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Conserved domains on  [gi|255708373|ref|NP_001157465|]
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ATP-binding cassette sub-family B member 5 isoform 4 [Homo sapiens]

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 ...
1-124 9.51e-78

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: 229.35  E-value: 9.51e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:cd03249   61 LLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQL 140
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03249  141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDR 184
 
Name Accession Description Interval E-value
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1-124 9.51e-78

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: 229.35  E-value: 9.51e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:cd03249   61 LLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQL 140
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03249  141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDR 184
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
2-124 3.99e-64

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 204.24  E-value: 3.99e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMS 81
Cdd:COG1132  399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLS 478
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 255708373  82 GGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:COG1132  479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALER 521
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
1-125 1.49e-50

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 169.90  E-value: 1.49e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:TIGR00958 539 LLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQL 618
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 255708373   81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKK 125
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRA 663
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
1-123 1.61e-49

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 165.90  E-value: 1.61e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:PRK13657 393 LIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQL 472
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALE 123
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALD 515
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
2-108 1.19e-28

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: 101.57  E-value: 1.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    2 VDENDIRALNVRHYRDHIGVVSQEPVLF-GTTISNNIKYGR------DDVTDEEMERAAREANAYDFImefpnkfNTLVG 74
Cdd:pfam00005  44 LDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENLRLGLllkglsKREKDARAEEALEKLGLGDLA-------DRPVG 116
                          90       100       110
                  ....*....|....*....|....*....|....
gi 255708373   75 EKGAQMSGGQKQRIAIARALVRNPKILILDEATS 108
Cdd:pfam00005 117 ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
80-122 4.73e-10

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 54.55  E-value: 4.73e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 255708373  80 MSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:NF040873 120 LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALL 162
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
70-123 7.23e-08

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 48.14  E-value: 7.23e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 255708373    70 NTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALE 123
Cdd:smart00382  51 LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
48-118 3.89e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 41.64  E-value: 3.89e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708373  48 EMERAAREANAYDFIMEFpnKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAV 118
Cdd:NF000106 115 DLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEV 183
GguA NF040905
sugar ABC transporter ATP-binding protein;
16-111 3.90e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 41.31  E-value: 3.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  16 RDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREanaydfimEFPNKFNTL---VGEKGAQMSGGQKQRIAIAR 92
Cdd:NF040905 346 RKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAE--------EYRKKMNIKtpsVFQKVGNLSGGNQQKVVLSK 417
                         90
                 ....*....|....*....
gi 255708373  93 ALVRNPKILILDEATSALD 111
Cdd:NF040905 418 WLFTDPDVLILDEPTRGID 436
GguA NF040905
sugar ABC transporter ATP-binding protein;
70-117 6.31e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.93  E-value: 6.31e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 255708373  70 NTLVGEKGAqmsgGQKQRIAIARALVRNPKILILDEATSALdSESKSA 117
Cdd:NF040905 134 DTLVTDIGV----GKQQLVEIAKALSKDVKLLILDEPTAAL-NEEDSA 176
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
83-111 9.49e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 40.49  E-value: 9.49e-05
                         10        20
                 ....*....|....*....|....*....
gi 255708373  83 GQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVD 429
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
81-111 1.06e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 37.41  E-value: 1.06e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
 
Name Accession Description Interval E-value
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1-124 9.51e-78

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: 229.35  E-value: 9.51e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:cd03249   61 LLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQL 140
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03249  141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDR 184
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
2-124 3.99e-64

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 204.24  E-value: 3.99e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMS 81
Cdd:COG1132  399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLS 478
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 255708373  82 GGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:COG1132  479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALER 521
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
2-124 3.84e-58

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: 179.35  E-value: 3.84e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMS 81
Cdd:cd03251   61 IDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLS 140
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 255708373  82 GGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03251  141 GGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALER 183
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
1-124 1.39e-57

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: 189.27  E-value: 1.39e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:COG2274  533 LIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNL 612
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:COG2274  613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRR 656
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
2-124 6.62e-55

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: 171.26  E-value: 6.62e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMS 81
Cdd:cd03253   60 IDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLS 139
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 255708373  82 GGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03253  140 GGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRD 182
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
1-124 1.05e-52

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: 174.62  E-value: 1.05e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:COG5265  416 LIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKL 495
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:COG5265  496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALRE 539
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
1-125 1.49e-50

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 169.90  E-value: 1.49e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:TIGR00958 539 LLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQL 618
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 255708373   81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKK 125
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRA 663
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
1-122 6.26e-50

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: 158.40  E-value: 6.26e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:cd03248   72 LLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQL 151
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:cd03248  152 SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQAL 193
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
2-124 1.22e-49

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: 157.77  E-value: 1.22e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMS 81
Cdd:cd03254   62 IDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLS 141
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 255708373  82 GGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03254  142 QGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEK 184
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
1-123 1.61e-49

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 165.90  E-value: 1.61e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:PRK13657 393 LIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQL 472
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALE 123
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALD 515
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
1-124 2.75e-49

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: 164.55  E-value: 2.75e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:COG4988  395 LINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGL 474
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:COG4988  475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR 518
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
1-123 9.16e-48

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 161.02  E-value: 9.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:TIGR02204 398 LLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTL 477
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 255708373   81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALE 123
Cdd:TIGR02204 478 SGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALE 520
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
1-124 9.06e-47

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 158.26  E-value: 9.06e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDV-TDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQ 79
Cdd:PRK11176 401 LLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVL 480
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 255708373  80 MSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDE 525
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
1-124 2.27e-45

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: 154.49  E-value: 2.27e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGR-DDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQ 79
Cdd:TIGR02203 390 LLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVL 469
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 255708373   80 MSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALER 514
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
1-124 4.87e-42

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: 138.39  E-value: 4.87e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:cd03252   60 LVDGHDLALADPAWLRRQVGVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGL 139
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03252  140 SGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHD 183
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
6-122 4.68e-41

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: 142.60  E-value: 4.68e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   6 DIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQK 85
Cdd:COG4987  398 DLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGER 477
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 255708373  86 QRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:COG4987  478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADL 514
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
1-124 4.76e-39

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


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 138.34  E-value: 4.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:TIGR01846 515 LVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANL 594
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 255708373   81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:TIGR01846 595 SGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMRE 638
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
1-122 1.53e-37

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: 126.55  E-value: 1.53e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:cd03245   62 LLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGL 141
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:cd03245  142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERL 183
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
1-122 2.19e-37

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 134.00  E-value: 2.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:PTZ00265 1280 LLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSL 1359
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 255708373   81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:PTZ00265 1360 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
2-124 3.86e-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: 128.94  E-value: 3.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMS 81
Cdd:TIGR02857 381 VNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLS 460
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 255708373   82 GGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA 503
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
2-111 1.98e-35

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 127.52  E-value: 1.98e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIR-------ALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVG 74
Cdd:PRK10789 367 VSEGDIRfhdipltKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVG 446
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 255708373  75 EKGAQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK10789 447 ERGVMLSGGQKQRISIARALLLNAEILILDDALSAVD 483
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
2-124 1.23e-34

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: 117.48  E-value: 1.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIkygrddvtdeemeraareanaydfimefpnkfntlvgekgaqMS 81
Cdd:cd03228   61 IDGVDLRDLDLESLRKNIAYVPQDPFLFSGTIRENI------------------------------------------LS 98
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 255708373  82 GGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03228   99 GGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRA 141
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
3-123 2.01e-34

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: 124.48  E-value: 2.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   3 DENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIkyGR-DDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMS 81
Cdd:COG4618  392 DGADLSQWDREELGRHIGYLPQDVELFDGTIAENI--ARfGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLS 469
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 255708373  82 GGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALE 123
Cdd:COG4618  470 GGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIR 511
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
8-124 1.83e-32

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 119.18  E-value: 1.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   8 RALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQR 87
Cdd:PRK11174 414 RELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQR 493
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 255708373  88 IAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:PRK11174 494 LALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA 530
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
2-122 2.88e-31

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: 110.28  E-value: 2.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNI----KYgrddvTDEEMERAAREANAYDFIMEFPNKFNTLVGEKG 77
Cdd:cd03244   63 IDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNLdpfgEY-----SDEELWQALERVGLKEFVESLPGGLDTVVEEGG 137
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:cd03244  138 ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTI 182
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
3-126 1.32e-30

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


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 113.98  E-value: 1.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    3 DENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSG 82
Cdd:TIGR01842 378 DGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSG 457
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 255708373   83 GQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKKK 126
Cdd:TIGR01842 458 GQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALK 501
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
2-122 4.17e-30

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: 112.45  E-value: 4.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMS 81
Cdd:TIGR02868 394 LDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLS 473
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 255708373   82 GGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL 514
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
3-126 1.08e-29

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 112.04  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    3 DENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYG------------------------------------------ 40
Cdd:PTZ00265  446 DSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlndm 525
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   41 ---------------RDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDE 105
Cdd:PTZ00265  526 snttdsneliemrknYQTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDE 605
                         170       180
                  ....*....|....*....|.
gi 255708373  106 ATSALDSESKSAVQAALEKKK 126
Cdd:PTZ00265  606 ATSSLDNKSEYLVQKTINNLK 626
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
2-108 1.19e-28

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: 101.57  E-value: 1.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    2 VDENDIRALNVRHYRDHIGVVSQEPVLF-GTTISNNIKYGR------DDVTDEEMERAAREANAYDFImefpnkfNTLVG 74
Cdd:pfam00005  44 LDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENLRLGLllkglsKREKDARAEEALEKLGLGDLA-------DRPVG 116
                          90       100       110
                  ....*....|....*....|....*....|....
gi 255708373   75 EKGAQMSGGQKQRIAIARALVRNPKILILDEATS 108
Cdd:pfam00005 117 ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
3-124 7.37e-28

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: 106.58  E-value: 7.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    3 DENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMErAAREANAYDFIMEFPNKFNTLVGEKGAQMSG 82
Cdd:TIGR03797 513 DGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWE-AARMAGLAEDIRAMPMGMHTVISEGGGTLSG 591
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 255708373   83 GQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:TIGR03797 592 GQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLER 633
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
16-122 6.38e-25

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 98.25  E-value: 6.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  16 RDHIGVVSQEPVLFGTTISNNIKYGRDdVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALV 95
Cdd:PRK10790 414 RQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLV 492
                         90       100
                 ....*....|....*....|....*..
gi 255708373  96 RNPKILILDEATSALDSESKSAVQAAL 122
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQAL 519
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
3-122 1.02e-24

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 93.34  E-value: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   3 DENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYG---RDDVTDEEMERAAREAnaydfiMEFPNKF-NTLVGEkga 78
Cdd:COG4619   60 DGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDNLPFPfqlRERKFDRERALELLER------LGLPPDIlDKPVER--- 130
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 255708373  79 qMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:COG4619  131 -LSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELL 173
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
18-126 3.92e-23

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: 89.07  E-value: 3.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  18 HIGVVSQEPVLFGTTISNNIKYGRDdvTDEEMERAAREANA--YDFIMeFPNKFNTLVGEKGAQMSGGQKQRIAIARALV 95
Cdd:cd03250   67 SIAYVSQEPWIQNGTIRENILFGKP--FDEERYEKVIKACAlePDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 255708373  96 RNPKILILDEATSALDSES-----KSAVQAALEKKK 126
Cdd:cd03250  144 SDADIYLLDDPLSAVDAHVgrhifENCILGLLLNNK 179
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
1-124 2.49e-22

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: 87.62  E-value: 2.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVR--HYRDHIGVVSQEPVLFGTTISNNIKYG-------RDDVTDEEMERAAREANAYDfimEFPNKFNt 71
Cdd:cd03260   63 LLDGKDIYDLDVDvlELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWD---EVKDRLH- 138
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255708373  72 lvgekGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03260  139 -----ALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAE 186
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
1-124 2.84e-22

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: 86.75  E-value: 2.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEP--VLFGTTISNNIKYG--RDDVTDEEMERAAREANAydfimefpnkfntLVGEK 76
Cdd:cd03225   59 LVDGKDLTKLSLKELRRKVGLVFQNPddQFFGPTVEEEVAFGleNLGLPEEEIEERVEEALE-------------LVGLE 125
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 255708373  77 G------AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03225  126 GlrdrspFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKK 179
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
2-123 1.13e-21

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: 84.58  E-value: 1.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIkygrddvtdeemeraareanaydfimefpnkfntlvgekgaqMS 81
Cdd:cd03246   61 LDGADISQWDPNELGDHVGYLPQDDELFSGSIAENI------------------------------------------LS 98
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 255708373  82 GGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALE 123
Cdd:cd03246   99 GGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
6-111 4.54e-21

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: 87.10  E-value: 4.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    6 DIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYG-RDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQ 84
Cdd:TIGR01193 537 SLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQ 616
                          90       100
                  ....*....|....*....|....*..
gi 255708373   85 KQRIAIARALVRNPKILILDEATSALD 111
Cdd:TIGR01193 617 KQRIALARALLTDSKVLILDESTSNLD 643
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
2-124 9.05e-21

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: 83.40  E-value: 9.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALN---VRHYRDHIGVVSQEPVLFGT-TISNNIKY-----GrddvtdeeMERAAREANAYDFImefpnkfnTL 72
Cdd:cd03258   64 VDGTDLTLLSgkeLRKARRRIGMIFQHFNLLSSrTVFENVALpleiaG--------VPKAEIEERVLELL--------EL 127
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255708373  73 VG--EKG----AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03258  128 VGleDKAdaypAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRD 185
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
18-124 1.91e-20

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: 82.52  E-value: 1.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  18 HIGVVSQEPVLFG-TTISNNIKYGRDDVtdeEMERAAREANAYDFImefpnkfnTLVGEKGA------QMSGGQKQRIAI 90
Cdd:cd03293   74 DRGYVFQQDALLPwLTVLDNVALGLELQ---GVPKAEARERAEELL--------ELVGLSGFenayphQLSGGMRQRVAL 142
                         90       100       110
                 ....*....|....*....|....*....|....
gi 255708373  91 ARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03293  143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLD 176
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
79-124 7.28e-20

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: 79.21  E-value: 7.28e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd00267   80 QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRE 125
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
2-124 1.33e-19

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: 80.45  E-value: 1.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEPV--LFGTTISNNIKYG--RDDVTDEEMERAAREA----NAYDFIMEFPNkfntlv 73
Cdd:COG1122   60 VDGKDITKKNLRELRRKVGLVFQNPDdqLFAPTVEEDVAFGpeNLGLPREEIRERVEEAlelvGLEHLADRPPH------ 133
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255708373  74 gekgaQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:COG1122  134 -----ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKR 179
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
2-113 1.79e-19

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 81.66  E-value: 1.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALN---VRHYRDHIGVVSQEPVLFGT-TISNNIKY-----GrddvtdeeMERAAREANAYDFImefpnkfnTL 72
Cdd:COG1135   64 VDGVDLTALSereLRAARRKIGMIFQHFNLLSSrTVAENVALpleiaG--------VPKAEIRKRVAELL--------EL 127
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 255708373  73 VG--EKG----AQMSGGQKQRIAIARALVRNPKILILDEATSALDSE 113
Cdd:COG1135  128 VGlsDKAdaypSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
2-124 2.72e-19

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: 79.46  E-value: 2.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVR---HYR-DHIGVVSQEPVLFGT-TISNNIKY-----GrddVTDEEMERAAREANAYdfiMEFPNKFNT 71
Cdd:cd03255   63 VDGTDISKLSEKelaAFRrRHIGFVFQSFNLLPDlTALENVELplllaG---VPKKERRERAEELLER---VGLGDRLNH 136
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255708373  72 LVgekgAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03255  137 YP----SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRE 185
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
1-124 3.35e-19

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 81.79  E-value: 3.35e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANaYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:PRK11160 398 LLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVG-LEKLLEDDKGLNAWLGEGGRQL 476
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE 520
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
2-114 5.84e-19

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 78.95  E-value: 5.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRAlNVRHYRDHIGVVSQEPVLFGT-TISNNIKYGRD--DVTDEEMERAAREANAydfIMEFPNKFNTLVGekga 78
Cdd:COG1131   59 VLGEDVAR-DPAEVRRRIGYVPQEPALYPDlTVRENLRFFARlyGLPRKEARERIDELLE---LFGLTDAADRKVG---- 130
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSES 114
Cdd:COG1131  131 TLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
1-122 7.60e-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: 80.76  E-value: 7.60e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373     1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIK-YGRddVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQ 79
Cdd:TIGR00957 1344 IIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGEN 1421
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 255708373    80 MSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:TIGR00957 1422 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI 1464
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-124 1.54e-18

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 77.39  E-value: 1.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALN------VRhyRDHIGVVSQEPVLFGT-TISNNIKYGR--DDVTDEEMERAAREANAY----DFIMEFPN 67
Cdd:COG1136   66 LIDGQDISSLSerelarLR--RRHIGFVFQFFNLLPElTALENVALPLllAGVSRKERRERARELLERvglgDRLDHRPS 143
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 255708373  68 kfntlvgekgaQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:COG1136  144 -----------QLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRE 189
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
15-122 1.68e-18

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 78.99  E-value: 1.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  15 YRDHIGVVSQEPVLFG-TTISNNIKYG--RDDVTDEEMERAAREAnaydfiMEfpnkfntLVGEKG------AQMSGGQK 85
Cdd:COG3842   75 EKRNVGMVFQDYALFPhLTVAENVAFGlrMRGVPKAEIRARVAEL------LE-------LVGLEGladrypHQLSGGQQ 141
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 255708373  86 QRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:COG3842  142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREEL 178
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
2-122 3.17e-18

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: 78.79  E-value: 3.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALN---VRHYRDHIGVVSQEPV--LF-GTTISNNIKYG---RDDVTDEEMERAAREANA-----YDFIMEFPn 67
Cdd:COG1123  324 FDGKDLTKLSrrsLRELRRRVQMVFQDPYssLNpRMTVGDIIAEPlrlHGLLSRAERRERVAELLErvglpPDLADRYP- 402
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 255708373  68 kfntlvgekgAQMSGGQKQRIAIARALVRNPKILILDEATSALDseskSAVQAAL 122
Cdd:COG1123  403 ----------HELSGGQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQI 443
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
12-124 3.36e-18

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 77.05  E-value: 3.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  12 VRHYRDHIGVVSQEPVLFG-TTISNNIKYGRDDVTdeeMERAAREANAYDFImefpnkfnTLVGEKGA------QMSGGQ 84
Cdd:COG1116   75 VTGPGPDRGVVFQEPALLPwLTVLDNVALGLELRG---VPKAERRERARELL--------ELVGLAGFedayphQLSGGM 143
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 255708373  85 KQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:COG1116  144 RQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLR 183
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
2-119 3.38e-18

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: 76.30  E-value: 3.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYgRDDVTDEEMERAAReanaydfimefpnkfntlVGEKGAQMS 81
Cdd:cd03369   67 IDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLDP-FDEYSDEEIYGALR------------------VSEGGLNLS 127
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 255708373  82 GGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQ 119
Cdd:cd03369  128 QGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
2-124 6.38e-18

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: 78.02  E-value: 6.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEP--VLFGTTISNNIKYG--RDDVTDEEMERAAREANAYDFIMEFPNKFNtlvgekg 77
Cdd:COG1123   68 LDGRDLLELSEALRGRRIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYP------- 140
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:COG1123  141 HQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRE 187
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
79-111 1.40e-17

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: 74.85  E-value: 1.40e-17
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:cd03257  145 ELSGGQRQRVAIARALALNPKLLIADEPTSALD 177
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
11-124 1.87e-17

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: 73.76  E-value: 1.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  11 NVRHYRDHIGVVSQEPVLF-GTTISNNIKYGrddvtdeemeraareanaydfimefpnkfntlvgekgaqMSGGQKQRIA 89
Cdd:cd03229   70 ELPPLRRRIGMVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVA 110
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 255708373  90 IARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03229  111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKS 145
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
15-124 1.96e-17

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: 74.48  E-value: 1.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  15 YRDHIGVVSQEPVLFGT-TISNNIKYG--RDDVTDEEMERAAREANAydfIMEFPNkfntLVGEKGAQMSGGQKQRIAIA 91
Cdd:cd03259   70 ERRNIGMVFQDYALFPHlTVAENIAFGlkLRGVPKAEIRARVRELLE---LVGLEG----LLNRYPHELSGGQQQRVALA 142
                         90       100       110
                 ....*....|....*....|....*....|...
gi 255708373  92 RALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03259  143 RALAREPSLLLLDEPLSALDAKLREELREELKE 175
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
79-120 2.95e-17

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: 74.45  E-value: 2.95e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDseskSAVQA 120
Cdd:COG1124  138 QLSGGQRQRVAIARALILEPELLLLDEPTSALD----VSVQA 175
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
2-111 3.26e-17

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: 74.31  E-value: 3.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEPVL-FGTTISNNIKYGR---------DDVTDEEM-ERAAREANAYDFIMEFpnkFN 70
Cdd:COG1120   60 LDGRDLASLSRRELARRIAYVPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREAvEEALERTGLEHLADRP---VD 136
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 255708373  71 TLvgekgaqmSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:COG1120  137 EL--------SGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
3-111 3.48e-17

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: 75.88  E-value: 3.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   3 DENDIRALN---VRHYRDHIGVVSQEPvlFGT-----TISNNIKYG----RDDVTDEEMERAAREAnaydfiME------ 64
Cdd:COG4172  345 DGQDLDGLSrraLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEA------LEevgldp 416
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 255708373  65 -----FPNKFntlvgekgaqmSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:COG4172  417 aarhrYPHEF-----------SGGQRQRIAIARALILEPKLLVLDEPTSALD 457
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
16-126 4.67e-17

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: 73.48  E-value: 4.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  16 RDHIGVVSQEPVLF-GTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEfpnkfntLVGEKGAQMSGGQKQRIAIARAL 94
Cdd:cd03297   74 QRKIGLVFQQYALFpHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDH-------LLNRYPAQLSGGEKQRVALARAL 146
                         90       100       110
                 ....*....|....*....|....*....|..
gi 255708373  95 VRNPKILILDEATSALDSESKSAVQAALEKKK 126
Cdd:cd03297  147 AAQPELLLLDEPFSALDRALRLQLLPELKQIK 178
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
16-122 4.84e-17

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 74.04  E-value: 4.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  16 RDHIGVVSQEPVLFGTTISNNIKYG------RD-DVTDEEMERAAREANAYDfimEFPNKFNtlvgEKGAQMSGGQKQRI 88
Cdd:PRK14239  85 RKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDkQVLDEAVEKSLKGASIWD---EVKDRLH----DSALGLSGGQQQRV 157
                         90       100       110
                 ....*....|....*....|....*....|....
gi 255708373  89 AIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETL 191
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-111 6.58e-17

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 73.53  E-value: 6.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRA--LNVRHYRDHIGVVSQEPVLFGTTISNNIKYG-------RDDVTDEEMERAAREANAYDfimEFPNKFNt 71
Cdd:COG1117   74 LLDGEDIYDpdVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgikSKSELDEIVEESLRKAALWD---EVKDRLK- 149
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 255708373  72 lvgEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:COG1117  150 ---KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
78-113 9.76e-17

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 73.10  E-value: 9.76e-17
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSE 113
Cdd:COG1126  135 AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE 170
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
13-124 1.06e-16

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: 72.97  E-value: 1.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  13 RHYRDHIGVVSQEPVLF-GTTISNNIKYGRddvTDEEMERAAREANAYDFI--MEFPNKFNTLVGEkgaqMSGGQKQRIA 89
Cdd:COG4555   70 REARRQIGVLPDERGLYdRLTVRENIRYFA---ELYGLFDEELKKRIEELIelLGLEEFLDRRVGE----LSTGMKKKVA 142
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 255708373  90 IARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:COG4555  143 LARALVHDPKVLLLDEPTNGLDVMARRLLREILRA 177
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
1-124 1.19e-16

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 72.75  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRhyRDHIGVVSQEPVLF-GTTISNNIKYGRDDVTDEEMERAAReanaydfIMEFPNKFNT--LVGEKG 77
Cdd:cd03299   57 LLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNIAYGLKKRKVDKKEIERK-------VLEIAEMLGIdhLLNRKP 127
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03299  128 ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
PLN03130 PLN03130
ABC transporter C family member; Provisional
1-119 1.34e-16

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 74.39  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIK-YGRDDVTD--EEMERAareaNAYDFIMEFPNKFNTLVGEKG 77
Cdd:PLN03130 1297 LIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDpFNEHNDADlwESLERA----HLKDVIRRNSLGLDAEVSEAG 1372
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 255708373   78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQ 119
Cdd:PLN03130 1373 ENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQ 1414
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
78-113 1.68e-16

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 73.68  E-value: 1.68e-16
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSE 113
Cdd:PRK11153 139 AQLSGGQKQRVAIARALASNPKVLLCDEATSALDPA 174
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
15-124 2.05e-16

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: 73.21  E-value: 2.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  15 YRDHIGVVSQEPVLFGT-TISNNIKYGrddvtdeeMERAAREANAYDF--IMEfpnkfntLVG-----EKG-AQMSGGQK 85
Cdd:COG4148   75 HRRRIGYVFQEARLFPHlSVRGNLLYG--------RKRAPRAERRISFdeVVE-------LLGighllDRRpATLSGGER 139
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 255708373  86 QRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:COG4148  140 QRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLER 178
PLN03232 PLN03232
ABC transporter C family member; Provisional
1-125 2.41e-16

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 73.86  E-value: 2.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDvTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:PLN03232 1294 MIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEH-NDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENF 1372
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 255708373   81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKK 125
Cdd:PLN03232 1373 SVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREE 1417
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
11-113 4.36e-16

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 70.64  E-value: 4.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  11 NVRHYRDHIGVVSQEPVLFG-TTISNNIKYGRddVTDEEMERAAREANAYDF-----IMEFPNKFNtlvgekgAQMSGGQ 84
Cdd:cd03262   70 NINELRQKVGMVFQQFNLFPhLTVLENITLAP--IKVKGMSKAEAEERALELlekvgLADKADAYP-------AQLSGGQ 140
                         90       100
                 ....*....|....*....|....*....
gi 255708373  85 KQRIAIARALVRNPKILILDEATSALDSE 113
Cdd:cd03262  141 QQRVAIARALAMNPKVMLFDEPTSALDPE 169
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
79-111 5.04e-16

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: 72.01  E-value: 5.04e-16
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:COG0444  150 ELSGGMRQRVMIARALALEPKLLIADEPTTALD 182
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
2-118 8.18e-16

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 71.18  E-value: 8.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEP--VLFGTTISNNIKYGRDD--VTDEEM----ERAAREANAYDFIMEFPNKfntlv 73
Cdd:PRK13632  68 IDGITISKENLKEIRKKIGIIFQNPdnQFIGATVEDDIAFGLENkkVPPKKMkdiiDDLAKKVGMEDYLDKEPQN----- 142
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 255708373  74 gekgaqMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAV 118
Cdd:PRK13632 143 ------LSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREI 181
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
1-111 1.15e-15

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: 69.96  E-value: 1.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIraLNVRHYRDHIGVVSQEPVLF-GTTISNNIKYGRDDVTDEEMERAAREANAYDFImefpnKFNTLVGEKGAQ 79
Cdd:cd03300   58 LLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTVFENIAFGLRLKKLPKAEIKERVAEALDLV-----QLEGYANRKPSQ 130
                         90       100       110
                 ....*....|....*....|....*....|..
gi 255708373  80 MSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:cd03300  131 LSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
6-118 1.25e-15

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 69.74  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   6 DIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYG---RDDVTDEEMERaareanayDFIMEFPNKFNTLvgEKG-AQMS 81
Cdd:PRK10247  70 DISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLIFPwqiRNQQPDPAIFL--------DDLERFALPDTIL--TKNiAELS 139
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 255708373  82 GGQKQRIAIARALVRNPKILILDEATSALDSESKSAV 118
Cdd:PRK10247 140 GGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-115 1.45e-15

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 70.53  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEP--VLFGTTISNNIKYGRDD--VTDEEMERAAREANAYDFIMEFPNKfntlvgeK 76
Cdd:PRK13650  65 IIDGDLLTEENVWDIRHKIGMVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEALELVGMQDFKER-------E 137
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 255708373  77 GAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESK 115
Cdd:PRK13650 138 PARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGR 176
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
79-124 2.82e-15

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 68.96  E-value: 2.82e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:COG1121  139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRE 184
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
1-114 3.43e-15

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 68.54  E-value: 3.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALN---VRHYRDHIGVVSQE-PVLFGTTISNNIKY-----GRDDvtdEEMERAAREAnaydfiMEfpnkfnt 71
Cdd:COG2884   60 LVNGQDLSRLKrreIPYLRRRIGVVFQDfRLLPDRTVYENVALplrvtGKSR---KEIRRRVREV------LD------- 123
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 255708373  72 LVG--EKG----AQMSGGQKQRIAIARALVRNPKILILDEATSALDSES 114
Cdd:COG2884  124 LVGlsDKAkalpHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPET 172
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
16-126 3.74e-15

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 69.04  E-value: 3.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  16 RDHIGVVSQEPVLFGTTISNNIKYG------RDDVtDEEMERAAREANAYDfimEFPNKFNtlvgEKGAQMSGGQKQRIA 89
Cdd:PRK14243  90 RRRIGMVFQKPNPFPKSIYDNIAYGaringyKGDM-DELVERSLRQAALWD---EVKDKLK----QSGLSLSGGQQQRLC 161
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 255708373  90 IARALVRNPKILILDEATSALDSESKSAVQAALEKKK 126
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELK 198
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
81-120 3.78e-15

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 69.76  E-value: 3.78e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDsesKSaVQA 120
Cdd:COG4608  159 SGGQRQRIGIARALALNPKLIVCDEPVSALD---VS-IQA 194
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
7-116 4.23e-15

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 69.01  E-value: 4.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   7 IRALNVRHYRDHIGVVSQEP--VLFGTTISNNIKYGRDD--VTDEEMER----AAREANAYDFIMEFPNkfntlvgekga 78
Cdd:PRK13648  73 ITDDNFEKLRKHIGIVFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHRrvseALKQVDMLERADYEPN----------- 141
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKS 116
Cdd:PRK13648 142 ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
42-124 4.43e-15

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: 4.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  42 DDVTDEEMERAAREANAYDFImefpNKFNTlVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAA 121
Cdd:COG4178  453 EAFSDAELREALEAVGLGHLA----ERLDE-EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL 527

                 ...
gi 255708373 122 LEK 124
Cdd:COG4178  528 LRE 530
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
11-118 5.41e-15

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: 68.61  E-value: 5.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   11 NVRHYRDHIGVVSQEP--VLFGTTISNNIKYGRDD--VTDEEMER----AAREANAYDFIMEFPnkfntlvgekgAQMSG 82
Cdd:TIGR04520  71 NLWEIRKKVGMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKrvdeALKLVGMEDFRDREP-----------HLLSG 139
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 255708373   83 GQKQRIAIARALVRNPKILILDEATSALDSESKSAV 118
Cdd:TIGR04520 140 GQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEV 175
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
1-119 6.79e-15

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: 68.40  E-value: 6.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDdVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQM 80
Cdd:cd03288   79 VIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENF 157
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQ 119
Cdd:cd03288  158 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQ 196
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
79-124 8.46e-15

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: 67.56  E-value: 8.46e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03235  132 ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRE 177
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
11-118 1.35e-14

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 67.73  E-value: 1.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  11 NVRHYRDHIGVVSQEP--VLFGTTISNNIKYGRDD--VTDEEM-ER---AAREANAYDFIMEFPnkfntlvgekgAQMSG 82
Cdd:PRK13635  75 TVWDVRRQVGMVFQNPdnQFVGATVQDDVAFGLENigVPREEMvERvdqALRQVGMEDFLNREP-----------HRLSG 143
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 255708373  83 GQKQRIAIARALVRNPKILILDEATSALDSESKSAV 118
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREV 179
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
61-124 1.67e-14

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: 65.88  E-value: 1.67e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255708373  61 FIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03230   77 YLPEEPSLYENLTVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRE 140
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
81-125 1.89e-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: 1.89e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKK 125
Cdd:cd03223   93 SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL 137
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
1-111 1.93e-14

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 67.68  E-value: 1.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHyrdHIGVVSQEPVLFGTTISnniKYGRDDVTDEEMERAAREANAYDfimEFPNKFntlvgekgaqm 80
Cdd:PRK11308  96 IVFQNPYGSLNPRK---KVGQILEEPLLINTSLS---AAERREKALAMMAKVGLRPEHYD---RYPHMF----------- 155
                         90       100       110
                 ....*....|....*....|....*....|.
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALD 186
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
16-118 2.00e-14

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: 65.80  E-value: 2.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  16 RDHIGVVSQEPVLFGTTISNNIkygrddvtdeemeraareanaydfimefpnkfntlvgekGAQMSGGQKQRIAIARALV 95
Cdd:cd03247   74 SSLISVLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILL 114
                         90       100
                 ....*....|....*....|...
gi 255708373  96 RNPKILILDEATSALDSESKSAV 118
Cdd:cd03247  115 QDAPIVLLDEPTVGLDPITERQL 137
PLN03232 PLN03232
ABC transporter C family member; Provisional
16-112 2.02e-14

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 68.46  E-value: 2.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   16 RDHIGVVSQEPVLFGTTISNNIKYGrddvTDEEMERAAREANA----YDFIMeFPNKFNTLVGEKGAQMSGGQKQRIAIA 91
Cdd:PLN03232  678 RGSVAYVPQVSWIFNATVRENILFG----SDFESERYWRAIDVtalqHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMA 752
                          90       100
                  ....*....|....*....|.
gi 255708373   92 RALVRNPKILILDEATSALDS 112
Cdd:PLN03232  753 RAVYSNSDIYIFDDPLSALDA 773
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
79-111 2.34e-14

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: 65.53  E-value: 2.34e-14
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:cd03214   97 ELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
21-111 3.91e-14

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 65.93  E-value: 3.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  21 VVSQEPVLFG-TTISNNIKYGRDD---VTDEE---MERAAREANAYDFIMEFPnkfntlvgekgAQMSGGQKQRIAIARA 93
Cdd:COG3840   75 MLFQENNLFPhLTVAQNIGLGLRPglkLTAEQraqVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARC 143
                         90
                 ....*....|....*...
gi 255708373  94 LVRNPKILILDEATSALD 111
Cdd:COG3840  144 LVRKRPILLLDEPFSALD 161
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
19-124 4.86e-14

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: 66.67  E-value: 4.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   19 IGVVSQEPVLFG-TTISNNIKYGRDDVTDEEmeRAAREANAYDFIMEFPnkfntLVGEKGAQMSGGQKQRIAIARALVRN 97
Cdd:TIGR02142  77 IGYVFQEARLFPhLSVRGNLRYGMKRARPSE--RRISFERVIELLGIGH-----LLGRLPGRLSGGEKQRVAIGRALLSS 149
                          90       100
                  ....*....|....*....|....*..
gi 255708373   98 PKILILDEATSALDSESKSAVQAALEK 124
Cdd:TIGR02142 150 PRLLLMDEPLAALDDPRKYEILPYLER 176
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
8-123 5.35e-14

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 66.21  E-value: 5.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   8 RALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDV-------TDEEMERAAREANAYDfimEFPNKFNtlvgEKGAQM 80
Cdd:PRK14258  79 RRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVgwrpkleIDDIVESALKDADLWD---EIKHKIH----KSALDL 151
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALE 123
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQ 194
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
79-111 5.55e-14

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: 64.37  E-value: 5.55e-14
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:cd03216   82 QLSVGERQMVEIARALARNARLLILDEPTAALT 114
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
78-111 5.98e-14

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 66.64  E-value: 5.98e-14
                         10        20        30
                 ....*....|....*....|....*....|....
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:COG3839  132 KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
78-112 6.07e-14

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 66.32  E-value: 6.07e-14
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDS 112
Cdd:COG1118  132 SQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA 166
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
2-111 6.89e-14

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 66.58  E-value: 6.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDH-IGVVSQEPVLFGT-TISNNIKYGRDDVT-----DEEMERAAREANAYdfiMEFPNKFNTLVG 74
Cdd:COG1129   63 LDGEPVRFRSPRDAQAAgIAIIHQELNLVPNlSVAENIFLGREPRRgglidWRAMRRRARELLAR---LGLDIDPDTPVG 139
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 255708373  75 EkgaqMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:COG1129  140 D----LSVAQQQLVEIARALSRDARVLILDEPTASLT 172
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
2-114 7.16e-14

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: 65.28  E-value: 7.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRAL---NVRHYRDHIGVVSQEPVLFG-TTISNNIKYGRDD-----------VTDEEMERAAREANAYDfIMEFP 66
Cdd:cd03256   60 IDGTDINKLkgkALRQLRRQIGMIFQQFNLIErLSVLENVLSGRLGrrstwrslfglFPKEEKQRALAALERVG-LLDKA 138
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 255708373  67 NKfntlvgeKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSES 114
Cdd:cd03256  139 YQ-------RADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPAS 179
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
78-123 7.58e-14

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: 64.81  E-value: 7.58e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALE 123
Cdd:COG4133  130 RQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
79-111 8.13e-14

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 65.46  E-value: 8.13e-14
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:COG3638  146 QLSGGQQQRVAIARALVQEPKLILADEPVASLD 178
cbiO PRK13640
energy-coupling factor transporter ATPase;
2-118 9.37e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 65.59  E-value: 9.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEP--VLFGTTISNNIKYGRDD--VTDEEMERAAREANAYDFIMEFPNKfntlvgeKG 77
Cdd:PRK13640  69 VDGITLTAKTVWDIREKVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLADVGMLDYIDS-------EP 141
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAV 118
Cdd:PRK13640 142 ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQI 182
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
76-111 9.82e-14

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 66.12  E-value: 9.82e-14
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 255708373  76 KGAQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK09452 141 KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
78-126 1.16e-13

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: 62.85  E-value: 1.16e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKKK 126
Cdd:cd03221   69 EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYP 117
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
11-124 1.31e-13

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: 64.72  E-value: 1.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  11 NVRHYRDHIGVVS---------QEPVL-------FGTTisnnikyGRDDVTDEEMERAAREanaydfIMEFpnkFN--TL 72
Cdd:COG1119   72 DVWELRKRIGLVSpalqlrfprDETVLdvvlsgfFDSI-------GLYREPTDEQRERARE------LLEL---LGlaHL 135
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 255708373  73 VGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:COG1119  136 ADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDK 187
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
1-118 2.27e-13

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 63.96  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIR--ALNVRHYRDHIGVVSQEPVLF-GTTISNNIKYGRDDVtdeemeRAAREANAYDFIMEFPNKfntlVG--E 75
Cdd:PRK09493  59 IVDGLKVNdpKVDERLIRQEAGMVFQQFYLFpHLTALENVMFGPLRV------RGASKEEAEKQARELLAK----VGlaE 128
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 255708373  76 KG----AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAV 118
Cdd:PRK09493 129 RAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEV 175
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
81-126 2.95e-13

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: 63.61  E-value: 2.95e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKKK 126
Cdd:COG4778  154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAK 199
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
14-113 3.12e-13

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 64.33  E-value: 3.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  14 HYRD-HIGVVSQEPVLF-GTTISNNIKYG---------------RDDVTDE-EMERAAREANAYdfimefPnkfntlvge 75
Cdd:PRK10851  70 HARDrKVGFVFQHYALFrHMTVFDNIAFGltvlprrerpnaaaiKAKVTQLlEMVQLAHLADRY------P--------- 134
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 255708373  76 kgAQMSGGQKQRIAIARALVRNPKILILDEATSALDSE 113
Cdd:PRK10851 135 --AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
2-124 3.43e-13

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: 63.20  E-value: 3.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEPVLFGT-TISNNIKYGRDdVTDEEMERAAREANAYDFIMEFPNKFNTLvgekGAQM 80
Cdd:cd03292   63 QDVSDLRGRAIPYLRRKIGVVFQDFRLLPDrNVYENVAFALE-VTGVPPREIRKRVPAALELVGLSHKHRAL----PAEL 137
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03292  138 SGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKK 181
cbiO PRK13637
energy-coupling factor transporter ATPase;
1-111 4.91e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 63.53  E-value: 4.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDI--RALNVRHYRDHIGVVSQEP--VLFGTTISNNIKYG--RDDVTDEEMERAAREAnaydfiMEFPN-KFNTLV 73
Cdd:PRK13637  65 IIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIEKDIAFGpiNLGLSEEEIENRVKRA------MNIVGlDYEDYK 138
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 255708373  74 GEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK13637 139 DKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
1-126 6.51e-13

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: 62.52  E-value: 6.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRAlNVRHYRDHIGVVSQEPVLFGT-TISNNIK-YGR-----DDVTDEEMERAAREANAYDFImefpnkfNTLV 73
Cdd:cd03263   60 YINGYSIRT-DRKAARQSLGYCPQFDALFDElTVREHLRfYARlkglpKSEIKEEVELLLRVLGLTDKA-------NKRA 131
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255708373  74 GekgaQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKKK 126
Cdd:cd03263  132 R----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR 180
cbiO PRK13646
energy-coupling factor transporter ATPase;
12-124 7.82e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 62.87  E-value: 7.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  12 VRHYRDHIGVVSQ--EPVLFGTTISNNIKYGRDDVtdeEMERAAREANAYDFIMEFpnKFNTLVGEKGA-QMSGGQKQRI 88
Cdd:PRK13646  80 IRPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNF---KMNLDEVKNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKI 154
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 255708373  89 AIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKS 190
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
1-111 9.52e-13

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 62.78  E-value: 9.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHyrdHIGVVSQEPVLFGTTISnnikygrddvtdeEMERAAREANAYDfIMEFPNkfnTLVGEKGAQM 80
Cdd:PRK10419  93 MVFQDSISAVNPRK---TVREIIREPLRHLLSLD-------------KAERLARASEMLR-AVDLDD---SVLDKRPPQL 152
                         90       100       110
                 ....*....|....*....|....*....|.
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
1-111 1.00e-12

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: 62.66  E-value: 1.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALN------VRhyRDHIGVVSQEPVLF-GTTISNNIKYGRD--DVTDEEMERAAREAnaydfiMEfpnkfnt 71
Cdd:cd03294   82 LIDGQDIAAMSrkelreLR--RKKISMVFQSFALLpHRTVLENVAFGLEvqGVPRAEREERAAEA------LE------- 146
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 255708373  72 LVGEKG------AQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:cd03294  147 LVGLEGwehkypDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
16-111 1.32e-12

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: 61.58  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  16 RDHIGVVSQEPVLFGTTISNNIKYGRDdvTDEEMERAAREANAYDFIME-FPNKFNTLVGEKGAQMSGGQKQRIAIARAL 94
Cdd:cd03290   78 RYSVAYAAQKPWLLNATVEENITFGSP--FNKQRYKAVTDACSLQPDIDlLPFGDQTEIGERGINLSGGQRQRICVARAL 155
                         90
                 ....*....|....*..
gi 255708373  95 VRNPKILILDEATSALD 111
Cdd:cd03290  156 YQNTNIVFLDDPFSALD 172
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
80-111 1.44e-12

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 62.16  E-value: 1.44e-12
                         10        20        30
                 ....*....|....*....|....*....|..
gi 255708373  80 MSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:COG4167  150 LSSGQKQRVALARALILQPKIIIADEALAALD 181
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
19-118 1.97e-12

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: 61.12  E-value: 1.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  19 IGVVSQEP--VLFGTTISNNIKYGRDDvTDEEMERAA---REANAYDFIMEFPnkfntlvgekgAQMSGGQKQRIAIARA 93
Cdd:cd03226   73 IGYVMQDVdyQLFTDSVREELLLGLKE-LDAGNEQAEtvlKDLDLYALKERHP-----------LSLSGGQKQRLAIAAA 140
                         90       100
                 ....*....|....*....|....*
gi 255708373  94 LVRNPKILILDEATSALDSESKSAV 118
Cdd:cd03226  141 LLSGKDLLIFDEPTSGLDYKNMERV 165
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
19-110 2.07e-12

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: 61.30  E-value: 2.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  19 IGVVSQEPVLFGT-TISNNIKYGRDDVTDEEmeRAAREANAYDFimeFPnKFNTLVGEKGAQMSGGQKQRIAIARALVRN 97
Cdd:cd03224   77 IGYVPEGRRIFPElTVEENLLLGAYARRRAK--RKARLERVYEL---FP-RLKERRKQLAGTLSGGEQQMLAIARALMSR 150
                         90
                 ....*....|...
gi 255708373  98 PKILILDEATSAL 110
Cdd:cd03224  151 PKLLLLDEPSEGL 163
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
78-122 2.35e-12

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: 61.30  E-value: 2.35e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:COG4181  145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLL 189
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
2-111 2.44e-12

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: 60.98  E-value: 2.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNV---RHYRDHIGVVSQEPVLFGT-TISNNIKYG---RDDVTDEEMERAAREanaydfIMEFpnkfntlVG 74
Cdd:cd03261   59 IDGEDISGLSEaelYRLRRRMGMLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIVLE------KLEA-------VG 125
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 255708373  75 EKG------AQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:cd03261  126 LRGaedlypAELSGGMKKRVALARALALDPELLLYDEPTAGLD 168
cbiO PRK13642
energy-coupling factor transporter ATPase;
2-126 3.05e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 61.26  E-value: 3.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEP--VLFGTTISNNIKYGRDD--VTDEEMERAAREANAYDFIMEFPNKfntlvgeKG 77
Cdd:PRK13642  66 IDGELLTAENVWNLRRKIGMVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEALLAVNMLDFKTR-------EP 138
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKKK 126
Cdd:PRK13642 139 ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIK 187
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
72-126 3.46e-12

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: 60.35  E-value: 3.46e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 255708373  72 LVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDseSKSAVQAALEKKK 126
Cdd:cd03301  123 LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD--AKLRVQMRAELKR 175
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
79-113 3.49e-12

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 60.80  E-value: 3.49e-12
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSE 113
Cdd:PRK11124 141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
78-120 5.07e-12

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 61.26  E-value: 5.07e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDseskSAVQA 120
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQA 462
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
79-113 5.36e-12

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 60.41  E-value: 5.36e-12
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSE 113
Cdd:COG4161  141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
24-111 5.66e-12

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 59.98  E-value: 5.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  24 QEPVLFG-TTISNNIKYGRD------DVTDEEMERAAREANAYDFIMEFPnkfntlvgekgAQMSGGQKQRIAIARALVR 96
Cdd:PRK10771  78 QENNLFShLTVAQNIGLGLNpglklnAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVR 146
                         90
                 ....*....|....*
gi 255708373  97 NPKILILDEATSALD 111
Cdd:PRK10771 147 EQPILLLDEPFSALD 161
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
2-119 6.07e-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: 60.01  E-value: 6.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEPVLF-GTTISNNIKYgrddV-TDEEMERAAREANAYDFI--MEFPNKfnTLVGEKG 77
Cdd:cd03295   60 IDGEDIREQDPVELRRKIGYVIQQIGLFpHMTVEENIAL----VpKLLKWPKEKIRERADELLalVGLDPA--EFADRYP 133
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQ 119
Cdd:cd03295  134 HELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQ 175
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
2-115 6.23e-12

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: 59.90  E-value: 6.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRAlNVRHYRDHIGVVSQEPVLF-GTTISNNIKYG------RDDVTDEEMERAAREANAYDFimefpnkfntlVG 74
Cdd:cd03264   58 IDGQDVLK-QPQKLRRRIGYLPQEFGVYpNFTVREFLDYIawlkgiPSKEVKARVDEVLELVNLGDR-----------AK 125
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 255708373  75 EKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESK 115
Cdd:cd03264  126 KKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEER 166
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
9-111 6.57e-12

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: 61.08  E-value: 6.57e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373     9 ALNVRHYRDHIGVVSQEPVLFGTTISNNIK-YGRddVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQR 87
Cdd:TIGR01271 1284 SVTLQTWRKAFGVIPQKVFIFSGTFRKNLDpYEQ--WSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQL 1361
                           90       100
                   ....*....|....*....|....
gi 255708373    88 IAIARALVRNPKILILDEATSALD 111
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLD 1385
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
15-119 7.11e-12

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 60.62  E-value: 7.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  15 YRDHIGVVSQEPVLF-GTTISNNIKYG--RDDVTDEEMERAAREANAYDFIMEFPNKfntlvgeKGAQMSGGQKQRIAIA 91
Cdd:PRK11607  89 YQRPINMMFQSYALFpHMTVEQNIAFGlkQDKLPKAEIASRVNEMLGLVHMQEFAKR-------KPHQLSGGQRQRVALA 161
                         90       100
                 ....*....|....*....|....*...
gi 255708373  92 RALVRNPKILILDEATSALDSESKSAVQ 119
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQ 189
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
19-114 7.26e-12

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 60.85  E-value: 7.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  19 IGVVSQEPVLF-GTTISNNIKYGRDDV----------------TDEEMERAAR------EANAYDF------IME---FP 66
Cdd:COG0488   63 IGYLPQEPPLDdDLTVLDTVLDGDAELraleaeleeleaklaePDEDLERLAElqeefeALGGWEAearaeeILSglgFP 142
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 255708373  67 -NKFNTLVGEkgaqMSGGQKQRIAIARALVRNPKILILDEATSALDSES 114
Cdd:COG0488  143 eEDLDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
16-112 1.09e-11

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 60.12  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  16 RDhIGVVSQEPVLF-GTTISNNIKYG--RDDVTDEEMERAAREANAYDFIMEFPNKFNTlvgekgaQMSGGQKQRIAIAR 92
Cdd:PRK11432  78 RD-ICMVFQSYALFpHMSLGENVGYGlkMLGVPKEERKQRVKEALELVDLAGFEDRYVD-------QISGGQQQRVALAR 149
                         90       100
                 ....*....|....*....|
gi 255708373  93 ALVRNPKILILDEATSALDS 112
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDA 169
cbiO PRK13649
energy-coupling factor transporter ATPase;
2-111 1.18e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 59.76  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRAL----NVRHYRDHIGVVSQ--EPVLFGTTISNNIKYGRDD--VTDEEMERAAREANAYDFIMEfpnkfnTLV 73
Cdd:PRK13649  66 VDDTLITSTsknkDIKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGISE------SLF 139
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 255708373  74 GEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK13649 140 EKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
49-122 1.60e-11

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 59.11  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  49 MERAAREANAYDFImefpnkfnTLVGEKGA------QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:COG4525  106 VPKAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELL 177
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
49-122 1.98e-11

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 58.94  E-value: 1.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  49 MERAAREANAYDFImefpnkfnTLVGEKGA------QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:PRK11248 100 VEKMQRLEIAHQML--------KKVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLL 171
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
78-126 2.45e-11

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 58.66  E-value: 2.45e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 255708373   78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKKK 126
Cdd:TIGR02769 149 RQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQ 197
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
2-111 2.59e-11

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: 58.45  E-value: 2.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHY---RDHIGVVSQEPVLFGT-TISNNIKYG---RDDVTDEEMERAARE-------ANAYDFimeFPn 67
Cdd:COG1127   64 VDGQDITGLSEKELyelRRRIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVLEklelvglPGAADK---MP- 139
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 255708373  68 kfntlvgekgAQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:COG1127  140 ----------SELSGGMRKRVALARALALDPEILLYDEPTAGLD 173
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
14-112 3.46e-11

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: 59.19  E-value: 3.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    14 HYRDHIGVVSQEPVLFGTTISNNIKYGRDdvTDEEMERAAREANAYDFIME-FPNKFNTLVGEKGAQMSGGQKQRIAIAR 92
Cdd:TIGR00957  696 HMKGSVAYVPQQAWIQNDSLRENILFGKA--LNEKYYQQVLEACALLPDLEiLPSGDRTEIGEKGVNLSGGQKQRVSLAR 773
                           90       100
                   ....*....|....*....|
gi 255708373    93 ALVRNPKILILDEATSALDS 112
Cdd:TIGR00957  774 AVYSNADIYLFDDPLSAVDA 793
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
12-111 3.68e-11

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: 58.33  E-value: 3.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  12 VRHYRDHIGVVSQEPVLFGTTISNNIK-YGRddVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAI 90
Cdd:cd03289   72 LQKWRKAFGVIPQKVFIFSGTFRKNLDpYGK--WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCL 149
                         90       100
                 ....*....|....*....|.
gi 255708373  91 ARALVRNPKILILDEATSALD 111
Cdd:cd03289  150 ARSVLSKAKILLLDEPSAHLD 170
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
78-122 4.12e-11

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: 57.86  E-value: 4.12e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 255708373   78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:TIGR01184 113 GQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
12-113 5.17e-11

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 57.84  E-value: 5.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  12 VRHYRDHIGVVSQEPVLF-GTTISNNIKYGRDDVTDEEMERAAREANaydfimEFPNKFNtLVGEKGA---QMSGGQKQR 87
Cdd:PRK11264  80 IRQLRQHVGFVFQNFNLFpHRTVLENIIEGPVIVKGEPKEEATARAR------ELLAKVG-LAGKETSyprRLSGGQQQR 152
                         90       100
                 ....*....|....*....|....*.
gi 255708373  88 IAIARALVRNPKILILDEATSALDSE 113
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPE 178
PLN03130 PLN03130
ABC transporter C family member; Provisional
16-112 5.41e-11

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 58.60  E-value: 5.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   16 RDHIGVVSQEPVLFGTTISNNIKYGrDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALV 95
Cdd:PLN03130  678 RGTVAYVPQVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVY 756
                          90
                  ....*....|....*..
gi 255708373   96 RNPKILILDEATSALDS 112
Cdd:PLN03130  757 SNSDVYIFDDPLSALDA 773
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
74-124 6.26e-11

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 57.38  E-value: 6.26e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255708373  74 GEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:PRK11247 128 NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIES 178
PTZ00243 PTZ00243
ABC transporter; Provisional
19-112 6.82e-11

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 58.25  E-value: 6.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   19 IGVVSQEPVLFGTTISNNIKYgrddvTDEEmeRAAREANAYDF------IMEFPNKFNTLVGEKGAQMSGGQKQRIAIAR 92
Cdd:PTZ00243  723 IAYVPQQAWIMNATVRGNILF-----FDEE--DAARLADAVRVsqleadLAQLGGGLETEIGEKGVNLSGGQKARVSLAR 795
                          90       100
                  ....*....|....*....|
gi 255708373   93 ALVRNPKILILDEATSALDS 112
Cdd:PTZ00243  796 AVYANRDVYLLDDPLSALDA 815
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
19-107 1.03e-10

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


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 56.76  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   19 IGVVSQEPVLFGT-TISNNIKYGrddvtdeeME-RAAREANAYDFIME-FPNKFNTLvGEKGAQMSGGQKQRIAIARALV 95
Cdd:TIGR03410  77 IAYVPQGREIFPRlTVEENLLTG--------LAaLPRRSRKIPDEIYElFPVLKEML-GRRGGDLSGGQQQQLAIARALV 147
                          90
                  ....*....|..
gi 255708373   96 RNPKILILDEAT 107
Cdd:TIGR03410 148 TRPKLLLLDEPT 159
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
79-111 1.17e-10

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 57.39  E-value: 1.17e-10
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:COG4172  156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
19-113 1.63e-10

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: 56.19  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  19 IGVVSQEPVLFG-TTISNNIKYGRddvtdeEMERAAREANAyDFIMEFPNKFNTLVGEKG------AQMSGGQKQRIAIA 91
Cdd:cd03296   76 VGFVFQHYALFRhMTVFDNVAFGL------RVKPRSERPPE-AEIRAKVHELLKLVQLDWladrypAQLSGGQRQRVALA 148
                         90       100
                 ....*....|....*....|..
gi 255708373  92 RALVRNPKILILDEATSALDSE 113
Cdd:cd03296  149 RALAVEPKVLLLDEPFGALDAK 170
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
16-122 1.80e-10

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 56.39  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  16 RDHIGVVSQEPVLF-GTTISNNIKYG--------RDDVTDEEMERAAREANAYDfimEFPNKFNtlvgEKGAQMSGGQKQ 86
Cdd:PRK14267  84 RREVGMVFQYPNPFpHLTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWD---EVKDRLN----DYPSNLSGGQRQ 156
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 255708373  87 RIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELL 192
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
18-124 1.83e-10

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 56.81  E-value: 1.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  18 HIGVVSQEPVLF-GTTISNNIKYGRDDVTDEEmeraareanaydfimefpnkFNTLVGEKG---------AQMSGGQKQR 87
Cdd:PRK11144  77 RIGYVFQDARLFpHYKVRGNLRYGMAKSMVAQ--------------------FDKIVALLGieplldrypGSLSGGEKQR 136
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 255708373  88 IAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:PRK11144 137 VAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
19-111 2.50e-10

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: 55.58  E-value: 2.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  19 IGVVSQEPVLFG-TTISNNIKYGR------DDVTDEEMERAAREANAYDFIMEFPNkfntlvgekgaQMSGGQKQRIAIA 91
Cdd:cd03298   72 VSMLFQENNLFAhLTVEQNVGLGLspglklTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALA 140
                         90       100
                 ....*....|....*....|
gi 255708373  92 RALVRNPKILILDEATSALD 111
Cdd:cd03298  141 RVLVRDKPVLLLDEPFAALD 160
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
76-107 3.16e-10

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: 55.37  E-value: 3.16e-10
                         10        20        30
                 ....*....|....*....|....*....|..
gi 255708373  76 KGAQMSGGQKQRIAIARALVRNPKILILDEAT 107
Cdd:COG0410  133 RAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
79-112 4.62e-10

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 54.97  E-value: 4.62e-10
                         10        20        30
                 ....*....|....*....|....*....|....
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDS 112
Cdd:cd03234  143 GISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
80-122 4.73e-10

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 54.55  E-value: 4.73e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 255708373  80 MSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:NF040873 120 LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALL 162
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
69-126 4.93e-10

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: 54.68  E-value: 4.93e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255708373  69 FNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKKK 126
Cdd:cd03266  126 MEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLR 183
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
81-114 5.31e-10

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 54.48  E-value: 5.31e-10
                         10        20        30
                 ....*....|....*....|....*....|....
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSES 114
Cdd:cd03213  113 SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
12-115 6.29e-10

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 55.22  E-value: 6.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  12 VRHYRDHIGVVSQEPVL---FgTTISNNIKYGRddvtdeEMERAAREANA-YDFIMEFP---NKFNTLVgekgAQMSGGQ 84
Cdd:PRK13536 109 ARLARARIGVVPQFDNLdleF-TVRENLLVFGR------YFGMSTREIEAvIPSLLEFArleSKADARV----SDLSGGM 177
                         90       100       110
                 ....*....|....*....|....*....|.
gi 255708373  85 KQRIAIARALVRNPKILILDEATSALDSESK 115
Cdd:PRK13536 178 KRRLTLARALINDPQLLILDEPTTGLDPHAR 208
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
70-124 6.63e-10

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 55.05  E-value: 6.63e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 255708373   70 NTLVGEKGAQ--MSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:TIGR00955 155 NTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKG 211
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
1-111 7.31e-10

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 54.02  E-value: 7.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVrhYRDHIGVVSQEPVLFG-TTISNNIKYGrddvTDEEMERAAREANAYDFIMEfpnkfntlVGEKG-- 77
Cdd:COG4136   62 LLNGRRLTALPA--EQRRIGILFQDDLLFPhLSVGENLAFA----LPPTIGRAQRRARVEQALEE--------AGLAGfa 127
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 255708373  78 ----AQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:COG4136  128 drdpATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
81-111 7.45e-10

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 55.10  E-value: 7.45e-10
                         10        20        30
                 ....*....|....*....|....*....|.
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALD 193
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
19-110 7.61e-10

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 55.03  E-value: 7.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  19 IGVVSQEPVLFGT-TISNNIKYGRDD----VTDeeMERAAREanaydfIMEFPNKF------NTLVGekgaQMSGGQKQR 87
Cdd:COG3845   82 IGMVHQHFMLVPNlTVAENIVLGLEPtkggRLD--RKAARAR------IRELSERYgldvdpDAKVE----DLSVGEQQR 149
                         90       100
                 ....*....|....*....|...
gi 255708373  88 IAIARALVRNPKILILDEATSAL 110
Cdd:COG3845  150 VEILKALYRGARILILDEPTAVL 172
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
11-111 9.96e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 54.26  E-value: 9.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  11 NVRHYRDHIGVVSQ--EPVLFGTTISNNIKYGRDD--VTDEEMERAAREANAydfimefpnkfntLVG------EKGA-Q 79
Cdd:PRK13634  79 KLKPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIE-------------LVGlpeellARSPfE 145
                         90       100       110
                 ....*....|....*....|....*....|..
gi 255708373  80 MSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
79-111 1.65e-09

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 54.09  E-value: 1.65e-09
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALD 495
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
76-126 1.69e-09

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 54.08  E-value: 1.69e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255708373  76 KGAQMSGGQKQRIAIARALVRNPKILILDEATSALDseSKSAVQAALEKKK 126
Cdd:PRK11650 131 KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD--AKLRVQMRLEIQR 179
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
50-124 1.75e-09

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 53.96  E-value: 1.75e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708373  50 ERAAREANAYDFIMEFpnKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:PRK10535 117 ERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQ 189
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
16-118 2.12e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 53.54  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  16 RDHIGVVSQEP--VLFGTTISNNIKYGRDDV--TDEEMERAAREANAYDFIMEFPNKfntlvgeKGAQMSGGQKQRIAIA 91
Cdd:PRK13639  77 RKTVGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEALKAVGMEGFENK-------PPHHLSGGQKKRVAIA 149
                         90       100
                 ....*....|....*....|....*..
gi 255708373  92 RALVRNPKILILDEATSALDSESKSAV 118
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQI 176
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
11-126 2.35e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 53.32  E-value: 2.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  11 NVRHYRDHIGVVSQEP--VLFGTTISNNIKYGRDDVTDEEmERAAREANAYDFIMEFPNKFntlVGEKGAQMSGGQKQRI 88
Cdd:PRK13631 110 NFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKK-SEAKKLAKFYLNKMGLDDSY---LERSPFGLSGGQKRRV 185
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 255708373  89 AIARALVRNPKILILDEATSALDSESKSA-VQAALEKKK 126
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPKGEHEmMQLILDAKA 224
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
6-126 2.36e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 53.13  E-value: 2.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   6 DIRALNVRHYRDHIGVVSQEPVLF-GTTISNNIKY--GRDDVTDEE-----MERAAREANAYDfimEFPNKFNTlvgeKG 77
Cdd:PRK14246  79 DIFQIDAIKLRKEVGMVFQQPNPFpHLSIYDNIAYplKSHGIKEKReikkiVEECLRKVGLWK---EVYDRLNS----PA 151
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKKK 126
Cdd:PRK14246 152 SQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELK 200
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
12-111 2.44e-09

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 53.76  E-value: 2.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    12 VRHyRDHIGVVSQEPVLFGTTISNNIKYGrddVTDEEMeRAAREANAYDF---IMEFPNKFNTLVGEKGAQMSGGQKQRI 88
Cdd:TIGR01271  483 IKH-SGRISFSPQTSWIMPGTIKDNIIFG---LSYDEY-RYTSVIKACQLeedIALFPEKDKTVLGEGGITLSGGQRARI 557
                           90       100
                   ....*....|....*....|...
gi 255708373    89 AIARALVRNPKILILDEATSALD 111
Cdd:TIGR01271  558 SLARAVYKDADLYLLDSPFTHLD 580
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
1-126 2.78e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 52.99  E-value: 2.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEPVLFGT-TISNNIKYG----RDDVTDEEMERAAREA-NAYDFIMEFPNKFNTLVG 74
Cdd:PRK14247  66 YLDGQDIFKMDVIELRRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWAlEKAQLWDEVKDRLDAPAG 145
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255708373  75 ekgaQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAA-LEKKK 126
Cdd:PRK14247 146 ----KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLfLELKK 194
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
11-111 3.85e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 52.78  E-value: 3.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  11 NVRHYRDHIGVVSQ--EPVLFGTTISNNIKYGRDD--VTDEEMERAAREanaYDFIMEFPNKFntlVGEKGAQMSGGQKQ 86
Cdd:PRK13651  99 KIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSmgVSKEEAKKRAAK---YIELVGLDESY---LQRSPFELSGGQKR 172
                         90       100
                 ....*....|....*....|....*
gi 255708373  87 RIAIARALVRNPKILILDEATSALD 111
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLD 197
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
13-126 4.01e-09

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: 52.37  E-value: 4.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  13 RHYRDHIGVVSQEPVLFG--TTISNNIKYGR-DDVTDEEMERAAREANAYDFIMEFPNKfntLVGekgaQMSGGQKQRIA 89
Cdd:cd03265   69 REVRRRIGIVFQDLSVDDelTGWENLYIHARlYGVPGAERRERIDELLDFVGLLEAADR---LVK----TYSGGMRRRLE 141
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 255708373  90 IARALVRNPKILILDEATSALDSESKSAVQAALEKKK 126
Cdd:cd03265  142 IARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLK 178
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
3-120 5.10e-09

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: 52.16  E-value: 5.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   3 DENDIRALNVrHYRDHIGV--VSQEPVLF-GTTISNNIKygrddVTDEEME--RAAREANAYDFIMEFpnKFNTLVGEKG 77
Cdd:cd03218   60 DGQDITKLPM-HKRARLGIgyLPQEASIFrKLTVEENIL-----AVLEIRGlsKKEREEKLEELLEEF--HITHLRKSKA 131
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQA 120
Cdd:cd03218  132 SSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQK 174
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
78-113 6.40e-09

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 51.89  E-value: 6.40e-09
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSE 113
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE 186
cbiO PRK13643
energy-coupling factor transporter ATPase;
12-123 6.41e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 52.04  E-value: 6.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  12 VRHYRDHIGVVSQEP--VLFGTTISNNIKYGRDD--VTDEEMERAAREAnaydfiMEFPNKFNTLVGEKGAQMSGGQKQR 87
Cdd:PRK13643  79 IKPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEK------LEMVGLADEFWEKSPFELSGGQMRR 152
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 255708373  88 IAIARALVRNPKILILDEATSALDSESKSAVQAALE 123
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFE 188
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
1-111 8.95e-09

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 51.43  E-value: 8.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVR-HYRDHIGVVSQEPVLFGT-TISNNIKYG---RDDVTDEEmeraaREANAYDFIMEFpnKFNTLVGE 75
Cdd:PRK10895  61 IIDDEDISLLPLHaRARRGIGYLPQEASIFRRlSVYDNLMAVlqiRDDLSAEQ-----REDRANELMEEF--HIEHLRDS 133
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 255708373  76 KGAQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK10895 134 MGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
7-122 1.37e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 51.27  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   7 IRALNVRHYRDHIGVVSQEP--VLFGTTISNNIKYGRDD--VTDEEMERAAREA----NAYDFIMEFPNkfntlvgekga 78
Cdd:PRK13647  69 VNAENEKWVRSKVGLVFQDPddQVFSSTVWDDVAFGPVNmgLDKDEVERRVEEAlkavRMWDFRDKPPY----------- 137
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:PRK13647 138 HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEIL 181
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
80-112 1.87e-08

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 50.80  E-value: 1.87e-08
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  80 MSGGQKQRIAIARALVRNPKILILDEATSALDS 112
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
78-118 2.68e-08

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 50.20  E-value: 2.68e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAV 118
Cdd:PRK11629 144 SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
79-120 2.75e-08

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 50.47  E-value: 2.75e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDseskSAVQA 120
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALD----VSVQA 193
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
16-111 2.87e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 50.23  E-value: 2.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  16 RDHIGVVSQEP--VLFGTTISNNIKYGRDDVT--DEEMERAAREANAYDFIMEFPNKfntlvgeKGAQMSGGQKQRIAIA 91
Cdd:PRK13636  81 RESVGMVFQDPdnQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIA 153
                         90       100
                 ....*....|....*....|
gi 255708373  92 RALVRNPKILILDEATSALD 111
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLD 173
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
62-111 3.04e-08

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 50.24  E-value: 3.04e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 255708373  62 IMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:cd03291  142 ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
13-115 3.74e-08

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 50.19  E-value: 3.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  13 RHYRDHIGVVSQ----EPVLfgTTISNNIKYGRDDVTDEEMERAAREAnaydfIMEFP---NKFNTLVGEkgaqMSGGQK 85
Cdd:PRK13537  76 RHARQRVGVVPQfdnlDPDF--TVRENLLVFGRYFGLSAAAARALVPP-----LLEFAkleNKADAKVGE----LSGGMK 144
                         90       100       110
                 ....*....|....*....|....*....|
gi 255708373  86 QRIAIARALVRNPKILILDEATSALDSESK 115
Cdd:PRK13537 145 RRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
11-119 3.83e-08

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 50.09  E-value: 3.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  11 NVRHYRDHIGVVSQEPVLFGTTISNNIKYG---RDDVTDEEMERAAR----EANAYDFIMEfpnkfntLVGEKGAQMSGG 83
Cdd:PRK14271  95 DVLEFRRRVGMLFQRPNPFPMSIMDNVLAGvraHKLVPRKEFRGVAQarltEVGLWDAVKD-------RLSDSPFRLSGG 167
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 255708373  84 QKQRIAIARALVRNPKILILDEATSALDSESKSAVQ 119
Cdd:PRK14271 168 QQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
79-111 4.47e-08

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 49.77  E-value: 4.47e-08
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 255708373  79 QMSGGQKQRIAIARALVR------NPKILILDEATSALD 111
Cdd:PRK13548 134 QLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALD 172
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
80-124 5.44e-08

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: 49.80  E-value: 5.44e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 255708373   80 MSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEE 213
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
75-122 5.86e-08

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 49.24  E-value: 5.86e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 255708373  75 EKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:PRK09984 148 QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTL 195
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
70-123 7.23e-08

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 48.14  E-value: 7.23e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 255708373    70 NTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALE 123
Cdd:smart00382  51 LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104
cbiO PRK13645
energy-coupling factor transporter ATPase;
12-111 7.63e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 49.24  E-value: 7.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  12 VRHYRDHIGVVSQEP--VLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFImEFPNKFntlVGEKGAQMSGGQKQRIA 89
Cdd:PRK13645  85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPEDY---VKRSPFELSGGQKRRVA 160
                         90       100
                 ....*....|....*....|..
gi 255708373  90 IARALVRNPKILILDEATSALD 111
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLD 182
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
75-111 7.74e-08

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 48.75  E-value: 7.74e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 255708373  75 EKGAQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:cd03268  122 KKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
11-113 7.90e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 49.03  E-value: 7.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  11 NVRHYRDHIGVVSQEP--VLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFImefpnKFNTLVGEKGAQMSGGQKQRI 88
Cdd:PRK13652  72 NIREVRKFVGLVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRV 146
                         90       100
                 ....*....|....*....|....*
gi 255708373  89 AIARALVRNPKILILDEATSALDSE 113
Cdd:PRK13652 147 AIAGVIAMEPQVLVLDEPTAGLDPQ 171
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
62-122 8.28e-08

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


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 48.20  E-value: 8.28e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708373  62 IMEFPNKFNTLVGekgAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:cd03215   90 VLDLSVAENIALS---SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLI 147
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
76-123 9.53e-08

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 48.33  E-value: 9.53e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 255708373  76 KGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALE 123
Cdd:PRK13539 124 PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIR 171
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
16-124 1.02e-07

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 48.85  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  16 RDHIGVVSQEP--VLFGTTISNNIKYGRDDVTDEEMERAAREANAYdfimefpnkfnTLVGEKGAQ------MSGGQKQR 87
Cdd:PRK13638  76 RQQVATVFQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEAL-----------TLVDAQHFRhqpiqcLSHGQKKR 144
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 255708373  88 IAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRR 181
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
79-120 1.21e-07

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 48.57  E-value: 1.21e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDseskSAVQA 120
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALD----VTVQA 198
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
2-111 1.62e-07

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 48.30  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   2 VDENDIRALNVRHYRDHIGVVSQEPVL-FGTTISNNIKYGRD------DVTDEEMERAAREANAYDFIMEFPNKFNTlvg 74
Cdd:PRK09536  62 VAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQVVEMGRTphrsrfDTWTETDRAAVERAMERTGVAQFADRPVT--- 138
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 255708373  75 ekgaQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK09536 139 ----SLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
PLN03211 PLN03211
ABC transporter G-25; Provisional
70-114 2.52e-07

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 47.95  E-value: 2.52e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 255708373  70 NTLVGEKGAQ-MSGGQKQRIAIARALVRNPKILILDEATSALDSES 114
Cdd:PLN03211 196 NTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
79-126 2.90e-07

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: 47.49  E-value: 2.90e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 255708373   79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKKK 126
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAR 474
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
83-116 3.15e-07

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 47.48  E-value: 3.15e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 255708373  83 GQKQRIAIARALVRNPKILILDEATSALDSESKS 116
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
80-123 3.50e-07

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 47.37  E-value: 3.50e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 255708373  80 MSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALE 123
Cdd:COG0488  433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD 476
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
78-114 3.52e-07

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 47.08  E-value: 3.52e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSES 114
Cdd:PRK10584 145 AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
51-115 3.64e-07

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 47.31  E-value: 3.64e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  51 RAAREANAY-DFIMEF----PNKfNTLVGEkgaqMSGGQKQRIAIARALVRNPKILILDEATSALDSESK 115
Cdd:PRK10762 367 KHADEQQAVsDFIRLFniktPSM-EQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAK 431
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
70-118 4.03e-07

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 47.23  E-value: 4.03e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 255708373  70 NTLVGEKGaqmsGGQKQRIAIARALVRNPKILILDEATSALdSESKSAV 118
Cdd:PRK13549 138 ATPVGNLG----LGQQQLVEIAKALNKQARLLILDEPTASL-TESETAV 181
cbiO PRK13641
energy-coupling factor transporter ATPase;
11-115 4.05e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 47.13  E-value: 4.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  11 NVRHYRDHIGVVSQ--EPVLFGTTISNNIKYGRDD--VTDEEMERAAREANAYDFIMEfpnkfnTLVGEKGAQMSGGQKQ 86
Cdd:PRK13641  79 NLKKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKALKWLKKVGLSE------DLISKSPFELSGGQMR 152
                         90       100
                 ....*....|....*....|....*....
gi 255708373  87 RIAIARALVRNPKILILDEATSALDSESK 115
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
79-111 4.28e-07

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 47.04  E-value: 4.28e-07
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
78-114 4.43e-07

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 47.24  E-value: 4.43e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 255708373   78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSES 114
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
41-112 5.06e-07

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 47.03  E-value: 5.06e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255708373    41 RDDVTDEEmERAAREANAYDFIMEFPNKFNTLVGE---KGaqMSGGQKQRIAIARALVRNPKILILDEATSALDS 112
Cdd:TIGR00956  171 RPDGVSRE-EYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
PTZ00243 PTZ00243
ABC transporter; Provisional
2-121 5.77e-07

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 47.08  E-value: 5.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373    2 VDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIkygrD---DVTDEEM----------ERAAREANAYDfimefpnk 68
Cdd:PTZ00243 1369 VNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV----DpflEASSAEVwaalelvglrERVASESEGID-------- 1436
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 255708373   69 fnTLVGEKGAQMSGGQKQRIAIARALVRNPKILIL-DEATS----ALDSESKSAVQAA 121
Cdd:PTZ00243 1437 --SRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATAnidpALDRQIQATVMSA 1492
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
80-111 6.26e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 46.62  E-value: 6.26e-07
                         10        20        30
                 ....*....|....*....|....*....|..
gi 255708373  80 MSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
79-124 6.77e-07

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 46.57  E-value: 6.77e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:PRK10070 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVK 209
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
79-113 7.00e-07

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 46.02  E-value: 7.00e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSE 113
Cdd:PRK10908 137 QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
81-122 7.17e-07

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 46.07  E-value: 7.17e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDseskSAVQAAL 122
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD----VSVQARL 190
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
76-105 7.86e-07

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 46.18  E-value: 7.86e-07
                         10        20        30
                 ....*....|....*....|....*....|
gi 255708373  76 KGAQMSGGQKQRIAIARALVRNPKILILDE 105
Cdd:COG1137  133 KAYSLSGGERRRVEIARALATNPKFILLDE 162
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
78-114 9.67e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 46.10  E-value: 9.67e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSES 114
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
78-114 1.04e-06

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 45.43  E-value: 1.04e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 255708373   78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSES 114
Cdd:TIGR01189 126 AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
78-114 1.09e-06

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 45.56  E-value: 1.09e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSES 114
Cdd:cd03231  124 AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
78-114 1.29e-06

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 45.88  E-value: 1.29e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSES 114
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
79-111 1.35e-06

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 45.48  E-value: 1.35e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:COG4152  129 ELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
80-110 1.68e-06

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: 45.51  E-value: 1.68e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 255708373   80 MSGGQKQRIAIARALVRNPKILILDEATSAL 110
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
cbiO PRK13644
energy-coupling factor transporter ATPase;
16-124 1.91e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 44.98  E-value: 1.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  16 RDHIGVVSQEP--VLFGTTISNNIKYGRDDV------TDEEMERAAREANAYDFIMEFPNkfntlvgekgaQMSGGQKQR 87
Cdd:PRK13644  76 RKLVGIVFQNPetQFVGRTVEEDLAFGPENLclppieIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQC 144
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 255708373  88 IAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKK 181
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
81-107 2.14e-06

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 45.01  E-value: 2.14e-06
                         10        20
                 ....*....|....*....|....*..
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEAT 107
Cdd:COG1129  396 SGGNQQKVVLAKWLATDPKVLILDEPT 422
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
72-118 2.35e-06

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 45.10  E-value: 2.35e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 255708373    72 LVGEKGAQMSGGQKQRIAIARALVRNPKILI-LDEATSALDSESKSAV 118
Cdd:TIGR00956  894 VVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSI 941
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
48-113 2.47e-06

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: 44.74  E-value: 2.47e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255708373  48 EMERAAREAnAYDfIMEF---PNKFNTLVGEkgaqMSGGQKQRIAIARALVRNPKILILDEATSALDSE 113
Cdd:cd03219  115 REEREARER-AEE-LLERvglADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPE 177
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
67-111 2.50e-06

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 44.69  E-value: 2.50e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 255708373  67 NKFNTLVGekgaQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:COG1101  140 NRLDTKVG----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
78-115 2.86e-06

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 44.92  E-value: 2.86e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESK 115
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAK 441
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
33-114 3.52e-06

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 43.79  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  33 ISNNIKYGRDDVtDEEMERAAREANaydFIMEFPNKFNTL-VGE--------KGAQM----SGGQKQRIAIARALVRNPK 99
Cdd:cd03233   63 VEGDIHYNGIPY-KEFAEKYPGEII---YVSEEDVHFPTLtVREtldfalrcKGNEFvrgiSGGERKRVSIAEALVSRAS 138
                         90
                 ....*....|....*
gi 255708373 100 ILILDEATSALDSES 114
Cdd:cd03233  139 VLCWDNSTRGLDSST 153
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
50-113 4.64e-06

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: 43.87  E-value: 4.64e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255708373  50 ERAAREAnAYDfIMEFPN---KFNTLVGEkgaqMSGGQKQRIAIARALVRNPKILILDEATSALDSE 113
Cdd:COG0411  126 EREARER-AEE-LLERVGladRADEPAGN----LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPE 186
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
36-124 5.20e-06

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 43.28  E-value: 5.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  36 NIKYGRDDVTDEEMERAAREA--NAYDFIMEFPN-KFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDS 112
Cdd:cd03217   58 EILFKGEDITDLPPEERARLGifLAFQYPPEIPGvKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
                         90
                 ....*....|..
gi 255708373 113 ESKSAVQAALEK 124
Cdd:cd03217  138 DALRLVAEVINK 149
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
1-111 5.70e-06

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 44.08  E-value: 5.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRD-HIGVVSQEPVL-------FGTTISNNIKYGRDDVTDEEMERAAREANAydfiMEFPNKfNTL 72
Cdd:PRK10261  87 VIELSEQSAAQMRHVRGaDMAMIFQEPMTslnpvftVGEQIAESIRLHQGASREEAMVEAKRMLDQ----VRIPEA-QTI 161
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 255708373  73 VGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK10261 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALD 200
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
79-122 6.24e-06

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: 43.48  E-value: 6.24e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:cd03267  153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFL 196
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
79-111 7.69e-06

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 43.04  E-value: 7.69e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:cd03269  128 ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
84-124 8.37e-06

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 43.00  E-value: 8.37e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 255708373  84 QKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03232  113 QRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKK 153
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
81-111 8.81e-06

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 43.13  E-value: 8.81e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:COG0396  142 SGGEKKRNEILQMLLLEPKLAILDETDSGLD 172
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
79-111 1.00e-05

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 42.79  E-value: 1.00e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK09544 120 KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
80-124 1.02e-05

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 42.56  E-value: 1.02e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 255708373  80 MSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03222   72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
80-124 1.19e-05

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 42.78  E-value: 1.19e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 255708373  80 MSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:cd03237  116 LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
79-111 1.30e-05

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 42.85  E-value: 1.30e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:COG1245  212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
79-111 1.34e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 42.87  E-value: 1.34e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
78-123 1.35e-05

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 42.48  E-value: 1.35e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDsesKSAVqAALE 123
Cdd:PRK13538 128 RQLSAGQQRRVALARLWLTRAPLWILDEPFTAID---KQGV-ARLE 169
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
79-122 1.64e-05

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 42.38  E-value: 1.64e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:COG4586  154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFL 197
PLN03140 PLN03140
ABC transporter G family member; Provisional
62-118 1.72e-05

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 42.53  E-value: 1.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 255708373   62 IMEFPNKFNTLVGEKGAQ-MSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAV 118
Cdd:PLN03140 1001 LVELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIV 1058
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
19-110 2.28e-05

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 42.35  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  19 IGVVSQEPVLFGT-TISNNIKYGrddvtdeemerAAREANAYdfimefpNKFNTLVGEKGAQ----MSGG-----QKQRI 88
Cdd:PRK15439  88 IYLVPQEPLLFPNlSVKENILFG-----------LPKRQASM-------QKMKQLLAALGCQldldSSAGslevaDRQIV 149
                         90       100
                 ....*....|....*....|..
gi 255708373  89 AIARALVRNPKILILDEATSAL 110
Cdd:PRK15439 150 EILRGLMRDSRILILDEPTASL 171
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
80-111 2.37e-05

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 42.31  E-value: 2.37e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  80 MSGGQkQRIA-IARALVRNPKILILDEATSALD 111
Cdd:PRK10938 402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1-111 2.38e-05

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 41.92  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDHIGVVSQEPVL-FGTTISNNIKYGRD-------DVTDEEMERAAREanaydfiMEfPNKFNTL 72
Cdd:PRK11231  60 FLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRELVAYGRSpwlslwgRLSAEDNARVNQA-------ME-QTRINHL 131
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 255708373  73 VGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK11231 132 ADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
78-115 3.50e-05

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 41.73  E-value: 3.50e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 255708373   78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESK 115
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAK 439
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
13-110 3.54e-05

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 41.40  E-value: 3.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  13 RHYRDHIGVVSQEPVLFG-TTISNNIKYGRDDVTDEEMERaaREANAYDFimeFPNKFNTLVGEKGAqMSGGQKQRIAIA 91
Cdd:PRK11614  76 KIMREAVAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERRIQRAGT-MSGGEQQMLAIG 149
                         90
                 ....*....|....*....
gi 255708373  92 RALVRNPKILILDEATSAL 110
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGL 168
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
48-118 3.89e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 41.64  E-value: 3.89e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255708373  48 EMERAAREANAYDFIMEFpnKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAV 118
Cdd:NF000106 115 DLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEV 183
GguA NF040905
sugar ABC transporter ATP-binding protein;
16-111 3.90e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 41.31  E-value: 3.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  16 RDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREanaydfimEFPNKFNTL---VGEKGAQMSGGQKQRIAIAR 92
Cdd:NF040905 346 RKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAE--------EYRKKMNIKtpsVFQKVGNLSGGNQQKVVLSK 417
                         90
                 ....*....|....*....
gi 255708373  93 ALVRNPKILILDEATSALD 111
Cdd:NF040905 418 WLFTDPDVLILDEPTRGID 436
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
80-111 4.84e-05

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 41.19  E-value: 4.84e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 255708373  80 MSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
PLN03073 PLN03073
ABC transporter F family; Provisional
79-111 4.95e-05

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 41.38  E-value: 4.95e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
19-116 5.66e-05

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 41.14  E-value: 5.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  19 IGVVSQEPVLFGT-TISNNIKYGRDDVTD------EEMERaarEANAYDFIMEFPNKFNTLVGEkgaqMSGGQKQRIAIA 91
Cdd:PRK10762  81 IGIIHQELNLIPQlTIAENIFLGREFVNRfgridwKKMYA---EADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIA 153
                         90       100
                 ....*....|....*....|....*.
gi 255708373  92 RALVRNPKILILDEATSAL-DSESKS 116
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALtDTETES 179
GguA NF040905
sugar ABC transporter ATP-binding protein;
70-117 6.31e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.93  E-value: 6.31e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 255708373  70 NTLVGEKGAqmsgGQKQRIAIARALVRNPKILILDEATSALdSESKSA 117
Cdd:NF040905 134 DTLVTDIGV----GKQQLVEIAKALSKDVKLLILDEPTAAL-NEEDSA 176
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
81-124 6.66e-05

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 40.65  E-value: 6.66e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEK 483
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
71-111 8.68e-05

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 40.16  E-value: 8.68e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 255708373  71 TLVGEKG-AQ-----MSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK10575 133 SLVGLKPlAHrlvdsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
83-111 9.49e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 40.49  E-value: 9.49e-05
                         10        20
                 ....*....|....*....|....*....
gi 255708373  83 GQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVD 429
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
80-112 1.09e-04

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 40.28  E-value: 1.09e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  80 MSGGQKQRIAIARALVRNPKILILDEATSALDS 112
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
81-118 1.20e-04

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 40.15  E-value: 1.20e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAV 118
Cdd:COG1245  457 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
81-118 1.20e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 40.18  E-value: 1.20e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALDSESKSAV 118
Cdd:PRK13409 455 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 492
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
75-126 1.24e-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: 40.38  E-value: 1.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 255708373    75 EKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKKK 126
Cdd:TIGR01257 1057 EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR 1108
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
79-111 1.26e-04

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 39.66  E-value: 1.26e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:cd03236  139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
78-124 1.84e-04

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 39.17  E-value: 1.84e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 255708373  78 AQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:COG2401  135 KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQK 181
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
75-113 3.24e-04

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 39.00  E-value: 3.24e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 255708373  75 EKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSE 113
Cdd:PRK09700 141 EKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
PLN03073 PLN03073
ABC transporter F family; Provisional
80-123 3.39e-04

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 39.07  E-value: 3.39e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 255708373  80 MSGGQKQRIAIARALVRNPKILILDEATSALDSEsksAVQAALE 123
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD---AVEALIQ 668
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
73-122 4.08e-04

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 38.61  E-value: 4.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 255708373  73 VGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:PRK10636 424 VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
79-110 4.19e-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: 4.19e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 255708373   79 QMSGGQKQRIAIARALVRNPKILILDEATSAL 110
Cdd:TIGR02633 141 DYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
80-115 4.30e-04

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 38.56  E-value: 4.30e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 255708373  80 MSGGQKQRIAIARALVRNPKILILDEATSALDSESK 115
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAK 427
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
79-111 5.31e-04

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 38.14  E-value: 5.31e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK10418 140 EMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
75-110 5.90e-04

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 38.17  E-value: 5.90e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 255708373  75 EKGAQMSGGQKQRIAIARALVRNPKILILDEATSAL 110
Cdd:PRK10982 130 AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
72-111 6.27e-04

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 38.04  E-value: 6.27e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 255708373  72 LVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK10253 136 LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
80-113 8.37e-04

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 37.62  E-value: 8.37e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 255708373  80 MSGGQKQRIAIARALVRNPKILILDEATSALDSE 113
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
79-123 8.40e-04

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: 37.61  E-value: 8.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 255708373   79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALE 123
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
81-111 1.06e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 37.41  E-value: 1.06e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 255708373  81 SGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
79-122 1.09e-03

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 37.17  E-value: 1.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAAL 122
Cdd:PRK15056 142 ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLL 185
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
83-120 1.54e-03

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 36.89  E-value: 1.54e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 255708373  83 GQKQRIAIARALVRNPKILILDEATSALDSESKSAVQA 120
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDE 194
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
79-114 1.80e-03

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


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 36.43  E-value: 1.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 255708373  79 QMSGGQKQ------RIAIARALVRNPKILILDEATSALDSES 114
Cdd:cd03240  115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN 156
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1-111 2.21e-03

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 36.54  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   1 MVDENDIRALNVRHYRDH-IGVVSQEPVLFGT----TISNNI--------KYGRDDVtdeeMERAAREANAYDFIMEF-- 65
Cdd:COG3845  316 RLDGEDITGLSPRERRRLgVAYIPEDRLGRGLvpdmSVAENLilgryrrpPFSRGGF----LDRKAIRAFAEELIEEFdv 391
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 255708373  66 -PNKFNTLVGekgaQMSGGQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:COG3845  392 rTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
79-124 2.28e-03

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 36.06  E-value: 2.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255708373  79 QMSGGQKQRIAIARALVR-----NP--KILILDEATSALDseskSAVQAALEK 124
Cdd:PRK03695 126 QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLD----VAQQAALDR 174
hmuV PRK13547
heme ABC transporter ATP-binding protein;
71-111 2.49e-03

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 36.34  E-value: 2.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 255708373  71 TLVGEKGAQMSGGQKQRIAIARAL---------VRNPKILILDEATSALD 111
Cdd:PRK13547 137 ALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALD 186
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
74-116 3.29e-03

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


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 35.38  E-value: 3.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 255708373  74 GEKGAQMSGGQKQRIAIARALVRNPK--ILILDEATSALDSESKS 116
Cdd:cd03238   82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
79-118 3.34e-03

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 35.92  E-value: 3.34e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAV 118
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEI 448
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
81-115 4.17e-03

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: 35.76  E-value: 4.17e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 255708373    81 SGGQKQRIAIARALVRNPKILILDEATSALDSESK 115
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
83-111 4.36e-03

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 35.64  E-value: 4.36e-03
                         10        20
                 ....*....|....*....|....*....
gi 255708373  83 GQKQRIAIARALVRNPKILILDEATSALD 111
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLD 187
PLN03140 PLN03140
ABC transporter G family member; Provisional
70-114 5.18e-03

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 35.59  E-value: 5.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 255708373   70 NTLVGEKGAQ-MSGGQKQRIAIARALVRNPKILILDEATSALDSES 114
Cdd:PLN03140  326 DTIVGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSST 371
SbcC_Walker_B pfam13558
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ...
78-124 5.48e-03

SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.


Pssm-ID: 463921 [Multi-domain]  Cd Length: 90  Bit Score: 33.75  E-value: 5.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373   78 AQMSGGQKQR---IAIARALV----------RNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:pfam13558  31 GGLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLRA 90
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
58-110 5.65e-03

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 35.37  E-value: 5.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255708373   58 AYDFIMEFPN---KFNTLV---------GEKGAQMSGGQKQRIAIARALVR---NPKILILDEATSAL 110
Cdd:TIGR00630 796 AYEFFEAVPSisrKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGL 863
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
79-118 7.52e-03

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 34.78  E-value: 7.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAV 118
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQI 197
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
28-124 8.37e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 34.60  E-value: 8.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255708373  28 LFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLvgEKGAQMSGGQKQRIAIARALVrnpkiLILDeaT 107
Cdd:COG0419  109 LLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSGL--DPIETLSGGERLRLALADLLS-----LILD--F 179
                         90
                 ....*....|....*..
gi 255708373 108 SALDSESKSAVQAALEK 124
Cdd:COG0419  180 GSLDEERLERLLDALEE 196
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
79-124 8.44e-03

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 34.61  E-value: 8.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 255708373  79 QMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEK 124
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLAS 180
 
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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