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Conserved domains on  [gi|5923929|gb|AAD56419|]
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bile salt export pump, partial [Mus musculus]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
1-173 6.79e-91

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


The actual alignment was detected with superfamily member cd03249:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 238  Bit Score: 264.79  E-value: 6.79e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:cd03249  44 TVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIM 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:cd03249 124 SLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRN 203
                       170
                ....*....|...
gi 5923929  161 ADVIIGFEHGVAV 173
Cdd:cd03249 204 ADLIAVLQNGQVV 216
 
Name Accession Description Interval E-value
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1-173 6.79e-91

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: 264.79  E-value: 6.79e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:cd03249  44 TVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIM 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:cd03249 124 SLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRN 203
                       170
                ....*....|...
gi 5923929  161 ADVIIGFEHGVAV 173
Cdd:cd03249 204 ADLIAVLQNGQVV 216
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1-170 2.26e-67

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 214.64  E-value: 2.26e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:COG1132 381 TLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIE 460
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFDTLVgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:COG1132 461 ALPDGYDTVVgergvnlsggqrqRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRN 540
                       170
                ....*....|
gi 5923929  161 ADVIIGFEHG 170
Cdd:COG1132 541 ADRILVLDDG 550
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
1-170 2.86e-55

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 183.24  E-value: 2.86e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:PRK13657 376 TLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIE 455
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:PRK13657 456 RKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRN 535
                        170
                 ....*....|
gi 5923929   161 ADVIIGFEHG 170
Cdd:PRK13657 536 ADRILVFDNG 545
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
1-173 3.54e-48

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 164.12  E-value: 3.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929      1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGR-EEATMEDIVQAAKDANAYNFI 79
Cdd:TIGR02203 373 TLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFV 452
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     80 MALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVR 159
Cdd:TIGR02203 453 DKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE 532
                         170
                  ....*....|....
gi 5923929    160 SADVIIGFEHGVAV 173
Cdd:TIGR02203 533 KADRIVVMDDGRIV 546
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1-125 4.67e-20

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: 81.16  E-value: 4.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929      1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFS-TTIAENIRLGREeatMEDIVQAAKDANAYNFI 79
Cdd:pfam00005  26 TLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENLRLGLL---LKGLSKREKDARAEEAL 102
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 5923929     80 MALPQQF--DTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATS 125
Cdd:pfam00005 103 EKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
104-162 2.47e-06

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 45.30  E-value: 2.47e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH-GHTIISVAHRLSTVRSAD 162
Cdd:NF040873 127 RALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRAD 186
GguA NF040905
sugar ABC transporter ATP-binding protein;
36-164 4.50e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 36.69  E-value: 4.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    36 IGIVEQE----PVLfstTIAENIRLGREEATM------EDIVQAAK-------DANAYNFIMAL---PQQFdtlvgeggg 95
Cdd:NF040905  80 IVIIHQElaliPYL---SIAENIFLGNERAKRgvidwnETNRRAREllakvglDESPDTLVTDIgvgKQQL--------- 147
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5923929    96 qmsggqkqrVAIARALIRKPKILLLDMATSAL-DNESEAKVQGALNKIQHGHTIISVAHRLSTVRS-ADVI 164
Cdd:NF040905 148 ---------VEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSI 209
 
Name Accession Description Interval E-value
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1-173 6.79e-91

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: 264.79  E-value: 6.79e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:cd03249  44 TVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIM 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:cd03249 124 SLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRN 203
                       170
                ....*....|...
gi 5923929  161 ADVIIGFEHGVAV 173
Cdd:cd03249 204 ADLIAVLQNGQVV 216
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1-170 2.26e-67

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 214.64  E-value: 2.26e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:COG1132 381 TLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIE 460
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFDTLVgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:COG1132 461 ALPDGYDTVVgergvnlsggqrqRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRN 540
                       170
                ....*....|
gi 5923929  161 ADVIIGFEHG 170
Cdd:COG1132 541 ADRILVLDDG 550
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
1-170 1.55e-64

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: 197.84  E-value: 1.55e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:cd03251  43 TLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIM 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:cd03251 123 ELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIEN 202
                       170
                ....*....|
gi 5923929  161 ADVIIGFEHG 170
Cdd:cd03251 203 ADRIVVLEDG 212
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
1-170 3.70e-63

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: 206.22  E-value: 3.70e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:COG2274 516 TLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIE 595
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:COG2274 596 ALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRL 675
                       170
                ....*....|
gi 5923929  161 ADVIIGFEHG 170
Cdd:COG2274 676 ADRIIVLDKG 685
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
1-170 1.45e-58

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: 182.43  E-value: 1.45e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:cd03254  44 TLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIM 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:cd03254 124 KLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKN 203
                       170
                ....*....|
gi 5923929  161 ADVIIGFEHG 170
Cdd:cd03254 204 ADKILVLDDG 213
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
1-173 3.52e-57

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 188.49  E-value: 3.52e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:COG5265 399 TLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIE 478
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFDTLVgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:COG5265 479 SLPDGYDTRVgerglklsggekqRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVD 558
                       170
                ....*....|...
gi 5923929  161 ADVIIGFEHGVAV 173
Cdd:COG5265 559 ADEILVLEAGRIV 571
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
1-165 9.59e-57

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: 177.81  E-value: 9.59e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:cd03253  42 TILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIM 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:cd03253 122 RFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVN 201

                ....*
gi 5923929  161 ADVII 165
Cdd:cd03253 202 ADKII 206
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
1-170 2.86e-55

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 183.24  E-value: 2.86e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:PRK13657 376 TLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIE 455
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:PRK13657 456 RKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRN 535
                        170
                 ....*....|
gi 5923929   161 ADVIIGFEHG 170
Cdd:PRK13657 536 ADRILVFDNG 545
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
1-173 7.66e-54

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: 170.74  E-value: 7.66e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:cd03252  43 TLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFIS 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:cd03252 123 ELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKN 202
                       170
                ....*....|...
gi 5923929  161 ADVIIGFEHGVAV 173
Cdd:cd03252 203 ADRIIVMEKGRIV 215
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
1-170 5.28e-50

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: 168.78  E-value: 5.28e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:COG4988 378 TLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVA 457
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:COG4988 458 ALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ 537
                       170
                ....*....|
gi 5923929  161 ADVIIGFEHG 170
Cdd:COG4988 538 ADRILVLDDG 547
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
1-173 3.54e-48

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 164.12  E-value: 3.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929      1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGR-EEATMEDIVQAAKDANAYNFI 79
Cdd:TIGR02203 373 TLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFV 452
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     80 MALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVR 159
Cdd:TIGR02203 453 DKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE 532
                         170
                  ....*....|....
gi 5923929    160 SADVIIGFEHGVAV 173
Cdd:TIGR02203 533 KADRIVVMDDGRIV 546
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
1-173 5.69e-48

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 165.28  E-value: 5.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929      1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:TIGR00958 522 TVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIM 601
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGAlnKIQHGHTIISVAHRLSTVRS 160
Cdd:TIGR00958 602 EFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVER 679
                         170
                  ....*....|...
gi 5923929    161 ADVIIGFEHGVAV 173
Cdd:TIGR00958 680 ADQILVLKKGSVV 692
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
1-170 2.05e-47

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: 152.15  E-value: 2.05e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREeatmedivqaakdanaynfim 80
Cdd:cd03228  43 TLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLFSGTIRENILSGGQ--------------------- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 alpQQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:cd03228 102 ---RQ------------------RIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRD 160
                       170
                ....*....|
gi 5923929  161 ADVIIGFEHG 170
Cdd:cd03228 161 ADRIIVLDDG 170
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
1-170 6.23e-47

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: 152.62  E-value: 6.23e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:cd03248  55 TVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFIS 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:cd03248 135 ELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER 214
                       170
                ....*....|
gi 5923929  161 ADVIIGFEHG 170
Cdd:cd03248 215 ADQILVLDGG 224
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
1-170 9.49e-46

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 157.49  E-value: 9.49e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEA-TMEDIVQAAKDANAYNFI 79
Cdd:PRK11176 384 TIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFI 463
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    80 MALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVR 159
Cdd:PRK11176 464 NKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIE 543
                        170
                 ....*....|.
gi 5923929   160 SADVIIGFEHG 170
Cdd:PRK11176 544 KADEILVVEDG 554
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
15-167 2.12e-37

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 136.31  E-value: 2.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     15 GMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGG 94
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYG 1356
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5923929     95 GQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVRSADVIIGF 167
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVF 1431
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
1-170 4.57e-36

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: 131.04  E-value: 4.57e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:COG4987 376 TLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLA 455
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:COG4987 456 ALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLER 535
                       170
                ....*....|
gi 5923929  161 ADVIIGFEHG 170
Cdd:COG4987 536 MDRILVLEDG 545
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
1-165 7.95e-36

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: 130.10  E-value: 7.95e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929      1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:TIGR02857 363 TLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVA 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:TIGR02857 443 ALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAAL 522

                  ....*
gi 5923929    161 ADVII 165
Cdd:TIGR02857 523 ADRIV 527
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
1-173 1.05e-35

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: 123.76  E-value: 1.05e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLgREEATMEDIVQAAKDANAYNFIM 80
Cdd:cd03244  45 SLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNLDP-FGEYSDEELWQALERVGLKEFVE 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:cd03244 124 SLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIID 203
                       170
                ....*....|...
gi 5923929  161 ADVIIGFEHGVAV 173
Cdd:cd03244 204 SDRILVLDKGRVV 216
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
1-170 1.37e-35

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: 123.47  E-value: 1.37e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:cd03245  45 TLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVN 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:cd03245 125 KHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDL 204
                       170
                ....*....|
gi 5923929  161 ADVIIGFEHG 170
Cdd:cd03245 205 VDRIIVMDSG 214
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
1-164 1.78e-35

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 130.53  E-value: 1.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929      1 TALQLIQRFYDPCEG-MVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIR------------------------ 55
Cdd:PTZ00265  426 TILKLIERLYDPTEGdIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKyslyslkdlealsnyynedgndsq 505
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     56 -------------------------------LGREEATMED--IVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQK 102
Cdd:PTZ00265  506 enknkrnscrakcagdlndmsnttdsnelieMRKNYQTIKDseVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQK 585
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5923929    103 QRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGH---TIIsVAHRLSTVRSADVI 164
Cdd:PTZ00265  586 QRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnriTII-IAHRLSTIRYANTI 649
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
1-170 2.86e-33

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 123.67  E-value: 2.86e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:PRK10789 356 TLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDIL 435
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:PRK10789 436 RLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTE 515
                        170
                 ....*....|
gi 5923929   161 ADVIIGFEHG 170
Cdd:PRK10789 516 ASEILVMQHG 525
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
1-173 1.99e-32

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 121.60  E-value: 1.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929      1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIrLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:TIGR03797 494 TLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIR 572
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQhgHTIISVAHRLSTVRS 160
Cdd:TIGR03797 573 AMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLK--VTRIVIAHRLSTIRN 650
                         170
                  ....*....|...
gi 5923929    161 ADVIIGFEHGVAV 173
Cdd:TIGR03797 651 ADRIYVLDAGRVV 663
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
12-170 1.57e-30

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 116.10  E-value: 1.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    12 PCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVG 91
Cdd:PRK11174 401 PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIG 480
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5923929    92 EGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHG 170
Cdd:PRK11174 481 DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDG 559
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
1-170 7.91e-27

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 105.59  E-value: 7.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929      1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLG-REEATMEDIVQAAKDANAYNFI 79
Cdd:TIGR01193 515 TLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDI 594
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     80 MALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHgHTIISVAHRLSTVR 159
Cdd:TIGR01193 595 ENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAK 673
                         170
                  ....*....|.
gi 5923929    160 SADVIIGFEHG 170
Cdd:TIGR01193 674 QSDKIIVLDHG 684
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
12-164 2.00e-26

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 104.06  E-value: 2.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   12 PCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENI-RLGreEATMEDIVQAAKDANAYNFIMALPQQFDTLV 90
Cdd:COG4618 384 PTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRI 461
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5923929   91 GEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRSADVI 164
Cdd:COG4618 462 GEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKL 536
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
1-173 2.32e-24

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 98.64  E-value: 2.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREeATMEDIVQAAKDANAYNFIM 80
Cdd:PRK10790 382 TLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELAR 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:PRK10790 461 SLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVE 540
                        170
                 ....*....|...
gi 5923929   161 ADVIIGFEHGVAV 173
Cdd:PRK10790 541 ADTILVLHRGQAV 553
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
1-155 3.67e-24

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: 97.82  E-value: 3.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929      1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:TIGR02868 376 TLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLR 455
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5923929     81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRL 155
Cdd:TIGR02868 456 ALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
1-173 1.01e-23

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: 92.63  E-value: 1.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYD-----PCEGMVTPDGHDIRSLNIR--WLRDQIGIVEQEPVLFSTTIAENIRLG------REEATMEDIV 67
Cdd:cd03260  41 TLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERV 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   68 Q-----AAKDANAYNFIMALP-----QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQG 137
Cdd:cd03260 121 EealrkAALWDEVKDRLHALGlsggqQQ------------------RLCLARALANEPEVLLLDEPTSALDPISTAKIEE 182
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 5923929  138 ALNKIQHGHTIISVAHRLSTV-RSADVIIGFEHGVAV 173
Cdd:cd03260 183 LIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLV 219
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
1-170 8.32e-23

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: 90.16  E-value: 8.32e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLgREEATMEDIVQAAKDANAYNFIM 80
Cdd:cd03369  49 TLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLDP-FDEYSDEEIYGALRVSEGGLNLS 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 ALPQQFdtlvgegggqmsggqkqrVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:cd03369 128 QGQRQL------------------LCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIID 189
                       170
                ....*....|
gi 5923929  161 ADVIIGFEHG 170
Cdd:cd03369 190 YDKILVMDAG 199
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
1-172 9.61e-22

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: 86.50  E-value: 9.61e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREeatmedivqaakdanaynfim 80
Cdd:cd03246  43 TLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSGSIAENILSGGQ--------------------- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 alpqqfdtlvgegggqmsggqKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ-HGHTIISVAHRLSTVR 159
Cdd:cd03246 102 ---------------------RQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLA 160
                       170
                ....*....|...
gi 5923929  160 SADVIIGFEHGVA 172
Cdd:cd03246 161 SADRILVLEDGRV 173
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1-125 4.67e-20

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: 81.16  E-value: 4.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929      1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFS-TTIAENIRLGREeatMEDIVQAAKDANAYNFI 79
Cdd:pfam00005  26 TLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENLRLGLL---LKGLSKREKDARAEEAL 102
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 5923929     80 MALPQQF--DTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATS 125
Cdd:pfam00005 103 EKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
3-153 5.27e-20

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 82.56  E-value: 5.27e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    3 LQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENI----RLGREEATMEDIVQAAKDANAYNF 78
Cdd:COG4619  43 LRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPD 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   79 IMALP--------QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTI 148
Cdd:COG4619 123 ILDKPverlsggeRQ------------------RLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAV 184

                ....*
gi 5923929  149 ISVAH 153
Cdd:COG4619 185 LWVSH 189
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
8-173 1.86e-19

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: 82.26  E-value: 1.86e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    8 RFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREeATMEDIVQAAKDANAYNFIMALPQQFD 87
Cdd:cd03288  69 RMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLD 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   88 TLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGF 167
Cdd:cd03288 148 AVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVL 227

                ....*.
gi 5923929  168 EHGVAV 173
Cdd:cd03288 228 SRGILV 233
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
8-171 4.13e-19

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 83.46  E-value: 4.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929       8 RFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRlGREEATMEDIVQAAKDANAYNFIMALPQQFD 87
Cdd:TIGR00957 1334 RINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLD 1412
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929      88 TLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGF 167
Cdd:TIGR00957 1413 HECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVL 1492

                   ....
gi 5923929     168 EHGV 171
Cdd:TIGR00957 1493 DKGE 1496
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
1-170 3.84e-18

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 78.14  E-value: 3.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPV--LFSTTIAENI-----RLGREEATMEDIVQAA--- 70
Cdd:COG1122  42 TLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQNPDdqLFAPTVEEDVafgpeNLGLPREEIRERVEEAlel 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   71 ------KDANAYNfimaLP---QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNK 141
Cdd:COG1122 122 vglehlADRPPHE----LSggqKQ------------------RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKR 179
                       170       180       190
                ....*....|....*....|....*....|.
gi 5923929  142 IQH-GHTIISVAHRLSTV-RSADVIIGFEHG 170
Cdd:COG1122 180 LNKeGKTVIIVTHDLDLVaELADRVIVLDDG 210
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
1-170 3.63e-17

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 77.94  E-value: 3.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAYNFIM 80
Cdd:PRK11160 381 TLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLE 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    81 AlPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:PRK11160 461 D-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQ 539
                        170
                 ....*....|
gi 5923929   161 ADVIIGFEHG 170
Cdd:PRK11160 540 FDRICVMDNG 549
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
1-170 4.08e-17

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: 74.27  E-value: 4.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNiRWLRDQIGIVEQEPVLFSTTIAENirLGREEATMEdivqaakdanaynfim 80
Cdd:cd03247  43 TLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRPYLFDTTLRNN--LGRRFSGGE---------------- 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 alpQQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:cd03247 104 ---RQ------------------RLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEH 162
                       170
                ....*....|
gi 5923929  161 ADVIIGFEHG 170
Cdd:cd03247 163 MDKILFLENG 172
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
1-170 1.09e-16

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: 73.38  E-value: 1.09e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLN--IRWLRDQIGIVEQEPVLFST-TIAENIRLGreeatmedivqaakdanayn 77
Cdd:cd03229  41 TLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALFPHlTVLENIALG-------------------- 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   78 fimaLP---QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVA 152
Cdd:cd03229 101 ----LSggqQQ------------------RVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVT 158
                       170
                ....*....|....*....
gi 5923929  153 HRLSTV-RSADVIIGFEHG 170
Cdd:cd03229 159 HDLDEAaRLADRVVVLRDG 177
PLN03130 PLN03130
ABC transporter C family member; Provisional
8-170 7.66e-16

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 74.39  E-value: 7.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929      8 RFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATMeDIVQAAKDANAYNFIMALPQQFD 87
Cdd:PLN03130 1287 RIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDA-DLWESLERAHLKDVIRRNSLGLD 1365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     88 TLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGF 167
Cdd:PLN03130 1366 AEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVL 1445

                  ...
gi 5923929    168 EHG 170
Cdd:PLN03130 1446 DAG 1448
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
1-170 1.14e-15

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: 71.34  E-value: 1.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEP--VLFSTTIAENI-----RLGREEATMEDIV-QAAKD 72
Cdd:cd03225  42 TLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPddQFFGPTVEEEVafgleNLGLPEEEIEERVeEALEL 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   73 ANAYNFIMALP-------QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH- 144
Cdd:cd03225 122 VGLEGLRDRSPftlsggqKQ------------------RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAe 183
                       170       180
                ....*....|....*....|....*..
gi 5923929  145 GHTIISVAHRLSTVRS-ADVIIGFEHG 170
Cdd:cd03225 184 GKTIIIVTHDLDLLLElADRVIVLEDG 210
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
1-170 1.59e-15

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: 69.58  E-value: 1.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQepvlFSttiaenirlGREeatmedivqaakdanaynfim 80
Cdd:cd00267  40 TLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ----LS---------GGQ--------------------- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 alpQQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTV- 158
Cdd:cd00267  86 ---RQ------------------RVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAe 144
                       170
                ....*....|..
gi 5923929  159 RSADVIIGFEHG 170
Cdd:cd00267 145 LAADRVIVLKDG 156
PLN03232 PLN03232
ABC transporter C family member; Provisional
14-170 3.09e-15

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 72.32  E-value: 3.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     14 EGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLGREEATmEDIVQAAKDANAYNFIMALPQQFDTLVGEG 93
Cdd:PLN03232 1290 KGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHND-ADLWEALERAHIKDVIDRNPFGLDAEVSEG 1368
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5923929     94 GGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRSADVIIGFEHG 170
Cdd:PLN03232 1369 GENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSG 1445
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
11-170 1.05e-14

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: 68.67  E-value: 1.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   11 DPCEGMVTPDGHDIRSLN----IRWLRDQIGIVEQEPVLFST-TIAENIRLG------REEATMEDIVQAAK----DANA 75
Cdd:cd03255  55 RPTSGEVRVDGTDISKLSekelAAFRRRHIGFVFQSFNLLPDlTALENVELPlllagvPKKERRERAEELLErvglGDRL 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   76 YNFIMALP---QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIIS 150
Cdd:cd03255 135 NHYPSELSggqQQ------------------RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVV 196
                       170       180
                ....*....|....*....|
gi 5923929  151 VAHRLSTVRSADVIIGFEHG 170
Cdd:cd03255 197 VTHDPELAEYADRIIELRDG 216
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
104-154 2.30e-14

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 69.84  E-value: 2.30e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHR 154
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
1-173 2.37e-14

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: 67.99  E-value: 2.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLN---IRWLRDQIGIVEQEPVLFST-TIAENIRLGREEATMEDIVQAAK----- 71
Cdd:cd03258  46 TLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKARRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERvlell 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   72 -------DANAYnfimalPQQFDtlvgegggqmsGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH 144
Cdd:cd03258 126 elvgledKADAY------PAQLS-----------GGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINR 188
                       170       180       190
                ....*....|....*....|....*....|..
gi 5923929  145 --GHTIISVAHRLSTVRS-ADVIIGFEHGVAV 173
Cdd:cd03258 189 elGLTIVLITHEMEVVKRiCDRVAVMEKGEVV 220
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
14-173 3.07e-14

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 69.16  E-value: 3.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   14 EGMVTPDGHDIRSLNIRWLRDQIGIVEQEP--VLFSTTIAENI-------RLGREEATmEDIVQAAKDANAYNFIMALPQ 84
Cdd:COG1123  63 SGEVLLDGRDLLELSEALRGRRIGMVFQDPmtQLNPVTVGDQIaealenlGLSRAEAR-ARVLELLEAVGLERRLDRYPH 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   85 QFdtlvgegggqmSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTV-RSA 161
Cdd:COG1123 142 QL-----------SGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVaEIA 210
                       170
                ....*....|..
gi 5923929  162 DVIIGFEHGVAV 173
Cdd:COG1123 211 DRVVVMDDGRIV 222
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
14-155 5.15e-14

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 67.37  E-value: 5.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   14 EGMVTPDGHDI--RSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLG------REEATMEDIV-----QAA-----KD--- 72
Cdd:COG1117  70 EGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVeeslrKAAlwdevKDrlk 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   73 ANAynfiMALP---QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTII 149
Cdd:COG1117 150 KSA----LGLSggqQQ------------------RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIV 207

                ....*.
gi 5923929  150 SVAHRL 155
Cdd:COG1117 208 IVTHNM 213
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
1-153 5.44e-14

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: 66.73  E-value: 5.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNirwlrDQIGIVEQEPVLFS-TTIAENIRLG----------REEATME--DIV 67
Cdd:cd03293  45 TLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDRGYVFQQDALLPwLTVLDNVALGlelqgvpkaeARERAEEllELV 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   68 QAAKDANAYnfimalP-------QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALN 140
Cdd:cd03293 120 GLSGFENAY------PhqlsggmRQ------------------RVALARALAVDPDVLLLDEPFSALDALTREQLQEELL 175
                       170
                ....*....|....*
gi 5923929  141 KI--QHGHTIISVAH 153
Cdd:cd03293 176 DIwrETGKTVLLVTH 190
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
104-154 6.01e-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: 65.64  E-value: 6.01e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNkiQHGHTIISVAHR 154
Cdd:cd03223  99 RLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK--ELGITVISVGHR 147
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
12-171 1.25e-13

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 65.84  E-value: 1.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   12 PCEGMVTPDGHDIRSLNI----RWLRDQIGIVEQEPVLFST-TIAENIRL-------GREEATmEDIVQAAKDANAYNFI 79
Cdd:COG1136  60 PTSGEVLIDGQDISSLSErelaRLRRRHIGFVFQFFNLLPElTALENVALplllagvSRKERR-ERARELLERVGLGDRL 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   80 MALP-------QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIIS 150
Cdd:COG1136 139 DHRPsqlsggqQQ------------------RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVM 200
                       170       180
                ....*....|....*....|.
gi 5923929  151 VAHRLSTVRSADVIIGFEHGV 171
Cdd:COG1136 201 VTHDPELAARADRVIRLRDGR 221
PTZ00243 PTZ00243
ABC transporter; Provisional
1-171 1.85e-13

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 67.50  E-value: 1.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929      1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRlGREEATMEDIVQAAKDANAYNFIM 80
Cdd:PTZ00243 1351 TLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVA 1429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     81 ALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRK-PKILLLDMATS----ALDNESEAKVQGALNkiqhGHTIISVAHRL 155
Cdd:PTZ00243 1430 SESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATAnidpALDRQIQATVMSAFS----AYTVITIAHRL 1505
                         170
                  ....*....|....*.
gi 5923929    156 STVRSADVIIGFEHGV 171
Cdd:PTZ00243 1506 HTVAQYDKIIVMDHGA 1521
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
1-155 2.45e-13

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 65.57  E-value: 2.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYD-----PCEGMVTPDGHDIRSLNIRW--LRDQIGIVEQEPVLFSTTIAENIRLG------REEATMEDIV 67
Cdd:PRK14239  46 TLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEAV 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    68 QAA-KDANAYNFIMalpqqfDTLvGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGH 146
Cdd:PRK14239 126 EKSlKGASIWDEVK------DRL-HDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY 198

                 ....*....
gi 5923929   147 TIISVAHRL 155
Cdd:PRK14239 199 TMLLVTRSM 207
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
1-171 2.92e-13

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: 64.86  E-value: 2.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDI--RSLNIRWLRDQIGIVEQEPVLFS-TTIAENIRLG--------REEAT---ME-- 64
Cdd:cd03262  41 TLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPhLTVLENITLApikvkgmsKAEAEeraLEll 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   65 DIVQAAKDANAYNFIMALPQQfdtlvgegggqmsggqkQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH 144
Cdd:cd03262 121 EKVGLADKADAYPAQLSGGQQ-----------------QRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAE 183
                       170       180
                ....*....|....*....|....*....
gi 5923929  145 -GHTIISVAHRLSTVRS-ADVIIGFEHGV 171
Cdd:cd03262 184 eGMTMVVVTHEMGFAREvADRVIFMDDGR 212
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
1-173 3.50e-13

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: 64.46  E-value: 3.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRwLRDqIGIVEQEPVLFST-TIAENI-----RLGREEATMEDIV-QAAKDA 73
Cdd:cd03259  41 TLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRN-IGMVFQDYALFPHlTVAENIafglkLRGVPKAEIRARVrELLELV 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   74 NAYNFIMALP-------QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH-- 144
Cdd:cd03259 119 GLEGLLNRYPhelsggqQQ------------------RVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRel 180
                       170       180       190
                ....*....|....*....|....*....|
gi 5923929  145 GHTIISVAHRLS-TVRSADVIIGFEHGVAV 173
Cdd:cd03259 181 GITTIYVTHDQEeALALADRIAVMNEGRIV 210
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
1-160 6.23e-13

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 63.92  E-value: 6.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLN---IRWLRDQIGIVEQE-PVLFSTTIAENIRL-----GREEATMEDIVQAAK 71
Cdd:COG2884  43 TLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRRIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRRVREVL 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   72 D-----ANAYNFIMALP---QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI- 142
Cdd:COG2884 123 DlvglsDKAKALPHELSggeQQ------------------RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIn 184
                       170
                ....*....|....*...
gi 5923929  143 QHGHTIISVAHRLSTVRS 160
Cdd:COG2884 185 RRGTTVLIATHDLELVDR 202
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
10-170 7.39e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 64.63  E-value: 7.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    10 YDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEP---VLFSTT---IA---ENIRLGREEatMEDIV-QAAKDANAYNFI 79
Cdd:PRK13632  59 LKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPdnqFIGATVeddIAfglENKKVPPKK--MKDIIdDLAKKVGMEDYL 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    80 MALPQQFDtlvgegggqmsGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLST 157
Cdd:PRK13632 137 DKEPQNLS-----------GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDE 205
                        170
                 ....*....|...
gi 5923929   158 VRSADVIIGFEHG 170
Cdd:PRK13632 206 AILADKVIVFSEG 218
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
12-170 9.39e-13

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 63.99  E-value: 9.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     12 PCEGMVTPDGHDIRSLNIRW-LRDQIGIVEQEP--VLFSTT----IA---ENIRLGREEatMEDIVQ-AAKDANAYNFIM 80
Cdd:TIGR04520  54 PTSGKVTVDGLDTLDEENLWeIRKKVGMVFQNPdnQFVGATveddVAfglENLGVPREE--MRKRVDeALKLVGMEDFRD 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     81 ALPQ-------QfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISV 151
Cdd:TIGR04520 132 REPHllsggqkQ------------------RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnkEEGITVISI 193
                         170
                  ....*....|....*....
gi 5923929    152 AHRLSTVRSADVIIGFEHG 170
Cdd:TIGR04520 194 THDMEEAVLADRVIVMNKG 212
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
3-170 1.05e-12

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: 63.51  E-value: 1.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    3 LQLIQRFYDPCEGMVTPDGHDIRSLNIRwlRDQIGIVEQEPVLF-STTIAENIRLG---REEATMED---IVQAAKDANa 75
Cdd:cd03299  42 LETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNIAYGlkkRKVDKKEIerkVLEIAEMLG- 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   76 ynfimalpqqFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAH 153
Cdd:cd03299 119 ----------IDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKefGVTVLHVTH 188
                       170
                ....*....|....*...
gi 5923929  154 RLSTVRS-ADVIIGFEHG 170
Cdd:cd03299 189 DFEEAWAlADKVAIMLNG 206
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
1-170 3.30e-12

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: 62.57  E-value: 3.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNiRWLRDQIGIVEQEPVLFST-TIAENIRLgreEATMEDIVQAAKDANAYNFI 79
Cdd:COG4555  42 TLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLPDERGLYDRlTVRENIRY---FAELYGLFDEELKKRIEELI 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   80 --MALPQQFDTLVGEGGGQMSGgqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLS 156
Cdd:COG4555 118 elLGLEEFLDRRVGELSTGMKK----KVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkKEGKTVLFSSHIMQ 193
                       170
                ....*....|....*
gi 5923929  157 TV-RSADVIIGFEHG 170
Cdd:COG4555 194 EVeALCDRVVILHKG 208
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1-173 3.37e-12

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 63.38  E-value: 3.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLN---IRWLRDQIGIVEQEPV--LF-STTIAENI-------RLGREEATMEDIV 67
Cdd:COG1123 306 TLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYssLNpRMTVGDIIaeplrlhGLLSRAERRERVA 385
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   68 QA-------AKDANAYnfimalPQQFdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALN 140
Cdd:COG1123 386 ELlervglpPDLADRY------PHELsgg-----------qrqRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLR 448
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 5923929  141 KIQ--HGHTIISVAHRLSTVRS-ADVIIGFEHGVAV 173
Cdd:COG1123 449 DLQreLGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
1-170 3.46e-12

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: 62.32  E-value: 3.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFS-TTIAENIRLgreEATMEDIVQAAKDANAYNFI 79
Cdd:cd03295  42 TTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPhMTVEENIAL---VPKLLKWPKEKIRERADELL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   80 --MALPQQfdTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRL 155
Cdd:cd03295 119 alVGLDPA--EFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDI 196
                       170
                ....*....|....*.
gi 5923929  156 -STVRSADVIIGFEHG 170
Cdd:cd03295 197 dEAFRLADRIAIMKNG 212
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
1-159 3.64e-12

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: 62.14  E-value: 3.64e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRD---QIGIVEQEPvlFST-----TIAENI---------------RLG 57
Cdd:cd03257  46 TLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrrkEIQMVFQDP--MSSlnprmTIGEQIaeplrihgklskkeaRKE 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   58 REEATMEDIVQAAKDANAYnfimalPQQFdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQG 137
Cdd:cd03257 124 AVLLLLVGVGLPEEVLNRY------PHELsgg-----------qrqRVAIARALALNPKLLIADEPTSALDVSVQAQILD 186
                       170       180
                ....*....|....*....|....
gi 5923929  138 ALNKIQ--HGHTIISVAHRLSTVR 159
Cdd:cd03257 187 LLKKLQeeLGLTLLFITHDLGVVA 210
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
1-170 1.21e-11

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 60.66  E-value: 1.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSL---NIRWLRDQIGIVEQEPVLFS-TTIAENI---RLGREEA--------TMED 65
Cdd:cd03256  42 TLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQIGMIFQQFNLIErLSVLENVlsgRLGRRSTwrslfglfPKEE 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   66 IVQAAKDANAYNFIMALPQQFDTLvgegggqmSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--Q 143
Cdd:cd03256 122 KQRALAALERVGLLDKAYQRADQL--------SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrE 193
                       170       180
                ....*....|....*....|....*...
gi 5923929  144 HGHTIISVAHRLSTVRS-ADVIIGFEHG 170
Cdd:cd03256 194 EGITVIVSLHQVDLAREyADRIVGLKDG 221
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
14-170 1.60e-11

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 60.82  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    14 EGMVTPDGHDI--RSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLG------REEATMEDIVQAA-KDANAYNfimalpq 84
Cdd:PRK14258  66 EGRVEFFNQNIyeRRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESAlKDADLWD------- 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    85 QFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALN--KIQHGHTIISVAHRLSTVRSAD 162
Cdd:PRK14258 139 EIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLS 218

                 ....*...
gi 5923929   163 VIIGFEHG 170
Cdd:PRK14258 219 DFTAFFKG 226
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
1-173 1.95e-11

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 60.01  E-value: 1.95e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDI--RSLNIRWLRDQIGIVEQEPVLFS-TTIAENIRLG--------REEAT---ME-- 64
Cdd:COG1126  42 TLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLFPhLTVLENVTLApikvkkmsKAEAEeraMEll 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   65 DIVQAAKDANAYnfimalP-------QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQG 137
Cdd:COG1126 122 ERVGLADKADAY------PaqlsggqQQ------------------RVAIARALAMEPKVMLFDEPTSALDPELVGEVLD 177
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 5923929  138 ALNKIQH-GHTIISVAHRLSTVRS-ADVIIGFEHGVAV 173
Cdd:COG1126 178 VMRDLAKeGMTMVVVTHEMGFAREvADRVVFMDGGRIV 215
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
104-173 2.05e-11

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 60.20  E-value: 2.05e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTV-RSADVIIGFEHGVAV 173
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDLAVVaHLCDRVAVMQNGRIV 218
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
104-158 3.14e-11

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: 59.47  E-value: 3.14e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTV 158
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLV 195
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
15-170 4.06e-11

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: 59.23  E-value: 4.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   15 GMVTPDGHDIR-----------SLNIRWLRDQIGIVEQEPVLFS-TTIAENIRLG-REEATMEDIVQAAKdanaynfIMA 81
Cdd:cd03297  45 GLEKPDGGTIVlngtvlfdsrkKINLPPQQRKIGLVFQQYALFPhLNVRENLAFGlKRKRNREDRISVDE-------LLD 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   82 LpQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ---HGHTIIsVAHRLSTV 158
Cdd:cd03297 118 L-LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKknlNIPVIF-VTHDLSEA 195
                       170
                ....*....|...
gi 5923929  159 -RSADVIIGFEHG 170
Cdd:cd03297 196 eYLADRIVVMEDG 208
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
1-164 4.15e-11

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: 59.58  E-value: 4.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWL----RDQIGIVEQEPVLF-STTIAENIRLG----------REEATMED 65
Cdd:cd03294  65 TLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLENVAFGlevqgvpraeREERAAEA 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   66 IVQAAKDANAYNFIMALP---QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI 142
Cdd:cd03294 145 LELVGLEGWEHKYPDELSggmQQ------------------RVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRL 206
                       170       180
                ....*....|....*....|....*
gi 5923929  143 Q--HGHTIISVAHRLS-TVRSADVI 164
Cdd:cd03294 207 QaeLQKTIVFITHDLDeALRLGDRI 231
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1-153 4.74e-11

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 59.33  E-value: 4.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRwlrdqIGIVEQEPVLFS-TTIAENIRLG----------REEATME--DIV 67
Cdd:COG1116  52 TLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----RGVVFQEPALLPwLTVLDNVALGlelrgvpkaeRRERAREllELV 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   68 QAAKDANAYnfimalP-------QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALN 140
Cdd:COG1116 127 GLAGFEDAY------PhqlsggmRQ------------------RVAIARALANDPEVLLMDEPFGALDALTRERLQDELL 182
                       170
                ....*....|....*
gi 5923929  141 KI--QHGHTIISVAH 153
Cdd:COG1116 183 RLwqETGKTVLFVTH 197
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
1-153 8.57e-11

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: 58.52  E-value: 8.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVL-FSTTIAENIRLGR---------EEATMEDIVQAA 70
Cdd:COG1120  42 TLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREAVEEA 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   71 -KDANAYNFIMalpQQFDTLvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHT 147
Cdd:COG1120 122 lERTGLEHLAD---RPVDELsgg--------erqRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRT 190

                ....*.
gi 5923929  148 IISVAH 153
Cdd:COG1120 191 VVMVLH 196
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
1-153 9.91e-11

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: 58.02  E-value: 9.91e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIrsLNIRWLRDQIGIVEQEPVLFS-TTIAENIRLG------------REEATMEDIV 67
Cdd:cd03300  41 TLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFPhLTVFENIAFGlrlkklpkaeikERVAEALDLV 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   68 QAAKDANAYNFIMALPQQfdtlvgegggqmsggqkQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--G 145
Cdd:cd03300 119 QLEGYANRKPSQLSGGQQ-----------------QRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelG 181

                ....*...
gi 5923929  146 HTIISVAH 153
Cdd:cd03300 182 ITFVFVTH 189
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
1-170 1.55e-10

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: 57.69  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929      1 TALQLIQRFYDPCEGMVTPDGHDIRSLN---IRWLRDQIGIVEQEPVLFS-TTIAENI---RLGREEA--------TMED 65
Cdd:TIGR02315  43 TLLRCINRLVEPSSGSILLEGTDITKLRgkkLRKLRRRIGMIFQHYNLIErLTVLENVlhgRLGYKPTwrsllgrfSEED 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     66 IVQAAKDANAYNFIMALPQQFDTLvgegggqmSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--Q 143
Cdd:TIGR02315 123 KERALSALERVGLADKAYQRADQL--------SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInkE 194
                         170       180
                  ....*....|....*....|....*...
gi 5923929    144 HGHTIISVAHRLSTVRS-ADVIIGFEHG 170
Cdd:TIGR02315 195 DGITVIINLHQVDLAKKyADRIVGLKAG 222
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1-153 1.83e-10

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 58.19  E-value: 1.83e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRwlRDQIGIVEQEPVLFS-TTIAENIRLG----------REEATME--DIV 67
Cdd:COG3842  46 TLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMVFQDYALFPhLTVAENVAFGlrmrgvpkaeIRARVAEllELV 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   68 QAAKDANAYnfIMALP---QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH 144
Cdd:COG3842 124 GLEGLADRY--PHQLSggqQQ------------------RVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQR 183
                       170
                ....*....|.
gi 5923929  145 --GHTIISVAH 153
Cdd:COG3842 184 elGITFIYVTH 194
cbiO PRK13637
energy-coupling factor transporter ATPase;
5-170 2.97e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 57.36  E-value: 2.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     5 LIQRF---YDPCEGMVTPDGHDI--RSLNIRWLRDQIGIVEQEP--VLFSTTIAENI-----RLGREEATMEDIVQAAKD 72
Cdd:PRK13637  49 LIQHLnglLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIEKDIafgpiNLGLSEEEIENRVKRAMN 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    73 anaynfIMALPqqFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVqgaLNKIQHGH-----T 147
Cdd:PRK13637 129 ------IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEI---LNKIKELHkeynmT 197
                        170       180
                 ....*....|....*....|....
gi 5923929   148 IISVAHRLSTV-RSADVIIGFEHG 170
Cdd:PRK13637 198 IILVSHSMEDVaKLADRIIVMNKG 221
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
1-165 4.13e-10

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 56.26  E-value: 4.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRLG---REEATMEDIVQAAKDAnayn 77
Cdd:PRK10247  48 TLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLIFPwqiRNQQPDPAIFLDDLER---- 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    78 fiMALPqqfDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRL 155
Cdd:PRK10247 124 --FALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDK 198
                        170
                 ....*....|
gi 5923929   156 STVRSADVII 165
Cdd:PRK10247 199 DEINHADKVI 208
cbiO PRK13642
energy-coupling factor transporter ATPase;
1-170 6.14e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 56.64  E-value: 6.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEP--VLFSTTIAENIRLGRE------EATMEDIVQAAKD 72
Cdd:PRK13642  48 TTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnQFVGATVEDDVAFGMEnqgiprEEMIKRVDEALLA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    73 ANAYNFIMALPQQFDTlvgegggqmsgGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGH--TIIS 150
Cdd:PRK13642 128 VNMLDFKTREPARLSG-----------GQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLS 196
                        170       180
                 ....*....|....*....|
gi 5923929   151 VAHRLSTVRSADVIIGFEHG 170
Cdd:PRK13642 197 ITHDLDEAASSDRILVMKAG 216
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
12-165 7.60e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 56.30  E-value: 7.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    12 PCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEP--VLFSTTIAENIRLGREEAT-----MEDIV-QAAKDANAYNFIMALP 83
Cdd:PRK13648  61 VKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPdnQFVGSIVKYDVAFGLENHAvpydeMHRRVsEALKQVDMLERADYEP 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    84 QQFDTlvgegggqmsgGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGH--TIISVAHRLSTVRSA 161
Cdd:PRK13648 141 NALSG-----------GQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEA 209

                 ....
gi 5923929   162 DVII 165
Cdd:PRK13648 210 DHVI 213
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
10-164 9.81e-10

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 56.18  E-value: 9.81e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   10 YDPCEGMVTPDGHDIRSLNIRWLRDQ-IGIVEQEPVLFST-TIAENIRLGRE--------EATMEDivQAAKDANAYNF- 78
Cdd:COG1129  54 YQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVPNlSVAENIFLGREprrgglidWRAMRR--RARELLARLGLd 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   79 ------IMALP---QQFdtlvgegggqmsggqkqrVAIARALIRKPKILLLDMATSALDnESEAKVqgaLNKI-----QH 144
Cdd:COG1129 132 idpdtpVGDLSvaqQQL------------------VEIARALSRDARVLILDEPTASLT-EREVER---LFRIirrlkAQ 189
                       170       180
                ....*....|....*....|.
gi 5923929  145 GHTIISVAHRLSTVRS-ADVI 164
Cdd:COG1129 190 GVAIIYISHRLDEVFEiADRV 210
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
1-165 1.27e-09

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: 55.20  E-value: 1.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLN---IRWLRDQIGIVEQEPVLF-STTIAENIRLG-RE-----EATMEDIVQAA 70
Cdd:cd03261  41 TLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMGMLFQSGALFdSLTVFENVAFPlREhtrlsEEEIREIVLEK 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   71 KDAnaynfiMALPQQFDTLVGEGGGQMSGgqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTI 148
Cdd:cd03261 121 LEA------VGLRGAEDLYPAELSGGMKK----RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKkeLGLTS 190
                       170
                ....*....|....*...
gi 5923929  149 ISVAHRLSTVRS-ADVII 165
Cdd:cd03261 191 IMVTHDLDTAFAiADRIA 208
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
1-165 1.64e-09

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: 53.94  E-value: 1.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSlNIRWLRDQIGIVEQEPVLFST-TIAENIRL--Greeatmedivqaakdanayn 77
Cdd:cd03230  41 TLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYENlTVRENLKLsgG-------------------- 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   78 fiMalpQQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLS 156
Cdd:cd03230 100 --M---KQ------------------RLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILE 156
                       170
                ....*....|
gi 5923929  157 TVRS-ADVII 165
Cdd:cd03230 157 EAERlCDRVA 166
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
1-170 1.77e-09

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 54.68  E-value: 1.77e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLN---IRWLRDQIGIVEQEPVLFS-TTIAENI---RLGREEA--------TMED 65
Cdd:COG3638  44 TLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRRIGMIFQQFNLVPrLSVLTNVlagRLGRTSTwrsllglfPPED 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   66 IVQAAKdanaynfimALP-------------------QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSA 126
Cdd:COG3638 124 RERALE---------ALErvgladkayqradqlsggqQQ------------------RVAIARALVQEPKLILADEPVAS 176
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 5923929  127 LDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRS-ADVIIGFEHG 170
Cdd:COG3638 177 LDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRyADRIIGLRDG 223
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
12-160 1.80e-09

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 55.47  E-value: 1.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   12 PCEGMVTPDGHDIRSLNIRWLRD---QIGIVEQEPVLFST-TIAENIRL-----GREEATMEDIVQ--------AAKdAN 74
Cdd:COG1135  57 PTSGSVLVDGVDLTALSERELRAarrKIGMIFQHFNLLSSrTVAENVALpleiaGVPKAEIRKRVAellelvglSDK-AD 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   75 AYnfimalP-------QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHG 145
Cdd:COG1135 136 AY------PsqlsggqKQ------------------RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInrELG 191
                       170
                ....*....|....*
gi 5923929  146 HTIISVAHRLSTVRS 160
Cdd:COG1135 192 LTIVLITHEMDVVRR 206
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
29-173 3.93e-09

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 53.99  E-value: 3.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    29 IRWLRDQIGIVEQEPVLFS-TTIAENIRLG--------REEATMEDIVQAAK-----DANAYNFIMALPQQfdtlvgegg 94
Cdd:PRK11264  80 IRQLRQHVGFVFQNFNLFPhRTVLENIIEGpvivkgepKEEATARARELLAKvglagKETSYPRRLSGGQQ--------- 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    95 gqmsggqkQRVAIARALIRKPKILLLDMATSALDNESEAKVqgaLNKI----QHGHTIISVAHRLSTVRS-ADVIIGFEH 169
Cdd:PRK11264 151 --------QRVAIARALAMRPEVILFDEPTSALDPELVGEV---LNTIrqlaQEKRTMVIVTHEMSFARDvADRAIFMDQ 219

                 ....
gi 5923929   170 GVAV 173
Cdd:PRK11264 220 GRIV 223
cbiO PRK13640
energy-coupling factor transporter ATPase;
14-170 4.91e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 54.04  E-value: 4.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    14 EGMVTPDGHDIRSLNIRWLRDQIGIVEQEP--VLFSTTIAENIRLGRE-----EATMEDIV-QAAKDANAYNFIMALPQQ 85
Cdd:PRK13640  64 NSKITVDGITLTAKTVWDIREKVGIVFQNPdnQFVGATVGDDVAFGLEnravpRPEMIKIVrDVLADVGMLDYIDSEPAN 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    86 FDTlvgegggqmsgGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTVRSADV 163
Cdd:PRK13640 144 LSG-----------GQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQ 212

                 ....*..
gi 5923929   164 IIGFEHG 170
Cdd:PRK13640 213 VLVLDDG 219
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-170 5.38e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 53.58  E-value: 5.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEP--VLFSTTIAENIRLGRE------EATMEDIVQAAKD 72
Cdd:PRK13650  48 TTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdnQFVGATVEDDVAFGLEnkgiphEEMKERVNEALEL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    73 ANAYNFIMALPQQFDTlvgegggqmsgGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIIS 150
Cdd:PRK13650 128 VGMQDFKEREPARLSG-----------GQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIrdDYQMTVIS 196
                        170       180
                 ....*....|....*....|
gi 5923929   151 VAHRLSTVRSADVIIGFEHG 170
Cdd:PRK13650 197 ITHDLDEVALSDRVLVMKNG 216
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
12-165 6.68e-09

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: 53.06  E-value: 6.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   12 PCEGMVTPDGHDIRSLN---IRWLRDQIGIVEQEPVLFST-TIAENIRLG-RE-----EATMEDIVQAAKDA----NAYN 77
Cdd:COG1127  57 PDSGEILVDGQDITGLSekeLYELRRRIGMLFQGGALFDSlTVFENVAFPlREhtdlsEAEIRELVLEKLELvglpGAAD 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   78 FI-------MAlpqqfdtlvgegggqmsggqkQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTI 148
Cdd:COG1127 137 KMpselsggMR---------------------KRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTS 195
                       170
                ....*....|....*...
gi 5923929  149 ISVAHRLSTVRS-ADVII 165
Cdd:COG1127 196 VVVTHDLDSAFAiADRVA 213
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
101-160 6.68e-09

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 53.17  E-value: 6.68e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5923929  101 QKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRS 160
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVRE 204
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
1-160 7.64e-09

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 53.65  E-value: 7.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLN---IRWLRDQIGIVEQE-PVLFSTTIAENIRL-----GREEATME------- 64
Cdd:PRK11153  46 TLIRCINLLERPTSGRVLVDGQDLTALSekeLRKARRQIGMIFQHfNLLSSRTVFDNVALplelaGTPKAEIKarvtell 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    65 DIVQAAKDANAYnfimalPQQFDtlvgegggqmsGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH 144
Cdd:PRK11153 126 ELVGLSDKADRY------PAQLS-----------GGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINR 188
                        170
                 ....*....|....*...
gi 5923929   145 --GHTIISVAHRLSTVRS 160
Cdd:PRK11153 189 elGLTIVLITHEMDVVKR 206
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
104-170 8.00e-09

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 53.14  E-value: 8.00e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLS-TVRSADVIIGFEHG 170
Cdd:PRK11247 141 RVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEG 210
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
36-170 1.40e-08

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: 51.70  E-value: 1.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   36 IGIVEQEPVLFSTTIAENIRLGRE--EATMEDIVQAA---KDanaynfIMALPQQFDTLVGEGGGQMSGGQKQRVAIARA 110
Cdd:cd03250  68 IAYVSQEPWIQNGTIRENILFGKPfdEERYEKVIKACalePD------LEILPDGDLTEIGEKGINLSGGQKQRISLARA 141
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5923929  111 LIRKPKILLLDMATSALDNESEAK-----VQGALnkiQHGHTIISVAHRLSTVRSADVIIGFEHG 170
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHifencILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNG 203
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
104-173 1.47e-08

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: 52.76  E-value: 1.47e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTVRS-ADVIIGFEHGVAV 173
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQreHGLAYLFISHDLAVVRAlAHRVMVMKDGKVV 505
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
10-173 1.75e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 52.43  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    10 YDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEP--VLFSTTIAE-------NIRLGREEatMEDIVQAAKDA-NAYNFI 79
Cdd:PRK13647  55 YLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDdvafgpvNMGLDKDE--VERRVEEALKAvRMWDFR 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    80 MALPQQFDtlvgegggqmsGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTV 158
Cdd:PRK13647 133 DKPPYHLS-----------YGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLA 201
                        170
                 ....*....|....*.
gi 5923929   159 RS-ADVIIGFEHGVAV 173
Cdd:PRK13647 202 AEwADQVIVLKEGRVL 217
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
104-160 1.94e-08

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 52.40  E-value: 1.94e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 5923929   104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTI--ISVAHRLSTVRS 160
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRA 491
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
1-173 2.34e-08

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 52.34  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRD----QIGIVEQEPVLFS-TTIAENIRLGREEATM------EDIVQA 69
Cdd:PRK10070  69 TMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTVLDNTAFGMELAGInaeerrEKALDA 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    70 AKDANAYNFIMALPQQFDTlvgegggqmsgGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHT 147
Cdd:PRK10070 149 LRQVGLENYAHSYPDELSG-----------GMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQakHQRT 217
                        170       180
                 ....*....|....*....|....*..
gi 5923929   148 IISVAHRL-STVRSADVIIGFEHGVAV 173
Cdd:PRK10070 218 IVFISHDLdEAMRIGDRIAIMQNGEVV 244
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
5-159 3.16e-08

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 51.66  E-value: 3.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    5 LIQRFYDPCEGMVTPDGHDIRSLN---IRWLRDQIGIVEQEPvlFS---------TTIAENIRLGR--EEATMEDIVQA- 69
Cdd:COG4608  63 LLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP--YAslnprmtvgDIIAEPLRIHGlaSKAERRERVAEl 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   70 -------AKDANAYnfimalPQQFdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI 142
Cdd:COG4608 141 lelvglrPEHADRY------PHEFsgg-----------qrqRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDL 203
                       170
                ....*....|....*....
gi 5923929  143 Q--HGHTIISVAHRLSTVR 159
Cdd:COG4608 204 QdeLGLTYLFISHDLSVVR 222
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
1-170 4.21e-08

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: 50.57  E-value: 4.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRwlRDQIGIVEQEPVLFS-TTIAENIRLGR------EEATMEDIVQAAKDA 73
Cdd:cd03298  39 TLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGLGLspglklTAEDRQAIEVALARV 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   74 NAYNFIMALPQQFDTlvgegggqmsgGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISV 151
Cdd:cd03298 117 GLAGLEKRLPGELSG-----------GERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMV 185
                       170       180
                ....*....|....*....|
gi 5923929  152 AHRLSTVRS-ADVIIGFEHG 170
Cdd:cd03298 186 THQPEDAKRlAQRVVFLDNG 205
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
104-173 5.30e-08

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: 49.73  E-value: 5.30e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ-HGHTIISVAHRLSTVRS-ADVIIGFEHGVAV 173
Cdd:cd03216  90 MVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
104-159 5.62e-08

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 50.86  E-value: 5.62e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 5923929   104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVR 159
Cdd:PRK15079 169 RIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVK 226
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
11-165 6.74e-08

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 50.78  E-value: 6.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    11 DPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEP--VLFSTTIA-------ENIRLGREEaTMEDIVQAAKDANAYNFIMA 81
Cdd:PRK13635  58 LPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPdnQFVGATVQddvafglENIGVPREE-MVERVDQALRQVGMEDFLNR 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    82 LPQQFDTlvgegggqmsgGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVR 159
Cdd:PRK13635 137 EPHRLSG-----------GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAA 205

                 ....*.
gi 5923929   160 SADVII 165
Cdd:PRK13635 206 QADRVI 211
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
1-153 7.67e-08

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: 50.10  E-value: 7.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLN---IRWLRDQIGIVEQEPVLFST-TIAENIRLGRE--EATMEDIVQAAKDAN 74
Cdd:cd03292  42 TLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRKRVPAAL 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   75 AynfIMALPQQFDTLvgegGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAH 153
Cdd:cd03292 122 E---LVGLSHKHRAL----PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATH 194
cbiO PRK13641
energy-coupling factor transporter ATPase;
5-170 7.82e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 50.60  E-value: 7.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     5 LIQRF---YDPCEGMVTPDGHDIR----SLNIRWLRDQIGIVEQ--EPVLFSTTIAENIRLGREEATMEDivQAAKDAnA 75
Cdd:PRK13641  49 LMQHFnalLKPSSGTITIAGYHITpetgNKNLKKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSE--DEAKEK-A 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    76 YNFI--MALPQQfdtLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKV-QGALNKIQHGHTIISVA 152
Cdd:PRK13641 126 LKWLkkVGLSED---LISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVT 202
                        170
                 ....*....|....*....
gi 5923929   153 HRLSTV-RSADVIIGFEHG 170
Cdd:PRK13641 203 HNMDDVaEYADDVLVLEHG 221
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
20-172 9.27e-08

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 50.09  E-value: 9.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    20 DGHDIR--SLNIRWLRDQIGIVEQEPVLF-STTIAENIRLG--------REEA-----TMEDIVQAAKDANAYNFIMALP 83
Cdd:PRK09493  61 DGLKVNdpKVDERLIRQEAGMVFQQFYLFpHLTALENVMFGplrvrgasKEEAekqarELLAKVGLAERAHHYPSELSGG 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    84 QQfdtlvgegggqmsggqkQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRlstvrsad 162
Cdd:PRK09493 141 QQ-----------------QRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLaEEGMTMVIVTHE-------- 195
                        170
                 ....*....|
gi 5923929   163 viIGFEHGVA 172
Cdd:PRK09493 196 --IGFAEKVA 203
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
104-170 1.06e-07

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 50.01  E-value: 1.06e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH-GHTIISVAHRLSTVRS-ADVIIGFEHG 170
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKvASQVVYMEKG 217
cbiO PRK13649
energy-coupling factor transporter ATPase;
1-170 1.15e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 50.13  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSL----NIRWLRDQIGIVEQ--EPVLFSTTIAENIRLGREE--ATMEDIVQAAKD 72
Cdd:PRK13649  48 TIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALARE 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    73 AnaynfiMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISV 151
Cdd:PRK13649 128 K------LALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLV 201
                        170       180
                 ....*....|....*....|
gi 5923929   152 AHRLSTVRS-ADVIIGFEHG 170
Cdd:PRK13649 202 THLMDDVANyADFVYVLEKG 221
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
1-165 1.18e-07

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 49.68  E-value: 1.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRdQIGIVEQEPVLFST-TIAENIRL-----GREEATMEDIVQAAKDA- 73
Cdd:COG1131  41 TTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR-RIGYVPQEPALYPDlTVRENLRFfarlyGLPRKEARERIDELLELf 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   74 ----NAYNFIMALP---QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHG 145
Cdd:COG1131 120 gltdAADRKVGTLSggmKQ------------------RLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaAEG 181
                       170       180
                ....*....|....*....|.
gi 5923929  146 HTIISVAHRLSTV-RSADVII 165
Cdd:COG1131 182 KTVLLSTHYLEEAeRLCDRVA 202
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
1-165 1.23e-07

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: 48.97  E-value: 1.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQepvlfsttiaenirlgreeatmedivqAAKDANAYNFIM 80
Cdd:cd03214  40 TLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ---------------------------ALELLGLAHLAD 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   81 alpQQFDTLvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLS-T 157
Cdd:cd03214  93 ---RPFNELsgg--------erqRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlA 161

                ....*...
gi 5923929  158 VRSADVII 165
Cdd:cd03214 162 ARYADRVI 169
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
1-153 1.31e-07

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: 49.65  E-value: 1.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRwlRDQIGIVEQEPVLFS-TTIAENIRLG-REEATMEDIVQAAKDANAYNF 78
Cdd:cd03296  43 TLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRhMTVFDNVAFGlRVKPRSERPPEAEIRAKVHEL 120
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5923929   79 IMALpqQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAH 153
Cdd:cd03296 121 LKLV--QLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTH 195
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
12-164 1.37e-07

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: 49.01  E-value: 1.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   12 PCEGMVTPDGHDIRSLNIRWlRDQIGIVEQEPVLFST-TIAENI----RLGREEATMEDIVQAAKdanaynfIMALPQQF 86
Cdd:COG4133  54 PSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKPElTVRENLrfwaALYGLRADREAIDEALE-------AVGLAGLA 125
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5923929   87 DTLVGEgggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNK-IQHGHTIISVAHRLSTVRSADVI 164
Cdd:COG4133 126 DLPVRQlsag----qkrRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
104-153 1.42e-07

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 49.95  E-value: 1.42e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 5923929   104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAH 153
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTH 203
cbiO PRK13646
energy-coupling factor transporter ATPase;
5-173 1.79e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 49.39  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     5 LIQRF---YDPCEGMVTPDG----HDIRSLNIRWLRDQIGIVEQ--EPVLFSTTIAENIRLGREEATMEdiVQAAKDaNA 75
Cdd:PRK13646  49 LIQNInalLKPTTGTVTVDDititHKTKDKYIRPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN--LDEVKN-YA 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    76 YNFIMALPQQFDTLvGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAH 153
Cdd:PRK13646 126 HRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSH 204
                        170       180
                 ....*....|....*....|.
gi 5923929   154 RLSTV-RSADVIIGFEHGVAV 173
Cdd:PRK13646 205 DMNEVaRYADEVIVMKEGSIV 225
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
104-159 2.72e-07

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 48.47  E-value: 2.72e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 5923929   104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH-GHTIISVAHRLSTVR 159
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVAR 205
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
12-153 4.15e-07

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: 48.20  E-value: 4.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   12 PCEGMVTPDGHDIRSLN----IRWLRDQIGIVEQ-EPVLFSTTIAENIRLGREEATMEDIVQAAKD----------ANAY 76
Cdd:COG4181  64 PTSGTVRLAGQDLFALDedarARLRARHVGFVFQsFQLLPTLTALENVMLPLELAGRRDARARARAllervglghrLDHY 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   77 nfimalP-------QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQG---ALNKiQHGH 146
Cdd:COG4181 144 ------PaqlsggeQQ------------------RVALARAFATEPAILFADEPTGNLDAATGEQIIDllfELNR-ERGT 198

                ....*..
gi 5923929  147 TIISVAH 153
Cdd:COG4181 199 TLVLVTH 205
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
1-153 4.76e-07

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: 47.64  E-value: 4.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSlniRWLRDQIGIVEQEP--VLFSTTIAENIRLGREEA--TMEDIVQAAKDANAY 76
Cdd:cd03226  41 TLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQDVdyQLFTDSVREELLLGLKELdaGNEQAETVLKDLDLY 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   77 NFIMALP-------QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ-HGHTI 148
Cdd:cd03226 118 ALKERHPlslsggqKQ------------------RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAaQGKAV 179

                ....*
gi 5923929  149 ISVAH 153
Cdd:cd03226 180 IVITH 184
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
104-153 5.60e-07

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: 47.63  E-value: 5.60e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAH 153
Cdd:cd03301 138 RVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQqrLGTTTIYVTH 189
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
28-158 5.94e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 47.77  E-value: 5.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    28 NIRWLRDQIGIVEQ--EPVLFSTTIAENIRLGREEATMEDiVQAAKDANAYNFIMALPQQFdtlVGEGGGQMSGGQKQRV 105
Cdd:PRK13651  99 KIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESY---LQRSPFELSGGQKRRV 174
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 5923929   106 AIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTV 158
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNV 228
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
104-169 6.24e-07

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: 47.77  E-value: 6.24e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLStvrsaDVIIGFEH 169
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVE-----EIPPGITH 212
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
1-128 6.78e-07

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 47.44  E-value: 6.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIrwlrDQ--IGIVEQEPVLFS-TTIAENIRLGRE------EATMEDIVQAAK 71
Cdd:COG3840  40 TLLNLIAGFLPPDSGRILWNGQDLTALPP----AErpVSMLFQENNLFPhLTVAQNIGLGLRpglkltAEQRAQVEQALE 115
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5923929   72 DANAYNFIMALP-------QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALD 128
Cdd:COG3840 116 RVGLAGLLDRLPgqlsggqRQ------------------RVALARCLVRKRPILLLDEPFSALD 161
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
14-153 7.53e-07

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 47.53  E-value: 7.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    14 EGMVTPDGHDIRSLNIRWL--RDQIGIVEQEPVLFS-TTIAENIRLG-------REEATMEDIVQ-AAKDAnaynfimAL 82
Cdd:PRK14267  63 EGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFPhLTIYDNVAIGvklnglvKSKKELDERVEwALKKA-------AL 135
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5923929    83 PQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAH 153
Cdd:PRK14267 136 WDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
14-155 8.27e-07

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 47.47  E-value: 8.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    14 EGMVTPDGHDIRSLNIR--WLRDQIGIVEQEPVLFSTTIAENIRLGRE----EATMEDIVQAA-KDAnaynfimALPQQF 86
Cdd:PRK14243  69 EGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPKSIYDNIAYGARingyKGDMDELVERSlRQA-------ALWDEV 141
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5923929    87 DTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRL 155
Cdd:PRK14243 142 KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
1-130 8.30e-07

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 47.18  E-value: 8.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIR---WLRDQIGIVEQEP-VLFSTTIAEN--IRLGREEATMEDI---VQAAK 71
Cdd:PRK10908  43 TLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRRQIGMIFQDHhLLMDRTVYDNvaIPLIIAGASGDDIrrrVSAAL 122
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5923929    72 DA-----NAYNFIMALP---QQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNE 130
Cdd:PRK10908 123 DKvglldKAKNFPIQLSggeQQ------------------RVGIARAVVNKPAVLLADEPTGNLDDA 171
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
4-153 8.59e-07

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 47.21  E-value: 8.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     4 QLIQRFYDP-CEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFST-TIAENIRLG-------REEATMEDIVQAAKDAn 74
Cdd:PRK14247  51 RLIELYPEArVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNlSIFENVALGlklnrlvKSKKELQERVRWALEK- 129
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5923929    75 aynfiMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAH 153
Cdd:PRK14247 130 -----AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
1-169 8.83e-07

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 47.27  E-value: 8.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSL-------------NIRWLRDQIGIVEQEPVLFS-TTIAENIR--------LGR 58
Cdd:PRK10619  46 TFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVFQHFNLWShMTVLENVMeapiqvlgLSK 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    59 EEATMEDIVQAAK---DANA---YNFIMALPQQfdtlvgegggqmsggqkQRVAIARALIRKPKILLLDMATSALDNESE 132
Cdd:PRK10619 126 QEARERAVKYLAKvgiDERAqgkYPVHLSGGQQ-----------------QRVSIARALAMEPEVLLFDEPTSALDPELV 188
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 5923929   133 AKVQGALNKI-QHGHTIISVAHRLSTVRSADVIIGFEH 169
Cdd:PRK10619 189 GEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLH 226
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
28-170 1.17e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 47.15  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    28 NIRWLRDQIGIVEQEP--VLFSTTIAENIRLGrEEATMEDIVQAAKDANAYNFIMALPQQFdtlVGEGGGQMSGGQKQRV 105
Cdd:PRK13631 110 NFKELRRRVSMVFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKMGLDDSY---LERSPFGLSGGQKRRV 185
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5923929   106 AIARALIRKPKILLLDMATSALDNESEAK-VQGALNKIQHGHTIISVAHRLSTV-RSADVIIGFEHG 170
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKG 252
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
104-159 1.35e-06

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 46.97  E-value: 1.35e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTVR 159
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQreLGLAILFITHDLGVVA 215
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
104-153 1.37e-06

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 46.66  E-value: 1.37e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALN-KIQHGHTIISVAH 153
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEeAKARGTAIIGIFH 210
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
1-164 2.02e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 46.19  E-value: 2.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRF---YDP---CEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFS-TTIAENIRLGREEATMEDIVQAAKDA 73
Cdd:PRK14246  51 TLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPhLSIYDNIAYPLKSHGIKEKREIKKIV 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    74 NAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAH 153
Cdd:PRK14246 131 EECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSH 210
                        170
                 ....*....|..
gi 5923929   154 RLSTV-RSADVI 164
Cdd:PRK14246 211 NPQQVaRVADYV 222
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
104-162 2.47e-06

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 45.30  E-value: 2.47e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH-GHTIISVAHRLSTVRSAD 162
Cdd:NF040873 127 RALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRAD 186
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
1-128 3.01e-06

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 45.87  E-value: 3.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWlRDqIGIVEQEPVLFS-TTIAENI-----RLGREEatmEDIVQAAKDAN 74
Cdd:PRK11432  47 TVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RD-ICMVFQSYALFPhMSLGENVgyglkMLGVPK---EERKQRVKEAL 121
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5923929    75 AY-----------NFIMALPQQfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALD 128
Cdd:PRK11432 122 ELvdlagfedryvDQISGGQQQ------------------RVALARALILKPKVLLFDEPLSNLD 168
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
15-170 3.09e-06

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 45.87  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     15 GMVTPDGHDIrSLNIRWLRD------------QIGIVEQEPVLFS-TTIAENIRLGREEATMEDiVQAAKDAnaynfIMA 81
Cdd:TIGR02142  45 GLTRPDEGEI-VLNGRTLFDsrkgiflppekrRIGYVFQEARLFPhLSVRGNLRYGMKRARPSE-RRISFER-----VIE 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     82 LpQQFDTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIqHGHT---IISVAHRLSTV 158
Cdd:TIGR02142 118 L-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERL-HAEFgipILYVSHSLQEV 195
                         170
                  ....*....|...
gi 5923929    159 -RSADVIIGFEHG 170
Cdd:TIGR02142 196 lRLADRVVVLEDG 208
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
104-165 3.40e-06

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 45.87  E-value: 3.40e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5923929   104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRSADVII 165
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVI 214
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
12-170 4.06e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 45.56  E-value: 4.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    12 PCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEP--VLFSTTIAENI-----RLGREEATMEDIVQAA-KDANAYNFIMALP 83
Cdd:PRK13652  56 PTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQDIafgpiNLGLDEETVAHRVSSAlHMLGLEELRDRVP 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    84 QQFDTlvgegggqmsgGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRS- 160
Cdd:PRK13652 136 HHLSG-----------GEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpeTYGMTVIFSTHQLDLVPEm 204
                        170
                 ....*....|
gi 5923929   161 ADVIIGFEHG 170
Cdd:PRK13652 205 ADYIYVMDKG 214
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
104-135 5.00e-06

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 45.14  E-value: 5.00e-06
                        10        20        30
                ....*....|....*....|....*....|..
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDneseAKV 135
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALD----AKV 168
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
36-164 6.45e-06

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 45.02  E-value: 6.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   36 IGIVEQEPVLFST-TIAENIRLGREEATME--DIVQAAKD----ANAYNF-------IMALP---QQfdtlvgegggqms 98
Cdd:COG3845  82 IGMVHQHFMLVPNlTVAENIVLGLEPTKGGrlDRKAARARirelSERYGLdvdpdakVEDLSvgeQQ------------- 148
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5923929   99 ggqkqRVAIARALIRKPKILLLDMATSAL-DNESEaKVQGALNKI-QHGHTIISVAHRLSTVRS-ADVI 164
Cdd:COG3845 149 -----RVEILKALYRGARILILDEPTAVLtPQEAD-ELFEILRRLaAEGKSIIFITHKLREVMAiADRV 211
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
104-153 6.79e-06

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: 44.76  E-value: 6.79e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 5923929    104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAH 153
Cdd:TIGR01184 122 RVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIweEHRVTVLMVTH 173
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
104-153 6.89e-06

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 45.06  E-value: 6.89e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAH 153
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRrlGTTTIYVTH 192
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
104-173 7.15e-06

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: 44.28  E-value: 7.15e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESeakVQGALNKIQH----GHTIISVAHRLSTVRS-ADVIIGFEHGVAV 173
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMA---TRALREFIRQlralGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
1-170 1.24e-05

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: 43.96  E-value: 1.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRwLRDQIGIVE--QEPVLFST-TIAENIRLGREEATMEDIVQAA-----KD 72
Cdd:cd03219  41 TLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPElTVLENVMVAAQARTGSGLLLARarreeRE 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   73 ANAYNF----IMALPQQFDTLVGEGGGQMSGgqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHT 147
Cdd:cd03219 120 ARERAEelleRVGLADLADRPAGELSYGQQR----RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELrERGIT 195
                       170       180
                ....*....|....*....|....
gi 5923929  148 IISVAHRLSTVRS-ADVIIGFEHG 170
Cdd:cd03219 196 VLLVEHDMDVVMSlADRVTVLDQG 219
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
1-128 1.46e-05

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 43.80  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRwlRDQIGIVEQEPVLFS-TTIAENIRLG---------REEATMEDIvqaA 70
Cdd:PRK10771  40 TLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGlnpglklnaAQREKLHAI---A 114
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 5923929    71 KDANAYNFIMALPQQFDTlvgegggqmsgGQKQRVAIARALIRKPKILLLDMATSALD 128
Cdd:PRK10771 115 RQMGIEDLLARLPGQLSG-----------GQRQRVALARCLVREQPILLLDEPFSALD 161
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
102-170 1.54e-05

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: 42.44  E-value: 1.54e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5923929  102 KQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQhgHTIISVAH-R--LSTVrsADVIIGFEHG 170
Cdd:cd03221  76 KMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYP--GTVILVSHdRyfLDQV--ATKIIELEDG 143
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
104-159 1.59e-05

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 43.80  E-value: 1.59e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 5923929   104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVR 159
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQelGLSYVFISHDLSVVE 219
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
15-159 1.66e-05

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 43.89  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    15 GMVTPDGHDIRSLNIRWLR------DQIGI--VEQEPVLF-STTIAENI--RLGREEATMEDIVQaakdanaynFIMALP 83
Cdd:PRK15439  59 GIVPPDSGTLEIGGNPCARltpakaHQLGIylVPQEPLLFpNLSVKENIlfGLPKRQASMQKMKQ---------LLAALG 129
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5923929    84 QQFDTLVGEGGGQMSGGQKqrVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ-HGHTIISVAHRLSTVR 159
Cdd:PRK15439 130 CQLDLDSSAGSLEVADRQI--VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLaQGVGIVFISHKLPEIR 204
cbiO PRK13643
energy-coupling factor transporter ATPase;
1-170 2.48e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 43.18  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLN----IRWLRDQIGIVEQEP--VLFSTTIAENIRLGREEATMEDiVQAAKDAN 74
Cdd:PRK13643  47 TLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPK-EKAEKIAA 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    75 AYNFIMALPQQFdtlVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAH 153
Cdd:PRK13643 126 EKLEMVGLADEF---WEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTH 202
                        170
                 ....*....|....*...
gi 5923929   154 RLSTVRS-ADVIIGFEHG 170
Cdd:PRK13643 203 LMDDVADyADYVYLLEKG 220
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
104-158 2.54e-05

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 43.17  E-value: 2.54e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 5923929   104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTV 158
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVV 225
cbiO PRK13644
energy-coupling factor transporter ATPase;
105-170 4.48e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 42.28  E-value: 4.48e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5923929   105 VAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLSTVRSADVIIGFEHG 170
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRG 211
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
12-170 4.62e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 42.38  E-value: 4.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    12 PCEGMVTPDGHDIRSLNIRW-LRDQIGIVEQEP--VLFSTTIAENIRLGRE------EATMEDIVQAAKDANAYNFIMAL 82
Cdd:PRK13633  62 PSEGKVYVDGLDTSDEENLWdIRNKAGMVFQNPdnQIVATIVEEDVAFGPEnlgippEEIRERVDESLKKVGMYEYRRHA 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    83 PQQFDTlvgegggqmsgGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRS 160
Cdd:PRK13633 142 PHLLSG-----------GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVE 210
                        170
                 ....*....|
gi 5923929   161 ADVIIGFEHG 170
Cdd:PRK13633 211 ADRIIVMDSG 220
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
1-153 6.47e-05

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 42.13  E-value: 6.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIrSLNIRWLRdQIGIVEQEPVLFS-TTIAENIRLGREEatmeDIVQAAKDANAYNFI 79
Cdd:PRK11607  60 TLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQR-PINMMFQSYALFPhMTVEQNIAFGLKQ----DKLPKAEIASRVNEM 133
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5923929    80 MALP--QQFdtlVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAH 153
Cdd:PRK11607 134 LGLVhmQEF---AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDIleRVGVTCVMVTH 208
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
104-128 6.61e-05

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: 42.01  E-value: 6.61e-05
                        10        20
                ....*....|....*....|....*
gi 5923929  104 RVAIARALIRKPKILLLDMATSALD 128
Cdd:COG4148 141 RVAIGRALLSSPRLLLMDEPLAALD 165
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
36-153 8.09e-05

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 41.84  E-value: 8.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     36 IGIVEQEPVLFST-TIAENI-----------------------------RLGREEATMEDIVQAAkdaNAYNFIMALPQQ 85
Cdd:TIGR03719  70 VGYLPQEPQLDPTkTVRENVeegvaeikdaldrfneisakyaepdadfdKLAAEQAELQEIIDAA---DAWDLDSQLEIA 146
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5923929     86 FDTLVGEGGGQMSGGQ----KQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALnkIQHGHTIISVAH 153
Cdd:TIGR03719 147 MDALRCPPWDADVTKLsggeRRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL--QEYPGTVVAVTH 216
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
104-173 8.77e-05

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 41.36  E-value: 8.77e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAHRLSTVRS-ADVIIGFEHGVAV 173
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQekLGISYIYVSQHLGIVKHiSDKVLVMHQGEVV 229
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
21-128 8.89e-05

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 41.61  E-value: 8.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    21 GHDIRSLNIRwlRDQIGIVEQEPVLFS-TTIAENIRLG------REEATME----------DIVQAAKDANAYnfimalP 83
Cdd:PRK10851  63 GTDVSRLHAR--DRKVGFVFQHYALFRhMTVFDNIAFGltvlprRERPNAAaikakvtqllEMVQLAHLADRY------P 134
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 5923929    84 QQFDTlvgegggqmsgGQKQRVAIARALIRKPKILLLDMATSALD 128
Cdd:PRK10851 135 AQLSG-----------GQKQRVALARALAVEPQILLLDEPFGALD 168
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
12-153 9.25e-05

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: 41.20  E-value: 9.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   12 PCEGMVTPDGHDIRSlNIRWLRDQIGIVEQEPvlfsttIAENIRLGREEATMEDIVQAAKDANAYNFI------MALPQQ 85
Cdd:cd03265  52 PTSGRATVAGHDVVR-EPREVRRRIGIVFQDL------SVDDELTGWENLYIHARLYGVPGAERRERIdelldfVGLLEA 124
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   86 FDTLVGEGGGQMSGgqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ--HGHTIISVAH 153
Cdd:cd03265 125 ADRLVKTYSGGMRR----RLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTH 190
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
1-170 1.52e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 40.77  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDI----RSLNIRWLRDQIGIVEQ--EPVLFSTTIAENIRLGREE--ATMEDIVQAAKD 72
Cdd:PRK13634  48 TLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKARE 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    73 ANAynfIMALPQQfdtLVGEGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIIS 150
Cdd:PRK13634 128 MIE---LVGLPEE---LLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVL 201
                        170       180
                 ....*....|....*....|.
gi 5923929   151 VAHRLSTV-RSADVIIGFEHG 170
Cdd:PRK13634 202 VTHSMEDAaRYADQIVVMHKG 222
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
14-155 1.78e-04

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 41.05  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929      14 EGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRlGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEG 93
Cdd:TIGR01271 1272 EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDG 1350
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5923929      94 GGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRL 155
Cdd:TIGR01271 1351 GYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
105-170 1.82e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 40.97  E-value: 1.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    105 VAIARALIRKPK---ILLLDMATSALDNESEAKVQGALNK-IQHGHTIISVAHRLSTVRSADVIIGFEHG 170
Cdd:PRK00635 1708 IKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLIEMGPG 1777
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
104-170 1.85e-04

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: 40.00  E-value: 1.85e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929  104 RVAIARALIRKPK--ILLLDMATSALDNESEAKVQGALNK-IQHGHTIISVAHRLSTVRSADVIIGFEHG 170
Cdd:cd03238  95 RVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPG 164
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
14-164 2.00e-04

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 40.68  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    14 EGMVTPDGHDIRSLNIRWL-RDQIGIVEQEPVLFST-TIAENIRLGRE--------EATM----EDIVQAAK-DANAYNF 78
Cdd:PRK13549  61 EGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKElSVLENIFLGNEitpggimdYDAMylraQKLLAQLKlDINPATP 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    79 IMALP---QQFdtlvgegggqmsggqkqrVAIARALIRKPKILLLDMATSALdNESEAKVqgALNKIQ----HGHTIISV 151
Cdd:PRK13549 141 VGNLGlgqQQL------------------VEIAKALNKQARLLILDEPTASL-TESETAV--LLDIIRdlkaHGIACIYI 199
                        170
                 ....*....|....
gi 5923929   152 AHRLSTVRS-ADVI 164
Cdd:PRK13549 200 SHKLNEVKAiSDTI 213
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
104-170 2.35e-04

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 40.38  E-value: 2.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLS-TVRSADVIIGFEHG 170
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQG 229
cbiO PRK13645
energy-coupling factor transporter ATPase;
29-170 2.81e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 39.99  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    29 IRWLRDQIGIVEQEP--VLFSTTIAENIRLGREEATmEDIVQAAKDANAYNFIMALPQQFdtlVGEGGGQMSGGQKQRVA 106
Cdd:PRK13645  85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVA 160
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5923929   107 IARALIRKPKILLLDMATSALDNESEAKVQG---ALNKiQHGHTIISVAHRLSTV-RSADVIIGFEHG 170
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINlfeRLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEG 227
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
104-173 2.81e-04

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 40.46  E-value: 2.81e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5923929   104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVRS-ADVIIGFEHGVAV 173
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCV 236
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
104-160 3.10e-04

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: 39.48  E-value: 3.10e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLSTVRS 160
Cdd:cd03264 138 RVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVES 194
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
104-156 3.15e-04

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 40.42  E-value: 3.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 5923929    104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAHRLS 156
Cdd:TIGR00955 174 RLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPS 227
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
14-155 3.64e-04

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: 39.84  E-value: 3.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   14 EGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRlGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVGEG 93
Cdd:cd03289  57 EGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDG 135
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5923929   94 GGQMSGGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRL 155
Cdd:cd03289 136 GCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI 197
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1-155 4.66e-04

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: 40.00  E-value: 4.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929       1 TALQLIQRFYDPCEGMVTPDGHDIRSlNIRWLRDQIGIVEQEPVLFS-TTIAENIRL-----GRE--------EATMEDI 66
Cdd:TIGR01257  971 TTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILFyaqlkGRSweeaqlemEAMLEDT 1049
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929      67 -VQAAKDANAYNFIMALPQqfdtlvgegggqmsggqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHG 145
Cdd:TIGR01257 1050 gLHHKRNEEAQDLSGGMQR-------------------KLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
                          170
                   ....*....|
gi 5923929     146 HTIISVAHRL 155
Cdd:TIGR01257 1111 RTIIMSTHHM 1120
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
104-153 4.72e-04

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 39.72  E-value: 4.72e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 5923929   104 RVAIARALIRKPKILLLDMATSALDNESEAKVQgalnkiQHGH----TIISVAH 153
Cdd:PRK11819 171 RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLE------QFLHdypgTVVAVTH 218
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
18-170 4.73e-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: 39.24  E-value: 4.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   18 TPDGHDIRSLNirwlRDQIGIVEQEPVLFSTTIAENIRLGreEATMEDIVQAAKDANAYN-FIMALPQQFDTLVGEGGGQ 96
Cdd:cd03290  67 EPSFEATRSRN----RYSVAYAAQKPWLLNATVEENITFG--SPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGIN 140
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5923929   97 MSGGQKQRVAIARALIRKPKILLLDMATSALD-NESEAKVQ-GALNKIQHG-HTIISVAHRLSTVRSADVIIGFEHG 170
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQeGILKFLQDDkRTLVLVTHKLQYLPHADWIIAMKDG 217
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
104-156 5.02e-04

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: 39.73  E-value: 5.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 5923929    104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIqhGHTIISVAHRLS 156
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
12-153 6.19e-04

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: 38.64  E-value: 6.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   12 PCEGMVTPDGHDIRSlNIRWLRDQIGIVEQEPVLFST-TIAENIRL-----GREEATMEDIVQAAKDanaynfIMALPQQ 85
Cdd:cd03263  54 PTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLR------VLGLTDK 126
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5923929   86 FDTLVGEGGGQMSGgqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAH 153
Cdd:cd03263 127 ANKRARTLSGGMKR----KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
104-128 6.23e-04

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 39.09  E-value: 6.23e-04
                         10        20
                 ....*....|....*....|....*
gi 5923929   104 RVAIARALIRKPKILLLDMATSALD 128
Cdd:PRK11144 136 RVAIGRALLTAPELLLMDEPLASLD 160
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
10-153 6.46e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 38.91  E-value: 6.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    10 YDPCEGMVTPDGHDIRSLNIRWL--RDQIGIVEQEP--VLFSTTIAENIRLG------REEATMEDIVQAAKDANAYNFI 79
Cdd:PRK13639  52 LKPTSGEVLIKGEPIKYDKKSLLevRKTVGIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFE 131
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5923929    80 MALPQQFDTlvgegggqmsgGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI-QHGHTIISVAH 153
Cdd:PRK13639 132 NKPPHHLSG-----------GQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTH 195
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
36-155 6.91e-04

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 39.22  E-value: 6.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    36 IGIVEQEPVLFST-TIAENIRLGREEATMEDIVQAAK---DANAYNFIMALPQQFDTLVGEGGGQMSGGqkqrVAIARAL 111
Cdd:PRK10762  81 IGIIHQELNLIPQlTIAENIFLGREFVNRFGRIDWKKmyaEADKLLARLNLRFSSDKLVGELSIGEQQM----VEIAKVL 156
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 5923929   112 IRKPKILLLDMATSAL-DNESEA--KVQGALNkiQHGHTIISVAHRL 155
Cdd:PRK10762 157 SFESKVIIMDEPTDALtDTETESlfRVIRELK--SQGRGIVYISHRL 201
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
33-159 7.23e-04

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 38.90  E-value: 7.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    33 RDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAAKDANAynfimaLPQQFDTlvgegggqmsgGQKQRVAIARALI 112
Cdd:PRK10419 105 RKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDK------RPPQLSG-----------GQLQRVCLARALA 167
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 5923929   113 RKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAHRLSTVR 159
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVE 216
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
13-128 7.25e-04

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 38.62  E-value: 7.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   13 CEGMVTPDGHDIRSLNIRwlRDQIGIVEQEPVLFS-TTIAENI------RLGREEAtmEDIVQAA-KDANAYNFIMALPq 84
Cdd:COG4136  57 ASGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPhLSVGENLafalppTIGRAQR--RARVEQAlEEAGLAGFADRDP- 131
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 5923929   85 qfDTLvgegggqmSGGQKQRVAIARALIRKPKILLLDMATSALD 128
Cdd:COG4136 132 --ATL--------SGGQRARVALLRALLAEPRALLLDEPFSKLD 165
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
12-127 8.22e-04

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: 38.57  E-value: 8.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929   12 PCEGMVTPDGHDIRSLN-IRWLRDQIGIVEQEPVLFST-TIAENIRLG-------REEATMEDIVQ------AAKDANAY 76
Cdd:cd03224  52 PRSGSIRFDGRDITGLPpHERARAGIGYVPEGRRIFPElTVEENLLLGayarrraKRKARLERVYElfprlkERRKQLAG 131
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 5923929   77 NfimaLP---QQFdtlvgegggqmsggqkqrVAIARALIRKPKILLLDMATSAL 127
Cdd:cd03224 132 T----LSggeQQM------------------LAIARALMSRPKLLLLDEPSEGL 163
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
104-170 8.27e-04

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: 38.48  E-value: 8.27e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIISVAHRLSTVRS-ADVIIGFEHG 170
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFG 229
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
104-159 8.42e-04

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: 39.02  E-value: 8.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 5923929    104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNK--IQHGHTIISVAHRLSTVR 159
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKarEEMEQTFIIVSHDMDFVL 492
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
14-160 9.64e-04

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 38.65  E-value: 9.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     14 EGMVTPDGHDIRSLNIRWL-RDQIGIVEQEPVLF-STTIAENIRLGREEATMEDIVQAAKDANAYNFIMALPQQFDTLVG 91
Cdd:TIGR02633  57 DGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVT 136
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5923929     92 EGGGQMSGGQKQRVAIARALIRKPKILLLDMATSALdneSEAKVQGALNKI----QHGHTIISVAHRLSTVRS 160
Cdd:TIGR02633 137 RPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL---TEKETEILLDIIrdlkAHGVACVYISHKLNEVKA 206
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
12-165 9.66e-04

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 38.21  E-value: 9.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    12 PCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVL-FSTTIAENIRLGR-----EEATMEDIVQAAKDAN-----AYNFIM 80
Cdd:PRK13548  54 PDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEVVAMGRaphglSRAEDDALVAAALAQVdlahlAGRDYP 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    81 ALP---QQfdtlvgegggqmsggqkqRVAIARALIR------KPKILLLDMATSALDneseakvqgalnkIQHGHTIISV 151
Cdd:PRK13548 134 QLSggeQQ------------------RVQLARVLAQlwepdgPPRWLLLDEPTSALD-------------LAHQHHVLRL 182
                        170
                 ....*....|....
gi 5923929   152 AHRLSTVRSADVII 165
Cdd:PRK13548 183 ARQLAHERGLAVIV 196
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
104-170 1.11e-03

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: 38.28  E-value: 1.11e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGAL-NKIQHGHTIISVAHRLSTVRS-ADVIIGFEHG 170
Cdd:cd03220 150 RLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRlCDRALVLEKG 218
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
1-158 1.28e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 38.29  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGH--DIRSLNIRWLRDQIGIVEQEP--VLFSTTIAENI-----RLGREEATMEDIVQAAK 71
Cdd:PRK13636  47 TLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMVFQDPdnQLFSASVYQDVsfgavNLKLPEDEVRKRVDNAL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    72 DANAYNFIMALPQQFDTLvgegggqmsgGQKQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTII 149
Cdd:PRK13636 127 KRTGIEHLKDKPTHCLSF----------GQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTII 196

                 ....*....
gi 5923929   150 SVAHRLSTV 158
Cdd:PRK13636 197 IATHDIDIV 205
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
104-128 1.50e-03

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: 37.64  E-value: 1.50e-03
                        10        20
                ....*....|....*....|....*
gi 5923929  104 RVAIARALIRKPKILLLDMATSALD 128
Cdd:cd03234 151 RVSIAVQLLWDPKVLILDEPTSGLD 175
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
104-131 1.65e-03

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 38.12  E-value: 1.65e-03
                        10        20
                ....*....|....*....|....*...
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNES 131
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLES 187
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
32-150 1.87e-03

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 37.68  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    32 LRDQIGIVEQEP--VLFSTTIAENI-----RLGREEAtmeDIVQAAKDAnaynFIMALPQQFDtlvGEGGGQMSGGQKQR 104
Cdd:PRK13638  75 LRQQVATVFQDPeqQIFYTDIDSDIafslrNLGVPEA---EITRRVDEA----LTLVDAQHFR---HQPIQCLSHGQKKR 144
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 5923929   105 VAIARALIRKPKILLLDMATSALDNESEAKVQGALNKI--QHGHTIIS 150
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvaQGNHVIIS 192
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
104-156 1.93e-03

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 37.49  E-value: 1.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 5923929   104 RVAIARALIRKPKILLLDMATSALDN---ESEAKVQGALNkIQHGHTIISVAHRLS 156
Cdd:PRK11629 153 RVAIARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELN-RLQGTAFLVVTHDLQ 207
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
104-170 2.18e-03

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: 37.31  E-value: 2.18e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5923929  104 RVAIARALIRKPKILLLDMATSALDNESEAKVQG---ALNKiQHGHTIISVAHRLSTVRS-ADVIIGFEHG 170
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNflkEYNR-ERGTTVLLTSHYMKDIEAlARRVLVIDKG 230
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
105-156 2.35e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 37.38  E-value: 2.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 5923929   105 VAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTIISVAHRLS 156
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLA 223
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
1-121 3.75e-03

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: 36.75  E-value: 3.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    1 TALQLIQRFYDPCEGMVTPDGHDIRSLNI-RWLRDQIGIVEQEPVLF-STTIAENIRLGREEATMEDIVQAAKdanaynf 78
Cdd:cd03218  41 TTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFrKLTVEENILAVLEIRGLSKKEREEK------- 113
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 5923929   79 IMALPQQF--DTLVGEGGGQMSGGQKQRVAIARALIRKPKILLLD 121
Cdd:cd03218 114 LEELLEEFhiTHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1-159 3.92e-03

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 37.07  E-value: 3.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRwLRDQ--IGIVEQE-PVLFSTTIAENIRLGR---EEATMEDIVQAAK--- 71
Cdd:PRK09700  46 TLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQlgIGIIYQElSVIDELTVLENLYIGRhltKKVCGVNIIDWREmrv 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    72 DANAYNFIMALPQQFDTLVGEGGGQMSGGqkqrVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQ-HGHTIIS 150
Cdd:PRK09700 125 RAAMMLLRVGLKVDLDEKVANLSISHKQM----LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVY 200

                 ....*....
gi 5923929   151 VAHRLSTVR 159
Cdd:PRK09700 201 ISHKLAEIR 209
GguA NF040905
sugar ABC transporter ATP-binding protein;
36-164 4.50e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 36.69  E-value: 4.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    36 IGIVEQE----PVLfstTIAENIRLGREEATM------EDIVQAAK-------DANAYNFIMAL---PQQFdtlvgeggg 95
Cdd:NF040905  80 IVIIHQElaliPYL---SIAENIFLGNERAKRgvidwnETNRRAREllakvglDESPDTLVTDIgvgKQQL--------- 147
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5923929    96 qmsggqkqrVAIARALIRKPKILLLDMATSAL-DNESEAKVQGALNKIQHGHTIISVAHRLSTVRS-ADVI 164
Cdd:NF040905 148 ---------VEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSI 209
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
104-128 5.61e-03

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 35.99  E-value: 5.61e-03
                        10        20
                ....*....|....*....|....*
gi 5923929  104 RVAIARALIRKPKILLLDMATSALD 128
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALD 166
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
104-173 6.17e-03

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 36.47  E-value: 6.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5923929   104 RVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQhgHTIISVAHRLSTVRS-ADVIIGFEHGVAV 173
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ--GSIIFISHDRSFIRNmATRIVDLDRGKLV 232
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
103-170 6.23e-03

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 36.16  E-value: 6.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5923929   103 QRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQH--GHTIISVAH-RLSTVRSADVIIGFEHG 170
Cdd:PRK11000 140 QRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAG 210
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
105-121 6.35e-03

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: 35.73  E-value: 6.35e-03
                        10
                ....*....|....*..
gi 5923929  105 VAIARALIRKPKILLLD 121
Cdd:COG0410 145 LAIGRALMSRPKLLLLD 161
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
15-173 6.85e-03

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 35.96  E-value: 6.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    15 GMVTPDGHDIRSLNI------RWLRDQIGIVEQEPVL-FSTTIAENIRL-GRE--------EATMEDIVQAAKdanaynf 78
Cdd:PRK13536  89 GMTSPDAGKITVLGVpvparaRLARARIGVVPQFDNLdLEFTVRENLLVfGRYfgmstreiEAVIPSLLEFAR------- 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    79 imaLPQQFDTLVGEGGGQMSGgqkqRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNK-IQHGHTIISVAHRLST 157
Cdd:PRK13536 162 ---LESKADARVSDLSGGMKR----RLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEE 234
                        170
                 ....*....|....*..
gi 5923929   158 V-RSADVIIGFEHGVAV 173
Cdd:PRK13536 235 AeRLCDRLCVLEAGRKI 251
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
1-128 7.23e-03

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 35.97  E-value: 7.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929     1 TALQLIQRFYDPCEGMVTPDGHDIRSLNIRWLRDQIGIVEQEPVL-FSTTIAENIRLGR----------EEATMEDIVQA 69
Cdd:PRK09536  44 TLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQVVEMGRtphrsrfdtwTETDRAAVERA 123
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 5923929    70 AKDANAYNFImalPQQFDTLvgegggqmSGGQKQRVAIARALIRKPKILLLDMATSALD 128
Cdd:PRK09536 124 MERTGVAQFA---DRPVTSL--------SGGERQRVLLARALAQATPVLLLDEPTASLD 171
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
15-173 9.29e-03

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 35.54  E-value: 9.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    15 GMVTPDGHDI--------------RSLNIRWL----------RDQIGIVEQEPVLFSTTIAENIRLGREEATMEDIVQAA 70
Cdd:PRK15112  61 GMIEPTSGELliddhplhfgdysyRSQRIRMIfqdpstslnpRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLP 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5923929    71 KDANAYNFIMALPQQfdtlvgegggqmsggqkQRVAIARALIRKPKILLLDMATSALDNESEAKVQGALNKIQHGHTI-- 148
Cdd:PRK15112 141 DHASYYPHMLAPGQK-----------------QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsy 203
                        170       180
                 ....*....|....*....|....*.
gi 5923929   149 ISVAHRLSTVRS-ADVIIGFEHGVAV 173
Cdd:PRK15112 204 IYVTQHLGMMKHiSDQVLVMHQGEVV 229
 
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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