdd:PRK09536 80 -ASVPQDTSLSFEFDVRQVVEmgrtphrsrfdtWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170
....*....|...
gi 1419237541 155 KLWILDEPFTAID 167
Cdd:PRK09536 159 PVLLLDEPTASLD 171
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-169 |
4.56e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 63.94 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 6 QLTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQ----KQRD-----E 76
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTdlppKDRNiamvfQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 77 YYSeLFylahhagvkPELSPWENLRFYQKIQGLALD--DEALWYALDKVGLigrEELACSY---LSAGQQRRVALAKLwL 151
Cdd:COG3839 83 SYA-LY---------PHMTVYENIAFPLKLRKVPKAeiDRRVREAAELLGL---EDLLDRKpkqLSGGQRQRVALGRA-L 148
|
170
....*....|....*....
gi 1419237541 152 IKQ-KLWILDEPFTAIDKK 169
Cdd:COG3839 149 VREpKVFLLDEPLSNLDAK 167
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-167 |
5.20e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.56 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWN--DIPIQKQRDEYYSelFYL 84
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgtDVSRLHARDRKVG--FVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 85 AHHAGVKpELSPWENLRF-------YQKIQGLALDDEALwYALDKVGLigrEELACSY---LSAGQQRRVALAKLWLIKQ 154
Cdd:PRK10851 81 QHYALFR-HMTVFDNIAFgltvlprRERPNAAAIKAKVT-QLLEMVQL---AHLADRYpaqLSGGQKQRVALARALAVEP 155
|
170
....*....|...
gi 1419237541 155 KLWILDEPFTAID 167
Cdd:PRK10851 156 QILLLDEPFGALD 168
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
26-211 |
5.98e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.28 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 26 NFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAE---------GYVL-----WN-----DIPIQKQRDEYYSEL----- 81
Cdd:PRK13640 27 SFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnskitvdGITLtaktvWDirekvGIVFQNPDNQFVGATvgddv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 82 -FYLAHHAGVKPELspwenlrfyQKIQGLALDDealwyaldkVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILD 160
Cdd:PRK13640 107 aFGLENRAVPRPEM---------IKIVRDVLAD---------VGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1419237541 161 EPFTAIDKKG---VSDLIVHIEKhcENGGMVIFTSHQAAE-SHKVKILSLDQFKL 211
Cdd:PRK13640 169 ESTSMLDPAGkeqILKLIRKLKK--KNNLTVISITHDIDEaNMADQVLVLDDGKL 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
17-167 |
7.45e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.90 E-value: 7.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 17 GENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQrdeyyselfylAHHA----GVKP 92
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR-----------ARHArqrvGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 93 E---LSP----WENLRFYQKIQGL--ALDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPF 163
Cdd:PRK13537 87 QfdnLDPdftvRENLLVFGRYFGLsaAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
....
gi 1419237541 164 TAID 167
Cdd:PRK13537 167 TGLD 170
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-193 |
7.47e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.83 E-value: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 19 NRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEyySELFYLAHHAGVK---PELS 95
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQ--KEIKPVRKKVGVVfqfPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 96 PWE-----NLRFYQKIQGLAlDDEALWYALDKVGLIGRE----ELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAI 166
Cdd:PRK13643 97 LFEetvlkDVAFGPQNFGIP-KEKAEKIAAEKLEMVGLAdefwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180
....*....|....*....|....*..
gi 1419237541 167 DKKGVSDLIVHIEKHCENGGMVIFTSH 193
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
26-206 |
7.60e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.94 E-value: 7.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 26 NFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRdeyySELFYLAHHAGV---KPE-----LSPW 97
Cdd:PRK13636 26 NINIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSR----KGLMKLRESVGMvfqDPDnqlfsASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 98 ENLRFYQKIQGLALDD--EALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSDLI 175
Cdd:PRK13636 102 QDVSFGAVNLKLPEDEvrKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM 181
|
170 180 190
....*....|....*....|....*....|.
gi 1419237541 176 VHIEKHCENGGMVIFTShqaaeSHKVKILSL 206
Cdd:PRK13636 182 KLLVEMQKELGLTIIIA-----THDIDIVPL 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
26-178 |
8.20e-12 |
|
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: 62.07 E-value: 8.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 26 NFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPI-QKQRDEyyselfyLAH--------HAGVKPELSP 96
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItGLPPHE-------IARlgigrtfqIPRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 97 WENLR------------FYQKIQGLALDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPF- 163
Cdd:cd03219 93 LENVMvaaqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAa 172
|
170
....*....|....*..
gi 1419237541 164 --TAIDKKGVSDLIVHI 178
Cdd:cd03219 173 glNPEETEELAELIREL 189
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-193 |
1.03e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.45 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 18 ENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEyySELFYLAHHAGVK---PEL 94
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKN--KDIKQIRKKVGLVfqfPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 95 SPWE-----NLRFYQKIQGLAlDDEALWYALDKVGLIG-REELACSY---LSAGQQRRVALAKLWLIKQKLWILDEPFTA 165
Cdd:PRK13649 97 QLFEetvlkDVAFGPQNFGVS-QEEAEALAREKLALVGiSESLFEKNpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180
....*....|....*....|....*...
gi 1419237541 166 IDKKGVSDLIVHIEKHCENGGMVIFTSH 193
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
23-193 |
1.05e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 62.80 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 23 ENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLW--NDIPIQKQRDEYYSELFYLAHHAGVKPELSPWENL 100
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifKDEKNKKKTKEKEKVLEKLVIQKTRFKKIKKIKEI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 101 R--------F--YQKIQGLALDD-------------EALWYALDKVGLIGREElacSYL-------SAGQQRRVALAKLW 150
Cdd:PRK13651 104 RrrvgvvfqFaeYQLFEQTIEKDiifgpvsmgvskeEAKKRAAKYIELVGLDE---SYLqrspfelSGGQKRRVALAGIL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1419237541 151 LIKQKLWILDEPFTAIDKKGVSDLIVHIEKHCENGGMVIFTSH 193
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-169 |
1.06e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.93 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDI----------PIQKQRDE 76
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvppyqrPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 77 YysELFylahhagvkPELSPWENLRFYQKIQGLALDDEALWYAlDKVGLIGREELACS---YLSAGQQRRVALAKLWLIK 153
Cdd:PRK11607 100 Y--ALF---------PHMTVEQNIAFGLKQDKLPKAEIASRVN-EMLGLVHMQEFAKRkphQLSGGQRQRVALARSLAKR 167
|
170
....*....|....*.
gi 1419237541 154 QKLWILDEPFTAIDKK 169
Cdd:PRK11607 168 PKLLLLDEPMGALDKK 183
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
39-167 |
1.07e-11 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 62.81 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 39 GHNGIGKTSLLRILAGLAMPAEGYV-----LWND------IPIQKQRDEY---YSELFylahhagvkPELSPWENLRFYQ 104
Cdd:COG4148 32 GPSGSGKTTLLRAIAGLERPDSGRIrlggeVLQDsargifLPPHRRRIGYvfqEARLF---------PHLSVRGNLLYGR 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1419237541 105 KIQGLALDDEALWYALDKVGLigrEELACSY---LSAGQQRRVALAKLWLIKQKLWILDEPFTAID 167
Cdd:COG4148 103 KRAPRAERRISFDEVVELLGI---GHLLDRRpatLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-193 |
1.15e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.99 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 3 HTNQLTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDipiqKQRDEYYSElf 82
Cdd:PRK15064 316 HRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSE----NANIGYYAQ-- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 83 ylAHHAGVKPELSPWENLRFYQKIQGlalDDEALWYALDKVgLIGREELACS--YLSAGQQRRVALAKLWLIKQKLWILD 160
Cdd:PRK15064 390 --DHAYDFENDLTLFDWMSQWRQEGD---DEQAVRGTLGRL-LFSQDDIKKSvkVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
170 180 190
....*....|....*....|....*....|...
gi 1419237541 161 EPFTAIDKKGVSDLIVHIEKHcenGGMVIFTSH 193
Cdd:PRK15064 464 EPTNHMDMESIESLNMALEKY---EGTLIFVSH 493
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-211 |
1.74e-11 |
|
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: 60.40 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENR--LFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEyyselfyL 84
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-------L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 85 AHHAGVkpelspwenlrfyqkiqglaLDDEALWYALDKVGLIGREelacsyLSAGQQRRVALAKLWLIKQKLWILDEPFT 164
Cdd:cd03247 74 SSLISV--------------------LNQRPYLFDTTLRNNLGRR------FSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1419237541 165 AIDKKGVSDLIVHIEKHCENGGMVIFTSHQAAESHKVKILSLDQFKL 211
Cdd:cd03247 128 GLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-167 |
1.77e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.57 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 6 QLTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSElfYLA 85
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR--RLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 86 ----HH---AGVK-PEL-----SPWENL--RfyqkiqgLALDDEAL-WYALDKVGLIGREELACSYLSAGQQRRVALAKL 149
Cdd:PRK11231 80 llpqHHltpEGITvRELvaygrSPWLSLwgR-------LSAEDNARvNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170
....*....|....*...
gi 1419237541 150 WLIKQKLWILDEPFTAID 167
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLD 170
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-201 |
2.76e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 61.26 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 15 ERGENRL-FENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDeyyseLFYLAHHAGV--- 90
Cdd:PRK13633 18 EESTEKLaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN-----LWDIRNKAGMvfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 91 KPE-------------LSPwENLrfyqkiqGLALDD--EALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQK 155
Cdd:PRK13633 93 NPDnqivativeedvaFGP-ENL-------GIPPEEirERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1419237541 156 LWILDEPFTAIDKKGVSDLIVHIEKHCENGGM-VIFTSH---QAAESHKV 201
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGItIILITHymeEAVEADRI 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
24-169 |
3.30e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.60 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 24 NCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSEL-------FYLAHHagVKPELSP 96
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqklgfIYQFHH--LLPDFTA 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1419237541 97 WENLRFYQKIQGLAlDDEALWYALD---KVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKK 169
Cdd:PRK11629 105 LENVAMPLLIGKKK-PAEINSRALEmlaAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-193 |
3.35e-11 |
|
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: 60.42 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 26 NFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSEL-FYLAHHAGVKPELSPWENLRFYQ 104
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIgVVFGQKTQLWWDLPVIDSFYLLA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 105 KIQGlaLDDEALWYALDK-VGLIGREELACS---YLSAGQQRRVALAKLWLIKQKLWILDEPFTAID---KKGVSDLIVH 177
Cdd:cd03267 121 AIYD--LPPARFKKRLDElSELLDLEELLDTpvrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDvvaQENIRNFLKE 198
|
170
....*....|....*.
gi 1419237541 178 IEKhcENGGMVIFTSH 193
Cdd:cd03267 199 YNR--ERGTTVLLTSH 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-194 |
3.37e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.19 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 18 ENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEyySELFYLAHHAGVK---PEL 94
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKN--KKLKPLRKKVGIVfqfPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 95 SPWE-----NLRFYQKIQGLAlDDEALWYALDKVGLIGREE--LACS--YLSAGQQRRVALAKLWLIKQKLWILDEPFTA 165
Cdd:PRK13634 97 QLFEetvekDICFGPMNFGVS-EEDAKQKAREMIELVGLPEelLARSpfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190
....*....|....*....|....*....|
gi 1419237541 166 IDKKGVSDLIVHIEK-HCENGGMVIFTSHQ 194
Cdd:PRK13634 176 LDPKGRKEMMEMFYKlHKEKGLTTVLVTHS 205
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
16-162 |
6.29e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 59.75 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 16 RGENRL--FENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQkQRDEYYSELFyLAHHAGVK-- 91
Cdd:COG4181 20 TGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF-ALDEDARARL-RARHVGFVfq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 92 -----PELSPWEN------LRFYQKIQGLALDdealwyALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILD 160
Cdd:COG4181 98 sfqllPTLTALENvmlpleLAGRRDARARARA------LLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFAD 171
|
..
gi 1419237541 161 EP 162
Cdd:COG4181 172 EP 173
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
16-113 |
7.77e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 59.71 E-value: 7.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 16 RGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVlwndipiqkQRDEYYSELfyLAHHAGVKPELS 95
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV---------EVNGRVSAL--LELGAGFHPELT 104
|
90
....*....|....*...
gi 1419237541 96 PWENLRFYQKIQGLALDD 113
Cdd:COG1134 105 GRENIYLNGRLLGLSRKE 122
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-193 |
8.92e-11 |
|
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: 59.08 E-value: 8.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 9 ITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVlwndipiqkQRDEYYSELFYLAhhA 88
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV---------TVRGRVSSLLGLG--G 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 89 GVKPELSPWENLRFYQKIQGL--ALDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAI 166
Cdd:cd03220 94 GFNPELTGRENIYLNGRLLGLsrKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180
....*....|....*....|....*..
gi 1419237541 167 DKKGVSDLIVHIEKHCENGGMVIFTSH 193
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQGKTVILVSH 200
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-167 |
1.03e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 59.21 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 26 NFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDI------PIQKQRDEYYSE--LFylahhagvkPELSPW 97
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttpPSRRPVSMLFQEnnLF---------SHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 98 EN----------LRFYQKIQglaLDDEAlwyalDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAID 167
Cdd:PRK10771 90 QNiglglnpglkLNAAQREK---LHAIA-----RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
17-167 |
1.22e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 60.18 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 17 GENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQK-QRDEYYSEL------FYLAHhag 89
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIgvvpqdTFLFS--- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 90 vkpeLSPWENLRFYQKiqglALDDEALWYALDKVGL--------------IGREElacSYLSAGQQRRVALAKLWLIKQK 155
Cdd:COG1132 428 ----GTIRENIRYGRP----DATDEEVEEAAKAAQAhefiealpdgydtvVGERG---VNLSGGQRQRIAIARALLKDPP 496
|
170
....*....|..
gi 1419237541 156 LWILDEPFTAID 167
Cdd:COG1132 497 ILILDEATSALD 508
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
15-193 |
1.34e-10 |
|
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: 59.82 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 15 ERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEG--YVL----WNDI----PIQKQRDEYYseLFYL 84
Cdd:TIGR03269 293 DRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRvgdeWVDMtkpgPDGRGRAKRY--IGIL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 85 AHHAGVKPELSPWENLrfyQKIQGLALDDE-----ALwYALDKVGLigREELACSYL-------SAGQQRRVALAKLwLI 152
Cdd:TIGR03269 371 HQEYDLYPHRTVLDNL---TEAIGLELPDElarmkAV-ITLKMVGF--DEEKAEEILdkypdelSEGERHRVALAQV-LI 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1419237541 153 KQ-KLWILDEPFTAID---KKGVSDLIVHIEKhcENGGMVIFTSH 193
Cdd:TIGR03269 444 KEpRIVILDEPTGTMDpitKVDVTHSILKARE--EMEQTFIIVSH 486
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-193 |
1.53e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 59.07 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 18 ENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEyySELFYLAHHAGVK---PEL 94
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGN--KNLKKLRKKVSLVfqfPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 95 SPWEN-----LRFYQKIQGLAlDDEALWYALD---KVGLigREELACSY---LSAGQQRRVALAKLWLIKQKLWILDEPF 163
Cdd:PRK13641 97 QLFENtvlkdVEFGPKNFGFS-EDEAKEKALKwlkKVGL--SEDLISKSpfeLSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190
....*....|....*....|....*....|
gi 1419237541 164 TAIDKKGVSDLIVHIEKHCENGGMVIFTSH 193
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
26-167 |
1.61e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 59.46 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 26 NFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFYLAHHAGVKPELSPWENLRFYQK 105
Cdd:PRK13536 61 SFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFGR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1419237541 106 IQGLALDD--EALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAID 167
Cdd:PRK13536 141 YFGMSTREieAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-175 |
1.65e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 58.85 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 18 ENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKqrdeyySELFYLAHHAG-------- 89
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK------ENLKEIRKKIGiifqnpdn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 90 ------VKPELS-PWENLRFYQKIQGLALDDEAlwyalDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEP 162
Cdd:PRK13632 95 qfigatVEDDIAfGLENKKVPPKKMKDIIDDLA-----KKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDES 169
|
170
....*....|...
gi 1419237541 163 FTAIDKKGVSDLI 175
Cdd:PRK13632 170 TSMLDPKGKREIK 182
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-176 |
2.57e-10 |
|
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: 57.83 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSE--LFYL 84
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARagIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 85 AHHAGVKPELSPWENLRfyqkIQGLALDDEALWYALDKV-----GLIGREELACSYLSAGQQRRVALAKLWLIKQKLWIL 159
Cdd:cd03224 81 PEGRRIFPELTVEENLL----LGAYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190
....*....|....*....|....*....|..
gi 1419237541 160 DEP------------FTAIDK---KGVSDLIV 176
Cdd:cd03224 157 DEPseglapkiveeiFEAIRElrdEGVTILLV 188
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-194 |
3.35e-10 |
|
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: 57.67 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 15 ERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAE---GYVLWNDIPIqkQRDEYYSELFYLAHHAGVK 91
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR--KPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 92 PELSPWENLRFYQKIQGLALDDEALWYALDKVGLIGREELA------CSYLSAGQQRRVALAKLWLIKQKLWILDEPFTA 165
Cdd:cd03234 94 PGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTriggnlVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180
....*....|....*....|....*....
gi 1419237541 166 IDKKGVSDLIVHIEKHCENGGMVIFTSHQ 194
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQ 202
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
9-208 |
3.64e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 57.72 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 9 ITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGyvlwnDIPIQKQRdeyyselFYLAHHA 88
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSG-----TLNIAGNH-------FDFSKTP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 89 GVK-------------------PELSPWENL-RFYQKIQGLAlDDEALWYALDKVGLIGREELACSY---LSAGQQRRVA 145
Cdd:PRK11124 73 SDKairelrrnvgmvfqqynlwPHLTVQQNLiEAPCRVLGLS-KDQALARAEKLLERLRLKPYADRFplhLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1419237541 146 LAKLWLIKQKLWILDEPFTAIDKKgVSDLIVHIEKHCENGGM--VIFTsHQAAESHKV--KILSLDQ 208
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPE-ITAQIVSIIRELAETGItqVIVT-HEVEVARKTasRVVYMEN 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-197 |
6.35e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 6.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 20 RLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQK--QRDEY-------YSELfylahhaGV 90
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKldHKLAAqlgigiiYQEL-------SV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 91 KPELSPWENLRF----YQKIQGLALDD-----EALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDE 161
Cdd:PRK09700 92 IDELTVLENLYIgrhlTKKVCGVNIIDwremrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1419237541 162 PFTAIDKKGVSDLIVHIEKHCENGGMVIFTSHQAAE 197
Cdd:PRK09700 172 PTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAE 207
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-211 |
7.25e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYV----------LWNDIPiqkqRDE 76
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdlivarLQQDPP----RNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 77 YYSELFYLA-------------HHAGVKPELSPWE-NLRFYQKIQGLaLDDEALWY-------ALDKVGLIGREELacSY 135
Cdd:PRK11147 80 EGTVYDFVAegieeqaeylkryHDISHLVETDPSEkNLNELAKLQEQ-LDHHNLWQlenrineVLAQLGLDPDAAL--SS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1419237541 136 LSAGQQRRVALAKLWLIKQKLWILDEPFTAIDkkgvSDLIVHIEKHCEN-GGMVIFTSHQAA--ESHKVKILSLDQFKL 211
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTfQGSIIFISHDRSfiRNMATRIVDLDRGKL 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
18-208 |
8.65e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 56.94 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 18 ENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAM---PAEGYV------------LWNDIPIQKQRDEYYSELF 82
Cdd:PRK09984 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSAGSHIellgrtvqregrLARDIRKSRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 83 YLAHHAGVKPEL-------SP-WEN-LRFYQKIQglalDDEALwYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIK 153
Cdd:PRK09984 96 NLVNRLSVLENVligalgsTPfWRTcFSWFTREQ----KQRAL-QALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1419237541 154 QKLWILDEPFTAIDKKGVSDLIVHIEKHCENGGM-VIFTSHQA--AESHKVKILSLDQ 208
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRDINQNDGItVVVTLHQVdyALRYCERIVALRQ 228
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-175 |
1.02e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.53 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 11 NLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQK-QRDEYYSELFYLAHHAG 89
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 90 VKPELSPWENL-RFYQKIQGLAL-----DDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPF 163
Cdd:PRK10253 92 TPGDITVQELVaRGRYPHQPLFTrwrkeDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170
....*....|..
gi 1419237541 164 TAIDKKGVSDLI 175
Cdd:PRK10253 172 TWLDISHQIDLL 183
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-175 |
1.08e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.18 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 21 LFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNdipiQKQRDEYYSE------------LFYLAH-H 87
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRS----AKVRMAVFSQhhvdgldlssnpLLYMMRcF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 88 AGVkPElspwenlrfyQKIQGlalddealwyALDKVGLIGREELACSY-LSAGQQRRVALAKLWLIKQKLWILDEPFTAI 166
Cdd:PLN03073 600 PGV-PE----------QKLRA----------HLGSFGVTGNLALQPMYtLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
....*....
gi 1419237541 167 DKKGVSDLI 175
Cdd:PLN03073 659 DLDAVEALI 667
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
26-175 |
1.78e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 56.25 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 26 NFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYV-----------LWN-----DIPIQKQRDEYyselfylahhAG 89
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVkidgelltaenVWNlrrkiGMVFQNPDNQF----------VG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 90 VKPElspwENLRFYQKIQGLALD------DEALwYALDKVGLIGREElacSYLSAGQQRRVALAKLWLIKQKLWILDEPF 163
Cdd:PRK13642 97 ATVE----DDVAFGMENQGIPREemikrvDEAL-LAVNMLDFKTREP---ARLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170
....*....|..
gi 1419237541 164 TAIDKKGVSDLI 175
Cdd:PRK13642 169 SMLDPTGRQEIM 180
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-167 |
1.86e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.80 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 1 MTHTNQLTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGlaMPA----EGYVLWNDIPIQKQRDE 76
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 77 YYSEL-FYLAHHAGVK-PELSPWENLRF-Y---QKIQGLALDD--EALWYALDKVGLIGREElacSYL--------SAGQ 140
Cdd:CHL00131 80 ERAHLgIFLAFQYPIEiPGVSNADFLRLaYnskRKFQGLPELDplEFLEIINEKLKLVGMDP---SFLsrnvnegfSGGE 156
|
170 180
....*....|....*....|....*..
gi 1419237541 141 QRRVALAKLWLIKQKLWILDEPFTAID 167
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLD 183
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-193 |
2.86e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 55.99 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 17 GENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKqrdeyYSE---------------L 81
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD-----YSEaalrqaisvvsqrvhL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 82 FylahhAGvkpelSPWENLRFYQKiqglALDDEALWYALDKVGLI----------------GREelacsyLSAGQQRRVA 145
Cdd:PRK11160 426 F-----SA-----TLRDNLLLAAP----NASDEALIEVLQQVGLEklleddkglnawlgegGRQ------LSGGEQRRLG 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1419237541 146 LAKLWLIKQKLWILDEPFTAIDKKGVSDLIVHIEKHCENgGMVIFTSH 193
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN-KTVLMITH 532
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
23-167 |
4.06e-09 |
|
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: 54.42 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 23 ENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRdeyyseLFYLAHHAGVKPElSPW----- 97
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG------LHDLRSRISIIPQ-DPVlfsgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 98 --ENLRFYQKiqglaLDDEALWYALDKVGLIG-----------REELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFT 164
Cdd:cd03244 94 irSNLDPFGE-----YSDEELWQALERVGLKEfveslpggldtVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATA 168
|
...
gi 1419237541 165 AID 167
Cdd:cd03244 169 SVD 171
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
16-194 |
4.23e-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: 54.51 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 16 RGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQ----KQRDEYYSELFYLAHHAGVK 91
Cdd:cd03258 15 GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRKARRRIGMIFQHFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 92 PELSPWENLRFYQKIQGLALD--DEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKK 169
Cdd:cd03258 95 SSRTVFENVALPLEIAGVPKAeiEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
170 180
....*....|....*....|....*...
gi 1419237541 170 ---GVSDLIVHIekHCENGGMVIFTSHQ 194
Cdd:cd03258 175 ttqSILALLRDI--NRELGLTIVLITHE 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-197 |
4.28e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.60 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLaMPA---EGYVLWNDIPIQKQ--RDEYYSEL 81
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASniRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 82 FYLAHHAGVKPELSPWENLRFYQKI--QGLALDDEALWYA----LDKVGL-IGREELACSYLSAGQQRRVALAKLWLIKQ 154
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEItlPGGRMAYNAMYLRaknlLRELQLdADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1419237541 155 KLWILDEP---FTAIDKKGVSDLIVHIEKHcenGGMVIFTSHQAAE 197
Cdd:TIGR02633 161 RLLILDEPsssLTEKETEILLDIIRDLKAH---GVACVYISHKLNE 203
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
24-174 |
5.84e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 54.23 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 24 NCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDeyyselFYLAHHAGVKP--------ELS 95
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG------HQIARMGVVRTfqhvrlfrEMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 96 PWENLRFYQKIQ-------GL------------ALDDEALWyaLDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKL 156
Cdd:PRK11300 97 VIENLLVAQHQQlktglfsGLlktpafrraeseALDRAATW--LERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170
....*....|....*...
gi 1419237541 157 WILDEPFTAIDKKGVSDL 174
Cdd:PRK11300 175 LMLDEPAAGLNPKETKEL 192
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
7-167 |
6.70e-09 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 53.84 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPI---QKQRDEYYSE--- 80
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdsKKDINKLRRKvgm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 81 ------LFylahhagvkPELSPWEN----LRfyqKIQGLAlDDEALWYA---LDKVGLIGREElacSY---LSAGQQRRV 144
Cdd:COG1126 82 vfqqfnLF---------PHLTVLENvtlaPI---KVKKMS-KAEAEERAmelLERVGLADKAD---AYpaqLSGGQQQRV 145
|
170 180
....*....|....*....|....*..
gi 1419237541 145 ----ALAklwlIKQKLWILDEPFTAID 167
Cdd:COG1126 146 aiarALA----MEPKVMLFDEPTSALD 168
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-194 |
6.89e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.48 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 6 QLTITNLACE--RGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLaMPAEGY-----VLWNDIPIQKQRDEYy 78
Cdd:cd03289 2 QMTVKDLTAKytEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDiqidgVSWNSVPLQKWRKAF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 79 selfylahhaGVKPEL------SPWENLRFYQKiqglaLDDEALWYALDKVGLI-------GREELACSY----LSAGQQ 141
Cdd:cd03289 80 ----------GVIPQKvfifsgTFRKNLDPYGK-----WSDEEIWKVAEEVGLKsvieqfpGQLDFVLVDggcvLSHGHK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1419237541 142 RRVALAKLWLIKQKLWILDEPFTAIDKKgVSDLIVHIEKHCENGGMVIFTSHQ 194
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDPI-TYQVIRKTLKQAFADCTVILSEHR 196
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-193 |
1.32e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.59 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 5 NQLTITNLA-CERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEG--YVLWNDIPIQKQR------- 74
Cdd:PRK13647 3 NIIEVEDLHfRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGrvKVMGREVNAENEKwvrskvg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 75 -------DEYYSElfylahhagvkpelSPWENLRFYQKIQGLALD--DEALWYALDKVGLIGREELACSYLSAGQQRRVA 145
Cdd:PRK13647 83 lvfqdpdDQVFSS--------------TVWDDVAFGPVNMGLDKDevERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1419237541 146 LAKLWLIKQKLWILDEPFTAIDKKGVSDLIVHIEKHCENGGMVIFTSH 193
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATH 196
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-165 |
1.41e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.04 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 15 ERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGlAMPAEGYVLWNDIPiqkqRDEYYSELFYLAHHAGVKPel 94
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG-ALKGTPVAGCVDVP----DNQFGREASLIDAIGRKGD-- 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1419237541 95 spwenlrFYQKIQGLA---LDDEALWYALDKVgligreelacsyLSAGQQRRVALAKLWLIKQKLWILDEpFTA 165
Cdd:COG2401 112 -------FKDAVELLNavgLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDE-FCS 165
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-167 |
1.80e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.15 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 11 NLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQK---------QRDeyySEL 81
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraqrkafRRD---IQM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 82 FYLAHHAGVKPELSPWENLRfyQKIQGLALDDEALWYA-----LDKVGLigREELAC---SYLSAGQQRRVALAKLWLIK 153
Cdd:PRK10419 94 VFQDSISAVNPRKTVREIIR--EPLRHLLSLDKAERLArasemLRAVDL--DDSVLDkrpPQLSGGQLQRVCLARALAVE 169
|
170
....*....|....
gi 1419237541 154 QKLWILDEPFTAID 167
Cdd:PRK10419 170 PKLLILDEAVSNLD 183
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-193 |
2.96e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.10 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 24 NCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQ--RDeyyselfylAHHAGVK---------P 92
Cdd:COG1129 22 GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRspRD---------AQAAGIAiihqelnlvP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 93 ELSPWENLRF-YQKIQGLALDDEALwYA-----LDKVGL-IGREELAcSYLSAGQQRRVALAKLWLIKQKLWILDEPFTA 165
Cdd:COG1129 93 NLSVAENIFLgREPRRGGLIDWRAM-RRrarelLARLGLdIDPDTPV-GDLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180
....*....|....*....|....*...
gi 1419237541 166 IDKKGVSDLIVHIEKHCENGGMVIFTSH 193
Cdd:COG1129 171 LTEREVERLFRIIRRLKAQGVAIIYISH 198
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-193 |
3.38e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.72 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 26 NFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIP--IQKQRDeyyselfylAHHAGVK---------PEL 94
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvrIRSPRD---------AIALGIGmvhqhfmlvPNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 95 SPWENLRfyqkiqgLALDDEALWyALDKVGLIGR-EELACSY------------LSAGQQRRVALAKLWLIKQKLWILDE 161
Cdd:COG3845 96 TVAENIV-------LGLEPTKGG-RLDRKAARARiRELSERYgldvdpdakvedLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1419237541 162 PfTA------IDKkgvsdLIVHIEKHCENGGMVIFTSH 193
Cdd:COG3845 168 P-TAvltpqeADE-----LFEILRRLAAEGKSIIFITH 199
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-211 |
3.77e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 52.30 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 22 FENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKqrdeyYSELFYLAHHAGV---KPElspwe 98
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGD-----FSKLQGIRKLVGIvfqNPE----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 99 nLRFYQKI--QGLALDDEALWY-----------ALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTA 165
Cdd:PRK13644 88 -TQFVGRTveEDLAFGPENLCLppieirkrvdrALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1419237541 166 IDKKGVSDLIVHIEKHCENGGMVIFTSHQAAESHKV-KILSLDQFKL 211
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDAdRIIVMDRGKI 213
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-190 |
3.88e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 51.56 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 24 NCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLW-NDIPIQKQRDEYYSELFYLAHHAGVKPEL-------- 94
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsNKNESEPSFEATRSRNRYSVAYAAQKPWLlnatveen 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 95 ----SPWENLRFYQKIQGLALDDEALWYALDKVGLIGREELAcsyLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDkkg 170
Cdd:cd03290 99 itfgSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGIN---LSGGQRQRICVARALYQNTNIVFLDDPFSALD--- 172
|
170 180
....*....|....*....|
gi 1419237541 171 vsdliVHIEKHCENGGMVIF 190
Cdd:cd03290 173 -----IHLSDHLMQEGILKF 187
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-165 |
4.18e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.54 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 20 RLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLaMPAEGYVLWNDIPI-QKQRDEYYSELFYLahhaGVKPEL---S 95
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELrELDPESWRKHLSWV----GQNPQLphgT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 96 PWENLRFYQKiqglALDDEALWYALDKVGL---IGREELACSY--------LSAGQQRRVALAKLWLIKQKLWILDEPfT 164
Cdd:PRK11174 439 LRDNVLLGNP----DASDEQLQQALENAWVsefLPLLPQGLDTpigdqaagLSVGQAQRLALARALLQPCQLLLLDEP-T 513
|
.
gi 1419237541 165 A 165
Cdd:PRK11174 514 A 514
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
23-201 |
5.86e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.03 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 23 ENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEG--YVLWNDIP------IQKQRDEYYSELFYLAHhagVKPEL 94
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyRVAGQDVAtldadaLAQLRREHFGFIFQRYH---LLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 95 SPWENLRFYQKIQGLALDD-----EALwyaLDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKK 169
Cdd:PRK10535 102 TAAQNVEVPAVYAGLERKQrllraQEL---LQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1419237541 170 GVSDLIVHIEKHCENGGMVIFTSHQ---AAESHKV 201
Cdd:PRK10535 179 SGEEVMAILHQLRDRGHTVIIVTHDpqvAAQAERV 213
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
29-193 |
1.24e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.16 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 29 VTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELfyLAHHAG-------VKPELSPWENLR 101
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL--RAKHVGfvfqsfmLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 102 FYQKIQGLAlDDEALWYA---LDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKG---VSDLI 175
Cdd:PRK10584 111 LPALLRGES-SRQSRNGAkalLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkIADLL 189
|
170
....*....|....*...
gi 1419237541 176 VHIEKhcENGGMVIFTSH 193
Cdd:PRK10584 190 FSLNR--EHGTTLILVTH 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-208 |
1.88e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 23 ENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWN--------DIPIQKQRDEYysELFYLAHHAGVKPEL 94
Cdd:PRK10261 341 EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqridtlsPGKLQALRRDI--QFIFQDPYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 95 ----SPWENLRFYQKIQGLALDDEALWYaLDKVGLigREELACSY---LSAGQQRRVALAKLWLIKQKLWILDEPFTAID 167
Cdd:PRK10261 419 tvgdSIMEPLRVHGLLPGKAAAARVAWL-LERVGL--LPEHAWRYpheFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1419237541 168 ---KKGVSDLIVHIEKhcENGGMVIFTSHQAAE----SHKVKILSLDQ 208
Cdd:PRK10261 496 vsiRGQIINLLLDLQR--DFGIAYLFISHDMAVveriSHRVAVMYLGQ 541
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-167 |
1.91e-07 |
|
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: 50.68 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 6 QLTITNLACERGE--NRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAmPAEGY-----VLWNDIPIQKQRDEY- 77
Cdd:TIGR01271 1217 QMDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEiqidgVSWNSVTLQTWRKAFg 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 78 --YSELFYLAhhAGVKPELSPWENlrfyqkiqglaLDDEALWYALDKVGLIGREEL-----------ACSYLSAGQQRRV 144
Cdd:TIGR01271 1296 viPQKVFIFS--GTFRKNLDPYEQ-----------WSDEEIWKVAEEVGLKSVIEQfpdkldfvlvdGGYVLSNGHKQLM 1362
|
170 180
....*....|....*....|...
gi 1419237541 145 ALAKLWLIKQKLWILDEPFTAID 167
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLD 1385
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-194 |
1.98e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.52 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 21 LFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLaMPAEGYVLWNDIPiqkqrdeyySELFYLAHhagvKPELS----- 95
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGRLTKPAK---------GKLFYVPQ----RPYMTlgtlr 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 96 -----PWENLRFYQKiqglALDDEALWYALDKVGL--IGREELACS-------YLSAGQQRRVALAKLWLIKQKLWILDE 161
Cdd:TIGR00954 533 dqiiyPDSSEDMKRR----GLSDKDLEQILDNVQLthILEREGGWSavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|....
gi 1419237541 162 PFTAIDkkgvSDLIVHIEKHCENGGMVIFT-SHQ 194
Cdd:TIGR00954 609 CTSAVS----VDVEGYMYRLCREFGITLFSvSHR 638
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
7-194 |
2.53e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 49.85 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLAC---ERGENRL--FENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSEL 81
Cdd:PRK13631 22 LRVKNLYCvfdEKQENELvaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 82 FYLAHHAGVKPELSPWENLRF----YQKIQGLALDD----------------EALWYALDKVGLiGREELACS--YLSAG 139
Cdd:PRK13631 102 NPYSKKIKNFKELRRRVSMVFqfpeYQLFKDTIEKDimfgpvalgvkkseakKLAKFYLNKMGL-DDSYLERSpfGLSGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1419237541 140 QQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSDLIVHIEKHCENGGMVIFTSHQ 194
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-167 |
2.98e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.87 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 37 IEGHNGIGKTSLLRILAGLAMPAEGYVLWND-----------IPIQKQRDEYY---SELFylaHHAGVKpelspwENLRF 102
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaekgicLPPEKRRIGYVfqdARLF---PHYKVR------GNLRY 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1419237541 103 yqkiqGLALDDEAlwYALDKVGLIGREELACSY---LSAGQQRRVALAKLWLIKQKLWILDEPFTAID 167
Cdd:PRK11144 100 -----GMAKSMVA--QFDKIVALLGIEPLLDRYpgsLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-193 |
3.04e-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: 49.93 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 21 LFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGL-------AMPAEGYvlwndipiqkqrdeyysELFYLAHHAGVKPE 93
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkdfngeARPQPGI-----------------KVGYLPQEPQLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 94 LSPWENL------------RFYQKIQGLALDDE----------ALWYALDKVGL--------IGREELAC-------SYL 136
Cdd:TIGR03719 83 KTVRENVeegvaeikdaldRFNEISAKYAEPDAdfdklaaeqaELQEIIDAADAwdldsqleIAMDALRCppwdadvTKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1419237541 137 SAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSDLivhiEKHCEN-GGMVIFTSH 193
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWL----ERHLQEyPGTVVAVTH 216
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-193 |
4.12e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.78 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 26 NFSVTSGEWVQIEGHNGIGKTSLLRILAGLaMPAEGYVLWNDIPIQKQRdeyYSELF----YLAHHAGVKPELSPWENLR 101
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWS---AAELArhraYLSQQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 102 FYQKIQG-LALDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLikQ---------KLWILDEPFTAID--KK 169
Cdd:PRK03695 92 LHQPDKTrTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVL--QvwpdinpagQLLLLDEPMNSLDvaQQ 169
|
170 180
....*....|....*....|....
gi 1419237541 170 GVSDLIvhIEKHCENGGMVIFTSH 193
Cdd:PRK03695 170 AALDRL--LSELCQQGIAVVMSSH 191
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-197 |
5.49e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLaMPA---EGYVLWNDIPIQKQ--RDeyySEl 81
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASniRD---TE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 82 fylahHAGVK---------PELSPWENLRFYQKI-QGLALDDEALwYA-----LDKVGLIGREELACSYLSAGQQRRVAL 146
Cdd:PRK13549 81 -----RAGIAiihqelalvKELSVLENIFLGNEItPGGIMDYDAM-YLraqklLAQLKLDINPATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1419237541 147 AKLwLIKQ-KLWILDEPFTAIDKKGVSDLIvHIEKHCENGGMV-IFTSHQAAE 197
Cdd:PRK13549 155 AKA-LNKQaRLLILDEPTASLTESETAVLL-DIIRDLKAHGIAcIYISHKLNE 205
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-167 |
6.62e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 48.95 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 16 RGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKqrdeyYSELFYLAHHAGVKPELS 95
Cdd:TIGR00958 491 RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQ-----YDHHYLHRQVALVGQEPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 96 PW-----EN----LRFYQKIQGLALDDEAlwYALDKVG--------LIGReelACSYLSAGQQRRVALAKLWLIKQKLWI 158
Cdd:TIGR00958 566 LFsgsvrENiaygLTDTPDEEIMAAAKAA--NAHDFIMefpngydtEVGE---KGSQLSGGQKQRIAIARALVRKPRVLI 640
|
....*....
gi 1419237541 159 LDEPFTAID 167
Cdd:TIGR00958 641 LDEATSALD 649
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-168 |
7.02e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 17 GENRLFENCNFSVTSGEWVQIEGHNGIGKTS----LLRILAglampAEGYVLWNDIPIQ----KQRDEYYS--ELFYLAH 86
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHnlnrRQLLPVRHriQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 87 HAGVKPELSPW----ENLRFYQKIQGLALDDEALWYALDKVGL--IGREELACSYlSAGQQRRVALAKLWLIKQKLWILD 160
Cdd:PRK15134 372 NSSLNPRLNVLqiieEGLRVHQPTLSAAQREQQVIAVMEEVGLdpETRHRYPAEF-SGGQRQRIAIARALILKPSLIILD 450
|
....*...
gi 1419237541 161 EPFTAIDK 168
Cdd:PRK15134 451 EPTSSLDK 458
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-201 |
7.60e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 48.12 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 21 LFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGL------AMPAEGYVLW--NDIpIQKQRDEYYSELFYLAHHAGVKP 92
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYfgKDI-FQIDAIKLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 93 ELSPWENLRFYQKIQGLALDDEA---LWYALDKVGL----IGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTA 165
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIkkiVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 1419237541 166 ID---KKGVSDLIVHIEKHCenggMVIFTSHQAAESHKV 201
Cdd:PRK14246 184 IDivnSQAIEKLITELKNEI----AIVIVSHNPQQVARV 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
11-167 |
8.48e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 48.09 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 11 NLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEG--YVLWNDIPIQKQRDEyySELFYLAHHA 88
Cdd:COG4161 7 NINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGqlNIAGHQFDFSQKPSE--KAIRLLRQKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 89 GVK-------PELSPWENL-RFYQKIQGLAlDDEALWYALDKVGLIGREELACSY---LSAGQQRRVALAKLWLIKQKLW 157
Cdd:COG4161 85 GMVfqqynlwPHLTVMENLiEAPCKVLGLS-KEQAREKAMKLLARLRLTDKADRFplhLSGGQQQRVAIARALMMEPQVL 163
|
170
....*....|
gi 1419237541 158 ILDEPFTAID 167
Cdd:COG4161 164 LFDEPTAALD 173
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
26-196 |
1.50e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 47.78 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 26 NFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSE------LFYLAHHAGVKPELSPW-- 97
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrsdiqMIFQDPLASLNPRMTIGei 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 98 --ENLR-FYQKIQGLALDDE--ALwyaLDKVGLIgrEELACSY---LSAGQQRRVALAKLWLIKQKLWILDEPFTAID-- 167
Cdd:PRK15079 121 iaEPLRtYHPKLSRQEVKDRvkAM---MLKVGLL--PNLINRYpheFSGGQCQRIGIARALILEPKLIICDEPVSALDvs 195
|
170 180 190
....*....|....*....|....*....|
gi 1419237541 168 -KKGVSDLIVHIEKhcENGGMVIFTSHQAA 196
Cdd:PRK15079 196 iQAQVVNLLQQLQR--EMGLSLIFIAHDLA 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
39-167 |
2.10e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.09 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 39 GHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYS-ELFYL------AHHAGVKpELS-----PWENL--RFYQ 104
Cdd:PRK10575 44 GHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFArKVAYLpqqlpaAEGMTVR-ELVaigryPWHGAlgRFGA 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1419237541 105 KiqglalDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAID 167
Cdd:PRK10575 123 A------DREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-197 |
2.19e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 27 FSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQ--RDeyyselfylAHHAGVK---------PELS 95
Cdd:PRK11288 25 FDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAstTA---------ALAAGVAiiyqelhlvPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 96 PWENLRFYQKIQGLALDDEALWYA-----LDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKG 170
Cdd:PRK11288 96 VAENLYLGQLPHKGGIVNRRLLNYeareqLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSARE 175
|
170 180
....*....|....*....|....*..
gi 1419237541 171 VSDLIVHIEKHCENGGMVIFTSHQAAE 197
Cdd:PRK11288 176 IEQLFRVIRELRAEGRVILYVSHRMEE 202
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
5-193 |
3.23e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.41 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 5 NQLTITnlacERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEyySELFYL 84
Cdd:PRK15056 10 NDVTVT----WRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK--NLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 85 AHHAGVK---PEL-------SPWENLRFYQKIQglALDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQ 154
Cdd:PRK15056 84 PQSEEVDwsfPVLvedvvmmGRYGHMGWLRRAK--KRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQG 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1419237541 155 KLWILDEPFTAIDKKGVSDLIVHIEKHCENGGMVIFTSH 193
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-175 |
3.56e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.92 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 12 LACERGENRL---------FENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGlAMPAEGYVLW---NDIPIQKQRDEYYS 79
Cdd:PRK10762 249 LDKAPGEVRLkvdnlsgpgVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYG-ALPRTSGYVTldgHEVVTRSPQDGLAN 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 80 ELFYLAH---HAGVKPELSPWEN-----LRFYQKIQG--------LALDDealWYALDKVGLIGREElACSYLSAGQQRR 143
Cdd:PRK10762 328 GIVYISEdrkRDGLVLGMSVKENmsltaLRYFSRAGGslkhadeqQAVSD---FIRLFNIKTPSMEQ-AIGLLSGGNQQK 403
|
170 180 190
....*....|....*....|....*....|....*
gi 1419237541 144 VALAKLWLIKQKLWILDEPFTAID---KKGVSDLI 175
Cdd:PRK10762 404 VAIARGLMTRPKVLILDEPTRGVDvgaKKEIYQLI 438
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-194 |
4.40e-06 |
|
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: 45.60 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLA--MPAEGYVLWNDIPIQkqrdeyyselfyl 84
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDIT------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 85 ahhagvkpELSPWENLRF-----YQ---KIQGLALDDeaLWYALDkVGligreelacsyLSAGQQRRVALAKLWLIKQKL 156
Cdd:cd03217 68 --------DLPPEERARLgiflaFQyppEIPGVKNAD--FLRYVN-EG-----------FSGGEKKRNEILQLLLLEPDL 125
|
170 180 190
....*....|....*....|....*....|....*....
gi 1419237541 157 WILDEPFTAIDKKGVSDLIVHIEK-HCENGGMVIFTSHQ 194
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHYQ 164
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-189 |
4.40e-06 |
|
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: 45.86 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 28 SVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGyvlwnDIPIQKQRDEYyselfylahhagvKP-ELSPWENLRFYQ-- 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-----DIEIELDTVSY-------------KPqYIKADYEGTVRDll 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 105 --KIQGLALDDEALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKG---VSDLIVHIE 179
Cdd:cd03237 83 ssITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmASKVIRRFA 162
|
170
....*....|
gi 1419237541 180 KHCENGGMVI 189
Cdd:cd03237 163 ENNEKTAFVV 172
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
24-169 |
5.37e-06 |
|
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: 45.68 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 24 NCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFylahhaGVKPElSPW------ 97
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI------GVVLQ-DTFlfsgti 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 98 -ENLRFyqkiQGLALDDEALWYALDKVG---LIGR------EEL--ACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTA 165
Cdd:cd03254 94 mENIRL----GRPNATDEEVIEAAKEAGahdFIMKlpngydTVLgeNGGNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
....
gi 1419237541 166 IDKK 169
Cdd:cd03254 170 IDTE 173
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-167 |
9.95e-06 |
|
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: 45.23 E-value: 9.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 19 NRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGyvlwndiPIQKQRDEYYSELFYLAHHAGVKPEL---S 95
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG-------KIKHSGRISFSSQFSWIMPGTIKENIifgV 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1419237541 96 PWENLRFYQKIQGLALDDEALWYALDKVGLIGREELAcsyLSAGQQRRVALAKLWLIKQKLWILDEPFTAID 167
Cdd:cd03291 123 SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGIT---LSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-161 |
1.11e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.35 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 26 NFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFylahhAGVKPELSPWENLrfyQK 105
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLF-----SAVFTDFHLFDQL---LG 414
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1419237541 106 IQGLALDDEALWYALDKVGL-----IGREELACSYLSAGQQRRVALAKLWLIKQKLWILDE 161
Cdd:PRK10522 415 PEGKPANPALVEKWLERLKMahkleLEDGRISNLKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-197 |
1.20e-05 |
|
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: 45.39 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 29 VTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQKQRDEYYSELFYLAHHAGVKPELSPWENLRFYQKIQG 108
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 109 LA---LDDEALWyALDKVGL-IGREELACSYlSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSDLIVHIEKHCEN 184
Cdd:TIGR01257 2042 VPaeeIEKVANW-SIQSLGLsLYADRLAGTY-SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE 2119
|
170
....*....|...
gi 1419237541 185 GGMVIFTSHQAAE 197
Cdd:TIGR01257 2120 GRAVVLTSHSMEE 2132
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
136-201 |
3.39e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 43.46 E-value: 3.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1419237541 136 LSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSDLIVHIEK-HCENGGMVIFTSHQAAESHKV 201
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlNKEYKKRIIMVTHNMDQVLRI 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-61 |
3.60e-05 |
|
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: 43.77 E-value: 3.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1419237541 11 NLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEG 61
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSG 377
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-197 |
4.61e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 23 ENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIQ-KQRDEYYSELFYLAHHagvkpEL------S 95
Cdd:PRK10982 15 DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQ-----ELnlvlqrS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 96 PWENL---RFYQKiqGLALDD-------EALWYALDkVGLIGREELACsyLSAGQQRRVALAKLWLIKQKLWILDEPFTA 165
Cdd:PRK10982 90 VMDNMwlgRYPTK--GMFVDQdkmyrdtKAIFDELD-IDIDPRAKVAT--LSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190
....*....|....*....|....*....|..
gi 1419237541 166 IDKKGVSDLIVHIEKHCENGGMVIFTSHQAAE 197
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKERGCGIVYISHKMEE 196
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-169 |
5.31e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 42.74 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 31 SGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVL----WNDIpIQKQRDEYYSELFYLAHHAGVKPELSPWENLRFYQKI 106
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdWDEI-LDEFRGSELQNYFTKLLEGDVKVIVKPQYVDLIPKAV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 107 QGLALD-----DE--ALWYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKK 169
Cdd:cd03236 104 KGKVGEllkkkDErgKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-167 |
6.52e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.08 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGenrlFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWND--IPIQKQRDeyyselfyl 84
Cdd:COG1129 257 LEVEGLSVGGV----VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRD--------- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 85 AHHAGVKpeLSPwENlRfyqKIQGLALDDEALW----YALDKV---GLI--GRE------------------ELACSYLS 137
Cdd:COG1129 324 AIRAGIA--YVP-ED-R---KGEGLVLDLSIREnitlASLDRLsrgGLLdrRREralaeeyikrlriktpspEQPVGNLS 396
|
170 180 190
....*....|....*....|....*....|.
gi 1419237541 138 AGQQRRVALAKlWLIKQ-KLWILDEPFTAID 167
Cdd:COG1129 397 GGNQQKVVLAK-WLATDpKVLILDEPTRGID 426
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-189 |
8.36e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.79 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 29 VTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDIPIqkqrdeyyselfylahhaGVKPelspwenlrfyQKIQg 108
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP------------------VYKP-----------QYID- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 109 lalddealwyaldkvgligreelacsyLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKK---GVSDLIVHIEKHCENG 185
Cdd:cd03222 72 ---------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlNAARAIRRLSEEGKKT 124
|
....
gi 1419237541 186 GMVI 189
Cdd:cd03222 125 ALVV 128
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
24-63 |
9.75e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.57 E-value: 9.75e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1419237541 24 NCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYV 63
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
24-167 |
1.10e-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: 41.48 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 24 NCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPA---EGYVLWNDIPIQKQRDEYYSELFYLAHHAGVKPELSPWENL 100
Cdd:cd03233 25 DFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETL 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1419237541 101 RFYQKIQGlaldDEALwyaldkvgligreelacSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAID 167
Cdd:cd03233 105 DFALRCKG----NEFV-----------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-205 |
1.41e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 42.17 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 32 GEWVQIEGHNGIGKTSLLRILAGL--AMPAEGYVLWNDIPIQKQ---RDEYYSELFYLAHHAGVKPELSPWENLRFYQKI 106
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTKQilkRTGFVTQDDILYPHLTVRETLVFCSLLRLPKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 107 QglalDDEALWYA---LDKVGLIGREE--LACSYL---SAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSDLIVHI 178
Cdd:PLN03211 174 T----KQEKILVAesvISELGLTKCENtiIGNSFIrgiSGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
170 180 190
....*....|....*....|....*....|..
gi 1419237541 179 EKHCENGGMVIFTSHQAAES-----HKVKILS 205
Cdd:PLN03211 250 GSLAQKGKTIVTSMHQPSSRvyqmfDSVLVLS 281
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-167 |
1.72e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.84 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENR---LFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGlAMPA--EGYVLWNDIP--IQKQRDEYYS 79
Cdd:PRK13549 260 LEVRNLTAWDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGrwEGEIFIDGKPvkIRNPQQAIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 80 ELFYLAH---HAGVKPELSPWEN--LRFYQKIQGLALDDEALwyaldKVGLIGRE-----------ELACSYLSAGQQRR 143
Cdd:PRK13549 339 GIAMVPEdrkRDGIVPVMGVGKNitLAALDRFTGGSRIDDAA-----ELKTILESiqrlkvktaspELAIARLSGGNQQK 413
|
170 180
....*....|....*....|....
gi 1419237541 144 VALAKLWLIKQKLWILDEPFTAID 167
Cdd:PRK13549 414 AVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-162 |
1.76e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 32 GEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWN-DIPIQKQR-----DEYYSELFylahhAGVKPEL-SPWENLRFyq 104
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElKISYKPQYikpdyDGTVEDLL-----RSITDDLgSSYYKSEI-- 437
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1419237541 105 kIQGLALDDealwyALDKvgligreELacSYLSAGQQRRVALAKLWLIKQKLWILDEP 162
Cdd:PRK13409 438 -IKPLQLER-----LLDK-------NV--KDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-197 |
1.81e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 41.73 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENR---LFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGlAMPA--EGYVLWNDIPIQKQrdeyySEL 81
Cdd:TIGR02633 258 LEARNLTCWDVINPhrkRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGkfEGNVFINGKPVDIR-----NPA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 82 FYLAH----------HAGVKPELSPWEN--LRFYQKIQGLA-LDDEAlwyaldKVGLIGRE-----------ELACSYLS 137
Cdd:TIGR02633 332 QAIRAgiamvpedrkRHGIVPILGVGKNitLSVLKSFCFKMrIDAAA------ELQIIGSAiqrlkvktaspFLPIGRLS 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 138 AGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSDLIVHIEKHCENGGMVIFTSHQAAE 197
Cdd:TIGR02633 406 GGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAE 465
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-201 |
2.05e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 40.98 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 11 NLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGL-----AMPAEGYV--LWNDI------PIQKQRdey 77
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVrlFGRNIyspdvdPIEVRR--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 78 ysELFYLAHHAGVKPELSPWENLRFYQKIQGLALD----DEALWYALDKVGLI----GREELACSYLSAGQQRRVALAKL 149
Cdd:PRK14267 86 --EVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSkkelDERVEWALKKAALWdevkDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1419237541 150 WLIKQKLWILDEPFTAIDKKG---VSDLIVHIEKHCenggMVIFTSHQAAESHKV 201
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGtakIEELLFELKKEY----TIVLVTHSPAQAARV 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-194 |
2.06e-04 |
|
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: 40.53 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 19 NRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWNDipiqkqRDEYYSElfylahhagvkpelSPW- 97
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------SIAYVSQ--------------EPWi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 98 ------ENLRFyqkiqGLALDDEalWY-------ALDK------------VGLIGreelacSYLSAGQQRRVALAKLWLI 152
Cdd:cd03250 78 qngtirENILF-----GKPFDEE--RYekvikacALEPdleilpdgdlteIGEKG------INLSGGQKQRISLARAVYS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1419237541 153 KQKLWILDEPFTAIDkkgvSDLIVHIEKHCENGGM-----VIFTSHQ 194
Cdd:cd03250 145 DADIYLLDDPLSAVD----AHVGRHIFENCILGLLlnnktRILVTHQ 187
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
136-194 |
3.53e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 39.65 E-value: 3.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1419237541 136 LSAGQQRRVALAK---LWLIKQK-LWILDEPFTAIDKKGVSDLIVHIEKHCENGGMVIFTSHQ 194
Cdd:cd03227 78 LSGGEKELSALALilaLASLKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL 140
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
7-167 |
3.96e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 40.20 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAG-LAMPAE-------GYVLWNDIP---IQKQRd 75
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPlaaIDAPR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 76 eyyselfyLAHHAGVKPE-------LSPWENL---RFYQKIQGLAL---DDEALWYALDKVG---LIGREelaCSYLSAG 139
Cdd:PRK13547 81 --------LARLRAVLPQaaqpafaFSAREIVllgRYPHARRAGALthrDGEIAWQALALAGataLVGRD---VTTLSGG 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 1419237541 140 QQRRV----ALAKLW-----LIKQKLWILDEPFTAID 167
Cdd:PRK13547 150 ELARVqfarVLAQLWpphdaAQPPRYLLLDEPTAALD 186
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-61 |
6.54e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.10 E-value: 6.54e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1419237541 17 GENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEG 61
Cdd:PRK11819 335 GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSG 379
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
39-162 |
6.91e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.72 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 39 GHNGIGKTSLLRILAGL-------AMPAEGYvlwndipiqkqrdeyysELFYLAHHAGVKPELSPWEN-----------L 100
Cdd:PRK11819 40 GLNGAGKSTLLRIMAGVdkefegeARPAPGI-----------------KVGYLPQEPQLDPEKTVRENveegvaevkaaL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 101 RFYQKIQGL---------ALDDE--ALWYALDKVGL--------IGREELAC-------SYLSAGQQRRVALAKLWLIKQ 154
Cdd:PRK11819 103 DRFNEIYAAyaepdadfdALAAEqgELQEIIDAADAwdldsqleIAMDALRCppwdakvTKLSGGERRRVALCRLLLEKP 182
|
....*...
gi 1419237541 155 KLWILDEP 162
Cdd:PRK11819 183 DMLLLDEP 190
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-162 |
7.15e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 39.77 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 32 GEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWnDIPI----QKQRDEYYSEL-FYLAHHAGVKPELSPWENlrfyQKI 106
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-DLKIsykpQYISPDYDGTVeEFLRSANTDDFGSSYYKT----EII 440
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1419237541 107 QGLALDDealwyALDKvgligreELacSYLSAGQQRRVALAKLWLIKQKLWILDEP 162
Cdd:COG1245 441 KPLGLEK-----LLDK-------NV--KDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-193 |
8.74e-04 |
|
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: 38.51 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 37 IEGHNGIGKTSLLRILAGLAMPAEGYVlwndipiqkqrdeyyselfylahhagvkpelspwenlrfyqkiqgLALDDEAL 116
Cdd:smart00382 7 IVGPPGSGKTTLARALARELGPPGGGV---------------------------------------------IYIDGEDI 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 117 WYALDKVGLIGREELACSYLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKGVSDLIVHIEKHC------ENGGMVIF 190
Cdd:smart00382 42 LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllksEKNLTVIL 121
|
...
gi 1419237541 191 TSH 193
Cdd:smart00382 122 TTN 124
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-167 |
9.56e-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: 39.28 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 1 MTHTNQLTITNL----ACERGENRLFENCNFSVTSGEWVQIEGHNGIGKT----SLLRILAGLAMPAEGYVLW------- 65
Cdd:COG4172 1 MMSMPLLSVEDLsvafGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFdgqdllg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 66 -----------NDI---------------PIQKQrdeyyselfyLAhhagvkpelspwENLRFYQKIQGLALDDEALWyA 119
Cdd:COG4172 81 lserelrrirgNRIamifqepmtslnplhTIGKQ----------IA------------EVLRLHRGLSGAAARARALE-L 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1419237541 120 LDKVGLIGREELACSY---LSAGQQRRV----ALAKlwliKQKLWILDEPFTAID 167
Cdd:COG4172 138 LERVGIPDPERRLDAYphqLSGGQRQRVmiamALAN----EPDLLIADEPTTALD 188
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-167 |
2.19e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 37.83 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 7 LTITNLACERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLA-----MPAEGYVLWNDIPIQKQRD---EYY 78
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpeVTITGSIVYNGHNIYSPRTdtvDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 79 SELFYLAHHAGVKPeLSPWENLRFYQKIQGLAlDDEALWYALDKvGLIG-------REELACSY--LSAGQQRRVALAKL 149
Cdd:PRK14239 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIK-DKQVLDEAVEK-SLKGasiwdevKDRLHDSAlgLSGGQQQRVCIARV 162
|
170
....*....|....*...
gi 1419237541 150 WLIKQKLWILDEPFTAID 167
Cdd:PRK14239 163 LATSPKIILLDEPTSALD 180
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-67 |
2.75e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.47 E-value: 2.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1419237541 16 RGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGYVLWND 67
Cdd:PTZ00265 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND 446
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-194 |
3.46e-03 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 37.22 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 15 ERGENRLFENCNFSVTSGEWVQIEGHNGIGKTSLLRILAG--LAMPAEGYVLWNDIPIQK--QRDEYYSELFYLahHAgv 90
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKnfQRSTGYVEQQDV--HS-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 91 kPELSPWENLRFYQKIQGlalddealwyaldkvgligreelacsyLSAGQQRRVALAKLWLIKQKLWILDEPFTAIDKKG 170
Cdd:cd03232 92 -PNLTVREALRFSALLRG---------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180
....*....|....*....|....
gi 1419237541 171 VSDLIVHIEKHCENGGMVIFTSHQ 194
Cdd:cd03232 144 AYNIVRFLKKLADSGQAILCTIHQ 167
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
27-167 |
4.30e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 37.25 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 27 FSVTSGEWVQIEGHNGIGKTSLLRILAGLAMPAEGyvlwndipiqkqrdeyysELFYLAHHAgVKPELSPWENLRfyQKI 106
Cdd:PRK11308 36 FTLERGKTLAVVGESGCGKSTLARLLTMIETPTGG------------------ELYYQGQDL-LKADPEAQKLLR--QKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419237541 107 Q----------------GLALDD--------------EALWYALDKVGLigREELACSY---LSAGQQRRVALAKLWLIK 153
Cdd:PRK11308 95 QivfqnpygslnprkkvGQILEEpllintslsaaerrEKALAMMAKVGL--RPEHYDRYphmFSGGQRQRIAIARALMLD 172
|
170
....*....|....
gi 1419237541 154 QKLWILDEPFTAID 167
Cdd:PRK11308 173 PDVVVADEPVSALD 186
|
|
| |
