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Conserved domains on  [gi|1877026690|ref|WP_180364729|]
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ATP-binding cassette domain-containing protein [Streptococcus pneumoniae]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SunT super family cl34455
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
2-178 2.34e-83

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


The actual alignment was detected with superfamily member COG2274:

Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 259.77  E-value: 2.34e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKN-EVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:COG2274   528 TSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDpDATDEEIIEAARLAGLHDFIEALPMGYDTVVGE 607
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS--QGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:COG2274   608 GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRllKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
                         170       180
                  ....*....|....*....|
gi 1877026690 159 VESGNHKYLMELGGEYYSLY 178
Cdd:COG2274   688 VEDGTHEELLARKGLYAELV 707
 
Name Accession Description Interval E-value
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
2-178 2.34e-83

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: 259.77  E-value: 2.34e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKN-EVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:COG2274   528 TSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDpDATDEEIIEAARLAGLHDFIEALPMGYDTVVGE 607
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS--QGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:COG2274   608 GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRllKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
                         170       180
                  ....*....|....*....|
gi 1877026690 159 VESGNHKYLMELGGEYYSLY 178
Cdd:COG2274   688 VEDGTHEELLARKGLYAELV 707
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
2-180 1.19e-68

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: 208.62  E-value: 1.19e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKN-EVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:cd03253    54 SSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYNIRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:cd03253   134 RGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRdvSKGRTTIVIAHRLSTIVNADKIIVLKDGRI 213
                         170       180
                  ....*....|....*....|..
gi 1877026690 159 VESGNHKYLMELGGEYYSLYTK 180
Cdd:cd03253   214 VERGTHEELLAKGGLYAEMWKA 235
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
3-177 7.17e-66

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 213.65  E-value: 7.17e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQK-IEEVCKAVQIYDEIMAMPMKFNTIISEM 81
Cdd:TIGR03796 533 SGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDAdLVRACKDAAIHDVITSRPGGYDAELAEG 612
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  82 GSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQGCTQIIVAHRLSTIKDADIIFVMKGGKIVES 161
Cdd:TIGR03796 613 GANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQR 692
                         170
                  ....*....|....*.
gi 1877026690 162 GNHKYLMELGGEYYSL 177
Cdd:TIGR03796 693 GTHEELWAVGGAYARL 708
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
2-177 3.47e-56

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 185.93  E-value: 3.47e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL-KNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:PRK13657  388 QSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVgRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGE 467
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:PRK13657  468 RGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDelMKGRTTFIIAHRLSTVRNADRILVFDNGRV 547
                         170
                  ....*....|....*....
gi 1877026690 159 VESGNHKYLMELGGEYYSL 177
Cdd:PRK13657  548 VESGSFDELVARGGRFAAL 566
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
2-113 1.93e-24

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: 93.10  E-value: 1.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNR-SILDNI-------TLKNEVTSQKIEEVCKAVQIYDEImampmk 73
Cdd:pfam00005  38 TEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLrlglllkGLSKREKDARAEEALEKLGLGDLA------ 111
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1877026690  74 fNTIISEMGSNISGGQRQRIALARALINNPSIVILDEATS 113
Cdd:pfam00005 112 -DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
85-148 3.39e-11

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 59.17  E-value: 3.39e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK---SQGCTQIIVAHRLSTIKDAD 148
Cdd:NF040873  120 LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAeehARGATVVVVTHDLELVRRAD 186
GguA NF040905
sugar ABC transporter ATP-binding protein;
3-161 2.26e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.79  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGI-----NINQIDKK---ILSQNLGVVPQdsfllnRSILDNITLKNEV----------TSQKIEEVCKAVQIY 64
Cdd:NF040905   57 EGEILFDGEvcrfkDIRDSEALgivIIHQELALIPY------LSIAENIFLGNERakrgvidwneTNRRARELLAKVGLD 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  65 DEimamPmkfNTIISEMGSnisgGQRQRIALARALINNPSIVILDEATSALdtiNEE------RITKYIKSQGCTQIIVA 138
Cdd:NF040905  131 ES----P---DTLVTDIGV----GKQQLVEIAKALSKDVKLLILDEPTAAL---NEEdsaallDLLLELKAQGITSIIIS 196
                         170       180
                  ....*....|....*....|....
gi 1877026690 139 HRLSTI-KDADIIFVMKGGKIVES 161
Cdd:NF040905  197 HKLNEIrRVADSITVLRDGRTIET 220
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
75-159 8.55e-06

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: 43.52  E-value: 8.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   75 NTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI--------KSQGCTQIIVAHRLSTIKD 146
Cdd:smart00382  51 LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrlllllKSEKNLTVILTTNDEKDLG 130
                           90
                   ....*....|...
gi 1877026690  147 ADIIFVMKGGKIV 159
Cdd:smart00382 131 PALLRRRFDRRIV 143
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
88-116 2.94e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 43.57  E-value: 2.94e-05
                          10        20
                  ....*....|....*....|....*....
gi 1877026690  88 GQRQRIALARALINNPSIVILDEATSALD 116
Cdd:NF033858  401 GIRQRLSLAVAVIHKPELLILDEPTSGVD 429
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
86-162 6.43e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 39.33  E-value: 6.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLSTIKD-ADIIFVMKGGKIVES 161
Cdd:NF000106  146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSmvrDGATVLLTTQYMEEAEQlAHELTVIDRGRVIAD 225

                  .
gi 1877026690 162 G 162
Cdd:NF000106  226 G 226
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
86-116 9.03e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 36.26  E-value: 9.03e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALD 116
Cdd:NF033858  138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
GguA NF040905
sugar ABC transporter ATP-binding protein;
3-116 9.90e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 35.92  E-value: 9.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDG--ININQIDKKIlSQNLGVVPQD----SFLLNRSILDNITLKN--EVTS----QKIEEVCKAVQIYDeimAM 70
Cdd:NF040905  316 SGTVFKDGkeVDVSTVSDAI-DAGLAYVTEDrkgyGLNLIDDIKRNITLANlgKVSRrgviDENEEIKVAEEYRK---KM 391
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1877026690  71 PMKFNTIISEMGsNISGGQRQRIALARALINNPSIVILDEATSALD 116
Cdd:NF040905  392 NIKTPSVFQKVG-NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
 
Name Accession Description Interval E-value
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
2-178 2.34e-83

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: 259.77  E-value: 2.34e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKN-EVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:COG2274   528 TSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDpDATDEEIIEAARLAGLHDFIEALPMGYDTVVGE 607
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS--QGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:COG2274   608 GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRllKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
                         170       180
                  ....*....|....*....|
gi 1877026690 159 VESGNHKYLMELGGEYYSLY 178
Cdd:COG2274   688 VEDGTHEELLARKGLYAELV 707
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
2-179 6.90e-79

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 245.07  E-value: 6.90e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL-KNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:COG1132   393 TSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYgRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGE 472
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:COG1132   473 RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALErlMKGRTTIVIAHRLSTIRNADRILVLDDGRI 552
                         170       180
                  ....*....|....*....|.
gi 1877026690 159 VESGNHKYLMELGGEYYSLYT 179
Cdd:COG1132   553 VEQGTHEELLARGGLYARLYR 573
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
2-180 1.19e-68

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: 208.62  E-value: 1.19e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKN-EVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:cd03253    54 SSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYNIRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:cd03253   134 RGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRdvSKGRTTIVIAHRLSTIVNADKIIVLKDGRI 213
                         170       180
                  ....*....|....*....|..
gi 1877026690 159 VESGNHKYLMELGGEYYSLYTK 180
Cdd:cd03253   214 VERGTHEELLAKGGLYAEMWKA 235
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
2-180 6.54e-67

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: 204.31  E-value: 6.54e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL-KNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:cd03249    56 TSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYgKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGE 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:cd03249   136 RGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDraMKGRTTIVIAHRLSTIRNADLIAVLQNGQV 215
                         170       180
                  ....*....|....*....|..
gi 1877026690 159 VESGNHKYLMELGGEYYSLYTK 180
Cdd:cd03249   216 VEQGTHDELMAQKGVYAKLVKA 237
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
3-177 7.17e-66

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 213.65  E-value: 7.17e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQK-IEEVCKAVQIYDEIMAMPMKFNTIISEM 81
Cdd:TIGR03796 533 SGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDAdLVRACKDAAIHDVITSRPGGYDAELAEG 612
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  82 GSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQGCTQIIVAHRLSTIKDADIIFVMKGGKIVES 161
Cdd:TIGR03796 613 GANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQR 692
                         170
                  ....*....|....*.
gi 1877026690 162 GNHKYLMELGGEYYSL 177
Cdd:TIGR03796 693 GTHEELWAVGGAYARL 708
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
2-172 8.72e-64

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: 195.91  E-value: 8.72e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL-KNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:cd03254    56 QKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENIRLgRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGE 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS--QGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:cd03254   136 NGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKlmKGRTSIIIAHRLSTIKNADKILVLDDGKI 215
                         170
                  ....*....|....
gi 1877026690 159 VESGNHKYLMELGG 172
Cdd:cd03254   216 IEEGTHDELLAKKG 229
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
2-178 2.68e-63

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: 194.76  E-value: 2.68e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL-KNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:cd03251    55 DSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENIAYgRPGATREEVEEAARAANAHEFIMELPEGYDTVIGE 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:cd03251   135 RGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALErlMKNRTTFVIAHRLSTIENADRIVVLEDGKI 214
                         170       180
                  ....*....|....*....|
gi 1877026690 159 VESGNHKYLMELGGEYYSLY 178
Cdd:cd03251   215 VERGTHEELLAQGGVYAKLH 234
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
2-172 9.65e-61

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: 197.29  E-value: 9.65e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL-KNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:COG4988   390 YSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLgRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGE 469
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:COG4988   470 GGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRrlAKGRTVILITHRLALLAQADRILVLDDGRI 549
                         170
                  ....*....|....
gi 1877026690 159 VESGNHKYLMELGG 172
Cdd:COG4988   550 VEQGTHEELLAKNG 563
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
2-181 9.47e-60

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: 186.15  E-value: 9.47e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTS-QKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:cd03252    55 ENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGE 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:cd03252   135 QGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHdiCAGRTVIIIAHRLSTVKNADRIIVMEKGRI 214
                         170       180
                  ....*....|....*....|...
gi 1877026690 159 VESGNHKYLMELGGEYYSLYTKR 181
Cdd:cd03252   215 VEQGSHDELLAENGLYAYLYQLQ 237
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
2-177 5.91e-58

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: 190.80  E-value: 5.91e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL-KNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:COG5265   411 TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYgRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGE 490
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:COG5265   491 RGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALRevARGRTTLVIAHRLSTIVDADEILVLEAGRI 570
                         170
                  ....*....|....*....
gi 1877026690 159 VESGNHKYLMELGGEYYSL 177
Cdd:COG5265   571 VERGTHAELLAQGGLYAQM 589
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
2-177 3.47e-56

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 185.93  E-value: 3.47e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL-KNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:PRK13657  388 QSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVgRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGE 467
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:PRK13657  468 RGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDelMKGRTTFIIAHRLSTVRNADRILVFDNGRV 547
                         170
                  ....*....|....*....
gi 1877026690 159 VESGNHKYLMELGGEYYSL 177
Cdd:PRK13657  548 VESGSFDELVARGGRFAAL 566
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
2-181 2.37e-54

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: 182.63  E-value: 2.37e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSqkIEEVCKAVQI---YDEIMAMPMKFNTII 78
Cdd:TIGR01846 510 QHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAP--FEHVIHAAKLagaHDFISELPQGYNTEV 587
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  79 SEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVMKGG 156
Cdd:TIGR01846 588 GEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMReiCRGRTVIIIAHRLSTVRACDRIIVLEKG 667
                         170       180
                  ....*....|....*....|....*
gi 1877026690 157 KIVESGNHKYLMELGGEYYSLYTKR 181
Cdd:TIGR01846 668 QIAESGRHEELLALQGLYARLWQQQ 692
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
2-177 6.03e-54

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: 181.69  E-value: 6.03e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEM 81
Cdd:TIGR03797 506 ESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEG 585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  82 GSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQGCTQIIVAHRLSTIKDADIIFVMKGGKIVES 161
Cdd:TIGR03797 586 GGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQ 665
                         170
                  ....*....|....*.
gi 1877026690 162 GNHKYLMELGGEYYSL 177
Cdd:TIGR03797 666 GTYDELMAREGLFAQL 681
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
2-178 9.83e-51

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: 171.10  E-value: 9.83e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL-KNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:COG4987   388 QSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLaRPDATDEELWAALERVGLGDWLAALPDGLDTWLGE 467
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:COG4987   468 GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLeaLAGRTVLLITHRLAGLERMDRILVLEDGRI 547
                         170       180
                  ....*....|....*....|
gi 1877026690 159 VESGNHKYLMELGGEYYSLY 178
Cdd:COG4987   548 VEQGTHEELLAQNGRYRQLY 567
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
2-157 2.89e-49

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: 157.16  E-value: 2.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNItlknevtsqkieevckavqiydeimampmkfntiisem 81
Cdd:cd03228    55 TSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLFSGTIRENI-------------------------------------- 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1877026690  82 gsnISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVMKGGK 157
Cdd:cd03228    97 ---LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRalAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
4-163 7.99e-49

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: 157.66  E-value: 7.99e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMGS 83
Cdd:cd03244    59 GSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGE 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  84 NISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQ--GCTQIIVAHRLSTIKDADIIFVMKGGKIVES 161
Cdd:cd03244   139 NLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAHRLDTIIDSDRILVLDKGRVVEF 218

                  ..
gi 1877026690 162 GN 163
Cdd:cd03244   219 DS 220
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
2-177 1.01e-48

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 167.59  E-value: 1.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLK-NEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:TIGR00958 534 TGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGE 613
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQGCTQIIVAHRLSTIKDADIIFVMKGGKIVE 160
Cdd:TIGR00958 614 KGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
                         170
                  ....*....|....*..
gi 1877026690 161 SGNHKYLMELGGEYYSL 177
Cdd:TIGR00958 694 MGTHKQLMEDQGCYKHL 710
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
4-177 4.51e-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: 164.10  E-value: 4.51e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKN-EVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMG 82
Cdd:TIGR02204 395 GRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRpDATDEEVEAAARAAHAHEFISALPEGYDTYLGERG 474
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVMKGGKIVE 160
Cdd:TIGR02204 475 VTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALEtlMKGRTTLIIAHRLATVLKADRIVVMDQGRIVA 554
                         170
                  ....*....|....*..
gi 1877026690 161 SGNHKYLMELGGEYYSL 177
Cdd:TIGR02204 555 QGTHAELIAKGGLYARL 571
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
2-178 2.56e-47

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: 162.19  E-value: 2.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL--KNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIIS 79
Cdd:TIGR02203 385 DSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYgrTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIG 464
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  80 EMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS--QGCTQIIVAHRLSTIKDADIIFVMKGGK 157
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERlmQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
                         170       180
                  ....*....|....*....|.
gi 1877026690 158 IVESGNHKYLMELGGEYYSLY 178
Cdd:TIGR02203 545 IVERGTHNELLARNGLYAQLH 565
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
4-162 5.39e-46

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: 158.37  E-value: 5.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMGS 83
Cdd:COG4618   387 GSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGA 466
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  84 NISGGQRQRIALARALINNPSIVILDEATSALDTINEERIT---KYIKSQGCTQIIVAHRLSTIKDADIIFVMKGGKIVE 160
Cdd:COG4618   467 RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAaaiRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQA 546

                  ..
gi 1877026690 161 SG 162
Cdd:COG4618   547 FG 548
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
4-179 6.16e-45

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: 157.21  E-value: 6.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL--KNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEM 81
Cdd:TIGR01193 529 GEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEE 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  82 GSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERI-TKYIKSQGCTQIIVAHRLSTIKDADIIFVMKGGKIVE 160
Cdd:TIGR01193 609 GSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIvNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIE 688
                         170
                  ....*....|....*....
gi 1877026690 161 SGNHKYLMELGGEYYSLYT 179
Cdd:TIGR01193 689 QGSHDELLDRNGFYASLIH 707
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
4-162 7.20e-45

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: 147.35  E-value: 7.20e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKN-EVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMG 82
Cdd:cd03245    59 GSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNITLGApLADDERILRAAELAGVTDFVNKHPNGLDLQIGERG 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQGC--TQIIVAHRLSTIKDADIIFVMKGGKIVE 160
Cdd:cd03245   139 RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLDLVDRIIVMDSGRIVA 218

                  ..
gi 1877026690 161 SG 162
Cdd:cd03245   219 DG 220
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
2-178 2.02e-44

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 154.41  E-value: 2.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL--KNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIIS 79
Cdd:PRK11176  396 DEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIG 475
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  80 EMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS--QGCTQIIVAHRLSTIKDADIIFVMKGGK 157
Cdd:PRK11176  476 ENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDElqKNRTSLVIAHRLSTIEKADEILVVEDGE 555
                         170       180
                  ....*....|....*....|.
gi 1877026690 158 IVESGNHKYLMELGGEYYSLY 178
Cdd:PRK11176  556 IVERGTHAELLAQNGVYAQLH 576
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
2-178 1.17e-43

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 152.56  E-value: 1.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEM 81
Cdd:PRK10790  394 TEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQ 473
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  82 GSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS--QGCTQIIVAHRLSTIKDADIIFVMKGGKIV 159
Cdd:PRK10790  474 GNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAvrEHTTLVVIAHRLSTIVEADTILVLHRGQAV 553
                         170
                  ....*....|....*....
gi 1877026690 160 ESGNHKYLMELGGEYYSLY 178
Cdd:PRK10790  554 EQGTHQQLLAAQGRYWQMY 572
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
4-182 6.77e-39

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 139.59  E-value: 6.77e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKN-EVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMG 82
Cdd:PRK11174  404 GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNpDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQA 483
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVMKGGKIVE 160
Cdd:PRK11174  484 AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNaaSRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQ 563
                         170       180
                  ....*....|....*....|..
gi 1877026690 161 SGNHKYLMELGGEYYSLYTKRK 182
Cdd:PRK11174  564 QGDYAELSQAGGLFATLLAHRQ 585
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
4-158 7.92e-38

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: 136.32  E-value: 7.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNIT-LKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMG 82
Cdd:TIGR01842 373 GSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIArFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGG 452
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDTINEE---RITKYIKSQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:TIGR01842 453 ATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQalaNAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
2-178 1.29e-37

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 136.00  E-value: 1.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL-KNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:PRK10789  368 SEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALgRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGE 447
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS--QGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:PRK10789  448 RGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQwgEGRTVIISAHRLSALTEASEILVMQHGHI 527
                         170       180
                  ....*....|....*....|
gi 1877026690 159 VESGNHKYLMELGGEYYSLY 178
Cdd:PRK10789  528 AQRGNHDQLAQQSGWYRDMY 547
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
4-158 1.35e-37

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: 129.13  E-value: 1.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKneVTSQKIEEVCKAVQIY---DEIMAMPMKFNTIISE 80
Cdd:cd03248    69 GQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYG--LQSCSFECVKEAAQKAhahSFISELASGYDTEVGE 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITK--YIKSQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:cd03248   147 KGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQalYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
4-158 8.15e-36

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: 122.71  E-value: 8.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNItlknevtsqkieevckavqiydeimampmkfntiisemgs 83
Cdd:cd03246    57 GRVRLDGADISQWDPNELGDHVGYLPQDDELFSGSIAENI---------------------------------------- 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1877026690  84 nISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI---KSQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:cd03246    97 -LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIaalKAAGATRIVIAHRPETLASADRILVLEDGRV 173
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
2-153 1.52e-32

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: 121.62  E-value: 1.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL-KNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:TIGR02857 375 TEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLaRPDASDAEIREALERAGLDEFVAALPQGLDTPIGE 454
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVM 153
Cdd:TIGR02857 455 GGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRalAQGRTVLLVTHRLALAALADRIVVL 529
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
2-180 1.02e-31

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 120.13  E-value: 1.02e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690    2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL-KNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:PTZ00265  1275 NSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFgKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGP 1354
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKY---IKSQGCTQII-VAHRLSTIKDADIIFVM--- 153
Cdd:PTZ00265  1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTivdIKDKADKTIItIAHRIASIKRSDKIVVFnnp 1434
                          170       180
                   ....*....|....*....|....*....
gi 1877026690  154 -KGGKIVES-GNHKYLMELGGEYYSLYTK 180
Cdd:PTZ00265  1435 dRTGSFVQAhGTHEELLSVQDGVYKKYVK 1463
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
2-162 1.09e-31

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: 113.28  E-value: 1.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQKIEEVCKavqiydeimampmkfntiISEM 81
Cdd:cd03369    61 EEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEG 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  82 GSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS--QGCTQIIVAHRLSTIKDADIIFVMKGGKIV 159
Cdd:cd03369   123 GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREefTNSTILTIAHRLRTIIDYDKILVMDAGEVK 202

                  ...
gi 1877026690 160 ESG 162
Cdd:cd03369   203 EYD 205
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
2-178 2.46e-31

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 118.39  E-value: 2.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL-KNEVTSQKIEEVCKAVQIyDEIMAMPMKFNTIISE 80
Cdd:PRK11160  393 QQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLaAPNASDEALIEVLQQVGL-EKLLEDDKGLNAWLGE 471
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:PRK11160  472 GGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAehAQNKTVLMITHRLTGLEQFDRICVMDNGQI 551
                         170       180
                  ....*....|....*....|
gi 1877026690 159 VESGNHKYLMELGGEYYSLY 178
Cdd:PRK11160  552 IEQGTHQELLAQQGRYYQLK 571
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
2-160 3.83e-31

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 112.44  E-value: 3.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILS----QNLGVVPQDSFLLNR-SILDNITL-------KNEVTSQKIEEVCKAVQIYDEIMA 69
Cdd:COG1136    61 TSGEVLIDGQDISSLSERELArlrrRHIGFVFQFFNLLPElTALENVALplllagvSRKERRERARELLERVGLGDRLDH 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  70 MPmkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERI----TKYIKSQGCTQIIVAHRLSTIK 145
Cdd:COG1136   141 RP-----------SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVlellRELNRELGTTIVMVTHDPELAA 209
                         170
                  ....*....|....*
gi 1877026690 146 DADIIFVMKGGKIVE 160
Cdd:COG1136   210 RADRVIRLRDGRIVS 224
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
2-158 6.90e-30

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 108.73  E-value: 6.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILS----QNLGVVPQDSFLLNR-SILDNITL-------KNEVTSQKIEEVCKAVQIYDEIMA 69
Cdd:cd03255    57 TSGEVRVDGTDISKLSEKELAafrrRHIGFVFQSFNLLPDlTALENVELplllagvPKKERRERAEELLERVGLGDRLNH 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  70 MPmkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS----QGCTQIIVAHRLSTIK 145
Cdd:cd03255   137 YP-----------SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnkeAGTTIVVVTHDPELAE 205
                         170
                  ....*....|...
gi 1877026690 146 DADIIFVMKGGKI 158
Cdd:cd03255   206 YADRIIELRDGKI 218
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
28-157 8.04e-30

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: 108.33  E-value: 8.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  28 VPQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMGSNISGGQRQRIALARALINNPSIVI 107
Cdd:cd03250    71 VSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYL 150
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1877026690 108 LDEATSALDT-----INEERITKYIKsQGCTQIIVAHRLSTIKDADIIFVMKGGK 157
Cdd:cd03250   151 LDDPLSAVDAhvgrhIFENCILGLLL-NNKTRILVTHQLQLLPHADQIVVLDNGR 204
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
2-162 1.26e-28

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: 110.38  E-value: 1.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDK---KILSQNLGVVPQDSFL-LN--RSILDNIT--LKN------EVTSQKIEEVCKAVQIYDEI 67
Cdd:COG1123   318 TSGSILFDGKDLTKLSRrslRELRRRVQMVFQDPYSsLNprMTVGDIIAepLRLhgllsrAERRERVAELLERVGLPPDL 397
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  68 M-AMPMKFntiisemgsniSGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK----SQGCTQIIVAHRLS 142
Cdd:COG1123   398 AdRYPHEL-----------SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlqrELGLTYLFISHDLA 466
                         170       180
                  ....*....|....*....|.
gi 1877026690 143 TIKD-ADIIFVMKGGKIVESG 162
Cdd:COG1123   467 VVRYiADRVAVMYDGRIVEDG 487
PLN03130 PLN03130
ABC transporter C family member; Provisional
1-160 2.25e-28

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 110.60  E-value: 2.25e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690    1 MDTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:PLN03130  1291 LERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSE 1370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQ--GCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:PLN03130  1371 AGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEfkSCTMLIIAHRLNTIIDCDRILVLDAGRV 1450

                   ..
gi 1877026690  159 VE 160
Cdd:PLN03130  1451 VE 1452
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
2-162 2.48e-28

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: 105.28  E-value: 2.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILS---QNLGVVPQDSFL-LN--RSILDNI--TLKNEVTSQKIEEvcKAVQIYDEIMAMPMK 73
Cdd:cd03257    58 TSGSIIFDGKDLLKLSRRLRKirrKEIQMVFQDPMSsLNprMTIGEQIaePLRIHGKLSKKEA--RKEAVLLLLVGVGLP 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  74 ---FNTIISEMgsniSGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK----SQGCTQIIVAHRLSTIKD 146
Cdd:cd03257   136 eevLNRYPHEL----SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKklqeELGLTLLFITHDLGVVAK 211
                         170
                  ....*....|....*..
gi 1877026690 147 -ADIIFVMKGGKIVESG 162
Cdd:cd03257   212 iADRVAVMYAGKIVEEG 228
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
4-177 1.25e-27

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: 108.49  E-value: 1.25e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690    4 GKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMGS 83
Cdd:TIGR00957 1341 GEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGE 1420
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   84 NISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQ--GCTQIIVAHRLSTIKDADIIFVMKGGKIVES 161
Cdd:TIGR00957 1421 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEF 1500
                          170
                   ....*....|....*.
gi 1877026690  162 GNHKYLMELGGEYYSL 177
Cdd:TIGR00957 1501 GAPSNLLQQRGIFYSM 1516
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
4-160 8.62e-27

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: 101.91  E-value: 8.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMGS 83
Cdd:cd03288    76 GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGE 155
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1877026690  84 NISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQGC--TQIIVAHRLSTIKDADIIFVMKGGKIVE 160
Cdd:cd03288   156 NFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAdrTVVTIAHRVSTILDADLVLVLSRGILVE 234
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
2-162 1.01e-26

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: 101.12  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKIL---SQNLGVVPQDSFLLN-RSILDNITL--------KNEVTsQKIEEVCKAVQIYDEIMA 69
Cdd:cd03258    58 TSGSVLVDGTDLTLLSGKELrkaRRRIGMIFQHFNLLSsRTVFENVALpleiagvpKAEIE-ERVLELLELVGLEDKADA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  70 MPmkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALD--TINE--ERITKYIKSQGCTQIIVAHRLSTIK 145
Cdd:cd03258   137 YP-----------AQLSGGQKQRVGIARALANNPKVLLCDEATSALDpeTTQSilALLRDINRELGLTIVLITHEMEVVK 205
                         170
                  ....*....|....*...
gi 1877026690 146 D-ADIIFVMKGGKIVESG 162
Cdd:cd03258   206 RiCDRVAVMEKGEVVEEG 223
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
2-162 8.55e-26

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 98.20  E-value: 8.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQI-DKKI--LSQNLGVVPQDSFLL-NRSILDNITLKNEVT-------SQKIEEVCKAVQIYDEIMAM 70
Cdd:COG2884    55 TSGQVLVNGQDLSRLkRREIpyLRRRIGVVFQDFRLLpDRTVYENVALPLRVTgksrkeiRRRVREVLDLVGLSDKAKAL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  71 PMkfntiisemgsNISGGQRQRIALARALINNPSIVILDEATSALDTINEERIT---KYIKSQGCTQIIVAHRLSTIKDA 147
Cdd:COG2884   135 PH-----------ELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMellEEINRRGTTVLIATHDLELVDRM 203
                         170
                  ....*....|....*.
gi 1877026690 148 DI-IFVMKGGKIVESG 162
Cdd:COG2884   204 PKrVLELEDGRLVRDE 219
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
3-162 1.55e-25

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 101.90  E-value: 1.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGININQIDKKILSQNLGVVPQD--SFLLNRSILDNI--TLKNEVTS-----QKIEEVCKAVQIYDEIMAMPMK 73
Cdd:COG1123    63 SGEVLLDGRDLLELSEALRGRRIGMVFQDpmTQLNPVTVGDQIaeALENLGLSraearARVLELLEAVGLERRLDRYPHQ 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  74 FntiisemgsniSGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS----QGCTQIIVAHRLSTIKD-AD 148
Cdd:COG1123   143 L-----------SGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqreRGTTVLLITHDLGVVAEiAD 211
                         170
                  ....*....|....
gi 1877026690 149 IIFVMKGGKIVESG 162
Cdd:COG1123   212 RVVVMDDGRIVEDG 225
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
2-141 2.09e-25

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: 101.67  E-value: 2.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL-KNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:TIGR02868 388 LQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLaRPDATDEELWAALERVGLADWLRALPDGLDTVLGE 467
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS--QGCTQIIVAHRL 141
Cdd:TIGR02868 468 GGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAalSGRTVVLITHHL 530
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
2-163 2.16e-25

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: 97.40  E-value: 2.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQ--DSFLLNRSILDNIT--LKN-----EVTSQKIEEVCKAVQIYDEIMAMPm 72
Cdd:COG1122    54 TSGEVLVDGKDITKKNLRELRRKVGLVFQnpDDQLFAPTVEEDVAfgPENlglprEEIRERVEEALELVGLEHLADRPP- 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  73 kfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLSTIKD-AD 148
Cdd:COG1122   133 ----------HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlnkEGKTVIIVTHDLDLVAElAD 202
                         170
                  ....*....|....*
gi 1877026690 149 IIFVMKGGKIVESGN 163
Cdd:COG1122   203 RVIVLDDGRIVADGT 217
PLN03232 PLN03232
ABC transporter C family member; Provisional
1-176 3.41e-25

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 101.59  E-value: 3.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690    1 MDTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:PLN03232  1288 LEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSE 1367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQ--GCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:PLN03232  1368 GGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEfkSCTMLVIAHRLNTIIDCDKILVLSSGQV 1447
                          170
                   ....*....|....*...
gi 1877026690  159 VESGNHKYLMELGGEYYS 176
Cdd:PLN03232  1448 LEYDSPQELLSRDTSAFF 1465
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
2-160 6.40e-25

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: 96.80  E-value: 6.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFL-LN-----RSILD---NITLKNEVTsQKIEEVCKAVQIYDEIMampm 72
Cdd:COG1124    58 WSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYAsLHprhtvDRILAeplRIHGLPDRE-ERIAELLEQVGLPPSFL---- 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  73 kFNTIISemgsnISGGQRQRIALARALINNPSIVILDEATSALDTINEERI----TKYIKSQGCTQIIVAHRLSTI-KDA 147
Cdd:COG1124   133 -DRYPHQ-----LSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEIlnllKDLREERGLTYLFVSHDLAVVaHLC 206
                         170
                  ....*....|...
gi 1877026690 148 DIIFVMKGGKIVE 160
Cdd:COG1124   207 DRVAVMQNGRIVE 219
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
2-162 1.67e-24

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: 95.33  E-value: 1.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILS--QNLGVVPQDSFLLNRSILDNITL--------KNEVTSQKIEEVCKAVQIYDEIMAmp 71
Cdd:cd03260    58 DEGEVLLDGKDIYDLDVDVLElrRRVGMVFQKPNPFPGSIYDNVAYglrlhgikLKEELDERVEEALRKAALWDEVKD-- 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  72 mkfntiiSEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQG--CTQIIVAHRLSTIKD-AD 148
Cdd:cd03260   136 -------RLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKkeYTIVIVTHNMQQAARvAD 208
                         170
                  ....*....|....
gi 1877026690 149 IIFVMKGGKIVESG 162
Cdd:cd03260   209 RTAFLLNGRLVEFG 222
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
2-113 1.93e-24

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: 93.10  E-value: 1.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNR-SILDNI-------TLKNEVTSQKIEEVCKAVQIYDEImampmk 73
Cdd:pfam00005  38 TEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLrlglllkGLSKREKDARAEEALEKLGLGDLA------ 111
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1877026690  74 fNTIISEMGSNISGGQRQRIALARALINNPSIVILDEATS 113
Cdd:pfam00005 112 -DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
2-162 3.45e-24

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 94.36  E-value: 3.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILsQNLGVVPQDSFL-LNRSILDNIT-------LKNEVTSQKIEEVCKAVQIYDEIMAMPMK 73
Cdd:COG1131    53 TSGEVRVLGEDVARDPAEVR-RRIGYVPQEPALyPDLTVRENLRffarlygLPRKEARERIDELLELFGLTDAADRKVGT 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  74 FntiisemgsniSGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLSTIKD-ADI 149
Cdd:COG1131   132 L-----------SGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRElaaEGKTVLLSTHYLEEAERlCDR 200
                         170
                  ....*....|...
gi 1877026690 150 IFVMKGGKIVESG 162
Cdd:COG1131   201 VAIIDKGRIVADG 213
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
47-153 3.73e-24

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 98.56  E-value: 3.73e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   47 NEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKY 126
Cdd:PTZ00265   542 QTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1877026690  127 IK----SQGCTQIIVAHRLSTIKDADIIFVM 153
Cdd:PTZ00265   622 INnlkgNENRITIIIAHRLSTIRYANTIFVL 652
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
2-163 5.02e-24

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 95.92  E-value: 5.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILS---QNLGVVPQDSFLLN-RSILDNITL--------KNEVTsQKIEEVCKAVQIYDEIMA 69
Cdd:COG1135    58 TSGSVLVDGVDLTALSERELRaarRKIGMIFQHFNLLSsRTVAENVALpleiagvpKAEIR-KRVAELLELVGLSDKADA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  70 MPmkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALD------------TINEERitkyiksqGCTQIIV 137
Cdd:COG1135   137 YP-----------SQLSGGQKQRVGIARALANNPKVLLCDEATSALDpettrsildllkDINREL--------GLTIVLI 197
                         170       180
                  ....*....|....*....|....*..
gi 1877026690 138 AHRLSTIKD-ADIIFVMKGGKIVESGN 163
Cdd:COG1135   198 THEMDVVRRiCDRVAVLENGRIVEQGP 224
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
30-156 8.64e-24

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: 93.16  E-value: 8.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  30 QDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMGSNISGGQRQRIALARALINNPSIVILD 109
Cdd:cd03290    86 QKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1877026690 110 EATSALDT-----INEERITKYIKSQGCTQIIVAHRLSTIKDADIIFVMKGG 156
Cdd:cd03290   166 DPFSALDIhlsdhLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
2-158 1.10e-23

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


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 92.59  E-value: 1.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKI--LSQNLGVVPQdSFLL--NRSILDNITL---------KNEVTsQKIEEVCKAVQIYDEIM 68
Cdd:cd03262    53 DSGTIIIDGLKLTDDKKNIneLRQKVGMVFQ-QFNLfpHLTVLENITLapikvkgmsKAEAE-ERALELLEKVGLADKAD 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  69 AMPmkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALD--TINE-ERITKYIKSQGCTQIIVAHRLSTIK 145
Cdd:cd03262   131 AYP-----------AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpeLVGEvLDVMKDLAEEGMTMVVVTHEMGFAR 199
                         170
                  ....*....|....*
gi 1877026690 146 D-AD-IIFvMKGGKI 158
Cdd:cd03262   200 EvADrVIF-MDDGRI 213
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
2-157 1.67e-23

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 92.14  E-value: 1.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQ--DSFLLNRSILD-------NITLKNEVTSQKIEEVCKAVQIYDEIMAMPm 72
Cdd:cd03225    54 TSGEVLVDGKDLTKLSLKELRRKVGLVFQnpDDQFFGPTVEEevafgleNLGLPEEEIEERVEEALELVGLEGLRDRSP- 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  73 kfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK---SQGCTQIIVAHRLSTIKD-AD 148
Cdd:cd03225   133 ----------FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKklkAEGKTIIIVTHDLDLLLElAD 202

                  ....*....
gi 1877026690 149 IIFVMKGGK 157
Cdd:cd03225   203 RVIVLEDGK 211
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
2-162 2.27e-23

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: 90.84  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGINInQIDKKILSQNLGVVPQDSFLLNRSILDNItlknevtsqkieevckavqiydeimampmkfntiisem 81
Cdd:cd03247    55 QQGEITLDGVPV-SDLEKALSSLISVLNQRPYLFDTTLRNNL-------------------------------------- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  82 GSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQ--GCTQIIVAHRLSTIKDADIIFVMKGGKIV 159
Cdd:cd03247    96 GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVlkDKTLIWITHHLTGIEHMDKILFLENGKII 175

                  ...
gi 1877026690 160 ESG 162
Cdd:cd03247   176 MQG 178
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
2-162 3.93e-23

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 91.98  E-value: 3.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKI--LSQNLGVVPQdSFLL--NRSILDNITL---------KNEVTsQKIEEVCKAVQIYDEIM 68
Cdd:COG1126    54 DSGTITVDGEDLTDSKKDInkLRRKVGMVFQ-QFNLfpHLTVLENVTLapikvkkmsKAEAE-ERAMELLERVGLADKAD 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  69 AMPmkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALD--TINE-ERITKYIKSQGCTQIIVAHRLSTIK 145
Cdd:COG1126   132 AYP-----------AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpeLVGEvLDVMRDLAKEGMTMVVVTHEMGFAR 200
                         170
                  ....*....|....*...
gi 1877026690 146 D-ADIIFVMKGGKIVESG 162
Cdd:COG1126   201 EvADRVVFMDGGRIVEEG 218
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
2-162 4.29e-23

ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 91.79  E-value: 4.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGINI---NQIDKKILSQNLGVVPQDSFLLNR-SILDNI--------TLKNEVTSQKIEEVCKAVQIYDEIMA 69
Cdd:cd03261    53 DSGEVLIDGEDIsglSEAELYRLRRRMGMLFQSGALFDSlTVFENVafplrehtRLSEEEIREIVLEKLEAVGLRGAEDL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  70 MPmkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI----KSQGCTQIIVAHRLSTIK 145
Cdd:cd03261   133 YP-----------AELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHDLDTAF 201
                         170
                  ....*....|....*...
gi 1877026690 146 D-ADIIFVMKGGKIVESG 162
Cdd:cd03261   202 AiADRIAVLYDGKIVAEG 219
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
1-162 8.72e-23

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: 90.27  E-value: 8.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   1 MDTGKVLFDGININQIDkkILSQNLGVVPQDSFLL-NRSILDNI-------TLKNEVTSQKIEEVCKAVQIYDEIMAMPm 72
Cdd:cd03259    52 PDSGEILIDGRDVTGVP--PERRNIGMVFQDYALFpHLTVAENIafglklrGVPKAEIRARVRELLELVGLEGLLNRYP- 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  73 kfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK----SQGCTQIIVAHRLS---TIk 145
Cdd:cd03259   129 ----------HELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKelqrELGITTIYVTHDQEealAL- 197
                         170
                  ....*....|....*..
gi 1877026690 146 dADIIFVMKGGKIVESG 162
Cdd:cd03259   198 -ADRIAVMNEGRIVQVG 213
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
2-162 9.62e-23

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: 92.42  E-value: 9.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQID----KKILSQNLGVVPQDSFL-LN------RSILDNITLKNEVTS----QKIEEVCKAVQIYD- 65
Cdd:COG0444    61 TSGEILFDGEDLLKLSekelRKIRGREIQMIFQDPMTsLNpvmtvgDQIAEPLRIHGGLSKaearERAIELLERVGLPDp 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  66 -EIMAM-PMKFntiisemgsniSGGQRQRIALARALINNPSIVILDEATSALD-TI-----------NEERitkyiksqG 131
Cdd:COG0444   141 eRRLDRyPHEL-----------SGGMRQRVMIARALALEPKLLIADEPTTALDvTIqaqilnllkdlQREL--------G 201
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1877026690 132 CTQIIVAHRLSTIKD-ADIIFVMKGGKIVESG 162
Cdd:COG0444   202 LAILFITHDLGVVAEiADRVAVMYAGRIVEEG 233
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
2-157 1.41e-22

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: 88.46  E-value: 1.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQdsfllnrsildnitlknevtsqkieevckavqiydeimampmkfntiisem 81
Cdd:cd00267    52 TSGEILIDGKDIAKLPLEELRRRIGYVPQ--------------------------------------------------- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  82 gsnISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLSTIKDA-DIIFVMKGGK 157
Cdd:cd00267    81 ---LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRElaeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
2-157 2.49e-22

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 88.40  E-value: 2.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKI--LSQNLGVVPQDSFLLNR-SILDNITLKnevtsqkieevckavqiydeimampmkfntii 78
Cdd:cd03229    53 DSGSILIDGEDLTDLEDELppLRRRIGMVFQDFALFPHlTVLENIALG-------------------------------- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  79 semgsnISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS----QGCTQIIVAHRLS-TIKDADIIFVM 153
Cdd:cd03229   101 ------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDeAARLADRVVVL 174

                  ....
gi 1877026690 154 KGGK 157
Cdd:cd03229   175 RDGK 178
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
28-174 5.29e-22

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: 92.32  E-value: 5.29e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   28 VPQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMGSNISGGQRQRIALARALINNPSIVI 107
Cdd:TIGR00957  704 VPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYL 783
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1877026690  108 LDEATSALDT-INEERITKYIKSQGC----TQIIVAHRLSTIKDADIIFVMKGGKIVESGNHKYLMELGGEY 174
Cdd:TIGR00957  784 FDDPLSAVDAhVGKHIFEHVIGPEGVlknkTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
4-163 9.04e-22

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: 88.85  E-value: 9.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKIL----SQNLGVVPQdSFLL--NRSILDNITLKNEVTS-------QKIEEVCKAVQIYDEIMAM 70
Cdd:cd03294    79 GKVLIDGQDIAAMSRKELrelrRKKISMVFQ-SFALlpHRTVLENVAFGLEVQGvpraereERAAEALELVGLEGWEHKY 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  71 PmkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALD-TINEERITKYIKSQ---GCTQIIVAHRLS-TIK 145
Cdd:cd03294   158 P-----------DELSGGMQQRVGLARALAVDPDILLMDEAFSALDpLIRREMQDELLRLQaelQKTIVFITHDLDeALR 226
                         170
                  ....*....|....*...
gi 1877026690 146 DADIIFVMKGGKIVESGN 163
Cdd:cd03294   227 LGDRIAIMKDGRLVQVGT 244
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
2-173 1.33e-21

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: 87.99  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQnLGVVPQDSFL-LNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:COG4555    54 DSGSILIDGEDVRKEPREARRQ-IGVLPDERGLyDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGE 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MgsniSGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI---KSQGCTQIIVAHRLSTIKD-ADIIFVMKGG 156
Cdd:COG4555   133 L----STGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILralKKEGKTVLFSSHIMQEVEAlCDRVVILHKG 208
                         170
                  ....*....|....*..
gi 1877026690 157 KIVESGNHKYLMELGGE 173
Cdd:COG4555   209 KVVAQGSLDELREEIGE 225
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
2-158 1.93e-21

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 86.79  E-value: 1.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL-----KNEVTSQKIEEVCKAVQIYDEIMAMPMkfnt 76
Cdd:COG4619    53 TSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDILDKPV---- 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  77 iisemgSNISGGQRQRIALARALINNPSIVILDEATSALDTINEER----ITKYIKSQGCTQIIVAH------RLstikd 146
Cdd:COG4619   129 ------ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRveelLREYLAEEGRAVLWVSHdpeqieRV----- 197
                         170
                  ....*....|..
gi 1877026690 147 ADIIFVMKGGKI 158
Cdd:COG4619   198 ADRVLTLEAGRL 209
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
2-162 2.39e-21

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 85.56  E-value: 2.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQdsfllnrsildnitlknevtsqkieeVCKAVQIYDEIMAMpmkFNTIisem 81
Cdd:cd03214    52 SSGEILLDGKDLASLSPKELARKIAYVPQ--------------------------ALELLGLAHLADRP---FNEL---- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  82 gsniSGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK----SQGCTQIIVAHRLS-TIKDADIIFVMKGG 156
Cdd:cd03214    99 ----SGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRrlarERGKTVVMVLHDLNlAARYADRVILLKDG 174

                  ....*.
gi 1877026690 157 KIVESG 162
Cdd:cd03214   175 RIVAQG 180
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
2-163 3.28e-21

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: 86.96  E-value: 3.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILS---QNLGVVPQDSFLL-NRSILDNI--------TLKNEVTSQKIEEVCKAVQIYDEIMA 69
Cdd:COG1127    58 DSGEILVDGQDITGLSEKELYelrRRIGMLFQGGALFdSLTVFENVafplrehtDLSEAEIRELVLEKLELVGLPGAADK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  70 MPmkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI----KSQGCTQIIVAHRLSTIK 145
Cdd:COG1127   138 MP-----------SELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIrelrDELGLTSVVVTHDLDSAF 206
                         170
                  ....*....|....*....
gi 1877026690 146 D-ADIIFVMKGGKIVESGN 163
Cdd:COG1127   207 AiADRVAVLADGKIIAEGT 225
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
2-163 3.19e-20

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: 84.31  E-value: 3.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKilSQNLGVVPQDSFLL-NRSILDNIT--LKNEVTSQKieEVCKAVqiyDEIMAMpMKFNTII 78
Cdd:cd03299    52 DSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNIAygLKKRKVDKK--EIERKV---LEIAEM-LGIDHLL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  79 SEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERI----TKYIKSQGCTQIIVAHRLSTIKD-ADIIFVM 153
Cdd:cd03299   124 NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLreelKKIRKEFGVTVLHVTHDFEEAWAlADKVAIM 203
                         170
                  ....*....|
gi 1877026690 154 KGGKIVESGN 163
Cdd:cd03299   204 LNGKLIQVGK 213
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
3-139 3.38e-20

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: 83.61  E-value: 3.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGININQIDKK---ILSQNLGVVPQDSFLL-NRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTII 78
Cdd:cd03292    55 SGTIRVNGQDVSDLRGRaipYLRRKIGVVFQDFRLLpDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALP 134
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1877026690  79 SEMgsniSGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAH 139
Cdd:cd03292   135 AEL----SGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKinkAGTTVVVATH 194
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
86-162 5.59e-20

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: 86.28  E-value: 5.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALD------------TINEERitkyiksqGCTQIIVAHRLSTIKD-ADIIFV 152
Cdd:COG4172   427 SGGQRQRIAIARALILEPKLLVLDEPTSALDvsvqaqildllrDLQREH--------GLAYLFISHDLAVVRAlAHRVMV 498
                          90
                  ....*....|
gi 1877026690 153 MKGGKIVESG 162
Cdd:COG4172   499 MKDGKVVEQG 508
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
2-162 7.59e-20

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 84.76  E-value: 7.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQI--DKKilsqNLGVVPQDsFLL--NRSILDNIT--LKNEVTS-----QKIEEVCKAVQIydeimam 70
Cdd:COG3842    58 DSGRILLDGRDVTGLppEKR----NVGMVFQD-YALfpHLTVAENVAfgLRMRGVPkaeirARVAELLELVGL------- 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  71 pmkfntiiSEMG----SNISGGQRQRIALARALINNPSIVILDEATSALD------TINEerITKYIKSQGCTQIIVAHR 140
Cdd:COG3842   126 --------EGLAdrypHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDaklreeMREE--LRRLQRELGITFIYVTHD 195
                         170       180
                  ....*....|....*....|....*
gi 1877026690 141 LS---TIkdADIIFVMKGGKIVESG 162
Cdd:COG3842   196 QEealAL--ADRIAVMNDGRIEQVG 218
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
2-158 8.45e-20

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: 81.68  E-value: 8.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILsQNLGVVPQDSFLLNR-SILDNITLknevtsqkieevckavqiydeimampmkfntiise 80
Cdd:cd03230    53 DSGEIKVLGKDIKKEPEEVK-RRIGYLPEEPSLYENlTVRENLKL----------------------------------- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 mgsniSGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLSTIKD-ADIIFVMKGG 156
Cdd:cd03230    97 -----SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRElkkEGKTILLSSHILEEAERlCDRVAILNNG 171

                  ..
gi 1877026690 157 KI 158
Cdd:cd03230   172 RI 173
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
2-163 1.51e-19

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: 82.35  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLL-NRSILDNITLK---NEVTSQKIEEvcKAvqiyDEIMAM----PMK 73
Cdd:cd03295    54 TSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFpHMTVEENIALVpklLKWPKEKIRE--RA----DELLALvgldPAE 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  74 FntiISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITK-YIKSQ---GCTQIIVAHRL-STIKDAD 148
Cdd:cd03295   128 F---ADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEeFKRLQqelGKTIVFVTHDIdEAFRLAD 204
                         170
                  ....*....|....*
gi 1877026690 149 IIFVMKGGKIVESGN 163
Cdd:cd03295   205 RIAIMKNGEIVQVGT 219
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
2-160 5.01e-19

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 81.29  E-value: 5.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKIlsqnlGVVPQDSFLLN-RSILDNITLknevtSQKIEEVCKAvQIYDEIMAMpmkfntiISE 80
Cdd:COG1116    64 TSGEVLVDGKPVTGPGPDR-----GVVFQEPALLPwLTVLDNVAL-----GLELRGVPKA-ERRERAREL-------LEL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MG---------SNISGGQRQRIALARALINNPSIVILDEATSALD-----TINEErITKYIKSQGCTQIIVAH------R 140
Cdd:COG1116   126 VGlagfedaypHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDaltreRLQDE-LLRLWQETGKTVLFVTHdvdeavF 204
                         170       180
                  ....*....|....*....|..
gi 1877026690 141 LstikdADIIFVMKG--GKIVE 160
Cdd:COG1116   205 L-----ADRVVVLSArpGRIVE 221
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
2-162 5.01e-19

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: 81.24  E-value: 5.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSF-----------LLNR----SILDNITLKNEvtsQKIEEVCKAVQIYDe 66
Cdd:COG1120    54 SSGEVLLDGRDLASLSRRELARRIAYVPQEPPapfgltvrelvALGRyphlGLFGRPSAEDR---EAVEEALERTGLEH- 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  67 iMAmpmkfNTIISEMgsniSGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS----QGCTQIIVAHRLS 142
Cdd:COG1120   130 -LA-----DRPVDEL----SGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlareRGRTVVMVLHDLN 199
                         170       180
                  ....*....|....*....|.
gi 1877026690 143 -TIKDADIIFVMKGGKIVESG 162
Cdd:COG1120   200 lAARYADRLVLLKDGRIVAQG 220
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
3-162 7.73e-19

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 82.16  E-value: 7.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGININQIDKKILS---QNLGVVPQDSFLLN-RSILDNITL--------KNEVTsQKIEEVCKAVQIYDEIMAM 70
Cdd:PRK11153   59 SGRVLVDGQDLTALSEKELRkarRQIGMIFQHFNLLSsRTVFDNVALplelagtpKAEIK-ARVTELLELVGLSDKADRY 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  71 PmkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALDT------------INEEritkyiksQGCTQIIVA 138
Cdd:PRK11153  138 P-----------AQLSGGQKQRVAIARALASNPKVLLCDEATSALDPattrsilellkdINRE--------LGLTIVLIT 198
                         170       180
                  ....*....|....*....|....*
gi 1877026690 139 HRLSTIKD-ADIIFVMKGGKIVESG 162
Cdd:PRK11153  199 HEMDVVKRiCDRVAVIDAGRLVEQG 223
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
2-162 1.26e-18

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 81.35  E-value: 1.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININqIDKKILSQNLGVVPQDsFLL--NRSILDNI--TLKNEVTS-----QKIEEVCKAVQIydeimampm 72
Cdd:COG1118    55 DSGRIVLNGRDLF-TNLPPRERRVGFVFQH-YALfpHMTVAENIafGLRVRPPSkaeirARVEELLELVQL--------- 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  73 kfntiiSEMG----SNISGGQRQRIALARALINNPSIVILDEATSALDTI--NEER--ITKYIKSQGCTQIIVAH----- 139
Cdd:COG1118   124 ------EGLAdrypSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKvrKELRrwLRRLHDELGGTTVFVTHdqeea 197
                         170       180
                  ....*....|....*....|....
gi 1877026690 140 -RLstikdADIIFVMKGGKIVESG 162
Cdd:COG1118   198 lEL-----ADRVVVMNQGRIEQVG 216
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
86-156 1.50e-18

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 82.16  E-value: 1.50e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQ--GCTQIIVAHRLSTIKDADIIFVMKGG 156
Cdd:COG4178   487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGHRSTLAAFHDRVLELTGD 559
PTZ00243 PTZ00243
ABC transporter; Provisional
28-169 4.69e-18

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 80.98  E-value: 4.69e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   28 VPQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMGSNISGGQRQRIALARALINNPSIVI 107
Cdd:PTZ00243   726 VPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYL 805
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1877026690  108 LDEATSALDTINEERITKYI---KSQGCTQIIVAHRLSTIKDADIIFVMKGGKIVESGNHKYLME 169
Cdd:PTZ00243   806 LDDPLSALDAHVGERVVEECflgALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
86-162 7.65e-18

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 79.01  E-value: 7.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDtineeritKYIKSQ------------GCTQIIVAHRLSTIKD-ADIIFV 152
Cdd:COG4608   159 SGGQRQRIGIARALALNPKLIVCDEPVSALD--------VSIQAQvlnlledlqdelGLTYLFISHDLSVVRHiSDRVAV 230
                          90
                  ....*....|
gi 1877026690 153 MKGGKIVESG 162
Cdd:COG4608   231 MYLGKIVEIA 240
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
4-159 8.89e-18

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 76.91  E-value: 8.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQidkKILSQNLGVVPQDS--FLLNRSILDNITLKNEVTS---QKIEEVCKAVQIYDEIMAMPMkfntii 78
Cdd:cd03226    55 GSILLNGKPIKA---KERRKSIGYVMQDVdyQLFTDSVREELLLGLKELDagnEQAETVLKDLDLYALKERHPL------ 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  79 semgsNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK---SQGCTQIIVAHRLSTIKD-ADIIFVMK 154
Cdd:cd03226   126 -----SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRelaAQGKAVIVITHDYEFLAKvCDRVLLLA 200

                  ....*
gi 1877026690 155 GGKIV 159
Cdd:cd03226   201 NGAIV 205
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
78-158 1.07e-17

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 77.44  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  78 ISEMgsniSGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK---SQGCTQIIVAHRLSTIKD-ADIIFVM 153
Cdd:COG1121   137 IGEL----SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRelrREGKTILVVTHDLGAVREyFDRVLLL 212

                  ....*
gi 1877026690 154 KGGKI 158
Cdd:COG1121   213 NRGLV 217
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
2-158 1.25e-17

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: 76.80  E-value: 1.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKIlsqnlGVVPQdSFLLNRSIldNITLKNEVTS-----------------QKIEEVCKAVQIY 64
Cdd:cd03235    52 TSGSIRVFGKPLEKERKRI-----GYVPQ-RRSIDRDF--PISVRDVVLMglyghkglfrrlskadkAKVDEALERVGLS 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  65 DeimampmKFNTIISEMgsniSGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK---SQGCTQIIVAHRL 141
Cdd:cd03235   124 E-------LADRQIGEL----SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRelrREGMTILVVTHDL 192
                         170
                  ....*....|....*...
gi 1877026690 142 STIKD-ADIIFVMKGGKI 158
Cdd:cd03235   193 GLVLEyFDRVLLLNRTVV 210
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
2-159 1.79e-17

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: 76.84  E-value: 1.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQ---NLGVVPQDSFLLNR-SILDNI------------TLKNEVTSQKIEEVCKA---VQ 62
Cdd:cd03256    54 TSGSVLIDGTDINKLKGKALRQlrrQIGMIFQQFNLIERlSVLENVlsgrlgrrstwrSLFGLFPKEEKQRALAAlerVG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  63 IYDeimampmKFNTiiseMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK----SQGCTQIIVA 138
Cdd:cd03256   134 LLD-------KAYQ----RADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKrinrEEGITVIVSL 202
                         170       180
                  ....*....|....*....|..
gi 1877026690 139 HRLSTIKD-ADIIFVMKGGKIV 159
Cdd:cd03256   203 HQVDLAREyADRIVGLKDGRIV 224
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
2-162 2.31e-17

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: 76.25  E-value: 2.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQiDKKILSQNLGVVPQDSFLLNR-SILDNIT-------LKNEVTSQKIEEVckavqiydeimAMPMK 73
Cdd:cd03266    58 DAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTARENLEyfaglygLKGDELTARLEEL-----------ADRLG 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  74 FNTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI---KSQGCTQIIVAHRLSTIKD-ADI 149
Cdd:cd03266   126 MEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIrqlRALGKCILFSTHIMQEVERlCDR 205
                         170
                  ....*....|...
gi 1877026690 150 IFVMKGGKIVESG 162
Cdd:cd03266   206 VVVLHRGRVVYEG 218
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
3-163 2.85e-17

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 76.80  E-value: 2.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGININQIDKKILSQNLGVVPQD-SFLLN-----RSILD-----NITLKNEVTSQKIEEVCKAVQIYDEIMAMP 71
Cdd:COG4167    67 SGEILINGHKLEYGDYKYRCKHIRMIFQDpNTSLNprlniGQILEeplrlNTDLTAEEREERIFATLRLVGLLPEHANFY 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  72 MKfntiiseMgsnISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI----KSQGCTQIIVAHRLSTIKD- 146
Cdd:COG4167   147 PH-------M---LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMlelqEKLGISYIYVSQHLGIVKHi 216
                         170
                  ....*....|....*..
gi 1877026690 147 ADIIFVMKGGKIVESGN 163
Cdd:COG4167   217 SDKVLVMHQGEVVEYGK 233
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
86-140 3.12e-17

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: 74.50  E-value: 3.12e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQGCTQIIVAHR 140
Cdd:cd03223    93 SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHR 147
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
85-159 4.03e-17

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


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 74.39  E-value: 4.03e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI---KSQGCTQIIVAHRLSTIKD-ADIIFVMKGGKIV 159
Cdd:cd03216    83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIrrlRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
2-163 4.59e-17

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: 75.74  E-value: 4.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDkkILSQNLGVVPQDSFLLNR-SILDNIT-------LKNEVTSQKIEEVCKAVQIYDEIMAMPmk 73
Cdd:cd03300    53 TSGEILLDGKDITNLP--PHKRPVNTVFQNYALFPHlTVFENIAfglrlkkLPKAEIKERVAEALDLVQLEGYANRKP-- 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  74 fntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALD-----TINEE--RITKYIksqGCTQIIVAHRLS-TIK 145
Cdd:cd03300   129 ---------SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDlklrkDMQLElkRLQKEL---GITFVFVTHDQEeALT 196
                         170
                  ....*....|....*...
gi 1877026690 146 DADIIFVMKGGKIVESGN 163
Cdd:cd03300   197 MSDRIAVMNKGKIQQIGT 214
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
3-163 4.64e-17

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 75.84  E-value: 4.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGININ--QIDKKILSQNLGVVPQDSFLLNRSILDNIT--LK-NEVTSQK-----IEEVCKAVQIYDEImampm 72
Cdd:COG1117    70 EGEILLDGEDIYdpDVDVVELRRRVGMVFQKPNPFPKSIYDNVAygLRlHGIKSKSeldeiVEESLRKAALWDEV----- 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  73 kfNTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI---KSQgCTQIIVAH------RLSt 143
Cdd:COG1117   145 --KDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELIlelKKD-YTIVIVTHnmqqaaRVS- 220
                         170       180
                  ....*....|....*....|
gi 1877026690 144 ikdaDIIFVMKGGKIVESGN 163
Cdd:COG1117   221 ----DYTAFFYLGELVEFGP 236
PLN03130 PLN03130
ABC transporter C family member; Provisional
28-171 5.28e-17

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 77.86  E-value: 5.28e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   28 VPQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMGSNISGGQRQRIALARALINNPSIVI 107
Cdd:PLN03130   684 VPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYI 763
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1877026690  108 LDEATSALDT-INEERITKYIKS--QGCTQIIVAHRLSTIKDADIIFVMKGGKIVESGNHKYLMELG 171
Cdd:PLN03130   764 FDDPLSALDAhVGRQVFDKCIKDelRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNG 830
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
2-160 6.27e-17

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: 75.20  E-value: 6.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKIlsqnlGVVPQDSFLLN-RSILDNITLknevtSQKIEEVCKAvQIYDEIMAMpmkfntiISE 80
Cdd:cd03293    57 TSGEVLVDGEPVTGPGPDR-----GYVFQQDALLPwLTVLDNVAL-----GLELQGVPKA-EARERAEEL-------LEL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MG---------SNISGGQRQRIALARALINNPSIVILDEATSALD-----TINEErITKYIKSQGCTQIIVAHRLS-TIK 145
Cdd:cd03293   119 VGlsgfenaypHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDaltreQLQEE-LLDIWRETGKTVLLVTHDIDeAVF 197
                         170
                  ....*....|....*..
gi 1877026690 146 DADIIFVMKG--GKIVE 160
Cdd:cd03293   198 LADRVVVLSArpGRIVA 214
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
1-162 9.02e-17

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: 74.54  E-value: 9.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   1 MDTGKVLFDGINInQIDKKILSQNLGVVPQDsFLLNRSI-----LDNITLKNEVTS----QKIEEVCKAVQIYDEImamp 71
Cdd:cd03264    51 PSSGTIRIDGQDV-LKQPQKLRRRIGYLPQE-FGVYPNFtvrefLDYIAWLKGIPSkevkARVDEVLELVNLGDRA---- 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  72 mkfntiiSEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTinEERIT--KYIKSQGCTQIIV--AHRLSTIKD- 146
Cdd:cd03264   125 -------KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP--EERIRfrNLLSELGEDRIVIlsTHIVEDVESl 195
                         170
                  ....*....|....*.
gi 1877026690 147 ADIIFVMKGGKIVESG 162
Cdd:cd03264   196 CNQVAVLNKGKLVFEG 211
PLN03232 PLN03232
ABC transporter C family member; Provisional
28-171 9.41e-17

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 77.32  E-value: 9.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   28 VPQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMGSNISGGQRQRIALARALINNPSIVI 107
Cdd:PLN03232   684 VPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYI 763
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1877026690  108 LDEATSALDT-INEERITKYIKS--QGCTQIIVAHRLSTIKDADIIFVMKGGKIVESGNHKYLMELG 171
Cdd:PLN03232   764 FDDPLSALDAhVAHQVFDSCMKDelKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSG 830
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
2-162 2.07e-16

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 75.49  E-value: 2.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQID-KKilsQNLGVVPQdSFLL--NRSILDNIT--LKNEVTS-----QKIEEVCKAVQIyDEIMA-M 70
Cdd:COG3839    56 TSGEILIGGRDVTDLPpKD---RNIAMVFQ-SYALypHMTVYENIAfpLKLRKVPkaeidRRVREAAELLGL-EDLLDrK 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  71 PmkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALD------TINEerITKYIKSQGCTQIIVAHrlsti 144
Cdd:COG3839   131 P-----------KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrveMRAE--IKRLHRRLGTTTIYVTH----- 192
                         170       180
                  ....*....|....*....|....*
gi 1877026690 145 kD-------ADIIFVMKGGKIVESG 162
Cdd:COG3839   193 -DqveamtlADRIAVMNDGRIQQVG 216
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
20-170 2.13e-16

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: 75.99  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  20 ILSQNLGVVPqdsfllNRSILDNIT------LKNEVTSQKIEEVCKAVQIYDEimampmKFNTIISEMGSNISGGQRQRI 93
Cdd:TIGR03269 369 ILHQEYDLYP------HRTVLDNLTeaigleLPDELARMKAVITLKMVGFDEE------KAEEILDKYPDELSEGERHRV 436
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  94 ALARALINNPSIVILDEATSALDTINEERITKYI----KSQGCTQIIVAHRLSTIKD-ADIIFVMKGGKIVESGNHKYLM 168
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516

                  ..
gi 1877026690 169 EL 170
Cdd:TIGR03269 517 EE 518
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
4-162 3.64e-16

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 73.87  E-value: 3.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVVPQ--DSFLLNRSI-------LDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPmkf 74
Cdd:PRK13632   64 GEIKIDGITISKENLKEIRKKIGIIFQnpDNQFIGATVeddiafgLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEP--- 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  75 ntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQII-VAHRLSTIKDADII 150
Cdd:PRK13632  141 --------QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrkTRKKTLIsITHDMDEAILADKV 212
                         170
                  ....*....|..
gi 1877026690 151 FVMKGGKIVESG 162
Cdd:PRK13632  213 IVFSEGKLIAQG 224
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
83-162 9.68e-16

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


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 71.43  E-value: 9.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK---SQGCTQIIVAHRLST--IKDADIIFVMKGGK 157
Cdd:cd03213   110 RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRrlaDTGRTIICSIHQPSSeiFELFDKLLLLSQGR 189

                  ....*
gi 1877026690 158 IVESG 162
Cdd:cd03213   190 VIYFG 194
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
29-156 1.04e-15

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: 74.18  E-value: 1.04e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   29 PQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMGSNISGGQRQRIALARALINNPSIVIL 108
Cdd:TIGR01271  493 PQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLL 572
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1877026690  109 DEATSALDTINEERI-----TKYIKSQgcTQIIVAHRLSTIKDADIIFVMKGG 156
Cdd:TIGR01271  573 DSPFTHLDVVTEKEIfesclCKLMSNK--TRILVTSKLEHLKKADKILLLHEG 623
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
4-160 1.39e-15

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: 72.15  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQID---KKILSQNLGVVPQDS---FLLNRSI-------LDNIT-LKNEVTSQKIEEVCKAVQIYDEIM- 68
Cdd:TIGR02769  66 GTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDSpsaVNPRMTVrqiigepLRHLTsLDESEQKARIAELLDMVGLRSEDAd 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  69 AMPMKFntiisemgsniSGGQRQRIALARALINNPSIVILDEATSALDTINE----ERITKYIKSQGCTQIIVAHRLSTI 144
Cdd:TIGR02769 146 KLPRQL-----------SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQavilELLRKLQQAFGTAYLFITHDLRLV 214
                         170
                  ....*....|....*..
gi 1877026690 145 -KDADIIFVMKGGKIVE 160
Cdd:TIGR02769 215 qSFCQRVAVMDKGQIVE 231
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
29-156 1.65e-15

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: 72.20  E-value: 1.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  29 PQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMGSNISGGQRQRIALARALINNPSIVIL 108
Cdd:cd03291   104 SQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLL 183
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1877026690 109 DEATSALDTINEERI-----TKYIKSQgcTQIIVAHRLSTIKDADIIFVMKGG 156
Cdd:cd03291   184 DSPFGYLDVFTEKEIfescvCKLMANK--TRILVTSKMEHLKKADKILILHEG 234
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
2-162 2.33e-15

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 72.14  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKIlsQNLGVVPQDSFLL-NRSILDNIT--LK-----NEVTSQKIEEVCKAVQIYDEIMAMPmk 73
Cdd:TIGR01187  23 DSGSIMLDGEDVTNVPPHL--RHINMVFQSYALFpHMTVEENVAfgLKmrkvpRAEIKPRVLEALRLVQLEEFADRKP-- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  74 fntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERIT---KYIKSQ-GCTQIIVAHRLS-TIKDAD 148
Cdd:TIGR01187  99 ---------HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQlelKTIQEQlGITFVFVTHDQEeAMTMSD 169
                         170
                  ....*....|....
gi 1877026690 149 IIFVMKGGKIVESG 162
Cdd:TIGR01187 170 RIAIMRKGKIAQIG 183
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
2-163 4.27e-15

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 71.97  E-value: 4.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGINInQIDKKILSQNLGV--VPQD-SFLLNRSILDNITLKNEVTS----------QKIEEVCKAVQIydeim 68
Cdd:COG1129    57 DSGEILLDGEPV-RFRSPRDAQAAGIaiIHQElNLVPNLSVAENIFLGREPRRgglidwramrRRARELLARLGL----- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  69 amPMKFNTIISEMgsniSGGQRQRIALARALINNPSIVILDEATSALDtiNEE-----RITKYIKSQGCTQIIVAHRLST 143
Cdd:COG1129   131 --DIDPDTPVGDL----SVAQQQLVEIARALSRDARVLILDEPTASLT--EREverlfRIIRRLKAQGVAIIYISHRLDE 202
                         170       180
                  ....*....|....*....|.
gi 1877026690 144 IKD-ADIIFVMKGGKIVESGN 163
Cdd:COG1129   203 VFEiADRVTVLRDGRLVGTGP 223
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
85-162 4.81e-15

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


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 70.02  E-value: 4.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQ----GCTQIIVAHRLSTI-KDADIIFVMKGGKIV 159
Cdd:cd03297   132 LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIkknlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211

                  ...
gi 1877026690 160 ESG 162
Cdd:cd03297   212 YIG 214
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
83-173 5.57e-15

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 70.81  E-value: 5.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI----KSQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:PRK13635  139 HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVrqlkEQKGITVLSITHDLDEAAQADRVIVMNKGEI 218
                          90
                  ....*....|....*
gi 1877026690 159 VESGNHKYLMELGGE 173
Cdd:PRK13635  219 LEEGTPEEIFKSGHM 233
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
2-148 7.64e-15

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 69.74  E-value: 7.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQKIEEvckavqiyDEIMAMPMKF---NTII 78
Cdd:PRK10247   60 TSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDP--------AIFLDDLERFalpDTIL 131
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1877026690  79 SEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINE----ERITKYIKSQGCTQIIVAHRLSTIKDAD 148
Cdd:PRK10247  132 TKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKhnvnEIIHRYVREQNIAVLWVTHDKDEINHAD 205
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
17-164 8.03e-15

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 69.66  E-value: 8.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  17 DKKI--LSQNLGVVPQDSFLL-NRSILDNIT--------LKNEVTSQKIEEVCKAVQIYDEIMAMPMkfntiisemgsNI 85
Cdd:PRK11124   74 DKAIreLRRNVGMVFQQYNLWpHLTVQQNLIeapcrvlgLSKDQALARAEKLLERLRLKPYADRFPL-----------HL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK--SQ-GCTQIIVAHRLSTI-KDADIIFVMKGGKIVES 161
Cdd:PRK11124  143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRelAEtGITQVIVTHEVEVArKTASRVVYMENGHIVEQ 222

                  ...
gi 1877026690 162 GNH 164
Cdd:PRK11124  223 GDA 225
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
4-158 1.23e-14

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: 71.09  E-value: 1.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690    4 GKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMGS 83
Cdd:TIGR01271 1273 GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGY 1352
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1877026690   84 NISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS--QGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:TIGR01271 1353 VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQsfSNCTVILSEHRVEALLECQQFLVIEGSSV 1429
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
3-165 1.40e-14

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 69.42  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGINI--NQIDKKILSQNLGVVPQDSFLLNRSILDNITL--------KNEVTSQKIEEVCKAVQIYDEImampm 72
Cdd:PRK14239   64 TGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYglrlkgikDKQVLDEAVEKSLKGASIWDEV----- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  73 kfNTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERI--TKYIKSQGCTQIIVAHRL---STIKDA 147
Cdd:PRK14239  139 --KDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIeeTLLGLKDDYTMLLVTRSMqqaSRISDR 216
                         170
                  ....*....|....*...
gi 1877026690 148 DIIFVmkGGKIVESGNHK 165
Cdd:PRK14239  217 TGFFL--DGDLIEYNDTK 232
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
4-141 2.93e-14

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 68.66  E-value: 2.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININ--QIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQK------IEEVCKAVQIYDEImampmkfN 75
Cdd:PRK14243   70 GKVTFHGKNLYapDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGARINGYKgdmdelVERSLRQAALWDEV-------K 142
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1877026690  76 TIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS--QGCTQIIVAHRL 141
Cdd:PRK14243  143 DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHElkEQYTIIIVTHNM 210
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
86-162 3.68e-14

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 68.84  E-value: 3.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDT------------INEERITKYiksqgctqIIVAHRLSTIKD-ADIIFV 152
Cdd:PRK11308  156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVsvqaqvlnlmmdLQQELGLSY--------VFISHDLSVVEHiADEVMV 227
                          90
                  ....*....|
gi 1877026690 153 MKGGKIVESG 162
Cdd:PRK11308  228 MYLGRCVEKG 237
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
4-158 5.98e-14

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: 67.96  E-value: 5.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMGS 83
Cdd:cd03289    58 GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGC 137
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1877026690  84 NISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS--QGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:cd03289   138 VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQafADCTVILSEHRIEAMLECQRFLVIEENKV 214
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
4-163 7.05e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 67.47  E-value: 7.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVV---PQDSFLlnRSI--------LDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPm 72
Cdd:PRK13648   64 GEIFYNNQAITDDNFEKLRKHIGIVfqnPDNQFV--GSIvkydvafgLENHAVPYDEMHRRVSEALKQVDMLERADYEP- 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  73 kfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALDTINEE---RITKYIKSQGCTQII-VAHRLSTIKDAD 148
Cdd:PRK13648  141 ----------NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQnllDLVRKVKSEHNITIIsITHDLSEAMEAD 210
                         170
                  ....*....|....*
gi 1877026690 149 IIFVMKGGKIVESGN 163
Cdd:PRK13648  211 HVIVMNKGTVYKEGT 225
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
1-167 7.42e-14

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: 66.76  E-value: 7.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   1 MDTGKVLFDGININQiDKKILSQNLGVVPQ-DSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIIS 79
Cdd:cd03263    54 PTSGTAYINGYSIRT-DRKAARQSLGYCPQfDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRAR 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  80 EMgsniSGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS--QGCTQIIVAHrlsTIKDADI----IFVM 153
Cdd:cd03263   133 TL----SGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEvrKGRSIILTTH---SMDEAEAlcdrIAIM 205
                         170
                  ....*....|....
gi 1877026690 154 KGGKIVESGNHKYL 167
Cdd:cd03263   206 SDGKLRCIGSPQEL 219
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
3-169 8.10e-14

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: 66.69  E-value: 8.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGINI-NQIDKKILSQNLGVVPQDSFLLNR-SILDNITL-----KNEVTSQKIEEVCKAVQIYDEIMampmkfn 75
Cdd:cd03224    54 SGSIRFDGRDItGLPPHERARAGIGYVPEGRRIFPElTVEENLLLgayarRRAKRKARLERVYELFPRLKERR------- 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  76 tiiSEMGSNISGGQRQRIALARALINNPSIVILDEATSAL-----DTIneERITKYIKSQGCTQIIVAHRLSTIKD-ADI 149
Cdd:cd03224   127 ---KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLapkivEEI--FEAIRELRDEGVTILLVEQNARFALEiADR 201
                         170       180
                  ....*....|....*....|
gi 1877026690 150 IFVMKGGKIVESGNHKYLME 169
Cdd:cd03224   202 AYVLERGRVVLEGTAAELLA 221
PTZ00243 PTZ00243
ABC transporter; Provisional
21-169 8.20e-14

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 68.65  E-value: 8.20e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   21 LSQNLGVVPQDSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMGSNISGGQRQRIALARALI 100
Cdd:PTZ00243  1382 LRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALL 1461
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1877026690  101 NNPSIVIL-DEATSALDTINEERITKYIKS--QGCTQIIVAHRLSTIKDADIIFVMKGGKIVESGNHKYLME 169
Cdd:PTZ00243  1462 KKGSGFILmDEATANIDPALDRQIQATVMSafSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVM 1533
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
62-167 1.26e-13

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 67.42  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  62 QIYDEIMAMPMKFN---TIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS----QGCTQ 134
Cdd:PRK15079  136 EVKDRVKAMMLKVGllpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQlqreMGLSL 215
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1877026690 135 IIVAHRLSTIKD-ADIIFVMKGGKIVESGNHKYL 167
Cdd:PRK15079  216 IFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
3-158 1.40e-13

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 66.38  E-value: 1.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGININQIDK----KILSQNLGVVPQDSFLL-NRSILDNITL-------KNEVTSQKIEEVCKAVQIYDEIMAM 70
Cdd:PRK11629   63 SGDVIFNGQPMSKLSSaakaELRNQKLGFIYQFHHLLpDFTALENVAMplligkkKPAEINSRALEMLAAVGLEHRANHR 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  71 PmkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI----KSQGCTQIIVAHRLSTIKD 146
Cdd:PRK11629  143 P-----------SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLgelnRLQGTAFLVVTHDLQLAKR 211
                         170
                  ....*....|..
gi 1877026690 147 ADIIFVMKGGKI 158
Cdd:PRK11629  212 MSRQLEMRDGRL 223
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
1-162 1.93e-13

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 65.74  E-value: 1.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   1 MDTGKVLFDGININQIDKKilSQNLGVVPQDSFLL-NRSILDNITL-------KNEVTSQKIEEVCKAVQIYDEIMAMPm 72
Cdd:cd03301    52 PTSGRIYIGGRDVTDLPPK--DRDIAMVFQNYALYpHMTVYDNIAFglklrkvPKDEIDERVREVAELLQIEHLLDRKP- 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  73 kfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALD-----TINEErITKYIKSQGCTQIIVAH-RLSTIKD 146
Cdd:cd03301   129 ----------KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrvQMRAE-LKRLQQRLGTTTIYVTHdQVEAMTM 197
                         170
                  ....*....|....*.
gi 1877026690 147 ADIIFVMKGGKIVESG 162
Cdd:cd03301   198 ADRIAVMNDGQIQQIG 213
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
83-169 2.16e-13

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 65.88  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALD-TINEE--RITKYIKSQGCTQIIVAHRLSTIKD--ADIIFvMKGGK 157
Cdd:PRK09493  135 SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDpELRHEvlKVMQDLAEEGMTMVIVTHEIGFAEKvaSRLIF-IDKGR 213
                          90
                  ....*....|..
gi 1877026690 158 IVESGNHKYLME 169
Cdd:PRK09493  214 IAEDGDPQVLIK 225
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
83-162 2.46e-13

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 67.04  E-value: 2.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS----QGCTQIIVAHRLSTIKD-ADIIFVMKGGK 157
Cdd:PRK15134  424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSlqqkHQLAYLFISHDLHVVRAlCHQVIVLRQGE 503

                  ....*
gi 1877026690 158 IVESG 162
Cdd:PRK15134  504 VVEQG 508
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
21-167 3.38e-13

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 65.54  E-value: 3.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  21 LSQNLGVVPQdSFLL--NRSILDNI-----TLKNEVTSQKIE---EVCKAVQIYDEIMAMPMKfntiisemgsnISGGQR 90
Cdd:PRK11264   83 LRQHVGFVFQ-NFNLfpHRTVLENIiegpvIVKGEPKEEATArarELLAKVGLAGKETSYPRR-----------LSGGQQ 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  91 QRIALARALINNPSIVILDEATSALDT--INEERIT-KYIKSQGCTQIIVAHRLSTIKD-ADIIFVMKGGKIVESGNHKY 166
Cdd:PRK11264  151 QRVAIARALAMRPEVILFDEPTSALDPelVGEVLNTiRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKA 230

                  .
gi 1877026690 167 L 167
Cdd:PRK11264  231 L 231
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
2-162 5.26e-13

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: 64.22  E-value: 5.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKkilsQNLGVVPQDSFL-LNRSILDNIT-------LKNEVTSQKIEEVCKAVQIYDeimampmK 73
Cdd:cd03269    53 DSGEVLFDGKPLDIAAR----NRIGYLPEERGLyPKMKVIDQLVylaqlkgLKKEEARRRIDEWLERLELSE-------Y 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  74 FNTIISEMgsniSGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI---KSQGCTQIIVAHRLSTIKD-ADI 149
Cdd:cd03269   122 ANKRVEEL----SKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIrelARAGKTVILSTHQMELVEElCDR 197
                         170
                  ....*....|...
gi 1877026690 150 IFVMKGGKIVESG 162
Cdd:cd03269   198 VLLLNKGRAVLYG 210
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
4-163 5.42e-13

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 65.07  E-value: 5.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVV-PQDSFLLNRSILDNIT--LKNEVTSQK------IEEVCKAVQIYDEIMAMpmkf 74
Cdd:PRK14246   71 GKVLYFGKDIFQIDAIKLRKEVGMVfQQPNPFPHLSIYDNIAypLKSHGIKEKreikkiVEECLRKVGLWKEVYDR---- 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  75 ntiISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS--QGCTQIIVAHRLSTI-KDADIIF 151
Cdd:PRK14246  147 ---LNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITElkNEIAIVIVSHNPQQVaRVADYVA 223
                         170
                  ....*....|..
gi 1877026690 152 VMKGGKIVESGN 163
Cdd:PRK14246  224 FLYNGELVEWGS 235
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
2-162 8.47e-13

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: 63.78  E-value: 8.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQiDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQKIEEVckavqiyDEIMAMpMKFNTIISEM 81
Cdd:cd03268    53 DSGEITFDGKSYQK-NIEALRRIGALIEAPGFYPNLTARENLRLLARLLGIRKKRI-------DEVLDV-VGLKDSAKKK 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  82 GSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI---KSQGCTQIIVAHRLSTI-KDADIIFVMKGGK 157
Cdd:cd03268   124 VKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELIlslRDQGITVLISSHLLSEIqKVADRIGIINKGK 203

                  ....*
gi 1877026690 158 IVESG 162
Cdd:cd03268   204 LIEEG 208
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
2-160 8.56e-13

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: 63.99  E-value: 8.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDK----KILSQNLGVVPQdSFLL--NRSILDNITLKNEVTS-----QKIEEVCKAVQIYDEIMAM 70
Cdd:COG4181    65 TSGTVRLAGQDLFALDEdaraRLRARHVGFVFQ-SFQLlpTLTALENVMLPLELAGrrdarARARALLERVGLGHRLDHY 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  71 PmkfntiiSEMgsniSGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI----KSQGCTQIIVAHRLSTIKD 146
Cdd:COG4181   144 P-------AQL----SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfelnRERGTTLVLVTHDPALAAR 212
                         170
                  ....*....|....
gi 1877026690 147 ADIIFVMKGGKIVE 160
Cdd:COG4181   213 CDRVLRLRAGRLVE 226
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
2-162 1.32e-12

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: 63.90  E-value: 1.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQidKKILSQNLGVVPQDSFLLNR-SILDNITLKNEVtsQKIEEVCKAVQIYDEIMAMP--MKFNTII 78
Cdd:cd03296    55 DSGTILFGGEDATD--VPVQERNVGFVFQHYALFRHmTVFDNVAFGLRV--KPRSERPPEAEIRAKVHELLklVQLDWLA 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  79 SEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK----SQGCTQIIVAHRLS-TIKDADIIFVM 153
Cdd:cd03296   131 DRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRrlhdELHVTTVFVTHDQEeALEVADRVVVM 210

                  ....*....
gi 1877026690 154 KGGKIVESG 162
Cdd:cd03296   211 NKGRIEQVG 219
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
86-162 1.38e-12

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: 64.71  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALD-TInEERITKYIKS----QGCTQIIVAHRLSTIKD-ADIIFVMKGGKIV 159
Cdd:COG4172   158 SGGQRQRVMIAMALANEPDLLIADEPTTALDvTV-QAQILDLLKDlqreLGMALLLITHDLGVVRRfADRVAVMRQGEIV 236

                  ...
gi 1877026690 160 ESG 162
Cdd:COG4172   237 EQG 239
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
2-162 1.48e-12

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 63.62  E-value: 1.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQ--IDK---KILSQ--NLgvvpqdsF--LlnrSILDNI------TLK-NEVTSQKIEEVCKAVQIYD 65
Cdd:COG3840    52 DSGRILWNGQDLTAlpPAErpvSMLFQenNL-------FphL---TVAQNIglglrpGLKlTAEQRAQVEQALERVGLAG 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  66 EIMAMPmkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALD------------TINEERitkyiksqGCT 133
Cdd:COG3840   122 LLDRLP-----------GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrqemldlvdELCRER--------GLT 182
                         170       180       190
                  ....*....|....*....|....*....|
gi 1877026690 134 QIIVAHRLSTIKD-ADIIFVMKGGKIVESG 162
Cdd:COG3840   183 VLMVTHDPEDAARiADRVLLVADGRIAADG 212
cbiO PRK13650
energy-coupling factor transporter ATPase;
83-177 1.87e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 63.60  E-value: 1.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS----QGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:PRK13650  139 ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGirddYQMTVISITHDLDEVALSDRVLVMKNGQV 218
                          90
                  ....*....|....*....
gi 1877026690 159 VESGNHKYLMELGGEYYSL 177
Cdd:PRK13650  219 ESTSTPRELFSRGNDLLQL 237
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
2-150 1.95e-12

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: 62.88  E-value: 1.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRSILDNITL-----KNEVTSQKIEEVCKAVQIYDeimampmkfnt 76
Cdd:COG4133    55 SAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPELTVRENLRFwaalyGLRADREAIDEALEAVGLAG----------- 123
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1877026690  77 IISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI---KSQGCTQIIVAHRLSTIKDADII 150
Cdd:COG4133   124 LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIaahLARGGAVLLTTHQPLELAAARVL 200
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
86-162 1.99e-12

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: 63.18  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDTINEER----ITKYIKSQGCTQIIVAHRLStikdaDII------FVMKG 155
Cdd:COG1119   144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELllalLDKLAAEGAPTLVLVTHHVE-----EIPpgithvLLLKD 218

                  ....*..
gi 1877026690 156 GKIVESG 162
Cdd:COG1119   219 GRVVAAG 225
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
85-165 3.07e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 63.18  E-value: 3.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK----SQGCTQIIVAHRLSTIKDADIIFVMKGGKIVE 160
Cdd:PRK13633  145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelnkKYGITIILITHYMEEAVEADRIIVMDSGKVVM 224

                  ....*
gi 1877026690 161 SGNHK 165
Cdd:PRK13633  225 EGTPK 229
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
4-162 4.01e-12

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 62.62  E-value: 4.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVVPQ-DSFLLNRSILDNITL----------KNEVtSQKIEEVCKAVQIYDEIMampm 72
Cdd:PRK14247   63 GEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIPNLSIFENVALglklnrlvksKKEL-QERVRWALEKAQLWDEVK---- 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  73 kfNTIISEMGSnISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS--QGCTQIIVAH------RLSti 144
Cdd:PRK14247  138 --DRLDAPAGK-LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLElkKDMTIVLVTHfpqqaaRIS-- 212
                         170
                  ....*....|....*...
gi 1877026690 145 kdaDIIFVMKGGKIVESG 162
Cdd:PRK14247  213 ---DYVAFLYKGQIVEWG 227
cbiO PRK13640
energy-coupling factor transporter ATPase;
83-162 4.78e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 62.51  E-value: 4.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI----KSQGCTQIIVAHRLSTIKDADIIFVMKGGKI 158
Cdd:PRK13640  142 ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIrklkKKNNLTVISITHDIDEANMADQVLVLDDGKL 221

                  ....
gi 1877026690 159 VESG 162
Cdd:PRK13640  222 LAQG 225
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
2-165 9.23e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 61.63  E-value: 9.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGINInQIDKKIL---SQNLGVVPQ--DSFLLNRSILD-------NITLKNEVTSQKIEEVCKAVQIYDEIMA 69
Cdd:PRK13639   55 TSGEVLIKGEPI-KYDKKSLlevRKTVGIVFQnpDDQLFAPTVEEdvafgplNLGLSKEEVEKRVKEALKAVGMEGFENK 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  70 MPmkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLSTI-K 145
Cdd:PRK13639  134 PP-----------HHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDlnkEGITIIISTHDVDLVpV 202
                         170       180
                  ....*....|....*....|
gi 1877026690 146 DADIIFVMKGGKIVESGNHK 165
Cdd:PRK13639  203 YADKVYVMSDGKIIKEGTPK 222
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
2-169 1.08e-11

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: 61.02  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQ-NLGVVPQDSFLLNR-SILDNITLKNEVT-------SQKIEEVCKAVQIYdeimampm 72
Cdd:cd03218    53 DSGKILLDGQDITKLPMHKRARlGIGYLPQEASIFRKlTVEENILAVLEIRglskkerEEKLEELLEEFHIT-------- 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  73 kfnTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTI---NEERITKYIKSQGCTQIIVAHRLS-TIKDAD 148
Cdd:cd03218   125 ---HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIavqDIQKIIKILKDRGIGVLITDHNVReTLSITD 201
                         170       180
                  ....*....|....*....|.
gi 1877026690 149 IIFVMKGGKIVESGNHKYLME 169
Cdd:cd03218   202 RAYIIYEGKVLAEGTPEEIAA 222
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
2-160 1.24e-11

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 61.24  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQID---KKILSQNLGVVPQDSF-LLN-----RSILDN-----ITLKNEVTSQKIEEVCKAVQIYDEI 67
Cdd:PRK10419   65 SQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSIsAVNprktvREIIREplrhlLSLDKAERLARASEMLRAVDLDDSV 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  68 MampmkfntiiSEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS----QGCTQIIVAHRLST 143
Cdd:PRK10419  145 L----------DKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKlqqqFGTACLFITHDLRL 214
                         170
                  ....*....|....*...
gi 1877026690 144 I-KDADIIFVMKGGKIVE 160
Cdd:PRK10419  215 VeRFCQRVMVMDNGQIVE 232
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
62-162 1.40e-11

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: 60.62  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  62 QIYDEIMAM-PmkfntIISEM----GSNISGGQRQRIALARALINNPSIVILDEAT-----SALDTIneERITKYIKSQ- 130
Cdd:TIGR03410 109 KIPDEIYELfP-----VLKEMlgrrGGDLSGGQQQQLAIARALVTRPKLLLLDEPTegiqpSIIKDI--GRVIRRLRAEg 181
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1877026690 131 GCTQIIVAHRLSTIKD-ADIIFVMKGGKIVESG 162
Cdd:TIGR03410 182 GMAILLVEQYLDFARElADRYYVMERGRVVASG 214
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
83-165 1.45e-11

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 62.05  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDTINEER---ITKYIKSQGCTQIIVAHRLSTIKDADIIFVMKGGKIV 159
Cdd:PRK10535  143 SQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEvmaILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222

                  ....*..
gi 1877026690 160 -ESGNHK 165
Cdd:PRK10535  223 rNPPAQE 229
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
47-158 1.97e-11

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 60.26  E-value: 1.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  47 NEVTSQKIEEVCKAVQIYDEIMAMPmkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKY 126
Cdd:TIGR01277 102 NAEQQEKVVDAAQQVGIADYLDRLP-----------EQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1877026690 127 IKS----QGCTQIIVAHRLS-TIKDADIIFVMKGGKI 158
Cdd:TIGR01277 171 VKQlcseRQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
85-167 2.04e-11

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 61.27  E-value: 2.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTiN-----EERITKYIKSQGCTQIIVAHRLS-TIKDADIIFVMKGGKI 158
Cdd:PRK11432  137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDA-NlrrsmREKIRELQQQFNITSLYVTHDQSeAFAVSDTVIVMNKGKI 215

                  ....*....
gi 1877026690 159 VESGNHKYL 167
Cdd:PRK11432  216 MQIGSPQEL 224
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
85-158 2.61e-11

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 60.46  E-value: 2.61e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS----QGCTQIIVAHRLS-TIKDADIIFVMKGGKI 158
Cdd:PRK11247  134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESlwqqHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
cbiO PRK13646
energy-coupling factor transporter ATPase;
3-167 2.68e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 60.56  E-value: 2.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGININQI--DKKI--LSQNLGVVPQ--DSFLLNRSILDNITLKNEVTSQKIEEVcKAvQIYDEIMAMPMKFNt 76
Cdd:PRK13646   61 TGTVTVDDITITHKtkDKYIrpVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEV-KN-YAHRLLMDLGFSRD- 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  77 IISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS----QGCTQIIVAHRLSTI-KDADIIF 151
Cdd:PRK13646  138 VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqtdENKTIILVSHDMNEVaRYADEVI 217
                         170
                  ....*....|....*.
gi 1877026690 152 VMKGGKIVESGNHKYL 167
Cdd:PRK13646  218 VMKEGSIVSQTSPKEL 233
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
24-162 3.10e-11

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: 59.69  E-value: 3.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  24 NLGVVPQDsfllnRSILDNIT-------------LKNEVTSQKIEEVCKAVQIYDeimampmkfntIISEMGSNISGGQR 90
Cdd:cd03265    74 RIGIVFQD-----LSVDDELTgwenlyiharlygVPGAERRERIDELLDFVGLLE-----------AADRLVKTYSGGMR 137
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1877026690  91 QRIALARALINNPSIVILDEATSALDTINEERITKYIK----SQGCTQIIVAHRLSTIKD-ADIIFVMKGGKIVESG 162
Cdd:cd03265   138 RRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEklkeEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEG 214
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
86-163 3.24e-11

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 60.51  E-value: 3.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI---KSQGCTQIIVAHRLSTIKD-ADIIFVMKGGKIVES 161
Cdd:COG4152   131 SKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIrelAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLS 210

                  ..
gi 1877026690 162 GN 163
Cdd:COG4152   211 GS 212
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
85-148 3.39e-11

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 59.17  E-value: 3.39e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK---SQGCTQIIVAHRLSTIKDAD 148
Cdd:NF040873  120 LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAeehARGATVVVVTHDLELVRRAD 186
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
78-162 3.80e-11

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 60.11  E-value: 3.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  78 ISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQG--CTQIIVAHRLST---IKDADIIFV 152
Cdd:PRK14271  157 LSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAdrLTVIIVTHNLAQaarISDRAALFF 236
                          90
                  ....*....|
gi 1877026690 153 mkGGKIVESG 162
Cdd:PRK14271  237 --DGRLVEEG 244
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
4-157 3.86e-11

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 60.71  E-value: 3.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDG-----ININQIDKK---ILSQNLGVVPQdsfllnRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMA---MPM 72
Cdd:PRK13549   62 GEIIFEGeelqaSNIRDTERAgiaIIHQELALVKE------LSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAqlkLDI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  73 KFNTIISEMGsnisGGQRQRIALARALINNPSIVILDEATSALdTINEER----ITKYIKSQGCTQIIVAHRLSTIKD-A 147
Cdd:PRK13549  136 NPATPVGNLG----LGQQQLVEIAKALNKQARLLILDEPTASL-TESETAvlldIIRDLKAHGIACIYISHKLNEVKAiS 210
                         170
                  ....*....|
gi 1877026690 148 DIIFVMKGGK 157
Cdd:PRK13549  211 DTICVIRDGR 220
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
25-172 4.76e-11

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 60.23  E-value: 4.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  25 LGVVPQ-DSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMgsniSGGQRQRIALARALINNP 103
Cdd:PRK13536  116 IGVVPQfDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDL----SGGMKRRLTLARALINDP 191
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1877026690 104 SIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLSTIKD-ADIIFVMKGG-KIVESGNHKYLMELGG 172
Cdd:PRK13536  192 QLLILDEPTTGLDPHARHLIWERLRSllaRGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPHALIDEHIG 265
cbiO PRK13637
energy-coupling factor transporter ATPase;
3-163 5.49e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 59.68  E-value: 5.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGININqiDKKI----LSQNLGVVPQ--DSFLLNRSI-------LDNITLKNEVTSQKIEEVCKAVQIYDEIMA 69
Cdd:PRK13637   61 SGKIIIDGVDIT--DKKVklsdIRKKVGLVFQypEYQLFEETIekdiafgPINLGLSEEEIENRVKRAMNIVGLDYEDYK 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  70 MPMKFNtiisemgsnISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS----QGCTQIIVAHRLSTI- 144
Cdd:PRK13637  139 DKSPFE---------LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElhkeYNMTIILVSHSMEDVa 209
                         170
                  ....*....|....*....
gi 1877026690 145 KDADIIFVMKGGKIVESGN 163
Cdd:PRK13637  210 KLADRIIVMNKGKCELQGT 228
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
3-162 5.60e-11

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 59.26  E-value: 5.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGININQIDKKILSQNLGVVPQDsfLLnrsILDNITLKNEVT-------------SQKIEE-VCKAVQIydeim 68
Cdd:PRK11231   56 SGTVFLGDKPISMLSSRQLARRLALLPQH--HL---TPEGITVRELVAygrspwlslwgrlSAEDNArVNQAMEQ----- 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  69 ampmkfnTIISEMG----SNISGGQRQRIALARALINNPSIVILDEATSALDtINEE----RITKYIKSQGCTQIIVAHR 140
Cdd:PRK11231  126 -------TRINHLAdrrlTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD-INHQvelmRLMRELNTQGKTVVTVLHD 197
                         170       180
                  ....*....|....*....|...
gi 1877026690 141 LS-TIKDADIIFVMKGGKIVESG 162
Cdd:PRK11231  198 LNqASRYCDHLVVLANGHVMAQG 220
cbiO PRK13649
energy-coupling factor transporter ATPase;
3-165 5.82e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 59.76  E-value: 5.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGININQIDK----KILSQNLGVVPQ--DSFLLNRSILDNITL--KNEVTSQKieevcKAVQIYDEIMAMPMKF 74
Cdd:PRK13649   61 QGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQfpESQLFEETVLKDVAFgpQNFGVSQE-----EAEALAREKLALVGIS 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  75 NTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEE---RITKYIKSQGCTQIIVAHRLSTIKD-ADII 150
Cdd:PRK13649  136 ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKelmTLFKKLHQSGMTIVLVTHLMDDVANyADFV 215
                         170
                  ....*....|....*
gi 1877026690 151 FVMKGGKIVESGNHK 165
Cdd:PRK13649  216 YVLEKGKLVLSGKPK 230
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
83-162 6.02e-11

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 59.96  E-value: 6.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDTineeRITKYIKSQ--------GCTQIIVAH-RLSTIKDADIIFVM 153
Cdd:PRK09452  143 HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY----KLRKQMQNElkalqrklGITFVFVTHdQEEALTMSDRIVVM 218

                  ....*....
gi 1877026690 154 KGGKIVESG 162
Cdd:PRK09452  219 RDGRIEQDG 227
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
73-162 6.23e-11

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: 58.69  E-value: 6.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  73 KFNTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITK---YIKSQGCTQIIVAH--RLSTIKDA 147
Cdd:cd03217    93 KNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEvinKLREEGKSVLIITHyqRLLDYIKP 172
                          90
                  ....*....|....*
gi 1877026690 148 DIIFVMKGGKIVESG 162
Cdd:cd03217   173 DRVHVLYDGRIVKSG 187
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
86-162 7.07e-11

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 59.17  E-value: 7.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS----QGCTQIIVAHRLSTIK-DADIIFVMKGGKIVE 160
Cdd:PRK11701  153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlvreLGLAVVIVTHDLAVARlLAHRLLVMKQGRVVE 232

                  ..
gi 1877026690 161 SG 162
Cdd:PRK11701  233 SG 234
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
85-162 7.17e-11

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: 58.66  E-value: 7.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI----KSQGCTQIIVAHRLSTIKD-ADIIFVMKGGKIV 159
Cdd:cd03298   129 LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVldlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208

                  ...
gi 1877026690 160 ESG 162
Cdd:cd03298   209 AQG 211
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
4-162 7.41e-11

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 59.66  E-value: 7.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQID----KKILSQNLGVVPQDSFLL-NRSILDNITLKNEVTSQKIEEvcKAVQIYDEIMAMPMKfnTII 78
Cdd:PRK10070   83 GQVLIDGVDIAKISdaelREVRRKKIAMVFQSFALMpHMTVLDNTAFGMELAGINAEE--RREKALDALRQVGLE--NYA 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  79 SEMGSNISGGQRQRIALARALINNPSIVILDEATSALDT-INEERITKYIKSQGCTQ---IIVAHRL-STIKDADIIFVM 153
Cdd:PRK10070  159 HSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlIRTEMQDELVKLQAKHQrtiVFISHDLdEAMRIGDRIAIM 238

                  ....*....
gi 1877026690 154 KGGKIVESG 162
Cdd:PRK10070  239 QNGEVVQVG 247
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
88-163 8.47e-11

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 59.03  E-value: 8.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  88 GQRQRIALARALINNPSIVILDEATSALDTINEERITKYI----KSQGCTQIIVAHRLSTIKD-ADIIFVMKGGKIVESG 162
Cdd:PRK15112  153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMlelqEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERG 232

                  .
gi 1877026690 163 N 163
Cdd:PRK15112  233 S 233
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
3-144 1.06e-10

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 58.35  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGININQIDKK---ILSQNLGVVPQDSFLL-NRSILDNITL-------KNEVTSQKIEEVCKAVQIYDEIMAMP 71
Cdd:PRK10908   56 AGKIWFSGHDITRLKNRevpFLRRQIGMIFQDHHLLmDRTVYDNVAIpliiagaSGDDIRRRVSAALDKVGLLDKAKNFP 135
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1877026690  72 MKfntiisemgsnISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLSTI 144
Cdd:PRK10908  136 IQ-----------LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEfnrVGVTVLMATHDIGLI 200
cbiO PRK13644
energy-coupling factor transporter ATPase;
85-162 1.15e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 58.85  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK---SQGCTQIIVAHRLSTIKDADIIFVMKGGKIVES 161
Cdd:PRK13644  137 LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKklhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLE 216

                  .
gi 1877026690 162 G 162
Cdd:PRK13644  217 G 217
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
86-169 1.31e-10

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 59.10  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALD-TINEERITKYIKSQ---GCTQIIVAHRLSTIKD-ADIIFVMKGGKIVE 160
Cdd:PRK10261  465 SGGQRQRICIARALALNPKVIIADEAVSALDvSIRGQIINLLLDLQrdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVE 544

                  ....*....
gi 1877026690 161 SGNHKYLME 169
Cdd:PRK10261  545 IGPRRAVFE 553
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
2-163 1.34e-10

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 58.88  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDG--ININQ----IDKKIlsqnlGVVPQDsFLL--NRSILDNITLKNEVT----------SQKIEEVCKAvqi 63
Cdd:COG3845    58 DSGEILIDGkpVRIRSprdaIALGI-----GMVHQH-FMLvpNLTVAENIVLGLEPTkggrldrkaaRARIRELSER--- 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  64 ydeiMAMPMKFNTIISEmgsnISGGQRQRIALARALINNPSIVILDEATSAL---------DTINEeritkyIKSQGCTQ 134
Cdd:COG3845   129 ----YGLDVDPDAKVED----LSVGEQQRVEILKALYRGARILILDEPTAVLtpqeadelfEILRR------LAAEGKSI 194
                         170       180       190
                  ....*....|....*....|....*....|
gi 1877026690 135 IIVAHRLSTIKD-ADIIFVMKGGKIVESGN 163
Cdd:COG3845   195 IFITHKLREVMAiADRVTVLRRGKVVGTVD 224
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
76-163 1.46e-10

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 59.10  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  76 TIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK------SQGCtqIIVAHRLSTIKD-AD 148
Cdd:PRK10261  160 TILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlqkemSMGV--IFITHDMGVVAEiAD 237
                          90
                  ....*....|....*
gi 1877026690 149 IIFVMKGGKIVESGN 163
Cdd:PRK10261  238 RVLVMYQGEAVETGS 252
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
1-162 1.47e-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: 58.05  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   1 MDTGKVLFDGiniNQIDKKILSQNLGVVPQDSFLLNR----------SILDNITLKNEVTSQKIEEVCKAVQIYDEIMAm 70
Cdd:cd03234    62 TTSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGltvretltytAILRLPRKSSDAIRKKRVEDVLLRDLALTRIG- 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  71 pmkfNTIISemgsNISGGQRQRIALARALINNPSIVILDEATSALDTI---NEERITKYIKSQGCTQIIVAH--RLSTIK 145
Cdd:cd03234   138 ----GNLVK----GISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFtalNLVSTLSQLARRNRIVILTIHqpRSDLFR 209
                         170
                  ....*....|....*..
gi 1877026690 146 DADIIFVMKGGKIVESG 162
Cdd:cd03234   210 LFDRILLLSSGEIVYSG 226
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
85-162 2.05e-10

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 58.50  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDT-----INEErITKYIKSQGCTQIIVAH-RLSTIKDADIIFVMKGGKI 158
Cdd:PRK11000  134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvqMRIE-ISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRV 212

                  ....
gi 1877026690 159 VESG 162
Cdd:PRK11000  213 AQVG 216
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
85-162 2.09e-10

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: 58.20  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQ----GCTQIIVAHRLSTIKD-ADIIFVMKGGKIV 159
Cdd:TIGR02142 132 LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLhaefGIPILYVSHSLQEVLRlADRVVVLEDGRVA 211

                  ...
gi 1877026690 160 ESG 162
Cdd:TIGR02142 212 AAG 214
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
2-162 2.13e-10

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 58.52  E-value: 2.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIdKKILSQNLGV--VPQDSFLL-NRSILDNITL---KNEVTSQKIEEVCKAVQIYdeiMAMPMKFN 75
Cdd:PRK15439   64 DSGTLEIGGNPCARL-TPAKAHQLGIylVPQEPLLFpNLSVKENILFglpKRQASMQKMKQLLAALGCQ---LDLDSSAG 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  76 TIisemgsNISggQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLSTIKD-ADIIF 151
Cdd:PRK15439  140 SL------EVA--DRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIREllaQGVGIVFISHKLPEIRQlADRIS 211
                         170
                  ....*....|.
gi 1877026690 152 VMKGGKIVESG 162
Cdd:PRK15439  212 VMRDGTIALSG 222
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
86-162 2.41e-10

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: 58.19  E-value: 2.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS-QGCTQI---IVAH------RLstikdADIIFVMKG 155
Cdd:COG4148   135 SGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERlRDELDIpilYVSHsldevaRL-----ADHVVLLEQ 209

                  ....*..
gi 1877026690 156 GKIVESG 162
Cdd:COG4148   210 GRVVASG 216
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
4-165 2.56e-10

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 57.74  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGINI--NQIDKKILSQNLGVVPQDSFLLNRSILDNITLKNEVTSQK--------IEEVCKAVQIYDEImampmk 73
Cdd:PRK14258   67 GRVEFFNQNIyeRRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRpkleiddiVESALKDADLWDEI------ 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  74 fNTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQG----CTQIIVAHRLSTI-KDAD 148
Cdd:PRK14258  141 -KHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNLHQVsRLSD 219
                         170       180
                  ....*....|....*....|..
gi 1877026690 149 IIFVMKG-----GKIVESGNHK 165
Cdd:PRK14258  220 FTAFFKGnenriGQLVEFGLTK 241
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
3-163 2.75e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 57.55  E-value: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGININQIDKKI--LSQNLGVVPQ--DSFLLNRSILDNITLKNEVTSQKIEEVCKAVqiyDEIMAmpmkfNTII 78
Cdd:PRK13636   60 SGRILFDGKPIDYSRKGLmkLRESVGMVFQdpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRV---DNALK-----RTGI 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  79 SEMGSN----ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQ----GCTQIIVAHRLSTIK-DADI 149
Cdd:PRK13636  132 EHLKDKpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMqkelGLTIIIATHDIDIVPlYCDN 211
                         170
                  ....*....|....
gi 1877026690 150 IFVMKGGKIVESGN 163
Cdd:PRK13636  212 VFVMKEGRVILQGN 225
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
81-162 3.17e-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: 56.91  E-value: 3.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSAL-----DTIneERITKYIKSQGCTQIIV---AHRLSTIkdADIIFV 152
Cdd:COG0410   133 RAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLaplivEEI--FEIIRRLNREGVTILLVeqnARFALEI--ADRAYV 208
                          90
                  ....*....|
gi 1877026690 153 MKGGKIVESG 162
Cdd:COG0410   209 LERGRIVLEG 218
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
23-173 3.78e-10

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: 57.84  E-value: 3.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  23 QNLGVVPQDSFLLNRSILDNIT--------LKNEVTSQKIEEVCKAVQIyDEIMAMPMKFNTIISEMgSNISGGQRQRIA 94
Cdd:TIGR00954 515 GKLFYVPQRPYMTLGTLRDQIIypdssedmKRRGLSDKDLEQILDNVQL-THILEREGGWSAVQDWM-DVLSGGEKQRIA 592
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1877026690  95 LARALINNPSIVILDEATSALDTINEERITKYIKSQGCTQIIVAHRLSTIKdadiifvmkggkivesgNHKYLMELGGE 173
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWK-----------------YHEYLLYMDGR 654
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
83-162 4.15e-10

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 56.90  E-value: 4.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDT--INEE-RITKYIKSQGCTQIIVAHRLSTIK--DADIIFVMKgGK 157
Cdd:PRK10619  151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPelVGEVlRIMQQLAEEGKTMVVVTHEMGFARhvSSHVIFLHQ-GK 229

                  ....*
gi 1877026690 158 IVESG 162
Cdd:PRK10619  230 IEEEG 234
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
52-139 4.90e-10

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 57.38  E-value: 4.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  52 QKIEEVCKAVQIYDEIMAMPMkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALD--TIN--EEritkYI 127
Cdd:COG0488   130 ARAEEILSGLGFPEEDLDRPV----------SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDleSIEwlEE----FL 195
                          90
                  ....*....|..
gi 1877026690 128 KSQGCTQIIVAH 139
Cdd:COG0488   196 KNYPGTVLVVSH 207
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
86-162 6.58e-10

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 56.32  E-value: 6.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALI------NNPSIVILDEATSALDTINEE---RITK-YIKSQGCTQIIVAHRLS-TIKDADIIFVMK 154
Cdd:PRK13548  136 SGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHhvlRLARqLAHERGLAVIVVLHDLNlAARYADRIVLLH 215

                  ....*...
gi 1877026690 155 GGKIVESG 162
Cdd:PRK13548  216 QGRLVADG 223
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
83-162 7.44e-10

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: 55.91  E-value: 7.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDTinEER-----ITKYIKSQGCTQIIVAHRLSTIKD-ADIIFVMKGG 156
Cdd:cd03219   142 GELSYGQQRRLEIARALATDPKLLLLDEPAAGLNP--EETeelaeLIRELRERGITVLLVEHDMDVVMSlADRVTVLDQG 219

                  ....*.
gi 1877026690 157 KIVESG 162
Cdd:cd03219   220 RVIAEG 225
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
2-163 8.37e-10

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 56.06  E-value: 8.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQID-KKILSQNLGVVPQDSFLLNR-SILDNIT----LKNEVTSQKIEEvcKAVQIYDEIMAMPMKFN 75
Cdd:PRK10895   56 DAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRRlSVYDNLMavlqIRDDLSAEQRED--RANELMEEFHIEHLRDS 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  76 tiiseMGSNISGGQRQRIALARALINNPSIVILDEATSALD---TINEERITKYIKSQGCTQIIVAHRL-STIKDADIIF 151
Cdd:PRK10895  134 -----MGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpisVIDIKRIIEHLRDSGLGVLITDHNVrETLAVCERAY 208
                         170
                  ....*....|..
gi 1877026690 152 VMKGGKIVESGN 163
Cdd:PRK10895  209 IVSQGHLIAHGT 220
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
86-157 1.07e-09

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: 53.99  E-value: 1.07e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQGCTQIIVAH-R--LSTIkdADIIFVMKGGK 157
Cdd:cd03221    72 SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
85-162 1.13e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 56.01  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI---KSQGCTQIIVAHRLSTIKD-ADIIFVMKGGKIVE 160
Cdd:PRK13631  177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIldaKANNKTVFVITHTMEHVLEvADEVIVMDKGKILK 256

                  ..
gi 1877026690 161 SG 162
Cdd:PRK13631  257 TG 258
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
29-162 1.23e-09

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: 55.42  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  29 PQDSFLLNRSILDnitLKNEVTSQKIEEVCKAVQIyDEIMAMPMKfntiisemgsNISGGQRQRIALARALINNPSIVIL 108
Cdd:cd03267   112 VIDSFYLLAAIYD---LPPARFKKRLDELSELLDL-EELLDTPVR----------QLSLGQRMRAEIAAALLHEPEILFL 177
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1877026690 109 DEATSALDTINEERITK----YIKSQGCTQIIVAHRLSTI-KDADIIFVMKGGKIVESG 162
Cdd:cd03267   178 DEPTIGLDVVAQENIRNflkeYNRERGTTVLLTSHYMKDIeALARRVLVIDKGRLLYDG 236
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
9-163 1.24e-09

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 56.35  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   9 DGININQIDKKILSQNLGVVPQDSFLL--NRSILDNITLK-NEVTSQKIEEVCKAVQIYDEImampmKFNTIISEMGSNI 85
Cdd:TIGR03269  95 DFWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVLEAlEEIGYEGKEAVGRAVDLIEMV-----QLSHRITHIARDL 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALD----TINEERITKYIKSQGCTQIIVAHRLSTIKD-ADIIFVMKGGKIVE 160
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtaKLVHNALEEAVKASGISMVLTSHWPEVIEDlSDKAIWLENGEIKE 249

                  ...
gi 1877026690 161 SGN 163
Cdd:TIGR03269 250 EGT 252
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
85-162 1.71e-09

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 55.61  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEER----ITKYIKSQGCTQIIVAH-RLSTIKDADIIFVMKGGKIV 159
Cdd:PRK11607  150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRmqleVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFV 229

                  ...
gi 1877026690 160 ESG 162
Cdd:PRK11607  230 QIG 232
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
4-139 2.54e-09

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: 54.39  E-value: 2.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQI--DKKILSQNLGVVPQdsfllnRSILDNITLK-NEVTSQKIEEvcKAVQIYDEIMAMpMKFNTIISE 80
Cdd:TIGR01184  40 GGVILEGKQITEPgpDRMVVFQNYSLLPW------LTVRENIALAvDRVLPDLSKS--ERRAIVEEHIAL-VGLTEAADK 110
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTIN----EERITKYIKSQGCTQIIVAH 139
Cdd:TIGR01184 111 RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTrgnlQEELMQIWEEHRVTVLMVTH 173
cbiO PRK13643
energy-coupling factor transporter ATPase;
15-162 2.88e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 54.74  E-value: 2.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  15 QIDKKILSQNLGVVPQ--DSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFntiISEMGSNISGGQRQR 92
Cdd:PRK13643   76 QKEIKPVRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEF---WEKSPFELSGGQMRR 152
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1877026690  93 IALARALINNPSIVILDEATSALDT---INEERITKYIKSQGCTQIIVAHRLSTIKD-ADIIFVMKGGKIVESG 162
Cdd:PRK13643  153 VAIAGILAMEPEVLVLDEPTAGLDPkarIEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
85-160 3.14e-09

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 55.10  E-value: 3.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK----SQGCTQIIVAHRLSTIKD-ADIIFVMKGGKIV 159
Cdd:PRK15134  157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelqqELNMGLLFITHNLSIVRKlADRVAVMQNGRCV 236

                  .
gi 1877026690 160 E 160
Cdd:PRK15134  237 E 237
cbiO PRK13642
energy-coupling factor transporter ATPase;
4-160 3.23e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 54.71  E-value: 3.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVVPQ--DSFLLNRSILDNITLKNEVTSQKIEEVCKAVQiyDEIMAMPM-KFNTiisE 80
Cdd:PRK13642   62 GKVKIDGELLTAENVWNLRRKIGMVFQnpDNQFVGATVEDDVAFGMENQGIPREEMIKRVD--EALLAVNMlDFKT---R 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS----QGCTQIIVAHRLSTIKDADIIFVMKGG 156
Cdd:PRK13642  137 EPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEikekYQLTVLSITHDLDEAASSDRILVMKAG 216

                  ....
gi 1877026690 157 KIVE 160
Cdd:PRK13642  217 EIIK 220
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
2-162 3.32e-09

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 54.35  E-value: 3.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDS-----FLlnrsildnitlknevtsqkIEEV------------CKAVQIY 64
Cdd:COG4559    54 SSGEVRLNGRPLAAWSPWELARRRAVLPQHSslafpFT-------------------VEEVvalgraphgssaAQDRQIV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  65 DEIMAMpmkfnTIISEMGSNI----SGGQRQRIALARALI-------NNPSIVILDEATSALDtINEE----RITKYIKS 129
Cdd:COG4559   115 REALAL-----VGLAHLAGRSyqtlSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD-LAHQhavlRLARQLAR 188
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1877026690 130 QGCTQIIVAHRLS-TIKDADIIFVMKGGKIVESG 162
Cdd:COG4559   189 RGGGVVAVLHDLNlAAQYADRILLLHQGRLVAQG 222
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
2-162 3.90e-09

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 54.85  E-value: 3.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKILSQNLGVVPQDSFLL---------------NRSILDNITlknEVTSQKIEEVCKAVQIyDE 66
Cdd:PRK09536   56 TAGTVLVAGDDVEALSARAASRRVASVPQDTSLSfefdvrqvvemgrtpHRSRFDTWT---ETDRAAVERAMERTGV-AQ 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  67 IMAMPMkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALDtINEERIT----KYIKSQGCTQIIVAHRLS 142
Cdd:PRK09536  132 FADRPV----------TSLSGGERQRVLLARALAQATPVLLLDEPTASLD-INHQVRTlelvRRLVDDGKTAVAAIHDLD 200
                         170       180
                  ....*....|....*....|.
gi 1877026690 143 -TIKDADIIFVMKGGKIVESG 162
Cdd:PRK09536  201 lAARYCDELVLLADGRVRAAG 221
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
86-159 3.94e-09

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 54.32  E-value: 3.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDTINEERIT----KYIKSQGCTQIIVAHRLstiKDA----DIIFVMKGGK 157
Cdd:COG1101   150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLelteKIVEENNLTTLMVTHNM---EQAldygNRLIMMHEGR 226

                  ..
gi 1877026690 158 IV 159
Cdd:COG1101   227 II 228
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
65-165 4.10e-09

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 53.62  E-value: 4.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  65 DEIMAMPMKFNTIISEMgsniSGGQRQRIALAraLI-----NNPS-IVILDEATSALDTINEERITKYIKSQ-GCTQ-II 136
Cdd:cd03278    98 SEIIEAPGKKVQRLSLL----SGGEKALTALA--LLfaifrVRPSpFCVLDEVDAALDDANVERFARLLKEFsKETQfIV 171
                          90       100
                  ....*....|....*....|....*....
gi 1877026690 137 VAHRLSTIKDADIIFvmkGGKIVESGNHK 165
Cdd:cd03278   172 ITHRKGTMEAADRLY---GVTMQESGVSK 197
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
83-162 4.21e-09

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 54.70  E-value: 4.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQ----GCTQIIVAH-RLSTIKDADIIFVMKGGK 157
Cdd:PRK10851  135 AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLheelKFTSVFVTHdQEEAMEVADRVVVMSQGN 214

                  ....*
gi 1877026690 158 IVESG 162
Cdd:PRK10851  215 IEQAG 219
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
68-168 4.83e-09

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 53.82  E-value: 4.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  68 MAMPMKFNTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALD-TINEERITkyIKSQGCTQ-----IIVAHRL 141
Cdd:PRK10771  113 IARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpALRQEMLT--LVSQVCQErqltlLMVSHSL 190
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1877026690 142 StikDADII----FVMKGGKIVESGNHKYLM 168
Cdd:PRK10771  191 E---DAARIaprsLVVADGRIAWDGPTDELL 218
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
86-123 5.85e-09

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 53.71  E-value: 5.85e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDTINEERI 123
Cdd:COG4525   136 SGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQM 173
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
75-162 5.93e-09

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 54.28  E-value: 5.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  75 NTIISEMGS--NISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLST--IKDA 147
Cdd:TIGR00955 155 NTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGlaqKGKTIICTIHQPSSelFELF 234
                          90
                  ....*....|....*
gi 1877026690 148 DIIFVMKGGKIVESG 162
Cdd:TIGR00955 235 DKIILMAEGRVAYLG 249
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
42-162 7.35e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 53.65  E-value: 7.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  42 NITLKNEVTSQKIEEVCKAVQIYDEIMAMPmkfntiisemgSNISGGQRQRIALARALINNPSIVILDEATSALDTINEE 121
Cdd:PRK13652  106 NLGLDEETVAHRVSSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVK 174
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1877026690 122 RITKYI----KSQGCTQIIVAHRLSTIKD-ADIIFVMKGGKIVESG 162
Cdd:PRK13652  175 ELIDFLndlpETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYG 220
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
86-156 7.48e-09

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: 53.21  E-value: 7.48e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI---KSQGCTQIIVAHRLSTIKD-ADIIFVMKGG 156
Cdd:COG4778   154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIeeaKARGTAIIGIFHDEEVREAvADRVVDVTPF 228
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
85-117 8.51e-09

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 52.87  E-value: 8.51e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDT 117
Cdd:COG4136   134 LSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
85-149 1.82e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 52.71  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQrQRIAL-ARALINNPSIVILDEATSALDTINEERITKYIK---SQGCTQII------------VAHRLSTIKDAD 148
Cdd:PRK10938  402 LSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDvliSEGETQLLfvshhaedapacITHRLEFVPDGD 480

                  .
gi 1877026690 149 I 149
Cdd:PRK10938  481 I 481
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
85-162 2.23e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 52.33  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI----KSQGCTQIIVAHRLSTIKD-ADIIFVMKGGKIV 159
Cdd:PRK13634  146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFyklhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVF 225

                  ...
gi 1877026690 160 ESG 162
Cdd:PRK13634  226 LQG 228
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
38-169 2.32e-08

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 52.15  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  38 SILDNIT----LKNEVTSQK-----IEEVCKAVQIYDEImampmkfNTIISEMGSNISGGQRQRIALARALINNPSIVIL 108
Cdd:PRK14267  101 TIYDNVAigvkLNGLVKSKKelderVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1877026690 109 DEATSALDTINEERITKYI--KSQGCTQIIVAHR-LSTIKDADIIFVMKGGKIVESGNHKYLME 169
Cdd:PRK14267  174 DEPTANIDPVGTAKIEELLfeLKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
4-167 2.38e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 52.05  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVVPQD--SFLLNRSILD-------NITLKNEVTSQKIEEVCKAVQIYDEIMAMPMkf 74
Cdd:PRK13647   60 GRVKVMGREVNAENEKWVRSKVGLVFQDpdDQVFSSTVWDdvafgpvNMGLDKDEVERRVEEALKAVRMWDFRDKPPY-- 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  75 ntiisemgsNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI---KSQGCTQIIVAHRLSTIKD-ADII 150
Cdd:PRK13647  138 ---------HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILdrlHNQGKTVIVATHDVDLAAEwADQV 208
                         170
                  ....*....|....*..
gi 1877026690 151 FVMKGGKIVESGNHKYL 167
Cdd:PRK13647  209 IVLKEGRVLAEGDKSLL 225
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
85-162 2.39e-08

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 52.19  E-value: 2.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERIT---KYIKSQGCTQIIVAHRLSTIKDADIIFVMKGGKIVES 161
Cdd:PRK15056  143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIIsllRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLAS 222

                  .
gi 1877026690 162 G 162
Cdd:PRK15056  223 G 223
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
84-163 2.66e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 52.01  E-value: 2.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  84 NISGGQRQRIALARALINNPSIVILDEATSALD---TINEERITKYIKSQGCTQIIVAHRL-STIKDADIIFVMKGGKIV 159
Cdd:PRK13651  165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGKII 244

                  ....
gi 1877026690 160 ESGN 163
Cdd:PRK13651  245 KDGD 248
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
3-139 3.16e-08

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 51.32  E-value: 3.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGININQIDK----KILSQNLGVVPQdSFLLNRSI--LDNITL----KNEVTSQKIEEvckAVQIYDEimampM 72
Cdd:PRK10584   64 SGEVSLVGQPLHQMDEearaKLRAKHVGFVFQ-SFMLIPTLnaLENVELpallRGESSRQSRNG---AKALLEQ-----L 134
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1877026690  73 KFNTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS----QGCTQIIVAH 139
Cdd:PRK10584  135 GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSlnreHGTTLILVTH 205
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
86-162 4.37e-08

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 51.22  E-value: 4.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALD---------TINEERitkyikSQGCTQIIVAH--RLSTIKDADIIFVMK 154
Cdd:COG0396   142 SGGEKKRNEILQMLLLEPKLAILDETDSGLDidalrivaeGVNKLR------SPDRGILIITHyqRILDYIKPDFVHVLV 215

                  ....*...
gi 1877026690 155 GGKIVESG 162
Cdd:COG0396   216 DGRIVKSG 223
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
85-162 4.41e-08

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 51.67  E-value: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALD-TINEERITKYIKSQGCTQ---IIVAHRLSTIKD-ADIIFVMKGGKIV 159
Cdd:PRK11022  154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLLELQQKENmalVLITHDLALVAEaAHKIIVMYAGQVV 233

                  ...
gi 1877026690 160 ESG 162
Cdd:PRK11022  234 ETG 236
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
83-162 4.91e-08

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: 50.40  E-value: 4.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNP--SIVILDEATSALDTINEERITKYIK---SQGCTQIIVAHRLSTIKDAD-IIFVMK-- 154
Cdd:cd03238    86 STLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKgliDLGNTVILIEHNLDVLSSADwIIDFGPgs 165
                          90
                  ....*....|.
gi 1877026690 155 ---GGKIVESG 162
Cdd:cd03238   166 gksGGKVVFSG 176
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
2-159 5.88e-08

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 51.27  E-value: 5.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININ-QIDKKILSQNLGVVPQD-SFLLNRSILDNITLKNE------VTSQKIEEVCKAvqIYDEimampMK 73
Cdd:PRK10982   51 DSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRSVMDNMWLGRYptkgmfVDQDKMYRDTKA--IFDE-----LD 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  74 FNTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEE---RITKYIKSQGCTQIIVAHRLSTI-KDADI 149
Cdd:PRK10982  124 IDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNhlfTIIRKLKERGCGIVYISHKMEEIfQLCDE 203
                         170
                  ....*....|
gi 1877026690 150 IFVMKGGKIV 159
Cdd:PRK10982  204 ITILRDGQWI 213
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
85-162 6.08e-08

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: 51.55  E-value: 6.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARAL---INNPSIVILDEATSALDTineERITKYI------KSQGCTQIIVAHRLSTIKDADIIFVM-- 153
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHF---DDIKKLLevlqrlVDKGNTVVVIEHNLDVIKTADYIIDLgp 906
                          90
                  ....*....|...
gi 1877026690 154 ----KGGKIVESG 162
Cdd:TIGR00630 907 eggdGGGTVVASG 919
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
3-182 6.35e-08

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: 51.55  E-value: 6.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690    3 TGKVLFDGINInQIDKKILSQNLGVVPQDSFLLNR-SILDNITLKNEVTSQKIEEVckavQIYDEIMAMPMKFNTIISEM 81
Cdd:TIGR01257  984 SGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFYAQLKGRSWEEA----QLEMEAMLEDTGLHHKRNEE 1058
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   82 GSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERI----TKYikSQGCTQIIVAHRLStikDADI----IFVM 153
Cdd:TIGR01257 1059 AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIwdllLKY--RSGRTIIMSTHHMD---EADLlgdrIAII 1133
                          170       180
                   ....*....|....*....|....*....
gi 1877026690  154 KGGKIVESGNHKYLMELGGEYYSLYTKRK 182
Cdd:TIGR01257 1134 SQGRLYCSGTPLFLKNCFGTGFYLTLVRK 1162
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
80-162 6.45e-08

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: 50.81  E-value: 6.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  80 EMGSNISGGQRQRIALARALINNPSIVILDEATSALDTiNE-ERITKYIKS----QGCTQIIVAHRLSTIKD-ADIIFVM 153
Cdd:COG0411   148 EPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNP-EEtEELAELIRRlrdeRGITILLIEHDMDLVMGlADRIVVL 226

                  ....*....
gi 1877026690 154 KGGKIVESG 162
Cdd:COG0411   227 DFGRVIAEG 235
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
23-139 7.29e-08

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 50.96  E-value: 7.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  23 QNLGVVPQ-DSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFNTIISEMgsniSGGQRQRIALARALIN 101
Cdd:PRK13537   80 QRVGVVPQfDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGEL----SGGMKRRLTLARALVN 155
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1877026690 102 NPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAH 139
Cdd:PRK13537  156 DPDVLVLDEPTTGLDPQARHLMWERLRSllaRGKTILLTTH 196
cbiO PRK13641
energy-coupling factor transporter ATPase;
85-160 8.80e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 50.60  E-value: 8.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLSTIKD-ADIIFVMKGGKIVE 160
Cdd:PRK13641  146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDyqkAGHTVILVTHNMDDVAEyADDVLVLEHGKLIK 225
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
4-162 1.02e-07

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 50.55  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQN-LGVVPQDSFLLNR-SILDNITLKNEVTsqkiEEVC-------KAVQIYDEIMAMPMKF 74
Cdd:PRK09700   60 GTITINNINYNKLDHKLAAQLgIGIIYQELSVIDElTVLENLYIGRHLT----KKVCgvniidwREMRVRAAMMLLRVGL 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  75 NTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALdtINEE-----RITKYIKSQGCTQIIVAHRLSTIKD-AD 148
Cdd:PRK09700  136 KVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL--TNKEvdylfLIMNQLRKEGTAIVYISHKLAEIRRiCD 213
                         170
                  ....*....|....
gi 1877026690 149 IIFVMKGGKIVESG 162
Cdd:PRK09700  214 RYTVMKDGSSVCSG 227
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
26-123 1.07e-07

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 50.08  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  26 GVVPQDSFLLN-RSILDNITLKNEVTSqkieeVCKAVQiydEIMAMPMKFNTIISEMGS----NISGGQRQRIALARALI 100
Cdd:PRK11248   73 GVVFQNEGLLPwRNVQDNVAFGLQLAG-----VEKMQR---LEIAHQMLKKVGLEGAEKryiwQLSGGQRQRVGIARALA 144
                          90       100
                  ....*....|....*....|...
gi 1877026690 101 NNPSIVILDEATSALDTINEERI 123
Cdd:PRK11248  145 ANPQLLLLDEPFGALDAFTREQM 167
PLN03211 PLN03211
ABC transporter G-25; Provisional
3-143 1.22e-07

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 50.65  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLfdgININQIDKKILsQNLGVVPQDSFLLnrsilDNITLKNEVTSQKIEEVCKAVQIYDEIMAMpmkfNTIISEMG 82
Cdd:PLN03211  124 TGTIL---ANNRKPTKQIL-KRTGFVTQDDILY-----PHLTVRETLVFCSLLRLPKSLTKQEKILVA----ESVISELG 190
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1877026690  83 --------------SNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLST 143
Cdd:PLN03211  191 ltkcentiignsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSlaqKGKTIVTSMHQPSS 268
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
70-163 1.53e-07

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 49.87  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  70 MPMKFNTIISEMG---------SNISGGQRQRIALARALINNPSIVILDEATSALDTINE-------ERITKYIKsqgcT 133
Cdd:PRK11144  105 MVAQFDKIVALLGieplldrypGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKrellpylERLAREIN----I 180
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1877026690 134 QII-VAHRLSTI-KDADIIFVMKGGKIVESGN 163
Cdd:PRK11144  181 PILyVSHSLDEIlRLADRVVVLEQGKVKAFGP 212
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
4-165 1.54e-07

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 49.60  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQNLGVVPQdsfllNRSILDNITLKNEVTSQKIEE---VCKAVQIYDEIMAMPMKFNTIISE 80
Cdd:PRK10253   62 GHVWLDGEHIQHYASKEVARRIGLLAQ-----NATTPGDITVQELVARGRYPHqplFTRWRKEDEEAVTKAMQATGITHL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNI---SGGQRQRIALARALINNPSIVILDEATSALDTINE----ERITKYIKSQGCTQIIVAHRLS-TIKDADIIFV 152
Cdd:PRK10253  137 ADQSVdtlSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQidllELLSELNREKGYTLAAVLHDLNqACRYASHLIA 216
                         170
                  ....*....|...
gi 1877026690 153 MKGGKIVESGNHK 165
Cdd:PRK10253  217 LREGKIVAQGAPK 229
cbiO PRK13645
energy-coupling factor transporter ATPase;
12-163 1.60e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 50.01  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  12 NINQIDK-KILSQNLGVVPQ--DSFLLNRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAMPMKFntiISEMGSNISGG 88
Cdd:PRK13645   78 NLKKIKEvKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGG 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  89 QRQRIALARALINNPSIVILDEATSALDTINEERITKYI----KSQGCTQIIVAHRLSTI-KDADIIFVMKGGKIVESGN 163
Cdd:PRK13645  155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFerlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGS 234
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
86-163 1.61e-07

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 49.72  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALD-TINEERIT--KYIKSQGCTQII-VAHRLSTIKD-ADIIFVMKGGKIVE 160
Cdd:PRK09473  163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDvTVQAQIMTllNELKREFNTAIImITHDLGVVAGiCDKVLVMYAGRTME 242

                  ...
gi 1877026690 161 SGN 163
Cdd:PRK09473  243 YGN 245
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
4-178 1.70e-07

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: 50.21  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGI-----NINQIDKK---ILSQNLGVVPqdsfllNRSILDNITLKNEVT-----------SQKIEEVCKAVQIY 64
Cdd:TIGR02633  58 GEIYWSGSplkasNIRDTERAgivIIHQELTLVP------ELSVAENIFLGNEITlpggrmaynamYLRAKNLLRELQLD 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  65 DEIMAMPmkfntiISEMGsnisGGQRQRIALARALINNPSIVILDEATSALDTINEE---RITKYIKSQGCTQIIVAHRL 141
Cdd:TIGR02633 132 ADNVTRP------VGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEillDIIRDLKAHGVACVYISHKL 201
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1877026690 142 STIKD-ADIIFVMKGGKIVESGNHKYL-------MELGGEYYSLY 178
Cdd:TIGR02633 202 NEVKAvCDTICVIRDGQHVATKDMSTMseddiitMMVGREITSLY 246
GguA NF040905
sugar ABC transporter ATP-binding protein;
3-161 2.26e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.79  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDGI-----NINQIDKK---ILSQNLGVVPQdsfllnRSILDNITLKNEV----------TSQKIEEVCKAVQIY 64
Cdd:NF040905   57 EGEILFDGEvcrfkDIRDSEALgivIIHQELALIPY------LSIAENIFLGNERakrgvidwneTNRRARELLAKVGLD 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  65 DEimamPmkfNTIISEMGSnisgGQRQRIALARALINNPSIVILDEATSALdtiNEE------RITKYIKSQGCTQIIVA 138
Cdd:NF040905  131 ES----P---DTLVTDIGV----GKQQLVEIAKALSKDVKLLILDEPTAAL---NEEdsaallDLLLELKAQGITSIIIS 196
                         170       180
                  ....*....|....*....|....
gi 1877026690 139 HRLSTI-KDADIIFVMKGGKIVES 161
Cdd:NF040905  197 HKLNEIrRVADSITVLRDGRTIET 220
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
67-158 2.35e-07

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: 48.58  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  67 IMAMPMKFNTIISEMgsnISGGQRQRIALARALINNPSIVILDEATSALD--TINE--ERITKyIKSQGCTQIIVAHRLS 142
Cdd:cd03215    90 VLDLSVAENIALSSL---LSGGNQQKVVLARWLARDPRVLILDEPTRGVDvgAKAEiyRLIRE-LADAGKAVLLISSELD 165
                          90
                  ....*....|....*..
gi 1877026690 143 TIKD-ADIIFVMKGGKI 158
Cdd:cd03215   166 ELLGlCDRILVMYEGRI 182
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
85-154 2.40e-07

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 48.12  E-value: 2.40e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1877026690  85 ISGGQRQRIALARAL----INNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLSTIKDADIIFVMK 154
Cdd:cd03227    78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEhlvKGAQVIVITHLPELAELADKLIHIK 154
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
4-159 3.62e-07

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 48.34  E-value: 3.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQID-KKILSQNLGVVPQDSFLLNR-SILDNITL-----KNEVTSQKIEEVckavqiYDeimAMPMKFNT 76
Cdd:PRK11614   60 GRIVFDGKDITDWQtAKIMREAVAIVPEGRRVFSRmTVEENLAMggffaERDQFQERIKWV------YE---LFPRLHER 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  77 IISEMGSnISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI---KSQGCTQIIVAHRLS-TIKDADIIFV 152
Cdd:PRK11614  131 RIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIeqlREQGMTIFLVEQNANqALKLADRGYV 209

                  ....*..
gi 1877026690 153 MKGGKIV 159
Cdd:PRK11614  210 LENGHVV 216
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
85-162 3.94e-07

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 48.54  E-value: 3.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERI----TKYIKSQGCTQIIVAHRLSTI-KDADIIFVMKGGKIV 159
Cdd:PRK10418  141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARIldllESIVQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIV 220

                  ...
gi 1877026690 160 ESG 162
Cdd:PRK10418  221 EQG 223
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
3-158 4.72e-07

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 48.77  E-value: 4.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDG--ININQIDKKIlSQNLGVVPQD----SFLLNRSILDNITL---KNEVTSQKIEEVCKAVQIYDEIMAMPMK 73
Cdd:PRK13549  317 EGEIFIDGkpVKIRNPQQAI-AQGIAMVPEDrkrdGIVPVMGVGKNITLaalDRFTGGSRIDDAAELKTILESIQRLKVK 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  74 FNTIISEMGsNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK---SQGCTQIIVAHRLSTIKD-ADI 149
Cdd:PRK13549  396 TASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINqlvQQGVAIIVISSELPEVLGlSDR 474

                  ....*....
gi 1877026690 150 IFVMKGGKI 158
Cdd:PRK13549  475 VLVMHEGKL 483
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
85-162 5.14e-07

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 48.46  E-value: 5.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEER---ITKYIKSQGCTQIIVAHRLSTIKD-ADIIFVMKGGKIVE 160
Cdd:PRK13638  137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQmiaIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILT 216

                  ..
gi 1877026690 161 SG 162
Cdd:PRK13638  217 HG 218
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
84-139 6.21e-07

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 47.56  E-value: 6.21e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1877026690  84 NISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAH 139
Cdd:PRK13539  127 YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAhlaQGGIVIAATH 185
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
2-169 7.74e-07

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 47.84  E-value: 7.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQIDKKIL---SQNLGVVPQDSFLL-NRSILDNITLKNEVTSQKIEEVCKAVqiydeIMampMKFNTI 77
Cdd:PRK11831   60 DHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFtDMNVFDNVAYPLREHTQLPAPLLHST-----VM---MKLEAV 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  78 -----ISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI----KSQGCTQIIVAHRLSTIKD-A 147
Cdd:PRK11831  132 glrgaAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLIselnSALGVTCVVVSHDVPEVLSiA 211
                         170       180
                  ....*....|....*....|..
gi 1877026690 148 DIIFVMKGGKIVESGNHKYLME 169
Cdd:PRK11831  212 DHAYIVADKKIVAHGSAQALQA 233
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
54-168 8.19e-07

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 47.62  E-value: 8.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  54 IEEVCKAVQIYDeimampmKFNTIISemgsNISGGQRQRIALARALI-----NNPS--IVILDEATSALDTINE---ERI 123
Cdd:PRK03695  107 LNEVAEALGLDD-------KLGRSVN----QLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLDVAQQaalDRL 175
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1877026690 124 TKYIKSQGCTQIIVAHRLS-TIKDADIIFVMKGGKIVESGNHKYLM 168
Cdd:PRK03695  176 LSELCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
43-152 1.01e-06

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 47.40  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  43 ITLKNEVT-----SQKIEEVCKAVQIYDEIMAmPMKFNTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDT 117
Cdd:cd03237    70 IKADYEGTvrdllSSITKDFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1877026690 118 inEER------ITKYIKSQGCTQIIVAHrlstikdaDIIFV 152
Cdd:cd03237   149 --EQRlmaskvIRRFAENNEKTAFVVEH--------DIIMI 179
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
2-163 1.39e-06

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 47.00  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDGININQiDKKILSQNLGVV------------PQDSFLLNRSILDnitLKNEVTSQKIEEVCKAVQIyDEIMA 69
Cdd:COG4586    75 TSGEVRVLGYVPFK-RRKEFARRIGVVfgqrsqlwwdlpAIDSFRLLKAIYR---IPDAEYKKRLDELVELLDL-GELLD 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  70 MPMKfntiisemgsNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIK----SQGCTQIIVAHRLSTIK 145
Cdd:COG4586   150 TPVR----------QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKeynrERGTTILLTSHDMDDIE 219
                         170
                  ....*....|....*....
gi 1877026690 146 D-ADIIFVMKGGKIVESGN 163
Cdd:COG4586   220 AlCDRVIVIDHGRIIYDGS 238
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
25-141 1.45e-06

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 47.03  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  25 LGVVPQDSFL---LNRSILDNITLKNEVTSQKIEEVCKAVQIyDEIMAMPMKfntiisemgsNISGGQRQRIALARALIN 101
Cdd:PRK09544   69 IGYVPQKLYLdttLPLTVNRFLRLRPGTKKEDILPALKRVQA-GHLIDAPMQ----------KLSGGETQRVLLARALLN 137
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1877026690 102 NPSIVILDEATSALDT---------INEERitkyiKSQGCTQIIVAHRL 141
Cdd:PRK09544  138 RPQLLVLDEPTQGVDVngqvalydlIDQLR-----RELDCAVLMVSHDL 181
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
74-137 1.48e-06

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


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 46.45  E-value: 1.48e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1877026690  74 FNTIISEMGSNISGGQRQ------RIALARALINNPSIVILDEATSALDTINEE----RITKYIKSQGCTQIIV 137
Cdd:cd03240   105 SNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeslaEIIEERKSQKNFQLIV 178
PLN03073 PLN03073
ABC transporter F family; Provisional
36-139 1.49e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 47.55  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  36 NRSILDNITLKNEVTSQKIEEVCKAVQIYDEIMAmPMKFNTII------SEM----GSNISGGQRQRIALARALINNPSI 105
Cdd:PLN03073  287 KGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTA-EARAASILaglsftPEMqvkaTKTFSGGWRMRIALARALFIEPDL 365
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1877026690 106 VILDEATSALDTIN----EERITKYIKsqgcTQIIVAH 139
Cdd:PLN03073  366 LLLDEPTNHLDLHAvlwlETYLLKWPK----TFIVVSH 399
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
86-158 1.64e-06

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 47.15  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDTinEER------ITKYIKSQGCTQIIVAH-RLSTIKDADIIFVMKGGKI 158
Cdd:PRK11650  136 SGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA--KLRvqmrleIQRLHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
2-159 1.69e-06

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 46.94  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   2 DTGKVLFDG--ININQIDKKIlSQNLGVVPQD----SFLLNRSILDNITL-------KNEVTSQK-----IEEVCKAVQI 63
Cdd:COG1129   305 DSGEIRLDGkpVRIRSPRDAI-RAGIAYVPEDrkgeGLVLDLSIRENITLasldrlsRGGLLDRRreralAEEYIKRLRI 383
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  64 ydeimampmKFNTIISEMGsNISGGQRQRIALARALINNPSIVILDEATSALD---------TINEeritkyIKSQGCTq 134
Cdd:COG1129   384 ---------KTPSPEQPVG-NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgakaeiyrLIRE------LAAEGKA- 446
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1877026690 135 IIV-----------AHRlstikdadiIFVMKGGKIV 159
Cdd:COG1129   447 VIVisselpellglSDR---------ILVMREGRIV 473
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
83-139 2.19e-06

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: 46.85  E-value: 2.19e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQGCTQIIVAH 139
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTH 216
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
84-158 2.42e-06

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 46.54  E-value: 2.42e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1877026690  84 NISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI---KSQGCTQIIVAHRLSTIKD-ADIIFVMKGGKI 158
Cdd:PRK10762  395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLInqfKAEGLSIILVSSEMPEVLGmSDRILVMHEGRI 473
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
56-116 2.43e-06

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 46.65  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  56 EVCKAVQIYDEI---MAMPM-KFNTIISEMG----------------------------------SNISGGQRQRIALAR 97
Cdd:PRK11819   97 EVKAALDRFNEIyaaYAEPDaDFDALAAEQGelqeiidaadawdldsqleiamdalrcppwdakvTKLSGGERRRVALCR 176
                          90
                  ....*....|....*....
gi 1877026690  98 ALINNPSIVILDEATSALD 116
Cdd:PRK11819  177 LLLEKPDMLLLDEPTNHLD 195
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
85-162 2.57e-06

ATP-binding cassette domain I 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: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 46.10  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPS--IVILDEATSALDTINEERIT---KYIKSQGCTQIIVAHRLSTIKDADIIFVM------ 153
Cdd:cd03270   138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIetlKRLRDLGNTVLVVEHDEDTIRAADHVIDIgpgagv 217

                  ....*....
gi 1877026690 154 KGGKIVESG 162
Cdd:cd03270   218 HGGEIVAQG 226
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
86-163 3.91e-06

ATP-binding cassette domain II 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: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 45.68  E-value: 3.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALIN---NPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLSTIKDADIIFVM------ 153
Cdd:cd03271   171 SGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlvdKGNTVVVIEHNLDVIKCADWIIDLgpeggd 250
                          90
                  ....*....|
gi 1877026690 154 KGGKIVESGN 163
Cdd:cd03271   251 GGGQVVASGT 260
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
85-139 4.64e-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: 45.18  E-value: 4.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAH 139
Cdd:cd03231   126 LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGhcaRGGMVVLTTH 183
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
1-162 5.05e-06

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 45.07  E-value: 5.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   1 MDTGKVLFDGININQIDKKILSQNLGVVPQDSFLLNRsildnITLKNEV------------TSQKIEEVCKAVQiYDEIM 68
Cdd:COG4604    53 PDSGEVLVDGLDVATTPSRELAKRLAILRQENHINSR-----LTVRELVafgrfpyskgrlTAEDREIIDEAIA-YLDLE 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  69 AMPMKFntiISEMgsniSGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS----QGCTQIIVAHrlsti 144
Cdd:COG4604   127 DLADRY---LDEL----SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRladeLGKTVVIVLH----- 194
                         170       180
                  ....*....|....*....|....*
gi 1877026690 145 kD-------ADIIFVMKGGKIVESG 162
Cdd:COG4604   195 -DinfascyADHIVAMKDGRVVAQG 218
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
83-167 5.51e-06

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 45.71  E-value: 5.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALD--TIneERITKYIKSQGCTQIIVAHRLSTIKD-ADIIFVMKGGKIV 159
Cdd:PRK11147  155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDieTI--EWLEGFLKTFQGSIIFISHDRSFIRNmATRIVDLDRGKLV 232
                          90
                  ....*....|
gi 1877026690 160 E-SGNH-KYL 167
Cdd:PRK11147  233 SyPGNYdQYL 242
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
83-155 5.66e-06

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: 45.05  E-value: 5.66e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDT---INEERITKYIKSQGCTQIIVAHRLStIKD--ADIIFVMKG 155
Cdd:cd03236   138 DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrLNAARLIRELAEDDNYVLVVEHDLA-VLDylSDYIHCLYG 214
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
84-169 5.89e-06

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 45.16  E-value: 5.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  84 NISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI----KSQGCTQIIVAHRLS-TIKDADIIFVMKGGKI 158
Cdd:PRK10575  147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVhrlsQERGLTVIAVLHDINmAARYCDYLVALRGGEM 226
                          90
                  ....*....|.
gi 1877026690 159 VESGNHKYLME 169
Cdd:PRK10575  227 IAQGTPAELMR 237
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
83-170 5.95e-06

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 45.59  E-value: 5.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   83 SNISGGQRQRIALARALIN---NPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLSTIKDADIIFVM--- 153
Cdd:PRK00635   808 SSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSlthQGHTVVIIEHNMHVVKVADYVLELgpe 887
                           90       100
                   ....*....|....*....|
gi 1877026690  154 ---KGGKIVESGNHKYLMEL 170
Cdd:PRK00635   888 ggnLGGYLLASCSPEELIHL 907
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
86-117 5.95e-06

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 44.79  E-value: 5.95e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDT 117
Cdd:PRK13538  131 SAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
4-158 6.12e-06

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: 45.59  E-value: 6.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDG--ININQIDKKIlSQNLGVVPQD----SFLLNRSILDNITL---KNEVTSQKIEEVCKAVQIYDEIMAMPMKF 74
Cdd:TIGR02633 316 GNVFINGkpVDIRNPAQAI-RAGIAMVPEDrkrhGIVPILGVGKNITLsvlKSFCFKMRIDAAAELQIIGSAIQRLKVKT 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  75 NTIISEMGSnISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI---KSQGCTQIIVAHRLSTIKD-ADII 150
Cdd:TIGR02633 395 ASPFLPIGR-LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLInqlAQEGVAIIVVSSELAEVLGlSDRV 473

                  ....*...
gi 1877026690 151 FVMKGGKI 158
Cdd:TIGR02633 474 LVIGEGKL 481
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
69-158 7.13e-06

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 45.43  E-value: 7.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  69 AMPMKFNTIISEMGSnISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLSTI- 144
Cdd:PRK15439  389 ALNIKFNHAEQAART-LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSiaaQNVAVLFISSDLEEIe 467
                          90
                  ....*....|....
gi 1877026690 145 KDADIIFVMKGGKI 158
Cdd:PRK15439  468 QMADRVLVMHQGEI 481
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
75-159 8.55e-06

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: 43.52  E-value: 8.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   75 NTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI--------KSQGCTQIIVAHRLSTIKD 146
Cdd:smart00382  51 LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrlllllKSEKNLTVILTTNDEKDLG 130
                           90
                   ....*....|...
gi 1877026690  147 ADIIFVMKGGKIV 159
Cdd:smart00382 131 PALLRRRFDRRIV 143
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
86-160 8.68e-06

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 45.06  E-value: 8.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALD--TIN--EERITKYiksQGCTqIIVAH-R--LSTIkdADIIFVMKGGKI 158
Cdd:COG0488   434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLDieTLEalEEALDDF---PGTV-LLVSHdRyfLDRV--ATRILEFEDGGV 507

                  ..
gi 1877026690 159 VE 160
Cdd:COG0488   508 RE 509
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
86-161 1.10e-05

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 44.52  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSAL---DTINEERITKYIKSQGCTQIIVAHRLSTIKD-ADIIFVMKGGKIVES 161
Cdd:PRK11288  142 SIGQRQMVEIAKALARNARVIAFDEPTSSLsarEIEQLFRVIRELRAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVAT 221
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
83-162 1.11e-05

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 44.23  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDT----INEERITKYIKSQGCTQIIVAHRLS-TIKDADIIFVMKGGK 157
Cdd:PRK09984  151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPesarIVMDTLRDINQNDGITVVVTLHQVDyALRYCERIVALRQGH 230

                  ....*
gi 1877026690 158 IVESG 162
Cdd:PRK09984  231 VFYDG 235
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
83-139 1.82e-05

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 44.11  E-value: 1.82e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALD--TIN--EERITKYiksqGCTQIIVAH 139
Cdd:PRK15064  154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDinTIRwlEDVLNER----NSTMIIISH 210
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
88-168 1.83e-05

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 44.02  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  88 GQRQRIALARALINNPSIVILDEATSALDTINEERI----TKYIKSQGCTQIIVAHRLSTI-KDADIIFVMKGGKIVESG 162
Cdd:PRK15093  162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIfrllTRLNQNNNTTILLISHDLQMLsQWADKINVLYCGQTVETA 241

                  ....*.
gi 1877026690 163 NHKYLM 168
Cdd:PRK15093  242 PSKELV 247
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
85-139 2.43e-05

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 43.79  E-value: 2.43e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALD--TIN--EERITKYiksQGcTQIIVAH 139
Cdd:PRK11147  441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDveTLEllEELLDSY---QG-TVLLVSH 495
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
88-116 2.94e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 43.57  E-value: 2.94e-05
                          10        20
                  ....*....|....*....|....*....
gi 1877026690  88 GQRQRIALARALINNPSIVILDEATSALD 116
Cdd:NF033858  401 GIRQRLSLAVAVIHKPELLILDEPTSGVD 429
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
20-161 3.11e-05

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 43.45  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  20 ILSQNLGVVPQdsfllnRSILDNITLKNEVTSQ--KIeevcKAVQIYDEIMAMPMKFNTIIS--EMGSNISGGQRQRIAL 95
Cdd:PRK10762   83 IIHQELNLIPQ------LTIAENIFLGREFVNRfgRI----DWKKMYAEADKLLARLNLRFSsdKLVGELSIGEQQMVEI 152
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1877026690  96 ARALINNPSIVILDEATSAL-DTINEE--RITKYIKSQGCTQIIVAHRLSTIKD-ADIIFVMKGGK-IVES 161
Cdd:PRK10762  153 AKVLSFESKVIIMDEPTDALtDTETESlfRVIRELKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQfIAER 223
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
27-160 3.26e-05

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 42.64  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  27 VVPQDSFLLNRSILDNITLKNEVTsQKIEeVCKAVQIYDEImAMPMKFntiisemgSNISGGQRQRIALARALINNPSIV 106
Cdd:COG2401    90 DVPDNQFGREASLIDAIGRKGDFK-DAVE-LLNAVGLSDAV-LWLRRF--------KELSTGQKFRFRLALLLAERPKLL 158
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1877026690 107 ILDEATSALDTINEERIT----KYIKSQGCTQIIVAHRLSTIKDAD---IIFVMKGGKIVE 160
Cdd:COG2401   159 VIDEFCSHLDRQTAKRVArnlqKLARRAGITLVVATHHYDVIDDLQpdlLIFVGYGGVPEE 219
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
80-162 3.32e-05

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: 42.63  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  80 EMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQ----GCTQIIVAHRLS--TIKDADIIFVM 153
Cdd:cd03233   114 EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMadvlKTTTFVSLYQASdeIYDLFDKVLVL 193

                  ....*....
gi 1877026690 154 KGGKIVESG 162
Cdd:cd03233   194 YEGRQIYYG 202
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
85-176 3.41e-05

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: 43.46  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIV--ILDEATSALDTINEERITKYIK---SQGCTQIIVAHRLSTIKDADIIFVM------ 153
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTGVlyVLDEPSIGLHQRDNRRLINTLKrlrDLGNTLIVVEHDEDTIRAADYVIDIgpgage 568
                          90       100
                  ....*....|....*....|....*..
gi 1877026690 154 KGGKIVESGNHKYLME----LGGEYYS 176
Cdd:TIGR00630 569 HGGEVVASGTPEEILAnpdsLTGQYLS 595
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
81-163 4.74e-05

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 42.32  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 MGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERItkyiksqgctQIIVAHrlstIKDADI---I------- 150
Cdd:COG1137   133 KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADI----------QKIIRH----LKERGIgvlItdhnvre 198
                          90       100
                  ....*....|....*....|.
gi 1877026690 151 --------FVMKGGKIVESGN 163
Cdd:COG1137   199 tlgicdraYIISEGKVLAEGT 219
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
84-155 6.35e-05

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 41.40  E-value: 6.35e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1877026690  84 NISGGQRQRIALARALINNPSIVILDEATSALDT---INEERITKYIKSQGC-TQIIVAHRLSTIKD-ADIIFVMKG 155
Cdd:cd03222    71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrLNAARAIRRLSEEGKkTALVVEHDLAVLDYlSDRIHVFEG 147
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
63-155 6.41e-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: 42.46  E-value: 6.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  63 IYDEImAMPMKFNTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTinEER------ITKYIKSQGCTQII 136
Cdd:COG1245   435 YKTEI-IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQRlavakaIRRFAENRGKTAMV 511
                          90       100
                  ....*....|....*....|.
gi 1877026690 137 VAHRLSTIkD--ADIIFVMKG 155
Cdd:COG1245   512 VDHDIYLI-DyiSDRLMVFEG 531
PLN03140 PLN03140
ABC transporter G family member; Provisional
85-162 8.41e-05

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 42.14  E-value: 8.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLST-IKDA-DIIFVMK-GGKI 158
Cdd:PLN03140  1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNtvdTGRTVVCTIHQPSIdIFEAfDELLLMKrGGQV 1099

                   ....
gi 1877026690  159 VESG 162
Cdd:PLN03140  1100 IYSG 1103
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
85-116 9.62e-05

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: 41.19  E-value: 9.62e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALD 116
Cdd:TIGR01189 128 LSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
66-151 9.67e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 9.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   66 EIMAMPM-KFNTIISEMgsniSGGQRQRIALAraLI-----NNPS-IVILDEATSALDTINEERITKYIKS-QGCTQ-II 136
Cdd:TIGR02168 1074 EIFAQPPgKKNQNLSLL----SGGEKALTALA--LLfaifkVKPApFCILDEVDAPLDDANVERFANLLKEfSKNTQfIV 1147
                           90
                   ....*....|....*
gi 1877026690  137 VAHRLSTIKDADIIF 151
Cdd:TIGR02168 1148 ITHNKGTMEVADQLY 1162
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
83-155 9.69e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 42.10  E-value: 9.69e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDTinEERIT--KYIK--SQGCTQIIVAHRLsTIKD--ADIIFVMKG 155
Cdd:PRK13409  211 SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI--RQRLNvaRLIRelAEGKYVLVVEHDL-AVLDylADNVHIAYG 286
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
63-155 1.12e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 41.72  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  63 IYDEIMAmPMKFNTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTinEERIT------KYIKSQGCTQII 136
Cdd:PRK13409  433 YKSEIIK-PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQRLAvakairRIAEEREATALV 509
                          90       100
                  ....*....|....*....|.
gi 1877026690 137 VAHRLSTIkD--ADIIFVMKG 155
Cdd:PRK13409  510 VDHDIYMI-DyiSDRLMVFEG 529
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
83-139 1.56e-04

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 41.31  E-value: 1.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQGCTQIIVAH 139
Cdd:PRK10636  148 SDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISH 204
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
83-155 1.89e-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: 40.92  E-value: 1.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1877026690  83 SNISGGQRQRIALARALINNPSIVILDEATSALDT---INEERITKYIKSQGCTQIIVAHRLsTIKD--ADIIFVMKG 155
Cdd:COG1245   211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIyqrLNVARLIRELAEEGKYVLVVEHDL-AILDylADYVHILYG 287
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
74-130 1.99e-04

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 41.25  E-value: 1.99e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1877026690   74 FNTII-SEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKSQ 130
Cdd:TIGR00956  198 RNTKVgNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTS 255
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
84-137 2.23e-04

ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213242 [Multi-domain]  Cd Length: 247  Bit Score: 40.25  E-value: 2.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1877026690  84 NISGGQRQRIALAraL---IN--NPS-IVILDEATSALDTINEERITKYIKSQGC--TQIIV 137
Cdd:cd03275   155 NLSGGEKTMAALA--LlfaIHsyQPApFFVLDEVDAALDNTNVGKVASYIREQAGpnFQFIV 214
ycf16 CHL00131
sulfate ABC transporter protein; Validated
4-163 2.92e-04

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 40.01  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   4 GKVLFDGININQIDKKILSQnLGVvpqdsFLLNRSILDNITLKNEvtsQKIEEVCKAVQIYDEIMAM-PMKFNTIISE-- 80
Cdd:CHL00131   64 GDILFKGESILDLEPEERAH-LGI-----FLAFQYPIEIPGVSNA---DFLRLAYNSKRKFQGLPELdPLEFLEIINEkl 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  81 ---------MGSNI----SGGQRQRIALARALINNPSIVILDEATSALD-----TINEErITKYIKSQGCTqIIVAH--R 140
Cdd:CHL00131  135 klvgmdpsfLSRNVnegfSGGEKKRNEILQMALLDSELAILDETDSGLDidalkIIAEG-INKLMTSENSI-ILITHyqR 212
                         170       180
                  ....*....|....*....|...
gi 1877026690 141 LSTIKDADIIFVMKGGKIVESGN 163
Cdd:CHL00131  213 LLDYIKPDYVHVMQNGKIIKTGD 235
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
83-151 4.39e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.95  E-value: 4.39e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1877026690   83 SNISGGQRQRIALAraLI-----NNPS-IVILDEATSALDTINEERITKYIKSQG-CTQIIV-AHRLSTIKDADIIF 151
Cdd:pfam02463 1076 DLLSGGEKTLVALA--LIfaiqkYKPApFYLLDEIDAALDDQNVSRVANLLKELSkNAQFIViSLREEMLEKADKLV 1150
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
83-165 4.48e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 40.20  E-value: 4.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   83 SNISGGQRQRIALARALI---NNPSIVILDEATSALDTINEERITKYIK---SQGCTQIIVAHRLSTIKDADIIFVM--- 153
Cdd:PRK00635  1698 SSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRtlvSLGHSVIYIDHDPALLKQADYLIEMgpg 1777
                           90
                   ....*....|....*
gi 1877026690  154 ---KGGKIVESGNHK 165
Cdd:PRK00635  1778 sgkTGGKILFSGPPK 1792
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
86-162 6.43e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 39.33  E-value: 6.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLSTIKD-ADIIFVMKGGKIVES 161
Cdd:NF000106  146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSmvrDGATVLLTTQYMEEAEQlAHELTVIDRGRVIAD 225

                  .
gi 1877026690 162 G 162
Cdd:NF000106  226 G 226
uvrA PRK00349
excinuclease ABC subunit UvrA;
86-162 1.10e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 38.90  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALINNP---SIVILDEATSALDTineERITKYIK------SQGCTQIIVAHRLSTIKDADIIFVM--- 153
Cdd:PRK00349  832 SGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHF---EDIRKLLEvlhrlvDKGNTVVVIEHNLDVIKTADWIIDLgpe 908
                          90
                  ....*....|..
gi 1877026690 154 ---KGGKIVESG 162
Cdd:PRK00349  909 ggdGGGEIVATG 920
PLN03140 PLN03140
ABC transporter G family member; Provisional
75-169 1.10e-03

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 39.06  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   75 NTII-SEMGSNISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKyiksqgCTQIIVAHRLSTIKDA------ 147
Cdd:PLN03140   326 DTIVgDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVK------CLQQIVHLTEATVLMSllqpap 399
                           90       100
                   ....*....|....*....|....*....
gi 1877026690  148 -------DIIFVMKgGKIVESGNHKYLME 169
Cdd:PLN03140   400 etfdlfdDIILLSE-GQIVYQGPRDHILE 427
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
23-116 1.28e-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: 38.84  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   23 QNLGVVPQ----DSFLLNRSILDNITLKNEVTSQKIEEVCK-AVQiydeimamPMKFNTIISEMGSNISGGQRQRIALAR 97
Cdd:TIGR01257 2012 QNMGYCPQfdaiDDLLTGREHLYLYARLRGVPAEEIEKVANwSIQ--------SLGLSLYADRLAGTYSGGNKRKLSTAI 2083
                           90
                   ....*....|....*....
gi 1877026690   98 ALINNPSIVILDEATSALD 116
Cdd:TIGR01257 2084 ALIGCPPLVLLDEPTTGMD 2102
PLN03073 PLN03073
ABC transporter F family; Provisional
85-116 1.39e-03

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 38.69  E-value: 1.39e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALD 116
Cdd:PLN03073  628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
85-159 1.99e-03

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


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 37.22  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDT---INEERITKYIKSQGCTQIIVAHRLS--TIKDADIIFVMK-GGKI 158
Cdd:cd03232   109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSqaaYNIVRFLKKLADSGQAILCTIHQPSasIFEKFDRLLLLKrGGKT 188

                  .
gi 1877026690 159 V 159
Cdd:cd03232   189 V 189
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
84-159 3.14e-03

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 37.20  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  84 NISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYI---KSQGCTQIIVAHRL-STIKDADIIFVMKGGKIV 159
Cdd:PRK11288  396 NLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIyelAAQGVAVLFVSSDLpEVLGVADRIVVMREGRIA 475
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
63-182 4.38e-03

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 36.69  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  63 IYDEIMAMPMKFNTIISEMGSNISGGQRQRIALARALINNPSIVILDEATSALDtINEERIT----KYIKSQGCTQIIVA 138
Cdd:PRK09580  124 MEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLD-IDALKIVadgvNSLRDGKRSFIIVT 202
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1877026690 139 HR---LSTIKdADIIFVMKGGKIVESGNHKYLMELGGEYYSLYTKRK 182
Cdd:PRK09580  203 HYqriLDYIK-PDYVHVLYQGRIVKSGDFTLVKQLEEQGYGWLTEQQ 248
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
47-171 5.41e-03

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 37.01  E-value: 5.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   47 NEVT-SQKIEEVCKAVqiydEIMAMPMKFNTIISEMGSNISGGQRQRIALARALINNP-SIVILDEATSALDTINEERIT 124
Cdd:TIGR00956  867 KSVSkSEKMEYVEEVI----KLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSIC 942
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1877026690  125 KYIK---SQGCTQIIVAHRLSTIKDAD---IIFVMKGGKIVesgnhkYLMELG 171
Cdd:TIGR00956  943 KLMRklaDHGQAILCTIHQPSAILFEEfdrLLLLQKGGQTV------YFGDLG 989
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
86-162 6.41e-03

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 36.54  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  86 SGGQRQRIALARALI---NNPSIVILDEATSAL---DtineerITKYIKS------QGCTQIIVAHRLSTIKDADIIFVM 153
Cdd:COG0178   828 SGGEAQRVKLASELSkrsTGKTLYILDEPTTGLhfhD------IRKLLEVlhrlvdKGNTVVVIEHNLDVIKTADWIIDL 901
                          90
                  ....*....|....*
gi 1877026690 154 ------KGGKIVESG 162
Cdd:COG0178   902 gpeggdGGGEIVAEG 916
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
84-157 8.31e-03

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 35.74  E-value: 8.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1877026690  84 NISGGQRQRIALARALINNPSIVILDEATSAL---DTIN-EERITKYIKSQGCTQIIVAHRLSTIKD-ADIIFVMKGGK 157
Cdd:PRK11300  153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLnpkETKElDELIAELRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGT 231
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
86-116 9.03e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 36.26  E-value: 9.03e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1877026690  86 SGGQRQRIALARALINNPSIVILDEATSALD 116
Cdd:NF033858  138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
85-168 9.59e-03

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 35.76  E-value: 9.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690  85 ISGGQRQRIALARALINNPSIVILDEATSALDTINEERITKYIKS---QGCTQIIVAHRLSTIKD-ADIIFVMKGGKIVE 160
Cdd:PRK10938  136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASlhqSGITLVLVLNRFDEIPDfVQFAGVLADCTLAE 215

                  ....*...
gi 1877026690 161 SGNHKYLM 168
Cdd:PRK10938  216 TGEREEIL 223
GguA NF040905
sugar ABC transporter ATP-binding protein;
3-116 9.90e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 35.92  E-value: 9.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877026690   3 TGKVLFDG--ININQIDKKIlSQNLGVVPQD----SFLLNRSILDNITLKN--EVTS----QKIEEVCKAVQIYDeimAM 70
Cdd:NF040905  316 SGTVFKDGkeVDVSTVSDAI-DAGLAYVTEDrkgyGLNLIDDIKRNITLANlgKVSRrgviDENEEIKVAEEYRK---KM 391
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1877026690  71 PMKFNTIISEMGsNISGGQRQRIALARALINNPSIVILDEATSALD 116
Cdd:NF040905  392 NIKTPSVFQKVG-NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
 
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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