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Conserved domains on  [gi|491074653|ref|WP_004936275|]
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MULTISPECIES: cytochrome c biogenesis heme-transporting ATPase CcmA [Serratia]

Protein Classification

heme ABC exporter ATP-binding protein CcmA( domain architecture ID 11486688)

heme ABC exporter ATP-binding protein CcmA is a heme-transporting ATPase that is part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; responsible for energy coupling to the transport system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
1-202 3.03e-129

cytochrome c biogenesis heme-transporting ATPase CcmA;


:

Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 362.20  E-value: 3.03e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG 80
Cdd:PRK13538   1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 HQPGIKAVLTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAI 160
Cdd:PRK13538  81 HQPGIKTELTALENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 491074653 161 DKQGVAELISLFEQHAQRGGMVLLTTHQDLAGVSQTVGKIRL 202
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRL 202
 
Name Accession Description Interval E-value
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
1-202 3.03e-129

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 362.20  E-value: 3.03e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG 80
Cdd:PRK13538   1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 HQPGIKAVLTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAI 160
Cdd:PRK13538  81 HQPGIKTELTALENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 491074653 161 DKQGVAELISLFEQHAQRGGMVLLTTHQDLAGVSQTVGKIRL 202
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRL 202
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
1-190 6.87e-100

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: 287.84  E-value: 6.87e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG 80
Cdd:COG4133    2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 HQPGIKAVLTPFENLQFYQAVRG-AAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:COG4133   82 HADGLKPELTVRENLRFWAALYGlRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
                        170       180       190
                 ....*....|....*....|....*....|.
gi 491074653 160 IDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:COG4133  162 LDAAGVALLAELIAAHLARGGAVLLTTHQPL 192
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
2-190 1.09e-90

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: 264.22  E-value: 1.09e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGH 81
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   82 QPGIKAVLTPFENLQFYQAVrGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:TIGR01189  81 LPGLKPELSALENLHFWAAI-HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
                         170       180
                  ....*....|....*....|....*....
gi 491074653  162 KQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:TIGR01189 160 KAGVALLAGLLRAHLARGGIVLLTTHQDL 188
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
2-203 5.20e-87

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: 255.11  E-value: 5.20e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGH 81
Cdd:cd03231    1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  82 QPGIKAVLTPFENLQFYQAVRGAAeqqAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:cd03231   81 APGIKTTLSVLENLRFWHADHSDE---QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 491074653 162 KQGVAELISLFEQHAQRGGMVLLTTHQDLAGVSQTVGKIRLA 203
Cdd:cd03231  158 KAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
20-158 1.12e-34

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: 120.06  E-value: 1.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQFY 98
Cdd:pfam00005   4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDlTDDERKSLRKEIGYVFQDPQLFPRLTVRENLRLG 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491074653   99 ---QAVRGAAEQQAIWRALEQVGLVGYEDLPV----AQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:pfam00005  84 lllKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
20-187 6.09e-07

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 48.96  E-value: 6.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLlRILAGLARPDGGEVCWRGRNTLRDRAAYQQDllfIG-HQP---GIKAVLTPFENL 95
Cdd:NF000106  32 VDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRT---IG*HRPvr*GRRESFSGRENL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  96 QFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLF 172
Cdd:NF000106 108 YMIGR*LDLSRKDARARAdelLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV 187
                        170
                 ....*....|....*
gi 491074653 173 EQHAQRGGMVLLTTH 187
Cdd:NF000106 188 RSMVRDGATVLLTTQ 202
GguA NF040905
sugar ABC transporter ATP-binding protein;
18-159 9.69e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 42.47  E-value: 9.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLaRPDG---------GEVCwrgrnTLRDRAAYQQDLLFIGHQpgiKAV 88
Cdd:NF040905  18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyegeilfdGEVC-----RFKDIRDSEALGIVIIHQ---ELA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  89 LTPF----ENLqFY---QAVRGAAE-QQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPl 157
Cdd:NF040905  89 LIPYlsiaENI-FLgneRAKRGVIDwNETNRRArelLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP- 166

                 ..
gi 491074653 158 TA 159
Cdd:NF040905 167 TA 168
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
26-187 1.30e-03

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: 37.74  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    26 PGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcwrgrntlrdraayqqdllfighqpgikavltpfenlqfyqaVRGAA 105
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV------------------------------------------IYIDG 38
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   106 EqqAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHA------QRG 179
Cdd:smart00382  39 E--DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllksEKN 116

                   ....*...
gi 491074653   180 GMVLLTTH 187
Cdd:smart00382 117 LTVILTTN 124
 
Name Accession Description Interval E-value
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
1-202 3.03e-129

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 362.20  E-value: 3.03e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG 80
Cdd:PRK13538   1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 HQPGIKAVLTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAI 160
Cdd:PRK13538  81 HQPGIKTELTALENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 491074653 161 DKQGVAELISLFEQHAQRGGMVLLTTHQDLAGVSQTVGKIRL 202
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRL 202
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
1-190 6.87e-100

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: 287.84  E-value: 6.87e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG 80
Cdd:COG4133    2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 HQPGIKAVLTPFENLQFYQAVRG-AAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:COG4133   82 HADGLKPELTVRENLRFWAALYGlRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
                        170       180       190
                 ....*....|....*....|....*....|.
gi 491074653 160 IDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:COG4133  162 LDAAGVALLAELIAAHLARGGAVLLTTHQPL 192
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
2-190 1.09e-90

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: 264.22  E-value: 1.09e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGH 81
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   82 QPGIKAVLTPFENLQFYQAVrGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:TIGR01189  81 LPGLKPELSALENLHFWAAI-HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
                         170       180
                  ....*....|....*....|....*....
gi 491074653  162 KQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:TIGR01189 160 KAGVALLAGLLRAHLARGGIVLLTTHQDL 188
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
2-203 5.20e-87

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: 255.11  E-value: 5.20e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGH 81
Cdd:cd03231    1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  82 QPGIKAVLTPFENLQFYQAVRGAAeqqAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:cd03231   81 APGIKTTLSVLENLRFWHADHSDE---QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 491074653 162 KQGVAELISLFEQHAQRGGMVLLTTHQDLAGVSQTVGKIRLA 203
Cdd:cd03231  158 KAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
1-190 8.34e-67

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 203.95  E-value: 8.34e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT----LRDRAAYqqdl 76
Cdd:PRK13539   2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIddpdVAEACHY---- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  77 lfIGHQPGIKAVLTPFENLQFYQAVRGAAEQqAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:PRK13539  78 --LGHRNAMKPALTVAENLEFWAAFLGGEEL-DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
                        170       180       190
                 ....*....|....*....|....*....|....
gi 491074653 157 LTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK13539 155 TAALDAAAVALFAELIRAHLAQGGIVIAATHIPL 188
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
1-191 2.68e-52

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 167.33  E-value: 2.68e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR-NTLRDRAAYqqdLLFI 79
Cdd:PRK13543  11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtATRGDRSRF---MAYL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  80 GHQPGIKAVLTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:PRK13543  88 GHLPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
                        170       180       190
                 ....*....|....*....|....*....|..
gi 491074653 160 IDKQGVAELISLFEQHAQRGGMVLLTTHQDLA 191
Cdd:PRK13543 168 LDLEGITLVNRMISAHLRGGGAALVTTHGAYA 199
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
1-191 2.77e-51

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 164.35  E-value: 2.77e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG 80
Cdd:PRK13540   1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 HQPGIKAVLTPFEN----LQFYQAVRGAAEQQAIWRaleqvgLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:PRK13540  81 HRSGINPYLTLRENclydIHFSPGAVGITELCRLFS------LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 491074653 157 LTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDLA 191
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLP 189
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-200 2.14e-44

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 147.93  E-value: 2.14e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRA--AY--QQ-- 74
Cdd:COG1121    6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRriGYvpQRae 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  75 ----------DLLFIGHQPGIKAVLTPfenlqfyqavrGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLW 144
Cdd:COG1121   86 vdwdfpitvrDVVLMGRYGRRGLFRRP-----------SRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491074653 145 LSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHqDLAGVSQTVGKI 200
Cdd:COG1121  155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTH-DLGAVREYFDRV 209
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
2-187 4.70e-44

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 146.75  E-value: 4.70e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGH 81
Cdd:COG1131    1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  82 QPGIKAVLTPFENLQFYQAVRGAAEQQA---IWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:COG1131   81 EPALYPDLTVRENLRFFARLYGLPRKEArerIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
                        170       180
                 ....*....|....*....|....*....
gi 491074653 159 AIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:COG1131  161 GLDPEARRELWELLRELAAEGKTVLLSTH 189
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
1-188 6.51e-44

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: 146.93  E-value: 6.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG 80
Cdd:COG4555    1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 HQPGIKAVLTPFENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:COG4555   81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIeelIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
                        170       180       190
                 ....*....|....*....|....*....|.
gi 491074653 158 TAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:COG4555  161 NGLDVMARRLLREILRALKKEGKTVLFSSHI 191
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
3-187 8.97e-37

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: 127.65  E-value: 8.97e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   3 EAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAyqqdllfIGHQ 82
Cdd:cd03235    1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-------IGYV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  83 PGIKAVLTPFeNLQFYQAVR-------------GAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAP 149
Cdd:cd03235   74 PQRRSIDRDF-PISVRDVVLmglyghkglfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 491074653 150 LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:cd03235  153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTH 190
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
18-200 3.60e-35

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: 123.10  E-value: 3.60e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQdllfIG---HQPGIKAVLTPFEN 94
Cdd:cd03268   17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR----IGaliEAPGFYPNLTAREN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  95 LQFYQAVRGAAEQqAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQ 174
Cdd:cd03268   93 LRLLARLLGIRKK-RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILS 171
                        170       180
                 ....*....|....*....|....*.
gi 491074653 175 HAQRGGMVLLTTHQdLAGVSQTVGKI 200
Cdd:cd03268  172 LRDQGITVLISSHL-LSEIQKVADRI 196
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
1-190 4.02e-35

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


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 124.39  E-value: 4.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN----TLRDRA---AY- 72
Cdd:COG1120    1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslSRRELArriAYv 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  73 -QQ----------DLLFIGHQPGIKAVLTPfenlqfyqavrGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALA 141
Cdd:COG1120   81 pQEppapfgltvrELVALGRYPHLGLFGRP-----------SAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIA 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 491074653 142 RLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGM-VLLTTHqDL 190
Cdd:COG1120  150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRtVVMVLH-DL 198
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
20-158 1.12e-34

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: 120.06  E-value: 1.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQFY 98
Cdd:pfam00005   4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDlTDDERKSLRKEIGYVFQDPQLFPRLTVRENLRLG 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491074653   99 ---QAVRGAAEQQAIWRALEQVGLVGYEDLPV----AQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:pfam00005  84 lllKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
2-187 9.69e-34

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 118.65  E-value: 9.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGH 81
Cdd:cd03230    1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  82 QPGIKAVLTPFENLqfyqavrgaaeqqaiwraleqvglvgyedlpvaQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:cd03230   81 EPSLYENLTVRENL---------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
                        170       180
                 ....*....|....*....|....*.
gi 491074653 162 KQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:cd03230  128 PESRREFWELLRELKKEGKTILLSSH 153
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
1-188 2.48e-33

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 119.09  E-value: 2.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILfsELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAA-------YQ 73
Cdd:COG3840    1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAerpvsmlFQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  74 QDLLF----------IGHQPGIKavLTpfenlqfyqavrgAAEQQAIWRALEQVGLVGYED-LPvAQLSAGQQRRVALAR 142
Cdd:COG3840   79 ENNLFphltvaqnigLGLRPGLK--LT-------------AEQRAQVEQALERVGLAGLLDrLP-GQLSGGQRQRVALAR 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 491074653 143 LWLSAAPLWILDEPLTAID---KQGVAELISlfEQHAQRGGMVLLTTHQ 188
Cdd:COG3840  143 CLVRKRPILLLDEPFSALDpalRQEMLDLVD--ELCRERGLTVLMVTHD 189
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
3-188 3.63e-33

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: 116.58  E-value: 3.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   3 EAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRaayqqdllfighq 82
Cdd:cd00267    1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  83 pgikavltpfenlqfyqavrgaaeqqaIWRALEQVGLVGyedlpvaQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDK 162
Cdd:cd00267   68 ---------------------------LEELRRRIGYVP-------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
                        170       180
                 ....*....|....*....|....*.
gi 491074653 163 QGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:cd00267  114 ASRERLLELLRELAEEGRTVIIVTHD 139
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
1-189 7.26e-33

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 116.89  E-value: 7.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFsELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYqqdLLFIG 80
Cdd:PRK13541   1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY---CTYIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 HQPGIKAVLTPFENLQFYQAVRGAAEqqAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAI 160
Cdd:PRK13541  77 HNLGLKLEMTVFENLKFWSEIYNSAE--TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL 154
                        170       180
                 ....*....|....*....|....*....
gi 491074653 161 DKQGVAELISLFEQHAQRGGMVLLTTHQD 189
Cdd:PRK13541 155 SKENRDLLNNLIVMKANSGGIVLLSSHLE 183
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
2-191 5.88e-32

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: 115.51  E-value: 5.88e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCV-RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRD--RAAYQQdllf 78
Cdd:COG1122    1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnlRELRRK---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  79 IG-------HQ---PgikavlTPFENLQF---YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLwL 145
Cdd:COG1122   77 VGlvfqnpdDQlfaP------TVEEDVAFgpeNLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV-L 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 491074653 146 SAAP-LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ-DLA 191
Cdd:COG1122  150 AMEPeVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDlDLV 197
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
11-188 8.02e-31

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: 112.18  E-value: 8.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT-------LRDRAAY--QQ-DLLFIG 80
Cdd:cd03225   11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtklslkeLRRKVGLvfQNpDDQFFG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 HqpgikavlTPFENLQFYQAVRGAAE---QQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:cd03225   91 P--------TVEEEVAFGLENLGLPEeeiEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
                        170       180       190
                 ....*....|....*....|....*....|.
gi 491074653 158 TAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:cd03225  163 AGLDPAGRRELLELLKKLKAEGKTIIIVTHD 193
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
2-187 1.11e-30

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: 111.84  E-value: 1.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN----TLRDRA---AYQQ 74
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvPPERRNigmVFQD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  75 DLLFiGHqpgikavLTPFENLQF---YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLW 151
Cdd:cd03259   81 YALF-PH-------LTVAENIAFglkLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 491074653 152 ILDEPLTAIDKQGVAELISLFEQ-HAQRGGMVLLTTH 187
Cdd:cd03259  153 LLDEPLSALDAKLREELREELKElQRELGITTIYVTH 189
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1-187 2.11e-30

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 114.42  E-value: 2.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRnTLRDRAAYQ------- 73
Cdd:COG3842    5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR-DVTGLPPEKrnvgmvf 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  74 QDL-LFiGHqpgikavLTPFENLQFYQAVRG--AAEQQA-IWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP 149
Cdd:COG3842   84 QDYaLF-PH-------LTVAENVAFGLRMRGvpKAEIRArVAELLELVGLEGLADRYPHQLSGGQQQRVALARA-LAPEP 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 491074653 150 -LWILDEPLTAIDKQGVAELIS-LFEQHAQRGGMVLLTTH 187
Cdd:COG3842  155 rVLLLDEPLSALDAKLREEMREeLRRLQRELGITFIYVTH 194
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
20-187 4.47e-30

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: 110.54  E-value: 4.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQFYQ 99
Cdd:cd03266   24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTGLYDRLTARENLEYFA 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 100 AVRGAAEQQAIWRALEQVGLVGYEDL---PVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHA 176
Cdd:cd03266  104 GLYGLKGDELTARLEELADRLGMEELldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLR 183
                        170
                 ....*....|.
gi 491074653 177 QRGGMVLLTTH 187
Cdd:cd03266  184 ALGKCILFSTH 194
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
21-191 5.03e-30

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: 110.27  E-value: 5.03e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTL----RDRAAY-QQDLLFIGHQPGIKAVLTPFEN- 94
Cdd:cd03255   24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklseKELAAFrRRHIGFVFQSFNLLPDLTALENv 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  95 ---LQFYQAVRGAAEQQAIWrALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISL 171
Cdd:cd03255  104 elpLLLAGVPKKERRERAEE-LLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMEL 182
                        170       180
                 ....*....|....*....|..
gi 491074653 172 F-EQHAQRGGMVLLTTH-QDLA 191
Cdd:cd03255  183 LrELNKEAGTTIVVVTHdPELA 204
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1-187 2.09e-29

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 109.79  E-value: 2.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCV----RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN---TLRDRA-AY 72
Cdd:COG1116    7 ALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvtgPGPDRGvVF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  73 QQDLLFighqPGikavLTPFENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAP 149
Cdd:COG1116   87 QEPALL----PW----LTVLDNVALGLELRGVPKAERRERArelLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491074653 150 LWILDEPLTAIDKQGVAELISLFEQHAQRGGM-VLLTTH 187
Cdd:COG1116  159 VLLMDEPFGALDALTRERLQDELLRLWQETGKtVLFVTH 197
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
20-191 2.32e-29

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 108.59  E-value: 2.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTL----RDRAAYQQDLL-FIGHQPGIKAVLTPFEN 94
Cdd:COG1136   27 VSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslseRELARLRRRHIgFVFQFFNLLPELTALEN 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  95 LQF---YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISL 171
Cdd:COG1136  107 VALpllLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL 186
                        170       180
                 ....*....|....*....|..
gi 491074653 172 FEQHAQRGGM-VLLTTH-QDLA 191
Cdd:COG1136  187 LRELNRELGTtIVMVTHdPELA 208
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
11-187 4.82e-29

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 107.83  E-value: 4.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRDRAAYQ---------QDLLFI 79
Cdd:COG2884   12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsRLKRREIPYlrrrigvvfQDFRLL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  80 GHqpgikavLTPFENLQFYQAVRGAAE---QQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:COG2884   92 PD-------RTVYENVALPLRVTGKSRkeiRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEP 164
                        170       180       190
                 ....*....|....*....|....*....|.
gi 491074653 157 LTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:COG2884  165 TGNLDPETSWEIMELLEEINRRGTTVLIATH 195
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
1-187 8.57e-29

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 106.80  E-value: 8.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDggeVCWRGRNTLRDRAA--------- 71
Cdd:COG4136    1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPA---FSASGEVLLNGRRLtalpaeqrr 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  72 ----YQQDLLFiGHqpgikavLTPFENLQFY--QAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWL 145
Cdd:COG4136   78 igilFQDDLLF-PH-------LSVGENLAFAlpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALL 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 491074653 146 SAAPLWILDEPLTAIDKQGVAELISL-FEQHAQRGGMVLLTTH 187
Cdd:COG4136  150 AEPRALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTH 192
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
12-188 1.32e-28

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


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 111.77  E-value: 1.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLR--DRAAYQQDLLFIGHQPGIkavl 89
Cdd:COG4988  348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD-LSdlDPASWRRQIAWVPQNPYL---- 422
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  90 tpF-----ENLQFYqavRGAAEQQAIWRALEQVGL--------VGYeDLPV----AQLSAGQQRRVALARLWLSAAPLWI 152
Cdd:COG4988  423 --FagtirENLRLG---RPDASDEELEAALEAAGLdefvaalpDGL-DTPLgeggRGLSGGQAQRLALARALLRDAPLLL 496
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 491074653 153 LDEPLTAIDKQGVAELISLFEQHAqRGGMVLLTTHQ 188
Cdd:COG4988  497 LDEPTAHLDAETEAEILQALRRLA-KGRTVILITHR 531
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
1-191 2.03e-28

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 106.68  E-value: 2.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCV-RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAA-------- 71
Cdd:COG3638    2 MLELRNLSKRyPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRalrrlrrr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  72 ----YQQDLLfIGHQPGIKAVLTP-FENLQFYQAVRG---AAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARL 143
Cdd:COG3638   82 igmiFQQFNL-VPRLSVLTNVLAGrLGRTSTWRSLLGlfpPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491074653 144 WLSAAPLWILDEPLTAID---KQGVAELisLFEQHAQRGGMVLLTTHQ-DLA 191
Cdd:COG3638  161 LVQEPKLILADEPVASLDpktARQVMDL--LRRIAREDGITVVVNLHQvDLA 210
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
20-187 2.35e-28

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: 106.05  E-value: 2.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQ--------DLLFIGhqpgikavLTP 91
Cdd:cd03263   21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQslgycpqfDALFDE--------LTV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  92 FENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID---KQGV 165
Cdd:cd03263   93 REHLRFYARLKGLPKSEIKEEVellLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDpasRRAI 172
                        170       180
                 ....*....|....*....|..
gi 491074653 166 AELIslfeQHAQRGGMVLLTTH 187
Cdd:cd03263  173 WDLI----LEVRKGRSIILTTH 190
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
20-187 8.19e-28

daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]


Pssm-ID: 130256 [Multi-domain]  Cd Length: 302  Bit Score: 106.71  E-value: 8.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQFYQ 99
Cdd:TIGR01188  12 VNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGRENLEMMG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  100 AVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHA 176
Cdd:TIGR01188  92 RLYGLPKDEAEERAeelLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRALK 171
                         170
                  ....*....|.
gi 491074653  177 QRGGMVLLTTH 187
Cdd:TIGR01188 172 EEGVTILLTTH 182
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
2-191 1.06e-27

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: 104.96  E-value: 1.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVR-DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRG--RNTLRDRAAYQ----- 73
Cdd:cd03256    1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdINKLKGKALRQlrrqi 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  74 ----QDLLFIGHQPGIKAVLTP-FENLQFYQAVRG---AAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLwL 145
Cdd:cd03256   81 gmifQQFNLIERLSVLENVLSGrLGRRSTWRSLFGlfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA-L 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 491074653 146 SAAPLWIL-DEPLTAIDKQGVAELISLFEQHAQRGGM-VLLTTHQ-DLA 191
Cdd:cd03256  160 MQQPKLILaDEPVASLDPASSRQVMDLLKRINREEGItVIVSLHQvDLA 208
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
1-190 2.00e-27

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 104.43  E-value: 2.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN----TLRDRAAyqqdl 76
Cdd:COG4559    1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPlaawSPWELAR----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  77 lfighqpgIKAVLTPFENLQF----YQAVR---------GAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALAR- 142
Cdd:COG4559   76 --------RRAVLPQHSSLAFpftvEEVVAlgraphgssAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARv 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491074653 143 ---LW--LSAAPLWI-LDEPLTAID---KQGVAELISlfeQHAQRGGMVLLTTHqDL 190
Cdd:COG4559  148 laqLWepVDGGPRWLfLDEPTSALDlahQHAVLRLAR---QLARRGGGVVAVLH-DL 200
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
1-188 3.78e-27

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: 103.63  E-value: 3.78e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCW-----RGRNTLRD-R----- 69
Cdd:COG1119    3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerRGGEDVWElRkrigl 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  70 --AAYQQDllFIGHQPGIKAVLTPFEN-LQFYQAVrGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLS 146
Cdd:COG1119   83 vsPALQLR--FPRDETVLDVVLSGFFDsIGLYREP-TDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 491074653 147 AAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGM-VLLTTHQ 188
Cdd:COG1119  160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPtLVLVTHH 202
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
13-195 1.05e-26

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


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 106.39  E-value: 1.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-------TLRDRAAY--QQDLLFIGhqp 83
Cdd:COG4987  347 GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDlrdldedDLRRRIAVvpQRPHLFDT--- 423
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  84 gikavlTPFENLQFyqaVRGAAEQQAIWRALEQVGL--------VGYeDLPV----AQLSAGQQRRVALARLWLSAAPLW 151
Cdd:COG4987  424 ------TLRENLRL---ARPDATDEELWAALERVGLgdwlaalpDGL-DTWLgeggRRLSGGERRRLALARALLRDAPIL 493
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 491074653 152 ILDEPLTAIDKQGVAELISLFEQHAQrGGMVLLTTHqDLAGVSQ 195
Cdd:COG4987  494 LLDEPTEGLDAATEQALLADLLEALA-GRTVLLITH-RLAGLER 535
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
19-187 1.24e-26

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: 101.68  E-value: 1.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQFY 98
Cdd:cd03265   18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSVDDELTGWENLYIH 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  99 ---QAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQH 175
Cdd:cd03265   98 arlYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKL 177
                        170
                 ....*....|...
gi 491074653 176 AQRGGM-VLLTTH 187
Cdd:cd03265  178 KEEFGMtILLTTH 190
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
17-187 1.92e-26

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: 101.01  E-value: 1.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  17 FSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRDRAAY--QQDLLFighqPGikavLTPF 92
Cdd:cd03293   20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvTGPGPDRGYvfQQDALL----PW----LTVL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  93 ENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAIDKQGVAEL 168
Cdd:cd03293   92 DNVALGLELQGVPKAEARERAeelLELVGLSGFENAYPHQLSGGMRQRVALARA-LAVDPdVLLLDEPFSALDALTREQL 170
                        170       180
                 ....*....|....*....|
gi 491074653 169 ISLFEQHAQRGGM-VLLTTH 187
Cdd:cd03293  171 QEELLDIWRETGKtVLLVTH 190
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
2-187 2.87e-26

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: 100.35  E-value: 2.87e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGdIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGH 81
Cdd:cd03264    1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  82 QPGIKAVLTPFENLQFYQAVRGAA---EQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:cd03264   80 EFGVYPNFTVREFLDYIAWLKGIPskeVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 491074653 159 AIDkqgVAELIS----LFEQHAQRggMVLLTTH 187
Cdd:cd03264  160 GLD---PEERIRfrnlLSELGEDR--IVILSTH 187
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
3-190 3.31e-26

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: 99.43  E-value: 3.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   3 EAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN----TLRDRAayqqdllf 78
Cdd:cd03214    1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslSPKELA-------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  79 ighqpGIKAVLtpfenLQfyqavrgaaeqqaiwrALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:cd03214   73 -----RKIAYV-----PQ----------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
                        170       180       190
                 ....*....|....*....|....*....|...
gi 491074653 159 AIDKQGVAELISLFEQHAQRGGM-VLLTTHqDL 190
Cdd:cd03214  127 HLDIAHQIELLELLRRLARERGKtVVMVLH-DL 158
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
18-189 1.22e-25

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: 98.63  E-value: 1.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT--LRDRA-AYQ--------QDLLFIGHqpgik 86
Cdd:cd03292   18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdLRGRAiPYLrrkigvvfQDFRLLPD----- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  87 avLTPFENLQFYQAVRGAAEQQAIWR---ALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQ 163
Cdd:cd03292   93 --RNVYENVAFALEVTGVPPREIRKRvpaALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
                        170       180
                 ....*....|....*....|....*.
gi 491074653 164 GVAELISLFEQHAQRGGMVLLTTHQD 189
Cdd:cd03292  171 TTWEIMNLLKKINKAGTTVVVATHAK 196
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
20-187 1.25e-25

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: 99.05  E-value: 1.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLLFIG--HQ-PGIKAVLTPFENLQ 96
Cdd:cd03219   19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGED-ITGLPPHEIARLGIGrtFQiPRLFPELTVLENVM 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  97 ------------FYQAVRGAAE-QQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAIDK 162
Cdd:cd03219   98 vaaqartgsgllLARARREEREaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARA-LATDPkLLLLDEPAAGLNP 176
                        170       180
                 ....*....|....*....|....*
gi 491074653 163 QGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:cd03219  177 EETEELAELIRELRERGITVLLVEH 201
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
19-188 2.37e-25

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: 97.74  E-value: 2.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTlrDRAAYQQdllfIGHQP---GIKAVLTPFENL 95
Cdd:cd03269   18 DISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL--DIAARNR----IGYLPeerGLYPKMKVIDQL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  96 QFYQAVRGAAEQQA---IWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLF 172
Cdd:cd03269   92 VYLAQLKGLKKEEArrrIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVI 171
                        170
                 ....*....|....*.
gi 491074653 173 EQHAQRGGMVLLTTHQ 188
Cdd:cd03269  172 RELARAGKTVILSTHQ 187
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
16-191 2.50e-25

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 100.61  E-value: 2.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  16 LFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAA--------YQQDLLFiGHqpgika 87
Cdd:COG1118   17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPrerrvgfvFQHYALF-PH------ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  88 vLTPFENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAIDKQ 163
Cdd:COG1118   90 -MTVAENIAFGLRVRPPSKAEIRARVeelLELVQLEGLADRYPSQLSGGQRQRVALARA-LAVEPeVLLLDEPFGALDAK 167
                        170       180       190
                 ....*....|....*....|....*....|
gi 491074653 164 GVAEL-ISLFEQHAQRGGMVLLTTH-QDLA 191
Cdd:COG1118  168 VRKELrRWLRRLHDELGGTTVFVTHdQEEA 197
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1-156 3.57e-25

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 102.07  E-value: 3.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcWRGRNTlrdRAAY--Qqdllf 78
Cdd:COG0488  315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETV---KIGYfdQ----- 385
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  79 igHQPGIKAVLTPFENLQfyQAVRGAAEQQAiwRA-LEQVGLVGyEDL--PVAQLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:COG0488  386 --HQEELDPDKTVLDELR--DGAPGGTEQEV--RGyLGRFLFSG-DDAfkPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458

                 .
gi 491074653 156 P 156
Cdd:COG0488  459 P 459
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
11-189 4.70e-25

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: 101.59  E-value: 4.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLR-DRAAYQQDLLFIGHQPGIKAVl 89
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWVPQHPFLFAG- 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   90 TPFENLQFYqavRGAAEQQAIWRALEQVGLVGY-EDLPV----------AQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:TIGR02857 411 TIAENIRLA---RPDASDAEIREALERAGLDEFvAALPQgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
                         170       180       190
                  ....*....|....*....|....*....|.
gi 491074653  159 AIDKQGVAELISLFEQHAQrGGMVLLTTHQD 189
Cdd:TIGR02857 488 HLDAETEAEVLEALRALAQ-GRTVLLVTHRL 517
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
21-191 5.49e-25

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: 101.52  E-value: 5.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTL----RDRAAYQQDLLFIGHQPG--------IKAV 88
Cdd:COG1123  285 SLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrRSLRELRRRVQMVFQDPYsslnprmtVGDI 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  89 LTpfENLQFYQAVRGAAEQQAIWRALEQVGLV-GYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAIDKQGVA 166
Cdd:COG1123  365 IA--EPLRLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARA-LALEPkLLILDEPTSALDVSVQA 441
                        170       180
                 ....*....|....*....|....*.
gi 491074653 167 ELISLFEQHAQRGGM-VLLTTHqDLA 191
Cdd:COG1123  442 QILNLLRDLQRELGLtYLFISH-DLA 466
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
20-163 9.47e-25

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: 96.92  E-value: 9.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAA-------YQQDLLFiGHqpgikavLTPF 92
Cdd:cd03300   19 VSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHkrpvntvFQNYALF-PH-------LTVF 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491074653  93 ENLQF---YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQ 163
Cdd:cd03300   91 ENIAFglrLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
2-197 1.88e-24

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: 94.56  E-value: 1.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN---TLRDRAAYQQDLLF 78
Cdd:cd03229    1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdLEDELPPLRRRIGM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  79 IGHQPGIKAVLTPFENLQFyqavrgaaeqqaiwraleqvglvgyedlpvaQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:cd03229   81 VFQDFALFPHLTVLENIAL-------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTS 129
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 491074653 159 AIDKQGVAELISLFEQ-HAQRGGMVLLTTHQ--DLAGVSQTV 197
Cdd:cd03229  130 ALDPITRREVRALLKSlQAQLGITVVLVTHDldEAARLADRV 171
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
1-191 2.71e-24

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: 95.82  E-value: 2.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRDRAAY------ 72
Cdd:COG1127    5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitGLSEKELYelrrri 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  73 ----QQDLLFIGhqpgikavLTPFENLQFY---------QAVRGAAEQqaiwrALEQVGLVGYEDLPVAQLSAGQQRRVA 139
Cdd:COG1127   85 gmlfQGGALFDS--------LTVFENVAFPlrehtdlseAEIRELVLE-----KLELVGLPGAADKMPSELSGGMRKRVA 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491074653 140 LARLWLSAAPLWILDEPLTAIDKQGVAELISLF-EQHAQRGGMVLLTTHqDLA 191
Cdd:COG1127  152 LARALALDPEILLYDEPTAGLDPITSAVIDELIrELRDELGLTSVVVTH-DLD 203
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
4-187 3.63e-24

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 98.98  E-value: 3.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   4 AKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcWRGRNTlrdRAAY-QQDLLFIGHQ 82
Cdd:COG0488    1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-SIPKGL---RIGYlPQEPPLDDDL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  83 PGIKAVLTPFENLQFYQAVRGAAEQQ------------AIWRALEQVGlvGYE-------------------DLPVAQLS 131
Cdd:COG0488   77 TVLDTVLDGDAELRALEAELEELEAKlaepdedlerlaELQEEFEALG--GWEaearaeeilsglgfpeedlDRPVSELS 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 132 AGQQRRVALARLWLSAAPLWILDEP---LtaiDkqgvAELISLFEQH-AQRGGMVLLTTH 187
Cdd:COG0488  155 GGWRRRVALARALLSEPDLLLLDEPtnhL---D----LESIEWLEEFlKNYPGTVLVVSH 207
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1-188 7.20e-24

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 95.95  E-value: 7.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtlRDRAAYQQdllfIG 80
Cdd:COG4152    1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP--LDPEDRRR----IG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 HQP---GIKAVLTPFENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALArlwlsAA----P- 149
Cdd:COG4152   75 YLPeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRAdewLERLGLGDRANKKVEELSKGNQQKVQLI-----AAllhdPe 149
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491074653 150 LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:COG4152  150 LLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQ 188
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
11-188 1.02e-23

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: 93.00  E-value: 1.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARP--DGGEVCWRGRN----TLRDRAAY-QQDLLFIGHqp 83
Cdd:cd03213   19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPldkrSFRKIIGYvPQDDILHPT-- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  84 gikavLTPFENLQFYQAVRGaaeqqaiwraleqvglvgyedlpvaqLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQ 163
Cdd:cd03213   97 -----LTVRETLMFAAKLRG--------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
                        170       180
                 ....*....|....*....|....*
gi 491074653 164 GVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:cd03213  146 SALQVMSLLRRLADTGRTIICSIHQ 170
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
20-188 1.40e-23

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: 93.36  E-value: 1.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR---------NTLRDRAA--YQQDLLFighqpgikAV 88
Cdd:cd03262   19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltddkkniNELRQKVGmvFQQFNLF--------PH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  89 LTPFENLQFYQ-AVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAPLWIL-DEPLTAIDKQ 163
Cdd:cd03262   91 LTVLENITLAPiKVKGMSKAEAEERAlelLEKVGLADKADAYPAQLSGGQQQRVAIARA-LAMNPKVMLfDEPTSALDPE 169
                        170       180
                 ....*....|....*....|....*
gi 491074653 164 GVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:cd03262  170 LVGEVLDVMKDLAEEGMTMVVVTHE 194
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
20-169 1.55e-23

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


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 94.34  E-value: 1.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLR----DRAA------YQQDLLF----------I 79
Cdd:COG0411   23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlpphRIARlgiartFQNPRLFpeltvlenvlV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  80 GHQPGIKA-VLTPFENLQFYQAVRGAAEQQAiWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEP- 156
Cdd:COG0411  103 AAHARLGRgLLAALLRLPRARREEREARERA-EELLERVGLADRADEPAGNLSYGQQRRLEIARA-LATEPkLLLLDEPa 180
                        170
                 ....*....|....*
gi 491074653 157 --LTAIDKQGVAELI 169
Cdd:COG0411  181 agLNPEETEELAELI 195
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
20-200 1.64e-23

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: 93.34  E-value: 1.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTL----RDRAAYQQDLLFIGHQPGikAVLTP---- 91
Cdd:cd03257   24 VSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLklsrRLRKIRRKEIQMVFQDPM--SSLNPrmti 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  92 ----FENLQFYQAVRGAAEQQ-AIWRALEQVGLV-GYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAIDKQG 164
Cdd:cd03257  102 geqiAEPLRIHGKLSKKEARKeAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARA-LALNPkLLIADEPTSALDVSV 180
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 491074653 165 VAELISLFEQHAQRGGM-VLLTTHqDLAGVSQTVGKI 200
Cdd:cd03257  181 QAQILDLLKKLQEELGLtLLFITH-DLGVVAKIADRV 216
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
20-187 2.05e-23

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: 92.71  E-value: 2.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT---LRDRAAY--QQDLlfiGHQPGIKAVltpFEN 94
Cdd:cd03226   19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakERRKSIGyvMQDV---DYQLFTDSV---REE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  95 LqFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQ 174
Cdd:cd03226   93 L-LLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRE 171
                        170
                 ....*....|...
gi 491074653 175 HAQRGGMVLLTTH 187
Cdd:cd03226  172 LAAQGKAVIVITH 184
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
2-187 2.45e-23

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 90.59  E-value: 2.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWrgrntlrdraayqqdllfigh 81
Cdd:cd03221    1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW--------------------- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  82 QPGIKavltpfenlqfyqavrgaaeqqaiwraleqvglVGYedlpVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:cd03221   60 GSTVK---------------------------------IGY----FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
                        170       180
                 ....*....|....*....|....*.
gi 491074653 162 KQGVAELISLFEQHAqrgGMVLLTTH 187
Cdd:cd03221  103 LESIEALEEALKEYP---GTVILVSH 125
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
11-188 7.86e-23

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: 91.79  E-value: 7.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDL------LFighQPG 84
Cdd:cd03261   10 FGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrmgmLF---QSG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  85 ikAV---LTPFENLQFYQAVRGAAEQQAIWR----ALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:cd03261   87 --ALfdsLTVFENVAFPLREHTRLSEEEIREivleKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPT 164
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 491074653 158 TAID---KQGVAELI-SLfeqHAQRGGMVLLTTHQ 188
Cdd:cd03261  165 AGLDpiaSGVIDDLIrSL---KKELGLTSIMVTHD 196
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
1-191 1.09e-22

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: 91.59  E-value: 1.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    1 MLEAKSLSCV--RDERILfSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR----------NTLRD 68
Cdd:TIGR02315   1 MLEVENLSKVypNGKQAL-KNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTditklrgkklRKLRR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   69 RAAYQ-QDLLFIGHQPGIKAVLTPFenLQFYQAVRG------AAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALA 141
Cdd:TIGR02315  80 RIGMIfQHYNLIERLTVLENVLHGR--LGYKPTWRSllgrfsEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 491074653  142 RLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGM-VLLTTHQ-DLA 191
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGItVIINLHQvDLA 209
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
12-187 1.41e-22

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: 94.90  E-value: 1.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRG-------RNTLRDRAAY--QQDLLFIGhq 82
Cdd:COG2274  486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidPASLRRQIGVvlQDVFLFSG-- 563
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  83 pgikavlTPFENLQFYqavRGAAEQQAIWRALEQVGLV--------GYeDLPV----AQLSAGQQRRVALARLWLSAAPL 150
Cdd:COG2274  564 -------TIRENITLG---DPDATDEEIIEAARLAGLHdfiealpmGY-DTVVgeggSNLSGGQRQRLAIARALLRNPRI 632
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 491074653 151 WILDEPLTAIDKQGVAELISLFEQHAQrGGMVLLTTH 187
Cdd:COG2274  633 LILDEATSALDAETEAIILENLRRLLK-GRTVIIIAH 668
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
21-161 1.57e-22

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: 93.18  E-value: 1.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT------LRDRA-AYQQDLLFighqPGikavLTPFE 93
Cdd:TIGR03265  24 SLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDItrlppqKRDYGiVFQSYALF----PN----LTVAD 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491074653   94 NLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:TIGR03265  96 NIAYGLKNRGMGRAEVAERVaelLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALD 166
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
1-188 4.63e-22

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: 89.95  E-value: 4.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCV----RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRDRA--AY 72
Cdd:cd03258    1 MIELKNVSKVfgdtGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltLLSGKElrKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  73 QQDLLFIGHQPGIKAVLTPFENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP 149
Cdd:cd03258   81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVlelLELVGLEDKADAYPAQLSGGQKQRVGIARA-LANNP 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 491074653 150 LWIL-DEPLTAIDKQGVAELISLFEQ-HAQRGGMVLLTTHQ 188
Cdd:cd03258  160 KVLLcDEATSALDPETTQSILALLRDiNRELGLTIVLITHE 200
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
20-187 6.44e-22

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: 89.71  E-value: 6.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN----TLRDRA---AYQQDLLFiGHqpgikavLTPF 92
Cdd:cd03296   21 VSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDatdvPVQERNvgfVFQHYALF-RH-------MTVF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  93 ENLQFYQAVRGAAE-------QQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAIDKQG 164
Cdd:cd03296   93 DNVAFGLRVKPRSErppeaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARA-LAVEPkVLLLDEPFGALDAKV 171
                        170       180
                 ....*....|....*....|....
gi 491074653 165 VAELIS-LFEQHAQRGGMVLLTTH 187
Cdd:cd03296  172 RKELRRwLRRLHDELHVTTVFVTH 195
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1-200 8.76e-22

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: 92.27  E-value: 8.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCV--RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDG---GEVCWRGRNTLR-DRAAYQQ 74
Cdd:COG1123    4 LLEVRDLSVRypGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLElSEALRGR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  75 DLLFIGHQPGikAVLTPF-------ENLQFYQAVRGAAEQQAIWrALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSA 147
Cdd:COG1123   84 RIGMVFQDPM--TQLNPVtvgdqiaEALENLGLSRAEARARVLE-LLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491074653 148 APLWILDEPLTAIDKQGVAELISLFEQHAQRGGM-VLLTTHqDLAGVSQTVGKI 200
Cdd:COG1123  161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTtVLLITH-DLGVVAEIADRV 213
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
1-161 3.61e-21

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 87.90  E-value: 3.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLlfig 80
Cdd:PRK13548   2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-LADWSPAELAR---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 hqpgIKAVLTPFENLQFYQAVR-------------GAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALAR----L 143
Cdd:PRK13548  77 ----RRAVLPQHSSLSFPFTVEevvamgraphglsRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARvlaqL 152
                        170       180
                 ....*....|....*....|
gi 491074653 144 WL-SAAPLW-ILDEPLTAID 161
Cdd:PRK13548 153 WEpDGPPRWlLLDEPTSALD 172
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
12-187 4.12e-21

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: 85.90  E-value: 4.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-------TLRDRAAY--QQDLLFIGhq 82
Cdd:cd03228   13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlrdldleSLRKNIAYvpQDPFLFSG-- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  83 pgikavlTPFENLqfyqavrgaaeqqaiwraleqvglvgyedlpvaqLSAGQQRRVALARLWLSAAPLWILDEPLTAIDK 162
Cdd:cd03228   91 -------TIRENI----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDP 129
                        170       180
                 ....*....|....*....|....*
gi 491074653 163 QGVAELISLFEQHAQrGGMVLLTTH 187
Cdd:cd03228  130 ETEALILEALRALAK-GKTVIVIAH 153
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
15-191 4.15e-21

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: 87.10  E-value: 4.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  15 ILfSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTL--RDRAAY--------QQDLLFIGHQ 82
Cdd:COG4181   27 IL-KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlFALdeDARARLrarhvgfvFQSFQLLPTL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  83 PGIKAVLTPFEnlqfyqaVRGA--AEQQAIwRALEQVGLVGYED-LPvAQLSAGQQRRVALARLWLSAAPLWILDEP--- 156
Cdd:COG4181  106 TALENVMLPLE-------LAGRrdARARAR-ALLERVGLGHRLDhYP-AQLSGGEQQRVALARAFATEPAILFADEPtgn 176
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 491074653 157 LTAIDKQGVAELisLFEQHAQRGGMVLLTTH-QDLA 191
Cdd:COG4181  177 LDAATGEQIIDL--LFELNRERGTTLVLVTHdPALA 210
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
20-188 8.04e-21

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: 86.01  E-value: 8.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRDRAAYQQDLLFigHQPGIKAVLTPFENLQFY 98
Cdd:cd03298   17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDvTAAPPADRPVSMLF--QENNLFAHLTVEQNVGLG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  99 QAVR---GAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLF-EQ 174
Cdd:cd03298   95 LSPGlklTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVlDL 174
                        170
                 ....*....|....
gi 491074653 175 HAQRGGMVLLTTHQ 188
Cdd:cd03298  175 HAETKMTVLMVTHQ 188
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
19-187 9.91e-21

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: 85.81  E-value: 9.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  19 ELSFSVqPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEV-----CW-RGRNTL----RDRA---AYQQDLLFiGHqpgi 85
Cdd:cd03297   16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtVLfDSRKKInlppQQRKiglVFQQYALF-PH---- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  86 kavLTPFENLQFyqAVRGAAEQQAIWRALEQVGLVGYEDL---PVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDK 162
Cdd:cd03297   90 ---LNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLlnrYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
                        170       180
                 ....*....|....*....|....*.
gi 491074653 163 QGVAELISLFEQ-HAQRGGMVLLTTH 187
Cdd:cd03297  165 ALRLQLLPELKQiKKNLNIPVIFVTH 190
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
20-187 1.50e-20

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 87.82  E-value: 1.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTL----RDRA-AYQQDLLFighqPGikavLTPF 92
Cdd:COG3839   22 IDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvTDLppkdRNIAmVFQSYALY----PH----MTVY 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  93 ENLQFYQAVRG--AAE-QQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARlwlsA----APLWILDEPLTAID---- 161
Cdd:COG3839   94 ENIAFPLKLRKvpKAEiDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGR----AlvrePKVFLLDEPLSNLDaklr 169
                        170       180
                 ....*....|....*....|....*.
gi 491074653 162 KQGVAELISLfeqHAQRGGMVLLTTH 187
Cdd:COG3839  170 VEMRAEIKRL---HRRLGTTTIYVTH 192
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
1-161 3.74e-20

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 87.20  E-value: 3.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRDRAAYQQdllf 78
Cdd:PRK09536   3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvEALSARAASRR---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  79 IGHQPGIKAVLTPFENLQFYQAVR----------GAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAA 148
Cdd:PRK09536  79 VASVPQDTSLSFEFDVRQVVEMGRtphrsrfdtwTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
                        170
                 ....*....|...
gi 491074653 149 PLWILDEPLTAID 161
Cdd:PRK09536 159 PVLLLDEPTASLD 171
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
2-187 7.70e-20

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: 83.46  E-value: 7.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcWRGRNTLRDRAAYQQDLLFIGH 81
Cdd:cd03301    1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI-YIGGRDVTDLPPKDRDIAMVFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  82 QPGIKAVLTPFENLQFYQAVRGAAEQ---QAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:cd03301   80 NYALYPHMTVYDNIAFGLKLRKVPKDeidERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 491074653 159 AIDK----QGVAELISLfeqHAQRGGMVLLTTH 187
Cdd:cd03301  160 NLDAklrvQMRAELKRL---QQRLGTTTIYVTH 189
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
12-187 8.54e-20

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 85.24  E-value: 8.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT-LRDRAAYQQdllfIGHQPGIKAV-- 88
Cdd:PRK13537  18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQR----VGVVPQFDNLdp 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  89 -LTPFENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQG 164
Cdd:PRK13537  94 dFTVRENLLVFGRYFGLSAAAARALVpplLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQA 173
                        170       180
                 ....*....|....*....|...
gi 491074653 165 VAELISLFEQHAQRGGMVLLTTH 187
Cdd:PRK13537 174 RHLMWERLRSLLARGKTILLTTH 196
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1-190 2.42e-19

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 83.14  E-value: 2.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRDRAaYQQDLLF 78
Cdd:PRK11231   2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpiSMLSSRQ-LARRLAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  79 IGHQPgikavLTPfENLQFYQAVR-------------GAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWL 145
Cdd:PRK11231  81 LPQHH-----LTP-EGITVRELVAygrspwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 491074653 146 SAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHqDL 190
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH-DL 198
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
19-205 3.32e-19

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: 84.00  E-value: 3.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRnTLRDRAA--------------YQQDLLFiGHqpg 84
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE-VLQDSARgiflpphrrrigyvFQEARLF-PH--- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  85 ikavLTPFENLQFYQAVRGAAEQQAiwrALEQ-VGLVGYEDL---PVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAI 160
Cdd:COG4148   92 ----LSVRGNLLYGRKRAPRAERRI---SFDEvVELLGIGHLldrRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 491074653 161 DKQGVAELISLFEQHAQRGGM-VLLTTHqDLAGVSqtvgkiRLAEH 205
Cdd:COG4148  165 DLARKAEILPYLERLRDELDIpILYVSH-SLDEVA------RLADH 203
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
11-188 4.98e-19

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 84.71  E-value: 4.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPD---GGEVCWRGR----NTLRDRAAY-QQDLLFIGHq 82
Cdd:TIGR00955  35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMpidaKEMRAISAYvQQDDLFIPT- 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   83 pgikavLTPFENLQFYQAVRGAAE------QQAIWRALEQVGL-------VGYEDLpVAQLSAGQQRRVALARLWLSAAP 149
Cdd:TIGR00955 114 ------LTVREHLMFQAHLRMPRRvtkkekRERVDEVLQALGLrkcantrIGVPGR-VKGLSGGERKRLAFASELLTDPP 186
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 491074653  150 LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQ 225
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
20-200 7.03e-19

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 83.23  E-value: 7.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQF-- 97
Cdd:PRK11432  25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED-VTHRSIQQRDICMVFQSYALFPHMSLGENVGYgl 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  98 -YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID---KQGVAELISLFE 173
Cdd:PRK11432 104 kMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDanlRRSMREKIRELQ 183
                        170       180       190
                 ....*....|....*....|....*....|....
gi 491074653 174 QhaQRGGMVLLTTH-QDLA-GVSQTV-----GKI 200
Cdd:PRK11432 184 Q--QFNITSLYVTHdQSEAfAVSDTVivmnkGKI 215
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
1-174 7.16e-19

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 82.12  E-value: 7.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRDRAAYQ----Q 74
Cdd:PRK11831   7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipAMSRSRLYTvrkrM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  75 DLLFighQPG-IKAVLTPFENLQF----YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAP 149
Cdd:PRK11831  87 SMLF---QSGaLFTDMNVFDNVAYplreHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
                        170       180
                 ....*....|....*....|....*
gi 491074653 150 LWILDEPLTAIDKQGVAELISLFEQ 174
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISE 188
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
15-176 1.38e-18

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: 80.17  E-value: 1.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  15 ILFsELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLLFIGHQP---GIKAVLTP 91
Cdd:cd03224   15 ILF-GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRD-ITGLPPHERARAGIGYVPegrRIFPELTV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  92 FENLQFYQAVRGAAEQQAIwraLEQVglvgYEDLPV---------AQLSAGQQRRVALARLWLSAAPLWILDEP------ 156
Cdd:cd03224   93 EENLLLGAYARRRAKRKAR---LERV----YELFPRlkerrkqlaGTLSGGEQQMLAIARALMSRPKLLLLDEPseglap 165
                        170       180
                 ....*....|....*....|....*....
gi 491074653 157 ---------LTAIDKQGVAelISLFEQHA 176
Cdd:cd03224  166 kiveeifeaIRELRDEGVT--ILLVEQNA 192
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
12-161 1.76e-18

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 82.91  E-value: 1.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-------TLRDRAAY--QQDLLFIGhq 82
Cdd:COG1132  351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDirdltleSLRRQIGVvpQDTFLFSG-- 428
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  83 pgikavlTPFENLQFYqavRGAAEQQAIWRALEQVGLV--------GYeDLPVAQ----LSAGQQRRVALARLWLSAAPL 150
Cdd:COG1132  429 -------TIRENIRYG---RPDATDEEVEEAAKAAQAHefiealpdGY-DTVVGErgvnLSGGQRQRIAIARALLKDPPI 497
                        170
                 ....*....|.
gi 491074653 151 WILDEPLTAID 161
Cdd:COG1132  498 LILDEATSALD 508
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
1-193 1.82e-18

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 80.89  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLS-CVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRaayqQDLLFI 79
Cdd:PRK13639   1 ILETRDLKySYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK----KSLLEV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  80 GHQPGI------KAVLTPF--ENLQFYQAVRGAAEQQAIWR---ALEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAA 148
Cdd:PRK13639  77 RKTVGIvfqnpdDQLFAPTveEDVAFGPLNLGLSKEEVEKRvkeALKAVGMEGFENKPPHHLSGGQKKRVAIAGI-LAMK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491074653 149 P-LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ-DLAGV 193
Cdd:PRK13639 156 PeIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDvDLVPV 202
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
20-187 1.83e-18

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


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 79.94  E-value: 1.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-------TLRDRAAY-QQDL-LFIGhqpgikavlT 90
Cdd:cd03245   23 VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDirqldpaDLRRNIGYvPQDVtLFYG---------T 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  91 PFENLQFYqavRGAAEQQAIWRALEQVGLV--------GYeDLPV----AQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:cd03245   94 LRDNITLG---APLADDERILRAAELAGVTdfvnkhpnGL-DLQIgergRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
                        170       180
                 ....*....|....*....|....*....
gi 491074653 159 AIDKQGVAELISLFEQHAqRGGMVLLTTH 187
Cdd:cd03245  170 AMDMNSEERLKERLRQLL-GDKTLIIITH 197
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
2-187 2.04e-18

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


Pssm-ID: 275199 [Multi-domain]  Cd Length: 239  Bit Score: 80.40  E-value: 2.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLLFIGH 81
Cdd:TIGR04406   2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQD-ITHLPMHERARLGIGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   82 ---QPGIKAVLTPFENLQFYQAVRG---AAEQQAIWRAL-EQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAPLWI-L 153
Cdd:TIGR04406  81 lpqEASIFRKLTVEENIMAVLEIRKdldRAEREERLEALlEEFQISHLRDNKAMSLSGGERRRVEIARA-LATNPKFIlL 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 491074653  154 DEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDH 193
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
11-187 3.48e-18

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 80.44  E-value: 3.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  11 RDERILFS-ELSFSVQPgdIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN---TLRDRAAYQQDLLFIGHQPGIK 86
Cdd:PRK13638  12 QDEPVLKGlNLDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldySKRGLLALRQQVATVFQDPEQQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  87 AVLTPFE-NLQFYQAVRGAAEQQAIWRALEQVGLV---GYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDK 162
Cdd:PRK13638  90 IFYTDIDsDIAFSLRNLGVPEAEITRRVDEALTLVdaqHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
                        170       180
                 ....*....|....*....|....*
gi 491074653 163 QGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGNHVIISSH 194
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
18-181 3.50e-18

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 81.28  E-value: 3.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRG----RNTLRDRA---AYQQDLLFiGHqpgikavLT 90
Cdd:PRK10851  19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsRLHARDRKvgfVFQHYALF-RH-------MT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  91 PFENLQFYQAV-------RGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAIDK 162
Cdd:PRK10851  91 VFDNIAFGLTVlprrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARA-LAVEPqILLLDEPFGALDA 169
                        170       180       190
                 ....*....|....*....|....*....|..
gi 491074653 163 QGVAEL-------------ISLFEQHAQRGGM 181
Cdd:PRK10851 170 QVRKELrrwlrqlheelkfTSVFVTHDQEEAM 201
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
21-185 3.65e-18

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 79.65  E-value: 3.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN---TLRDRAAYQQDL--------LFiGHqpgikavL 89
Cdd:COG1126   21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDltdSKKDINKLRRKVgmvfqqfnLF-PH-------L 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  90 TPFENLQFYQ-AVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAPLWIL-DEPLTAIDKQG 164
Cdd:COG1126   93 TVLENVTLAPiKVKKMSKAEAEERAmelLERVGLADKADAYPAQLSGGQQQRVAIARA-LAMEPKVMLfDEPTSALDPEL 171
                        170       180
                 ....*....|....*....|..
gi 491074653 165 VAELISLFEQHAQRG-GMVLLT 185
Cdd:COG1126  172 VGEVLDVMRDLAKEGmTMVVVT 193
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
20-197 5.25e-18

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: 78.91  E-value: 5.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFI-GHQPGIKAVLTPFENLQFY 98
Cdd:cd03267   40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQLWWDLPVIDSFYLL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  99 QAVRGAAEQQAIWRALEQVGLVGYEDL---PVAQLSAGQQRRVALARLWLSAAPLWILDEP---LTAIDKQGVAELISlf 172
Cdd:cd03267  120 AAIYDLPPARFKKRLDELSELLDLEELldtPVRQLSLGQRMRAEIAAALLHEPEILFLDEPtigLDVVAQENIRNFLK-- 197
                        170       180
                 ....*....|....*....|....*..
gi 491074653 173 EQHAQRGGMVLLTTH--QDLAGVSQTV 197
Cdd:cd03267  198 EYNRERGTTVLLTSHymKDIEALARRV 224
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
14-187 6.92e-18

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 80.26  E-value: 6.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  14 RILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT-LRDRAAYQQdllfIGHQPGIKAVLTPF 92
Cdd:PRK13536  54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLARAR----IGVVPQFDNLDLEF 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  93 ---ENLQFYQAVRGAAEQQ---AIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVA 166
Cdd:PRK13536 130 tvrENLLVFGRYFGMSTREieaVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209
                        170       180
                 ....*....|....*....|.
gi 491074653 167 ELISLFEQHAQRGGMVLLTTH 187
Cdd:PRK13536 210 LIWERLRSLLARGKTILLTTH 230
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
21-184 1.22e-17

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 78.09  E-value: 1.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAA-------YQQDLLF----------IGHQP 83
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSrrpvsmlFQENNLFshltvaqnigLGLNP 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  84 GIKavLTpfenlqfyqavrgAAEQQAIWRALEQVGLVGY-EDLPvAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDK 162
Cdd:PRK10771  99 GLK--LN-------------AAQREKLHAIARQMGIEDLlARLP-GQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
                        170       180
                 ....*....|....*....|..
gi 491074653 163 QGVAELISLFEQHAQRGGMVLL 184
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERQLTLL 184
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
2-187 1.36e-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: 77.61  E-value: 1.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGL-----ARPDGGEVCWRGRN---------TLR 67
Cdd:cd03260    1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDiydldvdvlELR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  68 DRAA--YQQDLLFIGhqpgikavlTPFENLQFYQAVRGAAEQQAIWR----ALEQVGLVGYED--LPVAQLSAGQQRRVA 139
Cdd:cd03260   81 RRVGmvFQKPNPFPG---------SIYDNVAYGLRLHGIKLKEELDErveeALRKAALWDEVKdrLHALGLSGGQQQRLC 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491074653 140 LARLWLSAAPLWILDEPLTAID---KQGVAELIslFEQHAQRggMVLLTTH 187
Cdd:cd03260  152 LARALANEPEVLLLDEPTSALDpisTAKIEELI--AELKKEY--TIVIVTH 198
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
20-190 1.63e-17

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 77.96  E-value: 1.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLArPDGGEVCWRGRN-------TLRDRAAY---QQDLLFIghqpgikavL 89
Cdd:COG4138   15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPlsdwsaaELARHRAYlsqQQSPPFA---------M 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  90 TPFENLQFYQAvrGAAEQQAIWRALEQV-GLVGYEDL---PVAQLSAGQQRRVALAR----LWLSAAP---LWILDEPLT 158
Cdd:COG4138   85 PVFQYLALHQP--AGASSEAVEQLLAQLaEALGLEDKlsrPLTQLSGGEWQRVRLAAvllqVWPTINPegqLLLLDEPMN 162
                        170       180       190
                 ....*....|....*....|....*....|..
gi 491074653 159 AIDKQGVAELISLFEQHAQRGGMVLLTTHqDL 190
Cdd:COG4138  163 SLDVAQQAALDRLLRELCQQGITVVMSSH-DL 193
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
21-187 1.78e-17

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


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 75.93  E-value: 1.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTlrdraayqqdllfighqpgikAVLTPFEnlqfyqa 100
Cdd:cd03216   20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV---------------------SFASPRD------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 101 vrgaAEQQAIWRaleqvglvgyedlpVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGG 180
Cdd:cd03216   72 ----ARRAGIAM--------------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGV 133

                 ....*..
gi 491074653 181 MVLLTTH 187
Cdd:cd03216  134 AVIFISH 140
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
21-190 1.84e-17

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: 78.07  E-value: 1.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRD---RAAYQQDLLFIGHQPGIKAVLTPFENL 95
Cdd:cd03294   44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiAAMSRkelRELRRKKISMVFQSFALLPHRTVLENV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  96 QFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID----KQGVAEL 168
Cdd:cd03294  124 AFGLEVQGVPRAEREERAaeaLELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDEL 203
                        170       180
                 ....*....|....*....|..
gi 491074653 169 ISLfeqHAQRGGMVLLTTHqDL 190
Cdd:cd03294  204 LRL---QAELQKTIVFITH-DL 221
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
11-188 3.22e-17

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: 76.93  E-value: 3.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDG---GEVCWRG----RNTLRDRAAY-QQDLLFIGHq 82
Cdd:cd03234   17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGqprkPDQFQKCVAYvRQDDILLPG- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  83 pgikavLTPFENLQFYQAVRGAAEQ-QAIWRAL-EQVGLVGYEDLPVA-----QLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:cd03234   96 ------LTVRETLTYTAILRLPRKSsDAIRKKRvEDVLLRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDE 169
                        170       180       190
                 ....*....|....*....|....*....|...
gi 491074653 156 PLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:cd03234  170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQ 202
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
20-208 3.63e-17

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 77.06  E-value: 3.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRnTLRDRAA------------YQQDLLFighqPGika 87
Cdd:PRK09493  20 IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGL-KVNDPKVderlirqeagmvFQQFYLF----PH--- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  88 vLTPFENLQF-YQAVRGAAEQQAIWRALEQVGLVGYED----LPvAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAID 161
Cdd:PRK09493  92 -LTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAErahhYP-SELSGGQQQRVAIARA-LAVKPkLMLFDEPTSALD 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491074653 162 KQGVAELISLFEQHAQRGGMVLLTTHQdlAGVSQTVGKiRLAEHDAG 208
Cdd:PRK09493 169 PELRHEVLKVMQDLAEEGMTMVIVTHE--IGFAEKVAS-RLIFIDKG 212
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
1-190 3.89e-17

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 77.08  E-value: 3.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcwrgrntlrdraaYQQDLLFIG 80
Cdd:PRK09544   4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKLRIG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 HQPGiKAVLTPFENLQF--YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:PRK09544  71 YVPQ-KLYLDTTLPLTVnrFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
                        170       180       190
                 ....*....|....*....|....*....|..
gi 491074653 159 AIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
34-187 4.01e-17

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: 77.92  E-value: 4.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   34 GPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQFYQAVRG--AAEQQA-I 110
Cdd:TIGR01187   3 GPSGCGKTTLLRLLAGFEQPDSGSIMLDGED-VTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKvpRAEIKPrV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  111 WRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDK----QGVAELISLfeqHAQRGGMVLLTT 186
Cdd:TIGR01187  82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKklrdQMQLELKTI---QEQLGITFVFVT 158

                  .
gi 491074653  187 H 187
Cdd:TIGR01187 159 H 159
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
20-187 4.41e-17

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: 76.43  E-value: 4.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcWRGRNTLRDRAAYQQDLLFIGH---QPGIKAVLTPFENLQ 96
Cdd:cd03218   19 VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKI-LLDGQDITKLPMHKRARLGIGYlpqEASIFRKLTVEENIL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  97 FYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAPLWI-LDEPLTAIDKQGVAELISLF 172
Cdd:cd03218   98 AVLEIRGLSKKEREEKLeelLEEFHITHLRKSKASSLSGGERRRVEIARA-LATNPKFLlLDEPFAGVDPIAVQDIQKII 176
                        170
                 ....*....|....*
gi 491074653 173 EQHAQRGGMVLLTTH 187
Cdd:cd03218  177 KILKDRGIGVLITDH 191
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
1-187 4.50e-17

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 76.29  E-value: 4.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVR------DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRDRaAY 72
Cdd:PRK10247   1 MQENSPLLQLQnvgylaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDisTLKPE-IY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  73 QQDLLFIGHQPgikaVL---TPFENLQF-YQAVRGAAEQQAIWRALEQVGLVGYE-DLPVAQLSAGQQRRVALARLWLSA 147
Cdd:PRK10247  80 RQQVSYCAQTP----TLfgdTVYDNLIFpWQIRNQQPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFM 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 491074653 148 APLWILDEPLTAID---KQGVAELISLFEQhaQRGGMVLLTTH 187
Cdd:PRK10247 156 PKVLLLDEITSALDesnKHNVNEIIHRYVR--EQNIAVLWVTH 196
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
15-188 4.70e-17

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 76.59  E-value: 4.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  15 ILFsELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcwrgrntlrDRAAYQQDLlfiGHQPGIKAV------ 88
Cdd:PRK11124  17 ALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL---------NIAGNHFDF---SKTPSDKAIrelrrn 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  89 -------------LTPFENLqfYQA---VRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAP 149
Cdd:PRK11124  84 vgmvfqqynlwphLTVQQNL--IEApcrVLGLSKDQALARAeklLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491074653 150 LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
1-178 5.84e-17

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


Pssm-ID: 440179 [Multi-domain]  Cd Length: 236  Bit Score: 76.17  E-value: 5.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDE-RILFsELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLLFI 79
Cdd:COG0410    3 MLEVENLHAGYGGiHVLH-GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-ITGLPPHRIARLGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  80 GHQP---GIKAVLTPFENLQFYQAVRGAAEQQAiwRALEQVglvgYEDLPV---------AQLSAGQQRRVALARLWLSA 147
Cdd:COG0410   81 GYVPegrRIFPSLTVEENLLLGAYARRDRAEVR--ADLERV----YELFPRlkerrrqraGTLSGGEQQMLAIGRALMSR 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 491074653 148 APLWILDEP---------------LTAIDKQGVAelISLFEQHAQR 178
Cdd:COG0410  155 PKLLLLDEPslglapliveeifeiIRRLNREGVT--ILLVEQNARF 198
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
12-188 7.48e-17

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 78.17  E-value: 7.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRntlrDRAAYQQDLL-----FIGHQPGIK 86
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV----PVSSLDQDEVrrrvsVCAQDAHLF 421
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   87 AVlTPFENLQFyqaVRGAAEQQAIWRALEQVGLVGY-EDLP----------VAQLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:TIGR02868 422 DT-TVRENLRL---ARPDATDEELWAALERVGLADWlRALPdgldtvlgegGARLSGGERQRLALARALLADAPILLLDE 497
                         170       180       190
                  ....*....|....*....|....*....|...
gi 491074653  156 PLTAIDKQGVAELISLFEQhAQRGGMVLLTTHQ 188
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLA-ALSGRTVVLITHH 529
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
1-188 8.92e-17

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 75.94  E-value: 8.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG 80
Cdd:PRK11264   3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIRQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 HQPGIKAVLTPF---------EN-LQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSA 147
Cdd:PRK11264  83 LRQHVGFVFQNFnlfphrtvlENiIEGPVIVKGEPKEEATARArelLAKVGLAGKETSYPRRLSGGQQQRVAIARA-LAM 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 491074653 148 APLWIL-DEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:PRK11264 162 RPEVILfDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
19-187 1.03e-16

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 75.62  E-value: 1.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRDRAAYQ---QDLLFIGHQPGIKAVLTPFE 93
Cdd:PRK11629  27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmSKLSSAAKAElrnQKLGFIYQFHHLLPDFTALE 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  94 NLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLP---VAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELIS 170
Cdd:PRK11629 107 NVAMPLLIGKKKPAEINSRALEMLAAVGLEHRAnhrPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ 186
                        170
                 ....*....|....*...
gi 491074653 171 LF-EQHAQRGGMVLLTTH 187
Cdd:PRK11629 187 LLgELNRLQGTAFLVVTH 204
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
11-187 1.60e-16

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: 75.03  E-value: 1.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT-------LRDRAAY--QQDLLFiGH 81
Cdd:cd03295   11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIreqdpveLRRKIGYviQQIGLF-PH 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  82 qpgikavLTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVA-----QLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:cd03295   90 -------MTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFAdryphELSGGQQQRVGVARALAADPPLLLMDEP 162
                        170       180       190
                 ....*....|....*....|....*....|..
gi 491074653 157 LTAIDKQGVAELISLFEQ-HAQRGGMVLLTTH 187
Cdd:cd03295  163 FGALDPITRDQLQEEFKRlQQELGKTIVFVTH 194
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
1-187 2.10e-16

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 74.68  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLLFIG 80
Cdd:COG1137    3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED-ITHLPMHKRARLGIG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 H---QPGIKAVLTPFENLqfyQAV-----RGAAEQQAIWRAL-EQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAPLW 151
Cdd:COG1137   82 YlpqEASIFRKLTVEDNI---LAVlelrkLSKKEREERLEELlEEFGITHLRKSKAYSLSGGERRRVEIARA-LATNPKF 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 491074653 152 I-LDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:COG1137  158 IlLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH 194
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
21-187 2.47e-16

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 75.03  E-value: 2.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTlrdraayqQDLlfIGHQPGIKAV------------ 88
Cdd:PRK11300  25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI--------EGL--PGHQIARMGVvrtfqhvrlfre 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  89 LTPFENL--------------------QFYQAVRGAAEQQAIWraLEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAA 148
Cdd:PRK11300  95 MTVIENLlvaqhqqlktglfsgllktpAFRRAESEALDRAATW--LERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 491074653 149 PLWILDEPLTAIDKQGVAELISLFEQ-HAQRGGMVLLTTH 187
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAElRNEHNVTVLLIEH 212
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
24-187 2.57e-16

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 74.43  E-value: 2.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  24 VQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLR----DRAAYQ-QDLLFIGHQPGIKAVLTPFENLQFY 98
Cdd:PRK10584  33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARAKLRaKHVGFVFQSFMLIPTLNALENVELP 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  99 QAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQG---VAELisLF 172
Cdd:PRK10584 113 ALLRGESSRQSRNGAkalLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkIADL--LF 190
                        170
                 ....*....|....*
gi 491074653 173 EQHAQRGGMVLLTTH 187
Cdd:PRK10584 191 SLNREHGTTLILVTH 205
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
2-161 2.95e-16

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 76.14  E-value: 2.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR------------NTLrdr 69
Cdd:PRK09452  15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvpaenrhvNTV--- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  70 aaYQQDLLFiGHqpgikavLTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLP---VAQLSAGQQRRVALARLWLS 146
Cdd:PRK09452  92 --FQSYALF-PH-------MTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAqrkPHQLSGGQQQRVAIARAVVN 161
                        170
                 ....*....|....*
gi 491074653 147 AAPLWILDEPLTAID 161
Cdd:PRK09452 162 KPKVLLLDESLSALD 176
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
20-195 3.03e-16

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: 73.12  E-value: 3.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVlTPFENLQfyq 99
Cdd:cd03247   21 LSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT-TLRNNLG--- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 100 avrgaaeqqaiwraleqvglvgyedlpvAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAqRG 179
Cdd:cd03247   97 ----------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVL-KD 147
                        170
                 ....*....|....*.
gi 491074653 180 GMVLLTTHQdLAGVSQ 195
Cdd:cd03247  148 KTLIWITHH-LTGIEH 162
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
20-187 3.49e-16

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: 76.59  E-value: 3.49e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQFYQ 99
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYA 2037
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   100 AVRGAA----EQQAIWrALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQH 175
Cdd:TIGR01257 2038 RLRGVPaeeiEKVANW-SIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
                          170
                   ....*....|..
gi 491074653   176 AQRGGMVLLTTH 187
Cdd:TIGR01257 2117 IREGRAVVLTSH 2128
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
2-161 5.01e-16

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: 75.74  E-value: 5.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCW----------RGRNTLRD-RA 70
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayvdQSRDALDPnKT 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   71 AYQ-----QDLLFIG-HQPGIKAVLTPFenlqfyqAVRGAAEQQaiwraleqvglvgyedlPVAQLSAGQQRRVALARLW 144
Cdd:TIGR03719 403 VWEeisggLDIIKLGkREIPSRAYVGRF-------NFKGSDQQK-----------------KVGQLSGGERNRVHLAKTL 458
                         170
                  ....*....|....*..
gi 491074653  145 LSAAPLWILDEPLTAID 161
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD 475
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
14-187 5.61e-16

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: 75.74  E-value: 5.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   14 RILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEvcwrgrntlrdraAYQQDLLFIGH---QPGIKAVLT 90
Cdd:TIGR03719  18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE-------------ARPQPGIKVGYlpqEPQLDPTKT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   91 PFEN-----------LQFYQAVRG------------AAEQQAIWRALEQVGLVGYE---------------DLPVAQLSA 132
Cdd:TIGR03719  85 VRENveegvaeikdaLDRFNEISAkyaepdadfdklAAEQAELQEIIDAADAWDLDsqleiamdalrcppwDADVTKLSG 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 491074653  133 GQQRRVALARLWLSAAPLWILDEPLTAIDkqgvAELISLFEQHAQR-GGMVLLTTH 187
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEyPGTVVAVTH 216
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
12-175 6.21e-16

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 75.61  E-value: 6.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGL--------ARPDGGEVCW--------RGrnTLRDraayqqd 75
Cdd:COG4178  374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwpygsgriARPAGARVLFlpqrpylpLG--TLRE------- 444
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  76 llfighqpgikAVLTPFENLQFyqavrgaaEQQAIWRALEQVGLVGY-EDLPVAQ-----LSAGQQRRVALARLWLSAAP 149
Cdd:COG4178  445 -----------ALLYPATAEAF--------SDAELREALEAVGLGHLaERLDEEAdwdqvLSLGEQQRLAFARLLLHKPD 505
                        170       180
                 ....*....|....*....|....*.
gi 491074653 150 LWILDEPLTAIDKQGVAELISLFEQH 175
Cdd:COG4178  506 WLFLDEATSALDEENEAALYQLLREE 531
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
10-187 6.59e-16

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: 73.52  E-value: 6.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  10 VRDERILFSE-----LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTL------RDRAAYQQDLLF 78
Cdd:cd03299    3 VENLSKDWKEfklknVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITnlppekRDISYVPQNYAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  79 IGHqpgikavLTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDL---PVAQLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:cd03299   83 FPH-------MTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLlnrKPETLSGGEQQRVAIARALVVNPKILLLDE 155
                        170       180       190
                 ....*....|....*....|....*....|...
gi 491074653 156 PLTAIDKQGVAELISLFEQ-HAQRGGMVLLTTH 187
Cdd:cd03299  156 PFSALDVRTKEKLREELKKiRKEFGVTVLHVTH 188
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
6-187 8.85e-16

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 73.57  E-value: 8.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   6 SLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLR----DRAAYQQDLLFIgH 81
Cdd:PRK10419  17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraQRKAFRRDIQMV-F 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  82 QPGIKAVltpfeNLQfyQAVR-------------GAAEQQAiwRALEQVGLVGYED-----LPvAQLSAGQQRRVALARL 143
Cdd:PRK10419  96 QDSISAV-----NPR--KTVReiireplrhllslDKAERLA--RASEMLRAVDLDDsvldkRP-PQLSGGQLQRVCLARA 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 491074653 144 wLSAAP-LWILDEPLTAIDKQGVAELISLFEQHAQRGGMV-LLTTH 187
Cdd:PRK10419 166 -LAVEPkLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITH 210
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
20-187 1.09e-15

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: 72.57  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLrdraayqqdLLFIGHqpGIKAVLTPFENLQFYQ 99
Cdd:cd03220   41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS---------LLGLGG--GFNPELTGRENIYLNG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 100 AVRG--AAEQQAIWRALEQV-GLVGYEDLPVAQLSAGQQRRVALArlwLSAA---PLWILDEPLTAIDKQGVAELISLFE 173
Cdd:cd03220  110 RLLGlsRKEIDEKIDEIIEFsELGDFIDLPVKTYSSGMKARLAFA---IATAlepDILLIDEVLAVGDAAFQEKCQRRLR 186
                        170
                 ....*....|....
gi 491074653 174 QHAQRGGMVLLTTH 187
Cdd:cd03220  187 ELLKQGKTVILVSH 200
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
20-191 1.29e-15

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 73.58  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDllfIGhqpgikAV----------L 89
Cdd:COG4586   41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARR---IG------VVfgqrsqlwwdL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  90 TPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDL---PVAQLSAGQQRRVALArlwlsAAPLW-----ILDEP---LT 158
Cdd:COG4586  112 PAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELldtPVRQLSLGQRMRCELA-----AALLHrpkilFLDEPtigLD 186
                        170       180       190
                 ....*....|....*....|....*....|...
gi 491074653 159 AIDKQGVAELISlfEQHAQRGGMVLLTTHqDLA 191
Cdd:COG4586  187 VVSKEAIREFLK--EYNRERGTTILLTSH-DMD 216
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
13-197 1.80e-15

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 72.40  E-value: 1.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCwRGRNTLrdrAAYQQD--LLFighQpgiKAVLT 90
Cdd:PRK11247  24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AGTAPL---AEAREDtrLMF---Q---DARLL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  91 PF----ENLQFyqAVRGAAEQQAIwRALEQVGLVGY-EDLPVAqLSAGQQRRVALARLWLSAAPLWILDEPLTAIDK--- 162
Cdd:PRK11247  94 PWkkviDNVGL--GLKGQWRDAAL-QALAAVGLADRaNEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLGALDAltr 169
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 491074653 163 ---QGVAEliSLFEQHaqrGGMVLLTTHQdlagVSQTV 197
Cdd:PRK11247 170 iemQDLIE--SLWQQH---GFTVLLVTHD----VSEAV 198
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
12-187 1.91e-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: 70.71  E-value: 1.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEV--------CWrGRNTLRDRAAY--QQDLLFIGh 81
Cdd:cd03246   13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisQW-DPNELGDHVGYlpQDDELFSG- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  82 qpgikavlTPFENLqfyqavrgaaeqqaiwraleqvglvgyedlpvaqLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:cd03246   91 --------SIAENI----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
                        170       180
                 ....*....|....*....|....*.
gi 491074653 162 KQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:cd03246  129 VEGERALNQAIAALKAAGATRIVIAH 154
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
1-187 2.20e-15

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 72.42  E-value: 2.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRA----AYQQDL 76
Cdd:PRK11248   1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAergvVFQNEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  77 LFighqPGIKAVltpfENLQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWIL 153
Cdd:PRK11248  81 LL----PWRNVQ----DNVAFGLQLAGVEKMQRLEIAhqmLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 491074653 154 DEPLTAIDKQGVAELISLFEQHAQRGG-MVLLTTH 187
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGkQVLLITH 187
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
20-190 2.55e-15

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 71.89  E-value: 2.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLArPDGGEVCWRGRN-------TLRDRAAY---QQDLLFIghqpgikavL 89
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPleawsaaELARHRAYlsqQQTPPFA---------M 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  90 TPFENLQFYQA--VRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALA----RLWLSAAP---LWILDEPLTAI 160
Cdd:PRK03695  85 PVFQYLTLHQPdkTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlQVWPDINPagqLLLLDEPMNSL 164
                        170       180       190
                 ....*....|....*....|....*....|
gi 491074653 161 DKQGVAELISLFEQHAQRGGMVLLTTHqDL 190
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGIAVVMSSH-DL 193
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
21-195 3.16e-15

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 72.22  E-value: 3.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTlrdRAAYQQDLlfIGHQPGIKAVLTPFENLQFYQA 100
Cdd:PRK15056  27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---RQALQKNL--VAYVPQSEEVDWSFPVLVEDVV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 101 VRG------------AAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAEL 168
Cdd:PRK15056 102 MMGryghmgwlrrakKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
                        170       180
                 ....*....|....*....|....*..
gi 491074653 169 ISLFEQHAQRGGMVLLTTHqDLAGVSQ 195
Cdd:PRK15056 182 ISLLRELRDEGKTMLVSTH-NLGSVTE 207
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
21-187 3.48e-15

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 73.14  E-value: 3.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRD-RAAYQqdlLFIG--HQ-----PgikaVLTP 91
Cdd:COG3845   25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvRIRSpRDAIA---LGIGmvHQhfmlvP----NLTV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  92 FENLQ------FYQAVRGAAEQQAIWRALEQVGL-VgyeDL--PVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDK 162
Cdd:COG3845   98 AENIVlgleptKGGRLDRKAARARIRELSERYGLdV---DPdaKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTP 174
                        170       180
                 ....*....|....*....|....*
gi 491074653 163 QGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:COG3845  175 QEADELFEILRRLAAEGKSIIFITH 199
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
20-187 3.75e-15

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 71.06  E-value: 3.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAA------YQQDLLFIGHQpgIKAVLTPFE 93
Cdd:PRK10908  21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpflrRQIGMIFQDHH--LLMDRTVYD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  94 NLQFYQAVRGAAEQQAIWR---ALEQVGLVG-YEDLPVaQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELI 169
Cdd:PRK10908  99 NVAIPLIIAGASGDDIRRRvsaALDKVGLLDkAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIL 177
                        170
                 ....*....|....*...
gi 491074653 170 SLFEQHAQRGGMVLLTTH 187
Cdd:PRK10908 178 RLFEEFNRVGVTVLMATH 195
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
20-188 1.13e-14

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 70.11  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRntlrdRAAyqqdLLFIGHqpGIKAVLTPFENLQFYQ 99
Cdd:COG1134   45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-----VSA----LLELGA--GFHPELTGRENIYLNG 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 100 AVRGAAEQQaIWRALEQV----GLVGYEDLPVAQLSAGQQRRVALArlwLSAA---PLWILDEPLTAIDKQGVAELISLF 172
Cdd:COG1134  114 RLLGLSRKE-IDEKFDEIvefaELGDFIDQPVKTYSSGMRARLAFA---VATAvdpDILLVDEVLAVGDAAFQKKCLARI 189
                        170
                 ....*....|....*.
gi 491074653 173 EQHAQRGGMVLLTTHQ 188
Cdd:COG1134  190 RELRESGRTVIFVSHS 205
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
1-163 1.43e-14

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 71.02  E-value: 1.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYQQDLLFIG 80
Cdd:PRK11607  19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRPINMMF 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 HQPGIKAVLTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVA---QLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:PRK11607  98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRkphQLSGGQRQRVALARSLAKRPKLLLLDEPM 177

                 ....*.
gi 491074653 158 TAIDKQ 163
Cdd:PRK11607 178 GALDKK 183
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
11-190 1.85e-14

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 69.22  E-value: 1.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRgrntlrdraayQQDLLFIGHQPGIKAVLt 90
Cdd:COG2401   40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----------VPDNQFGREASLIDAIG- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  91 pfENLQFYQAVrgaaeqqaiwRALEQVGLVgyeDL-----PVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGV 165
Cdd:COG2401  108 --RKGDFKDAV----------ELLNAVGLS---DAvlwlrRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
                        170       180
                 ....*....|....*....|....*..
gi 491074653 166 AELISLFEQHAQRGG--MVLLTTHQDL 190
Cdd:COG2401  173 KRVARNLQKLARRAGitLVVATHHYDV 199
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
13-162 1.87e-14

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: 69.18  E-value: 1.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-------TLRDRAAY--QQDLLFIGhqp 83
Cdd:cd03254   15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDirdisrkSLRSMIGVvlQDTFLFSG--- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  84 gikavlTPFENLQFYqavRGAAEQQAIWRALEQVGLV--------GYEDLPVAQ---LSAGQQRRVALARLWLSAAPLWI 152
Cdd:cd03254   92 ------TIMENIRLG---RPNATDEEVIEAAKEAGAHdfimklpnGYDTVLGENggnLSQGERQLLAIARAMLRDPKILI 162
                        170
                 ....*....|
gi 491074653 153 LDEPLTAIDK 162
Cdd:cd03254  163 LDEATSNIDT 172
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
21-193 2.53e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 70.11  E-value: 2.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLL---FIGHQPGIK----------- 86
Cdd:PRK13651  27 SVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVlekLVIQKTRFKkikkikeirrr 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  87 -AVLTPFENLQFYQAV-----------RGAAEQQAIWRALEQVGLVGyedLPVA-------QLSAGQQRRVALARLwLSA 147
Cdd:PRK13651 107 vGVVFQFAEYQLFEQTiekdiifgpvsMGVSKEEAKKRAAKYIELVG---LDESylqrspfELSGGQKRRVALAGI-LAM 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491074653 148 AP-LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHqDLAGV 193
Cdd:PRK13651 183 EPdFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH-DLDNV 228
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
20-187 2.98e-14

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: 68.65  E-value: 2.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLR---DR-AAYQQDLLFighqpgikAVLTPFENL 95
Cdd:TIGR01184   4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpDRmVVFQNYSLL--------PWLTVRENI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   96 qfYQAVRGA------AEQQAIWRA-LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAID---KQG 164
Cdd:TIGR01184  76 --ALAVDRVlpdlskSERRAIVEEhIALVGLTEAADKRPGQLSGGMKQRVAIARA-LSIRPkVLLLDEPFGALDaltRGN 152
                         170       180
                  ....*....|....*....|....
gi 491074653  165 VAE-LISLFEQHaqrGGMVLLTTH 187
Cdd:TIGR01184 153 LQEeLMQIWEEH---RVTVLMVTH 173
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
20-187 3.54e-14

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 70.24  E-value: 3.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-------TLRDRAAY--QQDLLFIGhqpgikavlT 90
Cdd:PRK11160 359 LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiadyseaALRQAISVvsQRVHLFSA---------T 429
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  91 PFENLQFyqAVRGAAEQQAIwRALEQVGLvgyEDLPVA-------------QLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:PRK11160 430 LRDNLLL--AAPNASDEALI-EVLQQVGL---EKLLEDdkglnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPT 503
                        170       180       190
                 ....*....|....*....|....*....|
gi 491074653 158 TAIDKQGVAELISLFEQHAQrGGMVLLTTH 187
Cdd:PRK11160 504 EGLDAETERQILELLAEHAQ-NKTVLMITH 532
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
30-188 3.93e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 69.06  E-value: 3.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  30 IQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVLTPF--ENLQFYQAVRGAAEQ 107
Cdd:PRK13652  33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIFSPTveQDIAFGPINLGLDEE 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 108 QAIWRALEQVGLVGYEDLPVA---QLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGM-VL 183
Cdd:PRK13652 113 TVAHRVSSALHMLGLEELRDRvphHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMtVI 192

                 ....*
gi 491074653 184 LTTHQ 188
Cdd:PRK13652 193 FSTHQ 197
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
20-187 4.26e-14

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 70.15  E-value: 4.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSvqPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEvcwrgrntlrdraAYQQDLLFIGHQP---------------- 83
Cdd:PRK11819  28 LSFF--PGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-------------ARPAPGIKVGYLPqepqldpektvrenve 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  84 ----GIKAVLTPFE--NLQF------YQAVrgAAEQ---QAI------W---RALEQV--------GlvgyeDLPVAQLS 131
Cdd:PRK11819  93 egvaEVKAALDRFNeiYAAYaepdadFDAL--AAEQgelQEIidaadaWdldSQLEIAmdalrcppW-----DAKVTKLS 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491074653 132 AGQQRRVALARLWLSAAPLWILDEPLTAIDkqgvAELISLFEQHAQR-GGMVLLTTH 187
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLEQFLHDyPGTVVAVTH 218
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
2-188 4.60e-14

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 68.50  E-value: 4.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRG-----RNTLRDRAAYQ--Q 74
Cdd:COG4161    3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfSQKPSEKAIRLlrQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  75 DLLFIGHQPGIKAVLTPFENLqfYQA---VRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAA 148
Cdd:COG4161   83 KVGMVFQQYNLWPHLTVMENL--IEApckVLGLSKEQAREKAmklLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 491074653 149 PLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:COG4161  161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHE 200
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
21-187 6.05e-14

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 69.66  E-value: 6.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRD-RAAYQ-------QDL-----------LFIG 80
Cdd:COG1129   24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPvRFRSpRDAQAagiaiihQELnlvpnlsvaenIFLG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 HQPGIKAVLTpfenlqfYQAVRGAAEQqaiwrALEQVGLvgyeDL----PVAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:COG1129  104 REPRRGGLID-------WRAMRRRARE-----LLARLGL----DIdpdtPVGDLSVAQQQLVEIARALSRDARVLILDEP 167
                        170       180       190
                 ....*....|....*....|....*....|.
gi 491074653 157 LTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:COG1129  168 TASLTEREVERLFRIIRRLKAQGVAIIYISH 198
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
2-195 6.70e-14

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 69.49  E-value: 6.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVR-DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLArPDGGEVCWRGRNtLR--DRAAYQQDLLF 78
Cdd:PRK11174 350 IEAEDLEILSpDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIE-LRelDPESWRKHLSW 427
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  79 IGHQPGIKAVlTPFENLQFYQAvrgAAEQQAIWRALEQV-----------GLvgyeDLPV----AQLSAGQQRRVALARL 143
Cdd:PRK11174 428 VGQNPQLPHG-TLRDNVLLGNP---DASDEQLQQALENAwvseflpllpqGL----DTPIgdqaAGLSVGQAQRLALARA 499
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491074653 144 WLSAAPLWILDEPLTAIDKQGvAELISLFEQHAQRGGMVLLTTHQ--DLAGVSQ 195
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHS-EQLVMQALNAASRRQTTLMVTHQleDLAQWDQ 552
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
20-188 6.94e-14

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 68.50  E-value: 6.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDG---------GEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVLT 90
Cdd:PRK09984  23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIRKSRANTGYIFQQFNLVNRLS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  91 PFENL--------QFYQAVR---GAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:PRK09984 103 VLENVligalgstPFWRTCFswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
                        170       180       190
                 ....*....|....*....|....*....|
gi 491074653 160 IDKQGVAELISLFEQHAQRGGM-VLLTTHQ 188
Cdd:PRK09984 183 LDPESARIVMDTLRDINQNDGItVVVTLHQ 212
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
2-187 7.14e-14

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 68.00  E-value: 7.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT----LRDRAayQQDLL 77
Cdd:PRK10895   4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllpLHARA--RRGIG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  78 FIGHQPGIKAVLTPFENLQFYQAVRG--AAEQQAIwRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAPLWI 152
Cdd:PRK10895  82 YLPQEASIFRRLSVYDNLMAVLQIRDdlSAEQRED-RAnelMEEFHIEHLRDSMGQSLSGGERRRVEIARA-LAANPKFI 159
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 491074653 153 -LDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:PRK10895 160 lLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
12-175 7.39e-14

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 66.41  E-value: 7.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLarpdggevcW---RGRNTLRDRAayqqDLLFIGHQPgikav 88
Cdd:cd03223   12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL---------WpwgSGRIGMPEGE----DLLFLPQRP----- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  89 LTPFENLqfyqavrgaaeQQAIWRALEQVglvgyedlpvaqLSAGQQRRVALARLWLsAAPLW-ILDEPLTAIDKQGVAE 167
Cdd:cd03223   74 YLPLGTL-----------REQLIYPWDDV------------LSGGEQQRLAFARLLL-HKPKFvFLDEATSALDEESEDR 129

                 ....*...
gi 491074653 168 LISLFEQH 175
Cdd:cd03223  130 LYQLLKEL 137
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
20-187 8.96e-14

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 69.37  E-value: 8.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRDRAAYQ---QDLLFIGHQPGIKAVLTPFEN 94
Cdd:PRK10535  27 ISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvaTLDADALAQlrrEHFGFIFQRYHLLSHLTAAQN 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  95 LQFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISL 171
Cdd:PRK10535 107 VEVPAVYAGLERKQRLLRAqelLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAI 186
                        170
                 ....*....|....*.
gi 491074653 172 FEQHAQRGGMVLLTTH 187
Cdd:PRK10535 187 LHQLRDRGHTVIIVTH 202
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
20-190 9.89e-14

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 67.17  E-value: 9.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRdRAAYQQDLLFIGHQP---GIKAVLTPFENLQ 96
Cdd:TIGR03410  19 VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITK-LPPHERARAGIAYVPqgrEIFPRLTVEENLL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   97 FYQAVRGAAEQQAIWRAleqvglvgYEDLPVAQ---------LSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAE 167
Cdd:TIGR03410  98 TGLAALPRRSRKIPDEI--------YELFPVLKemlgrrggdLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKD 169
                         170       180
                  ....*....|....*....|...
gi 491074653  168 LISLFEQHAQRGGMVLLTTHQDL 190
Cdd:TIGR03410 170 IGRVIRRLRAEGGMAILLVEQYL 192
cbiO PRK13643
energy-coupling factor transporter ATPase;
14-187 9.99e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 68.22  E-value: 9.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  14 RILFsELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcwRGRNTLRDRAAYQQDLLFIGHQPGIKAVL---- 89
Cdd:PRK13643  20 RALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV--TVGDIVVSSTSKQKEIKPVRKKVGVVFQFpesq 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  90 ----TPFENLQFYQAVRGAAEQQAIWRALEQVGLVG-----YEDLPVaQLSAGQQRRVALARLWLSAAPLWILDEPLTAI 160
Cdd:PRK13643  97 lfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGladefWEKSPF-ELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
                        170       180
                 ....*....|....*....|....*..
gi 491074653 161 DKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTH 202
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
20-188 1.98e-13

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 66.92  E-value: 1.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT--LRDRAA------------YQQDLLFIGHQPGI 85
Cdd:PRK10619  24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlVRDKDGqlkvadknqlrlLRTRLTMVFQHFNL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  86 KAVLTPFEN-LQFYQAVRGAAEQQAIWRALEQVGLVGYED-----LPVaQLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:PRK10619 104 WSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDEraqgkYPV-HLSGGQQQRVSIARALAMEPEVLLFDEPTSA 182
                        170       180
                 ....*....|....*....|....*....
gi 491074653 160 IDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:PRK10619 183 LDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
2-58 2.76e-13

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 67.84  E-value: 2.76e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEV 58
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
19-182 3.14e-13

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 66.28  E-value: 3.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  19 ELSFSVQPGD-----IIQVEGPNGAGKTSLLRILAGLARPDGGEVCWrgrntLRDRAAYQQDLLFIGHQPGIKAVLtpfe 93
Cdd:cd03237   12 EFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-----ELDTVSYKPQYIKADYEGTVRDLL---- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  94 nlqfYQAVRGAAEqQAIWRA--LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQG---VAEL 168
Cdd:cd03237   83 ----SSITKDFYT-HPYFKTeiAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmASKV 157
                        170
                 ....*....|....
gi 491074653 169 ISLFEQHAQRGGMV 182
Cdd:cd03237  158 IRRFAENNEKTAFV 171
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
20-187 4.65e-13

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 66.19  E-value: 4.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRnTLRDRAAYQqdllfIGHQPGIKavltpFENL--QF 97
Cdd:PRK13635  26 VSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM-VLSEETVWD-----VRRQVGMV-----FQNPdnQF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  98 YQA-----VRGAAEQQAIWR---------ALEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAIDK 162
Cdd:PRK13635  95 VGAtvqddVAFGLENIGVPReemvervdqALRQVGMEDFLNREPHRLSGGQKQRVAIAGV-LALQPdIIILDEATSMLDP 173
                        170       180
                 ....*....|....*....|....*.
gi 491074653 163 QGVAELISLFEQHAQRGGM-VLLTTH 187
Cdd:PRK13635 174 RGRREVLETVRQLKEQKGItVLSITH 199
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
13-188 5.60e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 66.20  E-value: 5.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcwrgrnTLRDR----AAYQQDLLFIGHQPGIkaV 88
Cdd:PRK13634  19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV------TIGERvitaGKKNKKLKPLRKKVGI--V 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  89 LTPFENLQFYQAVR----------GAAEQQAIWRALEQVGLVGY-EDL----PVaQLSAGQQRRVALARLwLSAAP-LWI 152
Cdd:PRK13634  91 FQFPEHQLFEETVEkdicfgpmnfGVSEEDAKQKAREMIELVGLpEELlarsPF-ELSGGQMRRVAIAGV-LAMEPeVLV 168
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 491074653 153 LDEPLTAIDKQGVAELISLFEQ-HAQRGGMVLLTTHQ 188
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKlHKEKGLTTVLVTHS 205
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-184 7.01e-13

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 66.58  E-value: 7.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRderiLFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR----NTLRD--RA--AY 72
Cdd:COG1129  256 VLEVEGLSVGG----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvriRSPRDaiRAgiAY 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  73 -----QQDLLFIGHqpGIK--AVLTPFENLQFYQAVRGAAEQQAIWRALEQVGL-VGYEDLPVAQLSAGQQRRVALARlW 144
Cdd:COG1129  332 vpedrKGEGLVLDL--SIRenITLASLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAK-W 408
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 491074653 145 LSAAP-LWILDEPlTaidkQGV-----AELISLFEQHAQRGGMVLL 184
Cdd:COG1129  409 LATDPkVLILDEP-T----RGIdvgakAEIYRLIRELAAEGKAVIV 449
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
2-191 7.13e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 65.53  E-value: 7.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLS-CVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT-------LRDRAA-- 71
Cdd:PRK13647   5 IEVEDLHfRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnaenekwVRSKVGlv 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  72 YQ--QDLLFIGhqpgikavlTPFENLQF---YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLS 146
Cdd:PRK13647  85 FQdpDDQVFSS---------TVWDDVAFgpvNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 491074653 147 AAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ-DLA 191
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDvDLA 201
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
1-197 7.35e-13

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 66.39  E-value: 7.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    1 MLEAKSLSC---VRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGlARPDG--GEVCWRGR--NTLRDRAAYQ 73
Cdd:TIGR02633 257 ILEARNLTCwdvINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKfeGNVFINGKpvDIRNPAQAIR 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   74 QDLLFI-------GHQP----GIKAVLTPFENLQFYQAVRGAAEQQAIWRALEQVGL-VGYEDLPVAQLSAGQQRRVALA 141
Cdd:TIGR02633 336 AGIAMVpedrkrhGIVPilgvGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLA 415
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 491074653  142 RLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ--DLAGVSQTV 197
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSElaEVLGLSDRV 473
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
34-191 7.42e-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: 66.96  E-value: 7.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    34 GPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVLTPFENLQFYQAVRGAAEQQA---I 110
Cdd:TIGR01257  963 GHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAqleM 1042
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   111 WRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:TIGR01257 1043 EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDE 1122

                   .
gi 491074653   191 A 191
Cdd:TIGR01257 1123 A 1123
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
16-188 8.83e-13

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: 64.41  E-value: 8.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  16 LFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR------------NTLRDraayqqDLLFiGHqp 83
Cdd:cd03250   20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiayvsqepwiqnGTIRE------NILF-GK-- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  84 gikavltPFENlQFYQAVRGAAeqqaiwrALEQvglvgyeDLPV-------------AQLSAGQQRRVALARLWLSAAPL 150
Cdd:cd03250   91 -------PFDE-ERYEKVIKAC-------ALEP-------DLEIlpdgdlteigekgINLSGGQKQRISLARAVYSDADI 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 491074653 151 WILDEPLTAIDKQgVAELIslFEQ----HAQRGGMVLLTTHQ 188
Cdd:cd03250  149 YLLDDPLSAVDAH-VGRHI--FENcilgLLLNNKTRILVTHQ 187
cbiO PRK13641
energy-coupling factor transporter ATPase;
13-205 1.04e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 65.24  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcwrgrntlrDRAAYQqdllfIGHQPGIKAVL--- 89
Cdd:PRK13641  19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI---------TIAGYH-----ITPETGNKNLKklr 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  90 -----------------TPFENLQFYQAVRGAAEQQAIWRALEQVGLVGY-EDL----PVaQLSAGQQRRVALARLWLSA 147
Cdd:PRK13641  85 kkvslvfqfpeaqlfenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLisksPF-ELSGGQMRRVAIAGVMAYE 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491074653 148 APLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHqDLAGVSQTVGKIRLAEH 205
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH-NMDDVAEYADDVLVLEH 220
cbiO PRK13649
energy-coupling factor transporter ATPase;
14-197 1.23e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 65.15  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  14 RILFsELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcwRGRNTLRDRAAYQQDLLFIGHQPGIkaVLTPFE 93
Cdd:PRK13649  21 RALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSV--RVDDTLITSTSKNKDIKQIRKKVGL--VFQFPE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  94 NLQFYQAVR----------GAAEQQAIWRALEQVGLVGY-EDL----PVaQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:PRK13649  96 SQLFEETVLkdvafgpqnfGVSQEEAEALAREKLALVGIsESLfeknPF-ELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 491074653 159 AIDKQGVAELISLFEQHAQRGGMVLLTTH--QDLAGVSQTV 197
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLHQSGMTIVLVTHlmDDVANYADFV 215
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
20-190 1.85e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 64.48  E-value: 1.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG-------HQPGIKAVltpF 92
Cdd:PRK13636  25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVGmvfqdpdNQLFSASV---Y 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  93 ENLQFYQAVRGAAE---QQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELI 169
Cdd:PRK13636 102 QDVSFGAVNLKLPEdevRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM 181
                        170       180
                 ....*....|....*....|.
gi 491074653 170 SLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK13636 182 KLLVEMQKELGLTIIIATHDI 202
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
2-156 2.78e-12

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 64.91  E-value: 2.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWrgrntlRDRAA---YQQDllf 78
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW------SENANigyYAQD--- 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  79 igHQPGIKAVLTPFENLQFY-------QAVRGAaeqqaiwraleqVG--LVGYEDL--PVAQLSAGQQRRVALARLWLSA 147
Cdd:PRK15064 391 --HAYDFENDLTLFDWMSQWrqegddeQAVRGT------------LGrlLFSQDDIkkSVKVLSGGEKGRMLFGKLMMQK 456

                 ....*....
gi 491074653 148 APLWILDEP 156
Cdd:PRK15064 457 PNVLVMDEP 465
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
12-161 7.23e-12

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


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 62.25  E-value: 7.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR-------NTLRDRAAY--QQDLLFIGhq 82
Cdd:cd03251   13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlASLRRQIGLvsQDVFLFND-- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  83 pgikavlTPFENLQFyqAVRGAAEQQAIwRALEQVGLV--------GYeDLPVAQ----LSAGQQRRVALARLWLSAAPL 150
Cdd:cd03251   91 -------TVAENIAY--GRPGATREEVE-EAARAANAHefimelpeGY-DTVIGErgvkLSGGQRQRIAIARALLKDPPI 159
                        170
                 ....*....|.
gi 491074653 151 WILDEPLTAID 161
Cdd:cd03251  160 LILDEATSALD 170
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
12-170 8.93e-12

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 62.37  E-value: 8.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLAR------PDGGEVCWRGRNTLR-DRAAYQQDLLFIGHQPG 84
Cdd:PRK14246  21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQiDAIKLRKEVGMVFQQPN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  85 IKAVLTPFENLQFYQAVRGAAEQQAIWRALEQ----VGLVG--YEDL--PVAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKEKREIKKIVEEclrkVGLWKevYDRLnsPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
                        170
                 ....*....|....*..
gi 491074653 157 LTAID---KQGVAELIS 170
Cdd:PRK14246 181 TSMIDivnSQAIEKLIT 197
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
11-188 9.12e-12

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: 61.49  E-value: 9.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGlaRPDG----GEVCWRGR---NTLRDRAAY--QQDLlfigH 81
Cdd:cd03232   17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAgvitGEILINGRpldKNFQRSTGYveQQDV----H 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  82 QPGikavLTPFENLQFYQAVRGaaeqqaiwraleqvglvgyedlpvaqLSAGQQRRVALArLWLSAAPLWI-LDEPLTAI 160
Cdd:cd03232   91 SPN----LTVREALRFSALLRG--------------------------LSVEQRKRLTIG-VELAAKPSILfLDEPTSGL 139
                        170       180
                 ....*....|....*....|....*...
gi 491074653 161 DKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:cd03232  140 DSQAAYNIVRFLKKLADSGQAILCTIHQ 167
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
1-184 1.07e-11

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


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 60.91  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCvrdeRILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRDRAAYQQDLLF 78
Cdd:cd03215    4 VLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvTRRSPRDAIRAGIAY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  79 IG---HQPGIKAVLTPFENLqfyqavrgaaeqqaiwrALEQvglvgyedlpvaQLSAGQQRRVALARlWLSAAP-LWILD 154
Cdd:cd03215   80 VPedrKREGLVLDLSVAENI-----------------ALSS------------LLSGGNQQKVVLAR-WLARDPrVLILD 129
                        170       180       190
                 ....*....|....*....|....*....|
gi 491074653 155 EPLTAIDKQGVAELISLFEQHAQRGGMVLL 184
Cdd:cd03215  130 EPTRGVDVGAKAEIYRLIRELADAGKAVLL 159
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
21-205 1.64e-11

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 62.64  E-value: 1.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLaRPDG---GEVCWRGR----NTLRDR-----AAYQQDL-----------L 77
Cdd:PRK13549  25 SLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEelqaSNIRDTeragiAIIHQELalvkelsvlenI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  78 FIGHQPgikavlTPFENLQFYQAVRGAAEqqaiwrALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:PRK13549 104 FLGNEI------TPGGIMDYDAMYLRAQK------LLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 491074653 158 TAIDKQGVAELISLFEQHAQRGGMVLLTTHQ--DLAGVSQTVGKIRLAEH 205
Cdd:PRK13549 172 ASLTESETAVLLDIIRDLKAHGIACIYISHKlnEVKAISDTICVIRDGRH 221
PLN03211 PLN03211
ABC transporter G-25; Provisional
13-195 1.72e-11

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 62.59  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDG--GEVCWRGRN----TLRDRAAYQQDLLFIGHqpgik 86
Cdd:PLN03211  80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKptkqILKRTGFVTQDDILYPH----- 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  87 avLTPFENLQFYQAVR--GAAEQQAIWRALEQV----GLVGYEDLPVAQ-----LSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:PLN03211 155 --LTVRETLVFCSLLRlpKSLTKQEKILVAESViselGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDE 232
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 491074653 156 PLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDLAGVSQ 195
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQ 272
hmuV PRK13547
heme ABC transporter ATP-binding protein;
1-210 2.21e-11

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 61.38  E-value: 2.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAG----LARPDG----GEVCWRGRNTLR---DR 69
Cdd:PRK13547   1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRGarvtGDVTLNGEPLAAidaPR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  70 AAYQQDLLFIGHQPGIKAVLTPFENLQFYQAVRGAAE-----QQAIWRALEQVGLVGYEDLPVAQLSAGQQRRV----AL 140
Cdd:PRK13547  81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGAlthrdGEIAWQALALAGATALVGRDVTTLSGGELARVqfarVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 141 ARLW-----LSAAPLWILDEPLTAIDkqgvaelisLFEQHAqrggmvLLTTHQDLA-----GVSQTVGKIRLAEHDAGSL 210
Cdd:PRK13547 161 AQLWpphdaAQPPRYLLLDEPTAALD---------LAHQHR------LLDTVRRLArdwnlGVLAIVHDPNLAARHADRI 225
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
10-185 4.12e-11

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 60.31  E-value: 4.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  10 VRDERILFSE------LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLAR--PDG---GEVCWRGRNTLR-DRAAYQQDLL 77
Cdd:PRK14247   6 IRDLKVSFGQvevldgVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKmDVIELRRRVQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  78 FIGHQPGIKAVLTPFEN----LQFYQAVRGAAE-QQAIWRALEQVGLvgYE------DLPVAQLSAGQQRRVALARLWLS 146
Cdd:PRK14247  86 MVFQIPNPIPNLSIFENvalgLKLNRLVKSKKElQERVRWALEKAQL--WDevkdrlDAPAGKLSGGQQQRLCIARALAF 163
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491074653 147 AAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLT 185
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVT 202
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
12-190 6.82e-11

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 60.15  E-value: 6.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWrgrntlRDRAAYQQDLLFIGHQPGIkaVLTP 91
Cdd:PRK13648  20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY------NNQAITDDNFEKLRKHIGI--VFQN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  92 FENlQFY--------------QAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:PRK13648  92 PDN-QFVgsivkydvafglenHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
                        170       180       190
                 ....*....|....*....|....*....|...
gi 491074653 158 TAIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDL 203
cbiO PRK13640
energy-coupling factor transporter ATPase;
13-190 7.14e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 60.20  E-value: 7.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPD--------------GGEVCWrgrnTLRDRAA--YQQ-D 75
Cdd:PRK13640  19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpnskitvdgitlTAKTVW----DIREKVGivFQNpD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  76 LLFIGHQPGiKAVLTPFENlqfyQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:PRK13640  95 NQFVGATVG-DDVAFGLEN----RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 491074653 156 PLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISITHDI 204
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
20-163 8.11e-11

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: 59.04  E-value: 8.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEV-------CWRGRNTLRDRAAY--QQDLLFIGhqpGIKAVLT 90
Cdd:cd03244   23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIlidgvdiSKIGLHDLRSRISIipQDPVLFSG---TIRSNLD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  91 PFenlqfyqavrGAAEQQAIWRALEQVGL-------VGYEDLPVA----QLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:cd03244  100 PF----------GEYSDEELWQALERVGLkefveslPGGLDTVVEeggeNLSVGQRQLLCLARALLRKSKILVLDEATAS 169

                 ....
gi 491074653 160 IDKQ 163
Cdd:cd03244  170 VDPE 173
cbiO PRK13650
energy-coupling factor transporter ATPase;
12-194 8.33e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 59.75  E-value: 8.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDraayqqDLLFIGHQPGIKavltp 91
Cdd:PRK13650  18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEE------NVWDIRHKIGMV----- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  92 FENL--QFYQAV-----------RGAAEQQAIWR---ALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:PRK13650  87 FQNPdnQFVGATveddvafglenKGIPHEEMKERvneALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDE 166
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491074653 156 PLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDLAGVS 194
Cdd:PRK13650 167 ATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA 205
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
18-187 8.80e-11

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 60.31  E-value: 8.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR-----NTlrdRAAYQQDLLFIGHQPGIKAVLTPF 92
Cdd:PRK11288  21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfaST---TAALAAGVAIIYQELHLVPEMTVA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  93 ENL---QFYQAVRGAAEQQAIWRALEQVGLVGYE---DLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVA 166
Cdd:PRK11288  98 ENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDidpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIE 177
                        170       180
                 ....*....|....*....|.
gi 491074653 167 ELISLFEQHAQRGGMVLLTTH 187
Cdd:PRK11288 178 QLFRVIRELRAEGRVILYVSH 198
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
21-188 9.23e-11

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 60.09  E-value: 9.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRD---RAA-------YQQDLLFighqpgikAV 88
Cdd:COG1135   25 SLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltALSErelRAArrkigmiFQHFNLL--------SS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  89 LTPFENLQF--YQAVRGAAEQQAiwRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAPLwIL--DEPLTAID 161
Cdd:COG1135   97 RTVAENVALplEIAGVPKAEIRK--RVaelLELVGLSDKADAYPSQLSGGQKQRVGIARA-LANNPK-VLlcDEATSALD 172
                        170       180
                 ....*....|....*....|....*...
gi 491074653 162 KQGVAELISLFEQ-HAQRGGMVLLTTHQ 188
Cdd:COG1135  173 PETTRSILDLLKDiNRELGLTIVLITHE 200
PLN03073 PLN03073
ABC transporter F family; Provisional
15-189 1.13e-10

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 60.26  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  15 ILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCwrgRNTLRDRAAYQQDllfigHQPGIKAVLTPFen 94
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---RSAKVRMAVFSQH-----HVDGLDLSSNPL-- 592
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  95 LQFYQAVRGAAEQQAiwRA-LEQVGLVGYEDL-PVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELIS-- 170
Cdd:PLN03073 593 LYMMRCFPGVPEQKL--RAhLGSFGVTGNLALqPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQgl 670
                        170       180
                 ....*....|....*....|
gi 491074653 171 -LFEqhaqrgGMVLLTTHQD 189
Cdd:PLN03073 671 vLFQ------GGVLMVSHDE 684
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
11-161 1.20e-10

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 58.64  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRDRAAYQQDLLFIGHQP------ 83
Cdd:cd03248   24 RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPiSQYEHKYLHSKVSLVGQEPvlfars 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  84 -------GIKAVltPFENLQFYQAVRGAAE-----QQAIWRALEQVGlvgyedlpvAQLSAGQQRRVALARLWLSAAPLW 151
Cdd:cd03248  104 lqdniayGLQSC--SFECVKEAAQKAHAHSfiselASGYDTEVGEKG---------SQLSGGQKQRVAIARALIRNPQVL 172
                        170
                 ....*....|
gi 491074653 152 ILDEPLTAID 161
Cdd:cd03248  173 ILDEATSALD 182
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
4-188 1.57e-10

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 59.80  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   4 AKSLSCVRderiLFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRDRAAYQ-------Q 74
Cdd:PRK09700  12 GKSFGPVH----ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInyNKLDHKLAAQlgigiiyQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  75 DL-----------LFIGHQPgIKAVLTPfeNLQFYQAVRGAAEQqaiwrALEQVGLVGYEDLPVAQLSAGQQRRVALARL 143
Cdd:PRK09700  88 ELsvideltvlenLYIGRHL-TKKVCGV--NIIDWREMRVRAAM-----MLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 491074653 144 WLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK 204
cbiO PRK13637
energy-coupling factor transporter ATPase;
13-202 1.59e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 58.91  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAayqqDLLFIGHQPGIkaVL--- 89
Cdd:PRK13637  19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKV----KLSDIRKKVGL--VFqyp 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  90 -------TPFENLQFYQAVRGAAEQQA---IWRALEQVGLV--GYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:PRK13637  93 eyqlfeeTIEKDIAFGPINLGLSEEEIenrVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491074653 158 TAIDKQGVAELISLFEQ-HAQRGGMVLLTTH--QDLAGVSQTV-----GKIRL 202
Cdd:PRK13637 173 AGLDPKGRDEILNKIKElHKEYNMTIILVSHsmEDVAKLADRIivmnkGKCEL 225
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
3-197 1.65e-10

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 59.58  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   3 EAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEV-CwrgrNTLRDRAAYQQdllfigh 81
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhC----GTKLEVAYFDQ------- 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  82 qpgIKAVLTP----FENLqfyqavrgAAEQQAIWRALEQVGLVGY-EDL---------PVAQLSAGQQRRVALARLWLSA 147
Cdd:PRK11147 390 ---HRAELDPektvMDNL--------AEGKQEVMVNGRPRHVLGYlQDFlfhpkramtPVKALSGGERNRLLLARLFLKP 458
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 491074653 148 APLWILDEPLTAIDKQGVAELISLFEQHAqrgGMVLLTTHqDLAGVSQTV 197
Cdd:PRK11147 459 SNLLILDEPTNDLDVETLELLEELLDSYQ---GTVLLVSH-DRQFVDNTV 504
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
20-205 1.75e-10

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: 59.45  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLaRPDG---GEVCWRGR----NTLRDRAA-----YQQDL----------- 76
Cdd:TIGR02633  20 IDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSplkaSNIRDTERagiviIHQELtlvpelsvaen 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   77 LFIGHQPGIKAVLTPfenlqfYQAVRGAAEQqaiwrALEQVGLVGYED-LPVAQLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:TIGR02633  99 IFLGNEITLPGGRMA------YNAMYLRAKN-----LLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 491074653  156 PLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ--DLAGVSQTVGKIRLAEH 205
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKAHGVACVYISHKlnEVKAVCDTICVIRDGQH 219
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
17-184 1.91e-10

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 59.29  E-value: 1.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  17 FSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN----TLRDRAAY---------QQDLLFIGHQP 83
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEinalSTAQRLARglvylpedrQSSGLYLDAPL 358
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  84 GIKAVLTPFENLQFYQavRGAAEQQAIWRALEQVGL-VGYEDLPVAQLSAGQQRRVALARLwLSAAP-LWILDEPLTAID 161
Cdd:PRK15439 359 AWNVCALTHNRRGFWI--KPARENAVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKC-LEASPqLLIVDEPTRGVD 435
                        170       180
                 ....*....|....*....|...
gi 491074653 162 KQGVAELISLFEQHAQRGGMVLL 184
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLF 458
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
20-195 3.17e-10

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: 58.93  E-value: 3.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKT----SLLRILAGLARPDGGEVCWRGRNTLR-DRAAYQ-----------QD-------L 76
Cdd:COG4172   29 VSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGlSERELRrirgnriamifQEpmtslnpL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  77 LFIGHQPGikavltpfENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVA---QLSAGQQRRV--ALArlwLSAAP-L 150
Cdd:COG4172  109 HTIGKQIA--------EVLRLHRGLSGAAARARALELLERVGIPDPERRLDAyphQLSGGQRQRVmiAMA---LANEPdL 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 491074653 151 WILDEPLTAIDkqgV---AELISLFEQHAQRGGM-VLLTTHqDLAGVSQ 195
Cdd:COG4172  178 LIADEPTTALD---VtvqAQILDLLKDLQRELGMaLLLITH-DLGVVRR 222
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
11-188 3.69e-10

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 58.58  E-value: 3.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRnTLRD----------RAAYQQDLLFIG 80
Cdd:TIGR00958 491 RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV-PLVQydhhylhrqvALVGQEPVLFSG 569
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   81 H-QPGIKAVLTPFENLQFYQAVRGAAEQQAIwRALEQ-----VGLVGyedlpvAQLSAGQQRRVALARLWLSAAPLWILD 154
Cdd:TIGR00958 570 SvRENIAYGLTDTPDEEIMAAAKAANAHDFI-MEFPNgydteVGEKG------SQLSGGQKQRIAIARALVRKPRVLILD 642
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 491074653  155 EPLTAIDkqgvAELISLFEQHAQRGGM-VLLTTHQ 188
Cdd:TIGR00958 643 EATSALD----AECEQLLQESRSRASRtVLLIAHR 673
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
12-161 4.43e-10

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 58.49  E-value: 4.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILfSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGlARPDGgevcwrgrntlrdraaYQQDLLFIGHQPG------- 84
Cdd:PRK10938 272 DRPIL-HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQG----------------YSNDLTLFGRRRGsgetiwd 333
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  85 IK------------------AVLTP-----FENLQFYQAVRGAAEQQAI-WraLEQVGLVGY-EDLPVAQLSAGQQRRVA 139
Cdd:PRK10938 334 IKkhigyvssslhldyrvstSVRNVilsgfFDSIGIYQAVSDRQQKLAQqW--LDILGIDKRtADAPFHSLSWGQQRLAL 411
                        170       180
                 ....*....|....*....|..
gi 491074653 140 LARLWLSAAPLWILDEPLTAID 161
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLD 433
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
19-190 5.63e-10

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 57.49  E-value: 5.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRDRAAYQQDLLFIGHQPGIKavLTPFEN--- 94
Cdd:PRK15112  31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlHFGDYSYRSQRIRMIFQDPSTS--LNPRQRisq 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  95 -----LQFYQAVRGAAEQQAIWRALEQVGL----VGYedLPVAqLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGV 165
Cdd:PRK15112 109 ildfpLRLNTDLEPEQREKQIIETLRQVGLlpdhASY--YPHM-LAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
                        170       180
                 ....*....|....*....|....*
gi 491074653 166 AELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHL 210
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
3-174 6.51e-10

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 57.75  E-value: 6.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   3 EAKSLSCVRDERILFS------ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRDRAAYQQ 74
Cdd:PRK15439   7 TAPPLLCARSISKQYSgvevlkGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPcaRLTPAKAHQL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  75 DLLFIGHQPGIKAVLTPFENLQFYQAvRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILD 154
Cdd:PRK15439  87 GIYLVPQEPLLFPNLSVKENILFGLP-KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
                        170       180
                 ....*....|....*....|
gi 491074653 155 EPLTAIDKqgvAELISLFEQ 174
Cdd:PRK15439 166 EPTASLTP---AETERLFSR 182
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
18-188 6.58e-10

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 57.50  E-value: 6.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN--TLRD---RAAYQQ--------DLLfighqpg 84
Cdd:PRK11153  22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltALSEkelRKARRQigmifqhfNLL------- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  85 ikAVLTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDL----PvAQLSAGQQRRVALARLwLSAAPLWIL-DEPLTA 159
Cdd:PRK11153  95 --SSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKadryP-AQLSGGQKQRVAIARA-LASNPKVLLcDEATSA 170
                        170       180       190
                 ....*....|....*....|....*....|
gi 491074653 160 IDKQGVAELISLFEQHAQRGGM-VLLTTHQ 188
Cdd:PRK11153 171 LDPATTRSILELLKDINRELGLtIVLITHE 200
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
20-169 1.14e-09

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: 57.12  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWR----------GRNTLRDRAAYQQDLLFigHQPGIKAVL 89
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkPGPDGRGRAKRYIGILH--QEYDLYPHR 380
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   90 TPFENLQfyQAVR-GAAEQQAIWRALEQVGLVGYED---------LPvAQLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:TIGR03269 381 TVLDNLT--EAIGlELPDELARMKAVITLKMVGFDEekaeeildkYP-DELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
                         170
                  ....*....|...
gi 491074653  160 ID---KQGVAELI 169
Cdd:TIGR03269 458 MDpitKVDVTHSI 470
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
11-187 1.90e-09

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 56.88  E-value: 1.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAY------QQDLLFiGHQpg 84
Cdd:TIGR00957  648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWiqndslRENILF-GKA-- 724
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    85 ikavLTPfenlQFYQAVRGAAeqqAIWRALE--------QVGLVGyedlpvAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:TIGR00957  725 ----LNE----KYYQQVLEAC---ALLPDLEilpsgdrtEIGEKG------VNLSGGQKQRVSLARAVYSNADIYLFDDP 787
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 491074653   157 LTAIDKQgVAELIslFEQHAQRGGMV-----LLTTH 187
Cdd:TIGR00957  788 LSAVDAH-VGKHI--FEHVIGPEGVLknktrILVTH 820
cbiO PRK13642
energy-coupling factor transporter ATPase;
20-190 1.91e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 55.87  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRG-RNTLRDRAAYQQDLLFIGHQPGIKAVLTPFEN-LQF 97
Cdd:PRK13642  26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGeLLTAENVWNLRRKIGMVFQNPDNQFVGATVEDdVAF 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  98 YQAVRGAAEQQAIWR---ALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQ 174
Cdd:PRK13642 106 GMENQGIPREEMIKRvdeALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE 185
                        170
                 ....*....|....*.
gi 491074653 175 HAQRGGMVLLTTHQDL 190
Cdd:PRK13642 186 IKEKYQLTVLSITHDL 201
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
1-188 2.07e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 56.01  E-value: 2.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDER-----ILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcWRGRNTLRDRAAYQQD 75
Cdd:PRK13631  21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI-QVGDIYIGDKKNNHEL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  76 LLFiGHQPGIKAvltpFENL--------QF--YQAVR--------------GAAEQQAIWRA---LEQVGLvGYEDLPVA 128
Cdd:PRK13631 100 ITN-PYSKKIKN----FKELrrrvsmvfQFpeYQLFKdtiekdimfgpvalGVKKSEAKKLAkfyLNKMGL-DDSYLERS 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491074653 129 --QLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:PRK13631 174 pfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT 235
PLN03232 PLN03232
ABC transporter C family member; Provisional
17-188 2.58e-09

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 56.52  E-value: 2.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   17 FSELSFSVQPGDIIQVEGPNGAGKTSLLRILAG-LARPDGGEVCWRGRntlrdrAAYQQDLLFIGHQPGIKAVL--TPFE 93
Cdd:PLN03232  633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS------VAYVPQVSWIFNATVRENILfgSDFE 706
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   94 NLQFYQAVRGAAEQQAI----WRALEQVGLVGyedlpvAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELI 169
Cdd:PLN03232  707 SERYWRAIDVTALQHDLdllpGRDLTEIGERG------VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
                         170
                  ....*....|....*....
gi 491074653  170 SLFEQHAQRGGMVLLTTHQ 188
Cdd:PLN03232  781 DSCMKDELKGKTRVLVTNQ 799
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
12-188 2.78e-09

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 56.27  E-value: 2.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGlaRPDGGEVCW-------RGRN-TLRDRAAY--QQDLlfigH 81
Cdd:TIGR00956  774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGgdrlvngRPLDsSFQRSIGYvqQQDL----H 847
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    82 QPgikaVLTPFENLQFYQAVRGAAE---------QQAIWRALEQ-------VGLVGyedlpvAQLSAGQQRRVALArLWL 145
Cdd:TIGR00956  848 LP----TSTVRESLRFSAYLRQPKSvsksekmeyVEEVIKLLEMesyadavVGVPG------EGLNVEQRKRLTIG-VEL 916
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 491074653   146 SAAP--LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:TIGR00956  917 VAKPklLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
15-185 3.36e-09

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 55.91  E-value: 3.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   15 ILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLarpdggevcWRGRNTLRDRAAyQQDLLFIGHQPGI------KAV 88
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL---------WPVYGGRLTKPA-KGKLFYVPQRPYMtlgtlrDQI 535
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   89 LTPFENLQFYQavRGAAEQQAIwRALEQVGL-------VGYE------DLpvaqLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:TIGR00954 536 IYPDSSEDMKR--RGLSDKDLE-QILDNVQLthilereGGWSavqdwmDV----LSGGEKQRIAMARLFYHKPQFAILDE 608
                         170       180       190
                  ....*....|....*....|....*....|..
gi 491074653  156 PLTAI--DKQGvaeliSLFeQHAQRGGMVLLT 185
Cdd:TIGR00954 609 CTSAVsvDVEG-----YMY-RLCREFGITLFS 634
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1-179 3.52e-09

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 55.71  E-value: 3.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSC---VRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGlARPdG---GEVCWRGR----NTLRDRA 70
Cdd:PRK13549 259 ILEVRNLTAwdpVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYP-GrweGEIFIDGKpvkiRNPQQAI 336
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  71 AYQqdllfIGHQP------GIKAVLTPFENL------QFYQAVR--GAAEQQAIWRALEQVGL-VGYEDLPVAQLSAGQQ 135
Cdd:PRK13549 337 AQG-----IAMVPedrkrdGIVPVMGVGKNItlaaldRFTGGSRidDAAELKTILESIQRLKVkTASPELAIARLSGGNQ 411
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 491074653 136 RRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRG 179
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQG 455
PLN03130 PLN03130
ABC transporter C family member; Provisional
13-161 4.06e-09

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 55.90  E-value: 4.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLR-ILAGLARPDGGEVcwrgrnTLRDRAAYQQDLLFIGHQPGIKAVL-- 89
Cdd:PLN03130  629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASV------VIRGTVAYVPQVSWIFNATVRDNILfg 702
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491074653   90 TPFENLQFYQAVRGAAEQQAI----WRALEQVGLVGyedlpvAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PLN03130  703 SPFDPERYERAIDVTALQHDLdllpGGDLTEIGERG------VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
1-191 4.20e-09

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 54.93  E-value: 4.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRDRAAY---QQDL 76
Cdd:PRK11701   6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgQLRDLYALseaERRR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  77 LF-----IGHQ-------PGIKAVLTPFENL-----QFYQAVRGAAEQqaiWraLEQV--GLVGYEDLPvAQLSAGQQRR 137
Cdd:PRK11701  86 LLrtewgFVHQhprdglrMQVSAGGNIGERLmavgaRHYGDIRATAGD---W--LERVeiDAARIDDLP-TTFSGGMQQR 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491074653 138 VALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHAQRGGM-VLLTTHqDLA 191
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLaVVIVTH-DLA 213
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
1-161 4.46e-09

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 54.70  E-value: 4.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLR-DRAAYQQDLLFI 79
Cdd:COG4604    1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAKRLAIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  80 GHQPGIKAVLTPFENLQF--YQAVRG---AAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILD 154
Cdd:COG4604   81 RQENHINSRLTVRELVAFgrFPYSKGrltAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160

                 ....*..
gi 491074653 155 EPLTAID 161
Cdd:COG4604  161 EPLNNLD 167
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
12-163 5.05e-09

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 54.41  E-value: 5.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRG-------RNTLRDRAAY--QQDLLFIGHQ 82
Cdd:cd03252   13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladPAWLRRQVGVvlQENVLFNRSI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  83 PGIKAVLTPFENLQFYQAVRGAAEQQAIWRALEQvglvGYEDLPVAQ---LSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:cd03252   93 RDNIALADPGMSMERVIEAAKLAGAHDFISELPE----GYDTIVGEQgagLSGGQRQRIAIARALIHNPRILIFDEATSA 168

                 ....
gi 491074653 160 IDKQ 163
Cdd:cd03252  169 LDYE 172
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
21-193 7.34e-09

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 54.33  E-value: 7.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLR----DRAAYQQDLLFIGHQPgiKAVLTP----- 91
Cdd:PRK15079  41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmkddEWRAVRSDIQMIFQDP--LASLNPrmtig 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  92 ---FENLQFYQAVRGAAEQQAIWRA-LEQVGLvgyedLPVA------QLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PRK15079 119 eiiAEPLRTYHPKLSRQEVKDRVKAmMLKVGL-----LPNLinryphEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
                        170       180       190
                 ....*....|....*....|....*....|..
gi 491074653 162 KQGVAELISLFEQHAQRGGMVLLTTHQDLAGV 193
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVV 225
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
12-161 7.42e-09

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 53.77  E-value: 7.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDraaYQQDLL--FIGHQPGiKAVL 89
Cdd:cd03253   12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD-IRE---VTLDSLrrAIGVVPQ-DTVL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  90 ---TPFENLQF------YQAVRGAAEQQAIWRALEQV-----GLVGYEDLpvaQLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:cd03253   87 fndTIGYNIRYgrpdatDEEVIEAAKAAQIHDKIMRFpdgydTIVGERGL---KLSGGEKQRVAIARAILKNPPILLLDE 163

                 ....*.
gi 491074653 156 PLTAID 161
Cdd:cd03253  164 ATSALD 169
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
12-161 9.38e-09

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 54.53  E-value: 9.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDG----GEVCWRGRNTLRDRAAY----QQDLLFIGhqp 83
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGeiqiDGVSWNSVTLQTWRKAFgvipQKVFIFSG--- 1306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    84 GIKAVLTPFENLQfyqavrgaaeQQAIWRALEQVGLVGY-EDLPVAQ----------LSAGQQRRVALARLWLSAAPLWI 152
Cdd:TIGR01271 1307 TFRKNLDPYEQWS----------DEEIWKVAEEVGLKSViEQFPDKLdfvlvdggyvLSNGHKQLMCLARSILSKAKILL 1376

                   ....*....
gi 491074653   153 LDEPLTAID 161
Cdd:TIGR01271 1377 LDEPSAHLD 1385
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
20-161 9.58e-09

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 54.58  E-value: 9.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRIL-------AGLARPDGGEVCWRGRNTLRDRAA--YQQDLLF---IGhqpgika 87
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILIDGTDIRTVTRASLRRNIAvvFQDAGLFnrsIE------- 426
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  88 vltpfENLQ----------FYQAVRGAAEQQAIWRALE----QVGLVGyedlpvAQLSAGQQRRVALARLWLSAAPLWIL 153
Cdd:PRK13657 427 -----DNIRvgrpdatdeeMRAAAERAQAHDFIERKPDgydtVVGERG------RQLSGGERQRLAIARALLKDPPILIL 495

                 ....*...
gi 491074653 154 DEPLTAID 161
Cdd:PRK13657 496 DEATSALD 503
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
13-187 1.09e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 53.55  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  13 ERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT--------LRDRAAyqqdLLFigHQPG 84
Cdd:PRK13633  22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdeenlwdIRNKAG----MVF--QNPD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  85 IKAVLTPFE-NLQFYQAVRGAAEQQAIWR---ALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAI 160
Cdd:PRK13633  96 NQIVATIVEeDVAFGPENLGIPPEEIRERvdeSLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
                        170       180
                 ....*....|....*....|....*...
gi 491074653 161 DKQGVAELISLFEQHAQRGGM-VLLTTH 187
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGItIILITH 203
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
11-175 1.69e-08

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 53.57  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR-------NTLRDRAAY-QQDllfighq 82
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsslshSVLRQGVAMvQQD------- 423
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  83 PGIKAVlTPFENLQFYqavRGAAEQQaIWRALEQVGLVGY-EDLPVA----------QLSAGQQRRVALARLWLSAAPLW 151
Cdd:PRK10790 424 PVVLAD-TFLANVTLG---RDISEEQ-VWQALETVQLAELaRSLPDGlytplgeqgnNLSVGQKQLLALARVLVQTPQIL 498
                        170       180
                 ....*....|....*....|....*..
gi 491074653 152 ILDEPLTAID---KQGVAELISLFEQH 175
Cdd:PRK10790 499 ILDEATANIDsgtEQAIQQALAAVREH 525
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
11-200 2.54e-08

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: 51.88  E-value: 2.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDG---GEVCWRGRNTLRDRAAYQQDLLFIG----HQP 83
Cdd:cd03233   17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEIIYVSeedvHFP 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  84 gikaVLTPFENLQF------YQAVRGaaeqqaiwraleqvglvgyedlpvaqLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:cd03233   97 ----TLTVRETLDFalrckgNEFVRG--------------------------ISGGERKRVSIAEALVSRASVLCWDNST 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 491074653 158 TAIDKQGVAELISLFEQHAQRGGMVLltthqdLAGVSQTVGKI 200
Cdd:cd03233  147 RGLDSSTALEILKCIRTMADVLKTTT------FVSLYQASDEI 183
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
34-161 2.64e-08

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 52.95  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  34 GPNGAGKTSLLRILAGLARPDGGEVCWRGRnTLRDRaayQQDLLFIGHQPGIKAV-----LTPF----ENLQFYQAVRGA 104
Cdd:PRK11144  31 GRSGAGKTSLINAISGLTRPQKGRIVLNGR-VLFDA---EKGICLPPEKRRIGYVfqdarLFPHykvrGNLRYGMAKSMV 106
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491074653 105 AEQQAIwraleqVGLVGYEDL----PvAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PRK11144 107 AQFDKI------VALLGIEPLldryP-GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
22-161 2.76e-08

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 53.03  E-value: 2.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  22 FSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRG------------RN---TLRDRAA----YQQDLLFIGHQ 82
Cdd:PRK11147  24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdppRNvegTVYDFVAegieEQAEYLKRYHD 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  83 PGIKAVLTPFE-NLQFYQAVRGAAEQQAIWR-------ALEQVGLVGyeDLPVAQLSAGQQRRVALARLWLSAAPLWILD 154
Cdd:PRK11147 104 ISHLVETDPSEkNLNELAKLQEQLDHHNLWQlenrineVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLD 181

                 ....*..
gi 491074653 155 EPLTAID 161
Cdd:PRK11147 182 EPTNHLD 188
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
2-190 2.91e-08

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 52.30  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcWRGRNTLRDRAAYQqdllfIGH 81
Cdd:PRK10253   8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYASKE-----VAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  82 QPGIKA--VLTPFENLQFYQAVRGAAEQQ------------AIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSA 147
Cdd:PRK10253  82 RIGLLAqnATTPGDITVQELVARGRYPHQplftrwrkedeeAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 491074653 148 APLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDL 204
cbiO PRK13644
energy-coupling factor transporter ATPase;
1-202 4.45e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 51.91  E-value: 4.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLS-CVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLrDRAAYQQDLLFI 79
Cdd:PRK13644   1 MIRLENVSySYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG-DFSKLQGIRKLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  80 G---HQPGIKAV-LTPFENLQF---YQAVRGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWI 152
Cdd:PRK13644  80 GivfQNPETQFVgRTVEEDLAFgpeNLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491074653 153 LDEPLTAID-KQGVAELISLFEQHaQRGGMVLLTTH--QDLAGVSQTV----GKIRL 202
Cdd:PRK13644 160 FDEVTSMLDpDSGIAVLERIKKLH-EKGKTIVYITHnlEELHDADRIIvmdrGKIVL 215
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
12-190 5.42e-08

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 52.01  E-value: 5.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILFSELSFSVQPGDIIQVEGPNGAGKTS----LLRILAGlarpdGGEVCWRGR--NTLRDRAayqqdLLFIGHQpgI 85
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQplHNLNRRQ-----LLPVRHR--I 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  86 KAV-------LTP--------FENLQFYQAVRGAAEQ-QAIWRALEQVGL--VGYEDLPvAQLSAGQQRRVALARLWLSA 147
Cdd:PRK15134 365 QVVfqdpnssLNPrlnvlqiiEEGLRVHQPTLSAAQReQQVIAVMEEVGLdpETRHRYP-AEFSGGQRQRIAIARALILK 443
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 491074653 148 APLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDL 486
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
2-187 6.22e-08

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: 50.99  E-value: 6.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLS-CVRDERILfSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLA--RPDGGEVCWRGRNTL------RDRAAy 72
Cdd:cd03217    1 LEIKDLHvSVGGKEIL-KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITdlppeeRARLG- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  73 qqdlLFIGHQ-----PGIKavltpfeNLQFYQAVrgaaeqqaiwraleQVGlvgyedlpvaqLSAGQQRRVALARLWLSA 147
Cdd:cd03217   79 ----IFLAFQyppeiPGVK-------NADFLRYV--------------NEG-----------FSGGEKKRNEILQLLLLE 122
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 491074653 148 APLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:cd03217  123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITH 162
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
19-161 6.76e-08

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: 51.40  E-value: 6.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQdllfighqPGikavlTPFENLQF- 97
Cdd:cd03291   55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIM--------PG-----TIKENIIFg 121
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491074653  98 -------YQAVRGAAE-QQAIWRALEQvglvgyEDLPVAQ----LSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:cd03291  122 vsydeyrYKSVVKACQlEEDITKFPEK------DNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
21-161 7.40e-08

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 51.57  E-value: 7.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRD-----RAAYQQDLLFIGHQPGIKAVLTPFENL 95
Cdd:PRK10070  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaelREVRRKKIAMVFQSFALMPHMTVLDNT 127
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074653  96 QFYQAVRGAA---EQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PRK10070 128 AFGMELAGINaeeRREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
23-191 8.65e-08

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: 50.83  E-value: 8.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  23 SVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVC----WRG-----RNT-LRDraaYQQDLLfighQPGIKAVLTPF 92
Cdd:cd03236   22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdWDEildefRGSeLQN---YFTKLL----EGDVKVIVKPQ 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  93 ENLQFYQAVRGAA--------EQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID-KQ 163
Cdd:cd03236   95 YVDLIPKAVKGKVgellkkkdERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDiKQ 174
                        170       180       190
                 ....*....|....*....|....*....|
gi 491074653 164 --GVAELIslfEQHAQRGGMVLLTTHqDLA 191
Cdd:cd03236  175 rlNAARLI---RELAEDDNYVLVVEH-DLA 200
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
24-191 1.28e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 50.96  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  24 VQPGDIIQVEGPNGAGKTSLLRILAGLARPD----GGEVCW-------RGrNTLRDraaYQQDLlfigHQPGIKAVLTPF 92
Cdd:PRK13409  96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNlgdyEEEPSWdevlkrfRG-TELQN---YFKKL----YNGEIKVVHKPQ 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  93 ENLQFYQAVRG-------AAEQQAIWRAL-EQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID-KQ 163
Cdd:PRK13409 168 YVDLIPKVFKGkvrellkKVDERGKLDEVvERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDiRQ 247
                        170       180       190
                 ....*....|....*....|....*....|
gi 491074653 164 --GVAELIslfeQHAQRGGMVLLTTHqDLA 191
Cdd:PRK13409 248 rlNVARLI----RELAEGKYVLVVEH-DLA 272
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
17-156 1.30e-07

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 50.94  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  17 FSELSFSVQPGDI-----IQVEGPNGAGKTSLLRILAGLARPDGGEVcwrgrnTLRDRAAYQ------------QDLLFi 79
Cdd:COG1245  351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLKISYKpqyispdydgtvEEFLR- 423
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491074653  80 ghqpgiKAVLTPFENLQFYQAVrgaAEQQAIWRALEQvglvgyedlPVAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:COG1245  424 ------SANTDDFGSSYYKTEI---IKPLGLEKLLDK---------NVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
21-174 1.80e-07

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 50.77  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT--------LRDRAAY-----QQDLLFIGHQPGIKA 87
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrspqdgLANGIVYisedrKRDGLVLGMSVKENM 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  88 VLTPFENL-QFYQAVRGAAEQQAIWRALEQVGL-VGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID---K 162
Cdd:PRK10762 352 SLTALRYFsRAGGSLKHADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDvgaK 431
                        170
                 ....*....|..
gi 491074653 163 QGVAELISLFEQ 174
Cdd:PRK10762 432 KEIYQLINQFKA 443
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
20-193 2.11e-07

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 50.62  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRDRA--AYQQDLLFIGHQPgiKAVLTP---- 91
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQriDTLSPGKlqALRRDIQFIFQDP--YASLDPrqtv 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  92 ----FENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVA-QLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVA 166
Cdd:PRK10261 421 gdsiMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPhEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
                        170       180
                 ....*....|....*....|....*..
gi 491074653 167 ELISLFEQHAQRGGMVLLTTHQDLAGV 193
Cdd:PRK10261 501 QIINLLLDLQRDFGIAYLFISHDMAVV 527
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
1-161 2.38e-07

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 49.77  E-value: 2.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRIL--AGLARPD---GGEVCWRGRNTLRDRAAYQQD 75
Cdd:PRK14239   5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTDTVDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  76 LLFIG---HQPGiKAVLTPFENLQFYQAVRGAAEQQAIWRALEQvGLVG----------YEDLPVAqLSAGQQRRVALAR 142
Cdd:PRK14239  85 RKEIGmvfQQPN-PFPMSIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGasiwdevkdrLHDSALG-LSGGQQQRVCIAR 161
                        170
                 ....*....|....*....
gi 491074653 143 LWLSAAPLWILDEPLTAID 161
Cdd:PRK14239 162 VLATSPKIILLDEPTSALD 180
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
11-163 2.67e-07

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 49.46  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  11 RDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT-------LRDRAAY--QQDLLFIGh 81
Cdd:cd03249   13 RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrdlnlrwLRSQIGLvsQEPVLFDG- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  82 qpgikavlTPFENLQFYQAVRGAAEQQAIWRALE--------------QVGLVGyedlpvAQLSAGQQRRVALARLWLSA 147
Cdd:cd03249   92 --------TIAENIRYGKPDATDEEVEEAAKKANihdfimslpdgydtLVGERG------SQLSGGQKQRIAIARALLRN 157
                        170
                 ....*....|....*.
gi 491074653 148 APLWILDEPLTAIDKQ 163
Cdd:cd03249  158 PKILLLDEATSALDAE 173
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
24-183 2.73e-07

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: 48.72  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  24 VQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWrgrntlrdraayqqdllfighqPGIKAVLTPfenlqfyqavrg 103
Cdd:cd03222   22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW----------------------DGITPVYKP------------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 104 aaeqQAIwraleqvglvgyedlpvaQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQ---GVAELISLFEQHAQRGG 180
Cdd:cd03222   68 ----QYI------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlNAARAIRRLSEEGKKTA 125

                 ...
gi 491074653 181 MVL 183
Cdd:cd03222  126 LVV 128
ycf16 CHL00131
sulfate ABC transporter protein; Validated
1-190 3.28e-07

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 49.26  E-value: 3.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSL-SCVRDERILfSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGlaRPD----GGEVCWRGRNTL----RDRA- 70
Cdd:CHL00131   7 ILEIKNLhASVNENEIL-KGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILdlepEERAh 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  71 -----AYQ----------QDLLFIGHQPGIKAV-LTPFENLQFYQAVRgaaeqqaiwralEQVGLVGYEDLPVAQ----- 129
Cdd:CHL00131  84 lgiflAFQypieipgvsnADFLRLAYNSKRKFQgLPELDPLEFLEIIN------------EKLKLVGMDPSFLSRnvneg 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491074653 130 LSAGQQRRVALARLWLSAAPLWILDEPLTAID---KQGVAELISLFEQHAQrgGMVLLTTHQDL 190
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLDidaLKIIAEGINKLMTSEN--SIILITHYQRL 213
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
19-161 3.73e-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: 49.91  E-value: 3.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGrntlrdRAAYQQDLLFIghQPGikavlTPFENLQF- 97
Cdd:TIGR01271  444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------RISFSPQTSWI--MPG-----TIKDNIIFg 510
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491074653    98 -------YQAVRGAAEQQaiwralEQVGLVGYEDLPV-----AQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:TIGR01271  511 lsydeyrYTSVIKACQLE------EDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
14-190 4.28e-07

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 49.02  E-value: 4.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  14 RILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVC--------WRGRNTLRDRAAYQQ----------- 74
Cdd:PRK10575  24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILldaqplesWSSKAFARKVAYLPQqlpaaegmtvr 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  75 DLLFIGHQPGIKAvLTPFenlqfyqavrGAAEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILD 154
Cdd:PRK10575 104 ELVAIGRYPWHGA-LGRF----------GAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 491074653 155 EPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDI 208
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
9-161 4.48e-07

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 49.56  E-value: 4.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653     9 CVR---DERILFSELSFSVQPGDIIQVEGPNGAGKTS----LLRIL---AGLARPDGGEVCWRGRNTLRDRAAY--QQDL 76
Cdd:TIGR00957 1291 CLRyreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINesaEGEIIIDGLNIAKIGLHDLRFKITIipQDPV 1370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    77 LFIGhqpGIKAVLTPFenlqfyqavrGAAEQQAIWRALEQVGLVGY-EDLPVA----------QLSAGQQRRVALARLWL 145
Cdd:TIGR00957 1371 LFSG---SLRMNLDPF----------SQYSDEEVWWALELAHLKTFvSALPDKldhecaeggeNLSVGQRQLVCLARALL 1437
                          170
                   ....*....|....*.
gi 491074653   146 SAAPLWILDEPLTAID 161
Cdd:TIGR00957 1438 RKTKILVLDEATAAVD 1453
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
13-195 4.54e-07

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 49.32  E-value: 4.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  13 ERILFSELSFSVQPGDIIQVEGPNGAGKT----SLLRIL--------AGLARPDGGEVCWRGRNTLRDRAAYQQDLLFig 80
Cdd:PRK15134  21 VRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypSGDIRFHGESLLHASEQTLRGVRGNKIAMIF-- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 HQPGIKavLTPFENL--QFYQ------AVRGAAEQQAIWRALEQVGLVG----YEDLPvAQLSAGQQRRVALARLWLSAA 148
Cdd:PRK15134  99 QEPMVS--LNPLHTLekQLYEvlslhrGMRREAARGEILNCLDRVGIRQaakrLTDYP-HQLSGGERQRVMIAMALLTRP 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491074653 149 PLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDLAGVSQ 195
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRK 222
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
20-161 4.73e-07

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 49.07  E-value: 4.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTL--RDRaayqqdllfighqpGIKAV------- 88
Cdd:PRK11650  23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvNELepADR--------------DIAMVfqnyaly 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074653  89 --LTPFENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDL----PvAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PRK11650  89 phMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLldrkP-RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
11-155 5.95e-07

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 49.20  E-value: 5.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  11 RDERILFSELSFSVQP-------GDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRDRAAYQQdlLFighq 82
Cdd:PRK10522 326 RNVTFAYQDNGFSVGPinltikrGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPvTAEQPEDYRK--LF---- 399
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  83 pgiKAVLT---PFENLQFYQAVRGAAEQQAIWraLEQVGL---VGYEDLPVA--QLSAGQQRRVALARLWLSAAPLWILD 154
Cdd:PRK10522 400 ---SAVFTdfhLFDQLLGPEGKPANPALVEKW--LERLKMahkLELEDGRISnlKLSKGQKKRLALLLALAEERDILLLD 474

                 .
gi 491074653 155 E 155
Cdd:PRK10522 475 E 475
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
20-187 6.09e-07

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 48.96  E-value: 6.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLlRILAGLARPDGGEVCWRGRNTLRDRAAYQQDllfIG-HQP---GIKAVLTPFENL 95
Cdd:NF000106  32 VDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRT---IG*HRPvr*GRRESFSGRENL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  96 QFYQAVRGAAEQQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLF 172
Cdd:NF000106 108 YMIGR*LDLSRKDARARAdelLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV 187
                        170
                 ....*....|....*
gi 491074653 173 EQHAQRGGMVLLTTH 187
Cdd:NF000106 188 RSMVRDGATVLLTTQ 202
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
34-161 6.63e-07

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 48.87  E-value: 6.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  34 GPNGAGKTSLLRILAGLARPDGGEvcwrgrntlrdraayqqdlLFIGHQ------P---GIKAV---------LTPFENL 95
Cdd:PRK11000  36 GPSGCGKSTLLRMIAGLEDITSGD-------------------LFIGEKrmndvpPaerGVGMVfqsyalyphLSVAENM 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491074653  96 QFYQAVRGAAEQQaIWRALEQVGlvgyEDLPVAQL--------SAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PRK11000  97 SFGLKLAGAKKEE-INQRVNQVA----EVLQLAHLldrkpkalSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-184 7.37e-07

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 48.34  E-value: 7.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAA--YQQDLLF 78
Cdd:PRK11614   5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  79 IGHQPGIKAVLTPFENLqfyqAVRG-AAEQQAIWRALEQVglvgYEDLP---------VAQLSAGQQRRVALARLWLSAA 148
Cdd:PRK11614  85 VPEGRRVFSRMTVEENL----AMGGfFAERDQFQERIKWV----YELFPrlherriqrAGTMSGGEQQMLAIGRALMSQP 156
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 491074653 149 PLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLL 184
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFL 192
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
15-188 9.11e-07

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: 46.97  E-value: 9.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  15 ILFSELSFSVqpgdiiqVEGPNGAGKTSLLRilaglarpdggEVCWrgrntlrdraayqqdlLFIGHQPgikavltpfen 94
Cdd:cd03227   16 VTFGEGSLTI-------ITGPNGSGKSTILD-----------AIGL----------------ALGGAQS----------- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  95 lqfyQAVRGAAEQQAIWRALEQVGLVgyedLPVAQLSAGQQRRVALA---RLWLSA-APLWILDEPLTAIDKQGVAELIS 170
Cdd:cd03227   51 ----ATRRRSGVKAGCIVAAVSAELI----FTRLQLSGGEKELSALAlilALASLKpRPLYILDEIDRGLDPRDGQALAE 122
                        170
                 ....*....|....*...
gi 491074653 171 LFEQHAQRGGMVLLTTHQ 188
Cdd:cd03227  123 AILEHLVKGAQVIVITHL 140
cbiO PRK13645
energy-coupling factor transporter ATPase;
21-187 1.30e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 47.70  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCW------RGRNTLRDRAAYQQDLLFIGHQPGIKAVLTPFE- 93
Cdd:PRK13645  31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKKIKEVKRLRKEIGLVFQFPEYQLFQETIEk 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  94 NLQFYQAVRGAAEQQAIWRALEQVGLVG----YEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELI 169
Cdd:PRK13645 111 DIAFGPVNLGENKQEAYKKVPELLKLVQlpedYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFI 190
                        170
                 ....*....|....*....
gi 491074653 170 SLFEQ-HAQRGGMVLLTTH 187
Cdd:PRK13645 191 NLFERlNKEYKKRIIMVTH 209
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
21-179 1.38e-06

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 48.09  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAVLTPFEN------ 94
Cdd:PRK10938  23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNNTDMLSPGEDdtgrtt 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  95 ---LQFYQAVRGAAEQQAiwralEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISL 171
Cdd:PRK10938 103 aeiIQDEVKDPARCEQLA-----QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAEL 177

                 ....*...
gi 491074653 172 FEQHAQRG 179
Cdd:PRK10938 178 LASLHQSG 185
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
17-156 2.74e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 47.11  E-value: 2.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  17 FSELSFSVQPGDI-----IQVEGPNGAGKTSLLRILAGLARPDGGEVCWrgrnTLrdRAAYQ------------QDLLfi 79
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP----EL--KISYKpqyikpdydgtvEDLL-- 421
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491074653  80 ghqpgiKAVLTPFENLQFYQAVrgaAEQQAIWRALEQvglvgyedlPVAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:PRK13409 422 ------RSITDDLGSSYYKSEI---IKPLQLERLLDK---------NVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
18-182 3.54e-06

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 46.92  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRDRAAYQQDLLFIGHQP-GIKAVLTPFENL 95
Cdd:PRK10762  21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEvTFNGPKSSQEAGIGIIHQElNLIPQLTIAENI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  96 ----QFYQAVrGAAEQQAIWRA----LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKqgvAE 167
Cdd:PRK10762 101 flgrEFVNRF-GRIDWKKMYAEadklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTD---TE 176
                        170
                 ....*....|....*....
gi 491074653 168 LISLF----EQHAQRGGMV 182
Cdd:PRK10762 177 TESLFrvirELKSQGRGIV 195
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
21-172 3.64e-06

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 46.50  E-value: 3.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLlfighQPGIKAVL-TPFENLQFYQ 99
Cdd:PRK11308  35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLL-----RQKIQIVFqNPYGSLNPRK 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 100 AVR-------------GAAEQQAiwRALEQVGLVG-----YEDLPvAQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PRK11308 110 KVGqileepllintslSAAERRE--KALAMMAKVGlrpehYDRYP-HMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
                        170
                 ....*....|.
gi 491074653 162 KQGVAELISLF 172
Cdd:PRK11308 187 VSVQAQVLNLM 197
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
18-163 3.80e-06

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 46.63  E-value: 3.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR-------NTLRDRAAY--QQDLLFIGHQPGIKAV 88
Cdd:PRK10789 332 ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpltklqlDSWRSRLAVvsQTPFLFSDTVANNIAL 411
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  89 LTP-FENLQFYQAVRGAAEQQAIWRALE----QVGLVGyedlpvAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQ 163
Cdd:PRK10789 412 GRPdATQQEIEHVARLASVHDDILRLPQgydtEVGERG------VMLSGGQKQRISIARALLLNAEILILDDALSAVDGR 485
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
25-191 4.27e-06

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: 46.70  E-value: 4.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  25 QPGDIIQVEGPNGAGKTSLLRILAGLARPDGG----EVCW-----RGRNT-LRDraaYQQDLLfighQPGIKAVLTPfen 94
Cdd:COG1245   97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGdydeEPSWdevlkRFRGTeLQD---YFKKLA----NGEIKVAHKP--- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  95 lqfyQAV--------------------RGAAEQQAiwralEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILD 154
Cdd:COG1245  167 ----QYVdlipkvfkgtvrellekvdeRGKLDELA-----EKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 491074653 155 EPLTAID-KQ--GVAELISLFeqhAQRGGMVLLTTHqDLA 191
Cdd:COG1245  238 EPSSYLDiYQrlNVARLIREL---AEEGKYVLVVEH-DLA 273
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
20-168 5.24e-06

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 45.48  E-value: 5.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNT-------LRDRAAY--QQDLLFIGhqpGIKAVLT 90
Cdd:cd03369   27 VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIstipledLRSSLTIipQDPTLFSG---TIRSNLD 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  91 PFE---NLQFYQAVRgaaeqqaiwraLEQVGLvgyedlpvaQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAE 167
Cdd:cd03369  104 PFDeysDEEIYGALR-----------VSEGGL---------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163

                 .
gi 491074653 168 L 168
Cdd:cd03369  164 I 164
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
34-187 7.07e-06

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 44.91  E-value: 7.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  34 GPNGAGKTSLLR----ILAGLARPDGgevcwRGRNTLRDRAA-----YQQDLLFIgHQPGIKavltpfenlqfYQAVRGA 104
Cdd:cd03240   29 GQNGAGKTTIIEalkyALTGELPPNS-----KGGAHDPKLIRegevrAQVKLAFE-NANGKK-----------YTITRSL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 105 AeqqaiwrALEQVGLVGYED------LPVAQLSAGQQR------RVALARLWLSAAPLWILDEPLTAIDKQGVAE-LISL 171
Cdd:cd03240   92 A-------ILENVIFCHQGEsnwpllDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEsLAEI 164
                        170
                 ....*....|....*..
gi 491074653 172 FE-QHAQRGGMVLLTTH 187
Cdd:cd03240  165 IEeRKSQKNFQLIVITH 181
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
21-193 7.35e-06

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 45.67  E-value: 7.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  21 SFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN-TLRD-RAAYQQDLLFIGH---QPGIKAVLTPFEN- 94
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPiDIRSpRDAIRAGIMLCPEdrkAEGIIPVHSVADNi 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  95 --------LQFYQAVRGAAEQQaiwRALEQVGLVGYE----DLPVAQLSAGQQRRVALARlWLSAA-PLWILDEPLTAID 161
Cdd:PRK11288 353 nisarrhhLRAGCLINNRWEAE---NADRFIRSLNIKtpsrEQLIMNLSGGNQQKAILGR-WLSEDmKVILLDEPTRGID 428
                        170       180       190
                 ....*....|....*....|....*....|..
gi 491074653 162 KQGVAELISLFEQHAQRGGMVLLTThQDLAGV 193
Cdd:PRK11288 429 VGAKHEIYNVIYELAAQGVAVLFVS-SDLPEV 459
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
20-200 7.86e-06

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 45.50  E-value: 7.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKT-SLLRILaglarpdgGEVCWRGRNTLRDRAAYQQDLLFIGHQPGIKAV---------- 88
Cdd:PRK11022  26 ISYSVKQGEVVGIVGESGSGKSvSSLAIM--------GLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVgaevamifqd 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  89 ----LTP-----FENLQFYQAVRGAAEQQAIWRALEQVGLVGYED----LPV--AQLSAGQQRRVALARLWLSAAPLWIL 153
Cdd:PRK11022  98 pmtsLNPcytvgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasrLDVypHQLSGGMSQRVMIAMAIACRPKLLIA 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491074653 154 DEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDLAGVSQTVGKI 200
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKI 224
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
12-187 9.55e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 44.98  E-value: 9.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  12 DERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGrNTLRdraayQQDLLFIGHQPGIKavltp 91
Cdd:PRK13632  20 SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG-ITIS-----KENLKEIRKKIGII----- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  92 FENL--QFYqavrGAAEQQAIWRALE------------------QVGLVGYEDLPVAQLSAGQQRRVALARLwLSAAP-L 150
Cdd:PRK13632  89 FQNPdnQFI----GATVEDDIAFGLEnkkvppkkmkdiiddlakKVGMEDYLDKEPQNLSGGQKQRVAIASV-LALNPeI 163
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 491074653 151 WILDEPLTAIDKQGVAELISLFEQ-HAQRGGMVLLTTH 187
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDlRKTRKKTLISITH 201
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
18-187 1.09e-05

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 45.27  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLrdraayqqdllfIGHQPGIKAVLTPFENLQF 97
Cdd:PRK13545  41 NNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL------------IAISSGLNGQLTGIENIEL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  98 YQAVRGAAEQQA---IWRALEQVGLVGYEDLPVAQLSAGQQRRVALArLWLSAAP-LWILDEPLTAIDKQGVAELISLFE 173
Cdd:PRK13545 109 KGLMMGLTKEKIkeiIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFA-ISVHINPdILVIDEALSVGDQTFTKKCLDKMN 187
                        170
                 ....*....|....
gi 491074653 174 QHAQRGGMVLLTTH 187
Cdd:PRK13545 188 EFKEQGKTIFFISH 201
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
17-187 1.10e-05

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 44.99  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  17 FSELSFSVQPGDIIQVeGPNGAGKTSLLRILAGLARPDGG---------------------EVCWRG--RNTLRDRAAYQ 73
Cdd:COG3593   14 IKDLSIELSDDLTVLV-GENNSGKSSILEALRLLLGPSSSrkfdeedfylgddpdlpeieiELTFGSllSRLLRLLLKEE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  74 QDLLFIGH----QPGIKAVLTPFENL---QFYQAVRGA-------AEQQAIWRALEQVGLVGYEDLPVAQLSAGQQRRVA 139
Cdd:COG3593   93 DKEELEEAleelNEELKEALKALNELlseYLKELLDGLdlelelsLDELEDLLKSLSLRIEDGKELPLDRLGSGFQRLIL 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491074653 140 LA-RLWLSAA------PLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:COG3593  173 LAlLSALAELkrapanPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
20-188 1.23e-05

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: 44.85  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDG----GEVCWRGRNTLRDRAAY----QQDLLFIGhqpgikavlTP 91
Cdd:cd03289   23 ISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGdiqiDGVSWNSVPLQKWRKAFgvipQKVFIFSG---------TF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  92 FENLQFYqavrGAAEQQAIWRALEQVGLV-------GYEDLPVAQ----LSAGQQRRVALARLWLSAAPLWILDEPLTAI 160
Cdd:cd03289   94 RKNLDPY----GKWSDEEIWKVAEEVGLKsvieqfpGQLDFVLVDggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
                        170       180
                 ....*....|....*....|....*...
gi 491074653 161 DKQgVAELISLFEQHAQRGGMVLLTTHQ 188
Cdd:cd03289  170 DPI-TYQVIRKTLKQAFADCTVILSEHR 196
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
1-70 2.52e-05

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 43.63  E-value: 2.52e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGlaRPD----GGEVCWRGRNTL----RDRA 70
Cdd:PRK09580   1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--REDyevtGGTVEFKGKDLLelspEDRA 76
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
19-186 3.82e-05

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 43.62  E-value: 3.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNtLRDRAAYqqdllfIGHQPGIKAVLTPFENLQFY 98
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKD-ISPRSPL------DAVKKGMAYITESRRDNGFF 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  99 QAVrGAAEQQAIWRALEQVGLVGY-----------------EDLP---------VAQLSAGQQRRVALARlWLSAAP-LW 151
Cdd:PRK09700 354 PNF-SIAQNMAISRSLKDGGYKGAmglfhevdeqrtaenqrELLAlkchsvnqnITELSGGNQQKVLISK-WLCCCPeVI 431
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 491074653 152 ILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTT 186
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS 466
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
121-190 6.00e-05

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 42.76  E-value: 6.00e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074653  121 GYEDLPVAQLSAGQQRRVALARLWLSAAP---LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDL 190
Cdd:pfam13304 228 GGGELPAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
9-207 6.49e-05

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 42.38  E-value: 6.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   9 CVRDERILFSELSFSVQPGDIIQVEGPNGAGKT----SLLRILAGLARPDGGEVCWRGR----NTLRDRAAYQqdllfIG 80
Cdd:PRK10418  11 ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKpvapCALRGRKIAT-----IM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 HQPgiKAVLTPFENLQFY-----QAVRGAAEQQAIWRALEQVGLVGYEDLPVA---QLSAGQQRRVALARLWLSAAPLWI 152
Cdd:PRK10418  86 QNP--RSAFNPLHTMHTHaretcLALGKPADDATLTAALEAVGLENAARVLKLypfEMSGGMLQRMMIALALLCEAPFII 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491074653 153 LDEPLTAIDKQGVAELISLFEQ-HAQRGGMVLLTTHqDLAGVSqtvgkiRLAEHDA 207
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESiVQKRALGMLLVTH-DMGVVA------RLADDVA 212
GguA NF040905
sugar ABC transporter ATP-binding protein;
18-159 9.69e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 42.47  E-value: 9.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  18 SELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLaRPDG---------GEVCwrgrnTLRDRAAYQQDLLFIGHQpgiKAV 88
Cdd:NF040905  18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyegeilfdGEVC-----RFKDIRDSEALGIVIIHQ---ELA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  89 LTPF----ENLqFY---QAVRGAAE-QQAIWRA---LEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPl 157
Cdd:NF040905  89 LIPYlsiaENI-FLgneRAKRGVIDwNETNRRArelLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP- 166

                 ..
gi 491074653 158 TA 159
Cdd:NF040905 167 TA 168
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
29-185 1.67e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 41.37  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  29 IIQVEGPNGAGKTSLLRILAGL------ARPDGgEVCWRGRNTlrdraaYQQDLLFIGHQPGIKAVL---TPFENLQFY- 98
Cdd:PRK14267  32 VFALMGPSGCGKSTLLRTFNRLlelneeARVEG-EVRLFGRNI------YSPDVDPIEVRREVGMVFqypNPFPHLTIYd 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  99 -------------------QAVRGAAEQQAIWRALEQvglvGYEDLPvAQLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:PRK14267 105 nvaigvklnglvkskkeldERVEWALKKAALWDEVKD----RLNDYP-SNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
                        170       180
                 ....*....|....*....|....*.
gi 491074653 160 IDKQGVAELISLFEQHAQRGGMVLLT 185
Cdd:PRK14267 180 IDPVGTAKIEELLFELKKEYTIVLVT 205
PTZ00243 PTZ00243
ABC transporter; Provisional
14-188 2.10e-04

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 41.69  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   14 RILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcWRGRNTlrdraAYqqdllfIGHQPGIKAVlTPFE 93
Cdd:PTZ00243  673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSI-----AY------VPQQAWIMNA-TVRG 739
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   94 NLQFYQAVRGAAEQQAIwR-------------ALE-QVGLVGyedlpvAQLSAGQQRRVALARLWLSAAPLWILDEPLTA 159
Cdd:PTZ00243  740 NILFFDEEDAARLADAV-RvsqleadlaqlggGLEtEIGEKG------VNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
                         170       180       190
                  ....*....|....*....|....*....|.
gi 491074653  160 IDKQgVAELI--SLFEQHAqRGGMVLLTTHQ 188
Cdd:PTZ00243  813 LDAH-VGERVveECFLGAL-AGKTRVLATHQ 841
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
14-185 2.31e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 40.85  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  14 RILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLA-RPDG----GEVCWRGRNTL--RDRAAYQQDLLFIGHQP--- 83
Cdd:PRK14271  34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdKVSGyrysGDVLLGGRSIFnyRDVLEFRRRVGMLFQRPnpf 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  84 ----------GIKA-VLTPFEnlQFYQAVRGAAEQQAIWRALEQvglvGYEDLPVaQLSAGQQRRVALARLWLSAAPLWI 152
Cdd:PRK14271 114 pmsimdnvlaGVRAhKLVPRK--EFRGVAQARLTEVGLWDAVKD----RLSDSPF-RLSGGQQQLLCLARTLAVNPEVLL 186
                        170       180       190
                 ....*....|....*....|....*....|...
gi 491074653 153 LDEPLTAIDKQGVAELISLFEQHAQRGGMVLLT 185
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADRLTVIIVT 219
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
20-191 2.52e-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: 41.21  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLArPDGGEVCWRGRN--TLRD------RAAYQ---QDllfighqpgikav 88
Cdd:COG4172  305 VSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDldGLSRralrplRRRMQvvfQD------------- 370
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  89 ltPF--------------ENLQFYQAVRGAAEQQA-IWRALEQVGLvgyedLPVA------QLSAGQQRRVALAR-LWLS 146
Cdd:COG4172  371 --PFgslsprmtvgqiiaEGLRVHGPGLSAAERRArVAEALEEVGL-----DPAArhryphEFSGGQRQRIAIARaLILE 443
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491074653 147 aaP-LWILDEPLTAIDKQGVAELISLFEQHAQRGGMV-LLTTHqDLA 191
Cdd:COG4172  444 --PkLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAyLFISH-DLA 487
PLN03130 PLN03130
ABC transporter C family member; Provisional
20-161 3.07e-04

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 41.26  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEV----CWRGRNTLRD-RAAY----QQDLLFIGhqpGIKAVLT 90
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIlidgCDISKFGLMDlRKVLgiipQAPVLFSG---TVRFNLD 1334
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491074653   91 PF---ENLQFYQAVRGAAEQQAIWRalEQVGLvgyeDLPVAQ----LSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PLN03130 1335 PFnehNDADLWESLERAHLKDVIRR--NSLGL----DAEVSEagenFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
19-187 3.54e-04

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 40.99  E-value: 3.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEV-----CWRGRN----TLRDRAAYQQ------DLLFIGHQP 83
Cdd:PRK10261  34 NLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSrqviELSEQSAAQMrhvrgaDMAMIFQEP 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  84 giKAVLTPF--------ENLQFYQAVRGAAEQQAIWRALEQVGLVGYEDLPVA---QLSAGQQRRVALArLWLSAAP-LW 151
Cdd:PRK10261 114 --MTSLNPVftvgeqiaESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRyphQLSGGMRQRVMIA-MALSCRPaVL 190
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491074653 152 ILDEPLTAID---KQGVAELISLFEQHAQRGgmVLLTTH 187
Cdd:PRK10261 191 IADEPTTALDvtiQAQILQLIKVLQKEMSMG--VIFITH 227
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
2-194 3.57e-04

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 40.54  E-value: 3.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   2 LEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGL------ARPDgGEVCWRGRN---------TL 66
Cdd:PRK14243  11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgFRVE-GKVTFHGKNlyapdvdpvEV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  67 RDRAAyqqdLLFIGHQPGIKAVltpFENLQF------YQA-----VRGAAEQQAIW----RALEQVGLvgyedlpvaQLS 131
Cdd:PRK14243  90 RRRIG----MVFQKPNPFPKSI---YDNIAYgaringYKGdmdelVERSLRQAALWdevkDKLKQSGL---------SLS 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 132 AGQQRRVALARLwLSAAPLWIL-DEPLTAID---KQGVAELI-SLFEQHAqrggmVLLTTH--QDLAGVS 194
Cdd:PRK14243 154 GGQQQRLCIARA-IAVQPEVILmDEPCSALDpisTLRIEELMhELKEQYT-----IIIVTHnmQQAARVS 217
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
1-173 4.21e-04

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 40.54  E-value: 4.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   1 MLEAKSLSCVRDERILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQDLLfig 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFL--- 388
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  81 hqpgiKAVLTPFENLqfyqaVRgAAEQQAIWRALEQVGLVGYE----DLPVAQLSAGQQRRVALARLWLSAAPLWILDEP 156
Cdd:PRK10636 389 -----RADESPLQHL-----AR-LAPQELEQKLRDYLGGFGFQgdkvTEETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
                        170       180
                 ....*....|....*....|
gi 491074653 157 LTAID---KQGVAELISLFE 173
Cdd:PRK10636 458 TNHLDldmRQALTEALIDFE 477
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
128-161 4.30e-04

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 40.39  E-value: 4.30e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 491074653 128 AQLSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
17-188 4.45e-04

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: 40.01  E-value: 4.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  17 FSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRNTLRDRAAYQQD-----LLFIGHQPGI-KAVL- 89
Cdd:cd03290   17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSrnrysVAYAAQKPWLlNATVe 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  90 ------TPFeNLQFYQAVRGAAEQQAIWRAL-----EQVGLVGYedlpvaQLSAGQQRRVALARLWLSAAPLWILDEPLT 158
Cdd:cd03290   97 enitfgSPF-NKQRYKAVTDACSLQPDIDLLpfgdqTEIGERGI------NLSGGQRQRICVARALYQNTNIVFLDDPFS 169
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 491074653 159 AID--------KQGVAELIslfeQHAQRggMVLLTTHQ 188
Cdd:cd03290  170 ALDihlsdhlmQEGILKFL----QDDKR--TLVLVTHK 201
PLN03232 PLN03232
ABC transporter C family member; Provisional
20-161 5.42e-04

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 40.34  E-value: 5.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   20 LSFSVQPGDIIQVEGPNGAGKTSLLRIL-------AGLARPDGGEVCWRGRNTLRDRAAY--QQDLLFIGhqpGIKAVLT 90
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALfriveleKGRIMIDDCDVAKFGLTDLRRVLSIipQSPVLFSG---TVRFNID 1331
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491074653   91 PFE---NLQFYQAVRGAAEQQAIWRalEQVGLvgyeDLPVAQ----LSAGQQRRVALARLWLSAAPLWILDEPLTAID 161
Cdd:PLN03232 1332 PFSehnDADLWEALERAHIKDVIDR--NPFGL----DAEVSEggenFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
24-170 7.04e-04

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 40.09  E-value: 7.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    24 VQPGDIIQVEGPNGAGKTSLLRILA----GLARPDGGEVCWRGRNTLRDRAAYQQDLLFIG----HQPgikaVLTPFENL 95
Cdd:TIGR00956   84 IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAetdvHFP----HLTVGETL 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    96 QFYQAVR-------GAAEQQAIWR----ALEQVGL-------VGyEDLpVAQLSAGQQRRVALARLWLSAAPLWILDEPL 157
Cdd:TIGR00956  160 DFAARCKtpqnrpdGVSREEYAKHiadvYMATYGLshtrntkVG-NDF-VRGVSGGERKRVSIAEASLGGAKIQCWDNAT 237
                          170
                   ....*....|...
gi 491074653   158 TAIDKQGVAELIS 170
Cdd:TIGR00956  238 RGLDSATALEFIR 250
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
23-188 7.58e-04

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 39.71  E-value: 7.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  23 SVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGR--NTLRDRAAYQQDLLFIgHQPgIKAVL--TPFENLQF- 97
Cdd:PRK10982  20 KVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFKSSKEALENGISMV-HQE-LNLVLqrSVMDNMWLg 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  98 -YQAVRGAAEQQAIWRALEQVglvgYEDL--------PVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAEL 168
Cdd:PRK10982  98 rYPTKGMFVDQDKMYRDTKAI----FDELdididpraKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHL 173
                        170       180
                 ....*....|....*....|
gi 491074653 169 ISLFEQHAQRGGMVLLTTHQ 188
Cdd:PRK10982 174 FTIIRKLKERGCGIVYISHK 193
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
89-187 9.05e-04

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 39.61  E-value: 9.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   89 LTPFENLQFYQAVrgaaeqQAIWRALE---QVGLvGYEDL--PVAQLSAGQQRRVALARlWLSA----APLWILDEPLTA 159
Cdd:TIGR00630 791 MTVEEAYEFFEAV------PSISRKLQtlcDVGL-GYIRLgqPATTLSGGEAQRIKLAK-ELSKrstgRTLYILDEPTTG 862
                          90       100
                  ....*....|....*....|....*...
gi 491074653  160 IDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:TIGR00630 863 LHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
26-187 1.30e-03

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: 37.74  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653    26 PGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVcwrgrntlrdraayqqdllfighqpgikavltpfenlqfyqaVRGAA 105
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV------------------------------------------IYIDG 38
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   106 EqqAIWRALEQVGLVGYEDLPVAQLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQHA------QRG 179
Cdd:smart00382  39 E--DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllksEKN 116

                   ....*...
gi 491074653   180 GMVLLTTH 187
Cdd:smart00382 117 LTVILTTN 124
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
19-97 1.37e-03

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 38.64  E-value: 1.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491074653  19 ELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGrntlrdraayqqDLLFIGHQPGIKAVLTPFENLQF 97
Cdd:PRK13546  42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------------EVSVIAISAGLSGQLTGIENIEF 108
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
20-200 1.53e-03

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 38.63  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDggevcWRgrnTLRDRAAYQQ-DLL---------FIGHQPGI---- 85
Cdd:PRK15093  26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDN-----WR---VTADRMRFDDiDLLrlsprerrkLVGHNVSMifqe 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  86 -KAVLTPFENL--QFYQAV-----RGAAEQQAIWR---ALEQVGLVGYED-------LPVaQLSAGQQRRVALARLWLSA 147
Cdd:PRK15093  98 pQSCLDPSERVgrQLMQNIpgwtyKGRWWQRFGWRkrrAIELLHRVGIKDhkdamrsFPY-ELTEGECQKVMIAIALANQ 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491074653 148 APLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQDLAGVSQTVGKI 200
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
126-187 2.10e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 38.66  E-value: 2.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491074653  126 PVAQLSAGQQRRVALARLWLSAAP---LWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTH 187
Cdd:PRK00635  806 PLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
2-64 3.04e-03

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 38.08  E-value: 3.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491074653   2 LEAKSLScVRDER--ILFSELSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGRN 64
Cdd:COG3845  258 LEVENLS-VRDDRgvPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED 321
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
9-161 3.27e-03

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 37.58  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   9 CVRDERIL---FSELSFSVQPGDIIQVEGPNGAGKTSL-------LRILAGLARPDGGEVCWRGRNTLRDRAA--YQQDL 76
Cdd:cd03288   26 CVRYENNLkpvLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIVIDGIDISKLPLHTLRSRLSiiLQDPI 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  77 LFIGhqpGIKAVLTPfenlqfyqavRGAAEQQAIWRALEQV-------GLVGYEDLPVAQ----LSAGQQRRVALARLWL 145
Cdd:cd03288  106 LFSG---SIRFNLDP----------ECKCTDDRLWEALEIAqlknmvkSLPGGLDAVVTEggenFSVGQRQLFCLARAFV 172
                        170
                 ....*....|....*.
gi 491074653 146 SAAPLWILDEPLTAID 161
Cdd:cd03288  173 RKSSILIMDEATASID 188
PTZ00243 PTZ00243
ABC transporter; Provisional
20-175 3.49e-03

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 37.84  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   20 LSFSVQPGDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCWRGrntlRDRAAY-------------QQDLLFIGhqpGIK 86
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG----REIGAYglrelrrqfsmipQDPVLFDG---TVR 1401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653   87 AVLTPFenLQfyqavrgaAEQQAIWRALEQVGL---VGYE----DLPV----AQLSAGQQRRVALARLWLSAAPLWILDE 155
Cdd:PTZ00243 1402 QNVDPF--LE--------ASSAEVWAALELVGLrerVASEsegiDSRVleggSNYSVGQRQLMCMARALLKKGSGFILMD 1471
                         170       180
                  ....*....|....*....|....*
gi 491074653  156 PLT-----AIDKQGVAELISLFEQH 175
Cdd:PTZ00243 1472 EATanidpALDRQIQATVMSAFSAY 1496
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
20-189 4.75e-03

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 36.53  E-value: 4.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653  20 LSFSVQPGDIIQVEGPNGAGKTSLLriLAGLARpdggEVCWRGRNTLrdRAAYQQDLLFIGhqpgikavltpfeNLQFyq 99
Cdd:cd03238   14 LDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYA----SGKARLISFL--PKFSRNKLIFID-------------QLQF-- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491074653 100 avrgaaeqqaiwraLEQVGLvGYEDL--PVAQLSAGQQRRVALAR-LWLSAAP-LWILDEPLTAIDKQGVAELISLFEQH 175
Cdd:cd03238   71 --------------LIDVGL-GYLTLgqKLSTLSGGELQRVKLASeLFSEPPGtLFILDEPSTGLHQQDINQLLEVIKGL 135
                        170
                 ....*....|....
gi 491074653 176 AQRGGMVLLTTHQD 189
Cdd:cd03238  136 IDLGNTVILIEHNL 149
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
127-189 4.85e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 37.50  E-value: 4.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491074653  127 VAQLSAGQQRRVALARlWLSA---APLWILDEPLTAIDKQGVAELISLFEQHAQRGGMVLLTTHQD 189
Cdd:PRK00635  474 LATLSGGEQERTALAK-HLGAeliGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDE 538
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
19-48 6.49e-03

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 36.51  E-value: 6.49e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 491074653  19 ELSFSVQPGDIIQVeGPNGAGKTSLLRILA 48
Cdd:COG3950   18 EIDFDNPPRLTVLV-GENGSGKTTLLEAIA 46
cbiO PRK13646
energy-coupling factor transporter ATPase;
129-200 7.35e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 36.68  E-value: 7.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491074653 129 QLSAGQQRRVALARLWLSAAPLWILDEPLTAIDKQGVAELISLFEQ-HAQRGGMVLLTTHqDLAGVSQTVGKI 200
Cdd:PRK13646 145 QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlQTDENKTIILVSH-DMNEVARYADEV 216
RecA-like cd01393
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
27-60 8.08e-03

RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange. While prokaryotes have a single RecA protein, eukaryotes have multiple RecA homologs such as Rad51, DMC1 and Rad55/57. Archaea have the RecA-like homologs RadA and RadB.


Pssm-ID: 410881 [Multi-domain]  Cd Length: 185  Bit Score: 35.79  E-value: 8.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 491074653  27 GDIIQVEGPNGAGKTSLLRILAGLARPDGGEVCW 60
Cdd:cd01393    1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVW 34
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
29-48 8.63e-03

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 35.92  E-value: 8.63e-03
                         10        20
                 ....*....|....*....|
gi 491074653  29 IIQVEGPNGAGKTSLLRILA 48
Cdd:COG1428    5 YIAVEGNIGAGKTTLARLLA 24
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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