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Conserved domains on  [gi|488289759|ref|WP_002360967|]
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ATP-binding cassette domain-containing protein [Enterococcus faecalis]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
1-221 7.08e-125

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


The actual alignment was detected with superfamily member cd03258:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 233  Bit Score: 353.42  E-value: 7.08e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQET----HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:cd03258    1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:cd03258   81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAgvpKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGEF-----LNNPQ 221
Cdd:cd03258  161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGtveevFANPQ 233
 
Name Accession Description Interval E-value
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
1-221 7.08e-125

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: 353.42  E-value: 7.08e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQET----HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:cd03258    1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:cd03258   81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAgvpKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGEF-----LNNPQ 221
Cdd:cd03258  161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGtveevFANPQ 233
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1-222 3.27e-108

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 315.09  E-value: 3.27e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVY----QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:COG1135    1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:COG1135   81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAgvpKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQ 222
Cdd:COG1135  161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVeqgpvLDVFANPQS 234
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
1-222 3.43e-95

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 282.07  E-value: 3.43e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:PRK11153   1 MIELKNISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:PRK11153  81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAgtpKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQ 222
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVeqgtvSEVFSHPKH 234
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
2-213 1.63e-49

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


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 162.98  E-value: 1.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNvqTFSKKEVRQQQQQ 79
Cdd:TIGR04520   1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENLWEIRKK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   80 MGMVFQhyNL----------------LENLKIydnvalPLKLLKEKqpekIERLLTFVDMAHKAEAYPAQLSGGEKQRVS 143
Cdd:TIGR04520  79 VGMVFQ--NPdnqfvgatveddvafgLENLGV------PREEMRKR----VDEALKLVGMEDFRDREPHLLSGGQKQRVA 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  144 IARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVkRLCNRILVMEKGQLI 213
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIV 215
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
17-162 3.31e-47

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: 153.19  E-value: 3.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQMGMVFQHYNLLENLKIY 96
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLR---KEIGYVFQDPQLFPRLTVR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759   97 DNVALPL---KLLKEKQPEKIERLLTFVDMAHKAE----AYPAQLSGGEKQRVSIARALSRNPKWLLCDEATS 162
Cdd:pfam00005  78 ENLRLGLllkGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
16-199 1.23e-17

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 78.04  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFskkeVRQQQQ-------------QMGm 82
Cdd:NF040873   7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAY----VPQRSEvpdslpltvrdlvAMG- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  83 VFQHYNLLENLKIYDNVAlplkllkekqpekIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATS 162
Cdd:NF040873  82 RWARRGLWRRLTRDDRAA-------------VDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 488289759 163 SLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKR 199
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGA-TVVVVTHDLELVRR 184
GguA NF040905
sugar ABC transporter ATP-binding protein;
1-213 9.97e-14

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 69.82  E-value: 9.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLnlmeqpS--------EGEIRIDGrNVQTFskKE 72
Cdd:NF040905   1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVL------SgvyphgsyEGEILFDG-EVCRF--KD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  73 VRQQQQQmGMVFQHYNL--LENLKIYDNVALPLKLLK------EKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSI 144
Cdd:NF040905  72 IRDSEAL-GIVIIHQELalIPYLSIAENIFLGNERAKrgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEI 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHkthqEFRP---TIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLL----ELKAqgiTSIIISHKLNEIRRVADSITVLRDGRTI 218
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
16-211 5.02e-12

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 65.15  E-value: 5.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIR-----IDGRNVQTfsKKEVrqqqqqmGMVFQHYNLL 90
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIAT--RRRV-------GYMSQAFSLY 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  91 ENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:NF033858 352 GELTVRQNLELHARLFhlpAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488289759 168 NTESVVRLLHKTHQEFRPTIFFVSH---ELEtvkRlCNRILVMEKGQ 211
Cdd:NF033858 432 ARDMFWRLLIELSREDGVTIFISTHfmnEAE---R-CDRISLMHAGR 474
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
27-204 2.78e-11

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: 59.69  E-value: 2.78e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    27 GEIVGIVGKSGSGKSTLLRLL-NLMEQPSEGEIRIDGrnvqtfskkevrqqqqqmgmvfqhynllenlkiydnvalplkl 105
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDG------------------------------------------- 38
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   106 lkekqpEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENT-----ESVVRLLHKTH 180
Cdd:smart00382  39 ------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELRLLLLLK 112
                          170       180
                   ....*....|....*....|....
gi 488289759   181 QEFRPTIFFVSHELETVKRLCNRI 204
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPALLRR 136
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
2-165 1.75e-08

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 54.36  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVRQQQ---- 77
Cdd:NF033858   2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM---ADARHRRAVcpri 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  78 ----QQMGMvfqhyNLLENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDMAHKAEAyPA-QLSGGEKQRVSIARALS 149
Cdd:NF033858  79 aympQGLGK-----NLYPTLSVFENLDFFGRLFGQDAAErrrRIDELLRATGLAPFADR-PAgKLSGGMKQKLGLCCALI 152
                        170
                 ....*....|....*.
gi 488289759 150 RNPKWLLCDEATSSLD 165
Cdd:NF033858 153 HDPDLLILDEPTTGVD 168
GguA NF040905
sugar ABC transporter ATP-binding protein;
10-216 6.13e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 46.71  E-value: 6.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  10 VYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLlrllnLME-------QPSEGEIRIDGRNVQTFSKKE--------VR 74
Cdd:NF040905 269 LHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTEL-----AMSvfgrsygRNISGTVFKDGKEVDVSTVSDaidaglayVT 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  75 QQQQQMGMvfqhyNLLENLKiyDNVALP-LKLLKEKqpekierllTFVDmAHK----AEAYPA--------------QLS 135
Cdd:NF040905 344 EDRKGYGL-----NLIDDIK--RNITLAnLGKVSRR---------GVID-ENEeikvAEEYRKkmniktpsvfqkvgNLS 406
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 136 GGEKQRVSIARALSRNPKWLLCDEATSSLD-----EENTesVVRLLHKTHQefrpTIFFVSHELETVKRLCNRILVMEKG 210
Cdd:NF040905 407 GGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgakyEIYT--IINELAAEGK----GVIVISSELPELLGMCDRIYVMNEG 480

                 ....*.
gi 488289759 211 QLIGEF 216
Cdd:NF040905 481 RITGEL 486
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
91-215 5.36e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 40.49  E-value: 5.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  91 ENLKIydnVALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTE 170
Cdd:NF000106 105 ENLYM---IGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRN 181
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 488289759 171 SVVRLLHKTHQEfRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:NF000106 182 EVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
 
Name Accession Description Interval E-value
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
1-221 7.08e-125

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: 353.42  E-value: 7.08e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQET----HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:cd03258    1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:cd03258   81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAgvpKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGEF-----LNNPQ 221
Cdd:cd03258  161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGtveevFANPQ 233
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1-222 3.27e-108

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 315.09  E-value: 3.27e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVY----QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:COG1135    1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:COG1135   81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAgvpKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQ 222
Cdd:COG1135  161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVeqgpvLDVFANPQS 234
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
1-222 3.43e-95

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 282.07  E-value: 3.43e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:PRK11153   1 MIELKNISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:PRK11153  81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAgtpKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQ 222
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVeqgtvSEVFSHPKH 234
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-215 7.71e-85

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 251.89  E-value: 7.71e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQ- 75
Cdd:COG1136    4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARl 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  76 QQQQMGMVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIER---LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:COG1136   84 RRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERareLLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELEtVKRLCNRILVMEKGQLIGE 215
Cdd:COG1136  164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLRDGRIVSD 225
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
2-212 4.27e-84

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: 249.71  E-value: 4.27e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKE-VRQQ 76
Cdd:cd03255    1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElAAFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIER---LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:cd03255   81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERaeeLLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELEtVKRLCNRILVMEKGQL 212
Cdd:cd03255  161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
1-222 1.78e-82

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 246.06  E-value: 1.78e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqTFSKKEVRQQQQQM 80
Cdd:COG1126    1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRKV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVAL-PLKLLKEKQPEKIER---LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:COG1126   80 GMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERameLLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 157 CDEATSSLDEENT---ESVVRLLHKTHQefrpTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQ 222
Cdd:COG1126  160 FDEPTSALDPELVgevLDVMRDLAKEGM----TMVVVTHEMGFAREVADRVVFMDGGRIVeegppEEFFENPQH 229
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
1-213 5.92e-78

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 234.18  E-value: 5.92e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETH-ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQ 79
Cdd:COG2884    1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:COG2884   81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEirrRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEfRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG2884  161 ADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLV 216
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
1-213 3.39e-77

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 233.03  E-value: 3.39e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQ-ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQ 79
Cdd:COG3638    2 MLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLENLKIYDNV---ALP--------LKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARAL 148
Cdd:COG3638   82 IGMIFQQFNLVPRLSVLTNVlagRLGrtstwrslLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG3638  162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1-222 5.66e-76

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: 238.26  E-value: 5.66e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVY-----QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQ 75
Cdd:COG1123  260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  76 QQQQMGMVFQHYN--LLENLKIYDNVALPLKLL----KEKQPEKIERLLTFVDM-AHKAEAYPAQLSGGEKQRVSIARAL 148
Cdd:COG1123  340 LRRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHgllsRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQ 222
Cdd:COG1123  420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVedgptEEVFANPQH 498
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
1-215 7.58e-72

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: 219.08  E-value: 7.58e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQM 80
Cdd:COG1127    5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIERL----LTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:COG1127   85 GMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELvlekLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:COG1127  165 YDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1-216 2.83e-71

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 218.42  E-value: 2.83e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGrnvqtfskKEVRQQ 76
Cdd:COG1116    7 ALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG--------KPVTGP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:COG1116   79 GPDRGVVFQEPALLPWLTVLDNVALGLELRgvpKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHEL-ETVkRLCNRILVMEK--GQLIGEF 216
Cdd:COG1116  159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVdEAV-FLADRVVVLSArpGRIVEEI 223
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
2-212 5.18e-71

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: 216.24  E-value: 5.18e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqTFSKKEVRQQQQQMG 81
Cdd:cd03262    1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQKVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVAL-PLKLLKEKQPEKIER---LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:cd03262   80 MVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERaleLLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 158 DEATSSLDEENTESVVRL---LHKTHQefrpTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:cd03262  160 DEPTSALDPELVGEVLDVmkdLAEEGM----TMVVVTHEMGFAREVADRVIFMDDGRI 213
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
2-213 2.31e-68

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: 209.30  E-value: 2.31e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskkeVRQQQQQMG 81
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-----VPPERRNIG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIER---LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:cd03259   76 MVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARvreLLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03259  156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
2-215 4.28e-67

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: 206.97  E-value: 4.28e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQMG 81
Cdd:cd03261    1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVALPL----KLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:cd03261   81 MLFQSGALFDSLTVFENVAFPLrehtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:cd03261  161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
2-213 1.48e-66

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: 205.88  E-value: 1.48e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVY-QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQM 80
Cdd:cd03256    1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNV---ALP--------LKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALS 149
Cdd:cd03256   81 GMIFQQFNLIERLSVLENVlsgRLGrrstwrslFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 150 RNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03256  161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1-216 1.77e-66

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: 205.81  E-value: 1.77e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVY----QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVRQQ 76
Cdd:COG1124    1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV---TRRRRKAF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVFQHYNLLEN--LKIYDNVALPLKLLKEKQPEK-IERLLTFVDM-AHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:COG1124   78 RRRVQMVFQDPYASLHprHTVDRILAEPLRIHGLPDREErIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEP 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGEF 216
Cdd:COG1124  158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEEL 221
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
2-213 2.62e-66

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: 204.87  E-value: 2.62e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQ-ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqM 80
Cdd:COG1122    1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK---V 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHY-NLLENLKIYDNVA---LPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:COG1122   78 GLVFQNPdDQLFAPTVEEDVAfgpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG1122  158 LDEPTAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLDLVAELADRVIVLDDGRIV 213
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
2-216 8.58e-66

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: 203.09  E-value: 8.58e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGrnvqtfskKEVRQQQ 77
Cdd:cd03293    1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--------EPVTGPG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  78 QQMGMVFQHYNLLENLKIYDNVALPLKL---LKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:cd03293   73 PDRGYVFQQDALLPWLTVLDNVALGLELqgvPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEK--GQLIGEF 216
Cdd:cd03293  153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEV 216
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
2-211 1.45e-65

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: 200.88  E-value: 1.45e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSkKEVRQQQQQMG 81
Cdd:cd03229    1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE-DELPPLRRRIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVALPlkllkekqpekierlltfvdmahkaeaypaqLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:cd03229   80 MVFQDFALFPHLTVLENIALG-------------------------------LSGGQQQRVALARALAMDPDVLLLDEPT 128
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 488289759 162 SSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:cd03229  129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
3-211 1.48e-65

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: 202.31  E-value: 1.48e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   3 ELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqM 80
Cdd:cd03225    1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK---V 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNL-LENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:cd03225   78 GLVFQNPDDqFFGPTVEEEVAFGLENLglpEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:cd03225  158 LDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDGK 211
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
2-221 2.06e-63

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 201.14  E-value: 2.06e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtFSKKEVRQQQqqMG 81
Cdd:COG1118    3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL--FTNLPPRERR--VG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVA--LP-LKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:COG1118   79 FVFQHYALFPHMTVAENIAfgLRvRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQL--IG---EFLNNPQ 221
Cdd:COG1118  159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIeqVGtpdEVYDRPA 226
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
1-213 8.21e-63

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: 195.80  E-value: 8.21e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQE----THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:cd03257    1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVFQHYNLLEN--LKIYDNVALPLKLL-----KEKQPEKIERLLTFVDMAHK-AEAYPAQLSGGEKQRVSIARAL 148
Cdd:cd03257   81 RKEIQMVFQDPMSSLNprMTIGEQIAEPLRIHgklskKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARAL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03257  161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1-213 2.36e-62

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 198.78  E-value: 2.36e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQM 80
Cdd:COG3842    5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-----GLPPEKRNV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:COG3842   80 GMVFQDYALFPHLTVAENVAFGLRMRgvpKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG3842  160 DEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
2-213 1.21e-61

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: 192.78  E-value: 1.21e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLM-----EQPSEGEIRIDGRNV--QTFSKKEVR 74
Cdd:cd03260    1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIydLDVDVLELR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  75 qqqQQMGMVFQHYNLLeNLKIYDNVALPLKL----LKEKQPEKIERLLTFVDMAH--KAEAYPAQLSGGEKQRVSIARAL 148
Cdd:cd03260   81 ---RRVGMVFQKPNPF-PGSIYDNVAYGLRLhgikLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARAL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03260  157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLV 219
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
1-215 1.28e-61

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: 193.03  E-value: 1.28e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKE---V 73
Cdd:COG4181    8 IIELRGLTKTVGtgagELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDArarL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  74 RQQQqqMGMVFQHYNLLENLKIYDNVALPLKLLKEKQPEKI-ERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:COG4181   88 RARH--VGFVFQSFQLLPTLTALENVMLPLELAGRRDARARaRALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRlCNRILVMEKGQLIGE 215
Cdd:COG4181  166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
2-213 4.40e-60

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 189.12  E-value: 4.40e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSkKEVRqqqQQMG 81
Cdd:COG1131    1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVR---RRIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:COG1131   77 YVPQEPALYPDLTVRENLRFFARLYglpRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG1131  157 EPTSGLDPEARRELWELLRELAAEGK-TVLLSTHYLEEAERLCDRVAIIDKGRIV 210
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
2-212 1.23e-59

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: 187.23  E-value: 1.23e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVY-QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQM 80
Cdd:cd03292    1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVALPLKLLKEKQ---PEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:cd03292   81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPreiRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEfRPTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:cd03292  161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
1-220 3.87e-59

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 190.28  E-value: 3.87e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQM 80
Cdd:COG3839    3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-----DLPPKDRNI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:COG3839   78 AMVFQSYALYPHMTVYENIAFPLKLRKVPKAEidrRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQL--IG---EFLNNP 220
Cdd:COG3839  158 DEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIqqVGtpeELYDRP 225
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
2-212 5.69e-59

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 185.40  E-value: 5.69e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqMG 81
Cdd:COG4619    1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ---VA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENlKIYDNVALPLKLLKEK-QPEKIERLLTFVDMAHKAEAYPA-QLSGGEKQRVSIARALSRNPKWLLCDE 159
Cdd:COG4619   78 YVPQEPALWGG-TVRDNLPFPFQLRERKfDRERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPDVLLLDE 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488289759 160 ATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:COG4619  157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
1-213 2.97e-58

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: 184.86  E-value: 2.97e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQM 80
Cdd:COG1120    1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA---RRI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVAL-------PLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:COG1120   78 AYVPQEPPAPFGLTVRELVALgryphlgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG1120  158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
2-220 5.65e-57

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: 181.34  E-value: 5.65e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETH-ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqM 80
Cdd:cd03295    1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK---I 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIER---LLTFVDM--AHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:cd03295   78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERadeLLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNP 220
Cdd:cd03295  158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVqvgtpDEILRSP 227
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
2-221 8.98e-57

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 180.98  E-value: 8.98e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNV---QTFSKKEVRQQQQ 78
Cdd:COG4161    3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  79 QMGMVFQHYNLLENLKIYDN-VALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:COG4161   83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLglsKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKThQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI----GEFLNNPQ 221
Cdd:COG4161  163 LLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIeqgdASHFTQPQ 232
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
14-221 1.00e-56

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: 181.69  E-value: 1.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  14 THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQ-QQQQMGMVFQHYNLLEN 92
Cdd:cd03294   37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElRRKKISMVFQSFALLPH 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  93 LKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD---- 165
Cdd:cd03294  117 RTVLENVAFGLEVQgvpRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplir 196
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 166 EENTESVVRLlhktHQEFRPTIFFVSHELETVKRLCNRILVMEKGQL--IG---EFLNNPQ 221
Cdd:cd03294  197 REMQDELLRL----QAELQKTIVFITHDLDEALRLGDRIAIMKDGRLvqVGtpeEILTNPA 253
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
1-220 5.00e-56

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 178.75  E-value: 5.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfSKKEVRQQQQQM 80
Cdd:PRK09493   1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIRQEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVAL-PLKL--LKEKQPEKIER-LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:PRK09493  80 GMVFQQFYLFPHLTALENVMFgPLRVrgASKEEAEKQAReLLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNP 220
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEGM-TMVIVTHEIGFAEKVASRLIFIDKGRIAedgdpQVLIKNP 227
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
2-211 6.16e-56

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: 176.42  E-value: 6.16e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETH--ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqq 79
Cdd:cd03228    1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLeNLKIYDNValplkllkekqpekierlltfvdmahkaeaypaqLSGGEKQRVSIARALSRNPKWLLCDE 159
Cdd:cd03228   78 IAYVPQDPFLF-SGTIRENI----------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488289759 160 ATSSLDEENTESVVRLLHKTHQEfrPTIFFVSHELETVKRlCNRILVMEKGQ 211
Cdd:cd03228  123 ATSALDPETEALILEALRALAKG--KTVIVIAHRLSTIRD-ADRIIVLDDGR 171
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
2-229 2.67e-55

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 180.66  E-value: 2.67e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrqqqQQMG 81
Cdd:PRK10851   3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-----RKVG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVALPLKLL-KEKQP------EKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:PRK10851  78 FVFQHYALFRHMTVFDNIAFGLTVLpRRERPnaaaikAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLigEFLNNPQQYEEEPLS 229
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI--EQAGTPDQVWREPAT 230
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1-221 3.23e-55

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: 179.09  E-value: 3.23e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLMEQP--SEGEIRIDGRNVQTFSKKEV 73
Cdd:COG0444    1 LLEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  74 RQ-QQQQMGMVFQH-YNLLeN--LKIYDNVALPLKLL----KEKQPEKIERLLTFVDMAHKAE---AYPAQLSGGEKQRV 142
Cdd:COG0444   81 RKiRGREIQMIFQDpMTSL-NpvMTVGDQIAEPLRIHgglsKAEARERAIELLERVGLPDPERrldRYPHELSGGMRQRV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 143 SIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFL 217
Cdd:COG0444  160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVeegpvEELF 239

                 ....
gi 488289759 218 NNPQ 221
Cdd:COG0444  240 ENPR 243
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
2-227 1.74e-54

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: 174.73  E-value: 1.74e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQMG 81
Cdd:cd03300    1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-----NLPPHKRPVN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:cd03300   76 TVFQNYALFPHLTVFENIAFGLRLKKLPKAEikeRVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLigEFLNNPQQYEEEP 227
Cdd:cd03300  156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI--QQIGTPEEIYEEP 222
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
2-213 8.45e-54

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 173.28  E-value: 8.45e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNV---QTFSKKEVRQQQQ 78
Cdd:PRK11124   3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELRR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  79 QMGMVFQHYNLLENLKIYDN-VALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:PRK11124  83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVLglsKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKThQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
2-229 1.60e-53

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: 172.52  E-value: 1.60e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVrqQQQQMG 81
Cdd:cd03296    3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPV--QERNVG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVALPLKLLKEKQP-------EKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:cd03296   78 FVFQHYALFRHMTVFDNVAFGLRVKPRSERppeaeirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLigEFLNNPQQYEEEPLS 229
Cdd:cd03296  158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI--EQVGTPDEVYDHPAS 230
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
2-212 1.98e-53

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: 171.28  E-value: 1.98e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrqqqQQMG 81
Cdd:cd03301    1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-----RDIA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:cd03301   76 MVFQNYALYPHMTVYDNIAFGLKLRKVPKDEideRVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:cd03301  156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1-227 4.31e-53

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: 178.56  E-value: 4.31e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLN-LMEQPSE--GEIRIDGRNVQTFSkkeVRQ 75
Cdd:COG1123    4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMgLLPHGGRisGEVLLDGRDLLELS---EAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  76 QQQQMGMVFQHY-NLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRN 151
Cdd:COG1123   81 RGRRIGMVFQDPmTQLNPVTVGDQIAEALENLglsRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 152 PKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQYEEE 226
Cdd:COG1123  161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVedgppEEILAAPQALAAV 240

                 .
gi 488289759 227 P 227
Cdd:COG1123  241 P 241
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
2-213 1.74e-52

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: 180.42  E-value: 1.74e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQ 79
Cdd:COG2274  474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLR---RQ 550
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLENlKIYDNVALPLKLLKEkqpEKIERLLTFVDMAHKAEAYP-----------AQLSGGEKQRVSIARAL 148
Cdd:COG2274  551 IGVVLQDVFLFSG-TIRENITLGDPDATD---EEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARAL 626
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLhktHQEFRP-TIFFVSHELETVkRLCNRILVMEKGQLI 213
Cdd:COG2274  627 LRNPRILILDEATSALDAETEAIILENL---RRLLKGrTVIIIAHRLSTI-RLADRIIVLDKGRIV 688
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
3-211 4.49e-52

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: 165.88  E-value: 4.49e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   3 ELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqMGM 82
Cdd:cd00267    1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRR---IGY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  83 VFQhynllenlkiydnvalplkllkekqpekierlltfvdmahkaeaypaqLSGGEKQRVSIARALSRNPKWLLCDEATS 162
Cdd:cd00267   78 VPQ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488289759 163 SLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:cd00267  110 GLDPASRERLLELLRELAEEGR-TVIIVTHDPELAELAADRVIVLKDGK 157
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-212 9.25e-52

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 167.96  E-value: 9.25e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLMeQPSEGEIRIDGRNVqtfskkevRQQQQQ 79
Cdd:COG1121    6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILGLL-PPTSGTVRLFGKPP--------RRARRR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLENLKI--YDNVAL-------PLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSR 150
Cdd:COG1121   77 IGYVPQRAEVDWDFPItvRDVVLMgrygrrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:COG1121  157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGK-TILVVTHDLGAVREYFDRVLLLNRGLV 217
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
2-212 1.10e-51

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: 165.65  E-value: 1.10e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfsKKEVRQQQQQMG 81
Cdd:cd03230    1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVKRRIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNValplkllkekqpekierlltfvdmahkaeaypaQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:cd03230   77 YLPEEPSLYENLTVRENL---------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488289759 162 SSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:cd03230  124 SGLDPESRREFWELLRELKKEGK-TILLSSHILEEAERLCDRVAILNNGRI 173
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
1-226 1.75e-51

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: 167.34  E-value: 1.75e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskKEVRQQQQQM 80
Cdd:COG4555    1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR----KEPREARRQI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVAL--PLKLLKEKQ-PEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:COG4555   77 GVLPDERGLYDRLTVRENIRYfaELYGLFDEElKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIgeFLNNPQQYEEE 226
Cdd:COG4555  157 DEPTNGLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEALCDRVVILHKGKVV--AQGSLDELREE 222
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
3-210 5.60e-51

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: 165.01  E-value: 5.60e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   3 ELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLMeQPSEGEIRIDGrnvqtfskKEVRQQQQQMG 81
Cdd:cd03235    1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLL-KPTSGSIRVFG--------KPLEKERKRIG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLEN--LKIYDNVAL-------PLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:cd03235   72 YVPQRRSIDRDfpISVRDVVLMglyghkgLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKG 210
Cdd:cd03235  152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGM-TILVVTHDLGLVLEYFDRVLLLNRT 208
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
2-215 2.48e-50

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 172.66  E-value: 2.48e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQ-ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLN-LMEqPSEGEIRIDGRNVQTFSKKEVRqqqQQ 79
Cdd:COG1132  340 IEFENVSFSYPgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLrFYD-PTSGRILIDGVDIRDLTLESLR---RQ 415
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLeNLKIYDNVALPlklLKEKQPEKIERLLTFVDMAHKAEAYP-----------AQLSGGEKQRVSIARAL 148
Cdd:COG1132  416 IGVVPQDTFLF-SGTIRENIRYG---RPDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARAL 491
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 149 SRNPKWLLCDEATSSLDEEnTEsvvRLLHKTHQEFRP--TIFFVSHELETVKRlCNRILVMEKGQLIGE 215
Cdd:COG1132  492 LKDPPILILDEATSALDTE-TE---ALIQEALERLMKgrTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
15-207 1.45e-49

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 164.90  E-value: 1.45e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  15 HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVFQH-YNLLeN- 92
Cdd:COG4608   32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQDpYASL-Np 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  93 -LKIYDNVALPLK---LLKEKQP-EKIERLLTFVDM--AHkAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:COG4608  111 rMTVGDIIAEPLRihgLASKAERrERVAELLELVGLrpEH-ADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488289759 166 EENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVM 207
Cdd:COG4608  190 VSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVM 231
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
2-213 1.63e-49

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


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 162.98  E-value: 1.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNvqTFSKKEVRQQQQQ 79
Cdd:TIGR04520   1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENLWEIRKK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   80 MGMVFQhyNL----------------LENLKIydnvalPLKLLKEKqpekIERLLTFVDMAHKAEAYPAQLSGGEKQRVS 143
Cdd:TIGR04520  79 VGMVFQ--NPdnqfvgatveddvafgLENLGV------PREEMRKR----VDEALKLVGMEDFRDREPHLLSGGQKQRVA 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  144 IARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVkRLCNRILVMEKGQLI 213
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIV 215
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
1-233 1.37e-48

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 160.30  E-value: 1.37e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIR-----IDGRNVQTFSKKEVRQ 75
Cdd:PRK11264   3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditIDTARSLSQQKGLIRQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  76 QQQQMGMVFQHYNLLENLKIYDNVAL-PLKLLKEKQPEKIER---LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRN 151
Cdd:PRK11264  83 LRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARareLLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 152 PKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQyeEE 226
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVeqgpaKALFADPQQ--PR 239

                 ....*..
gi 488289759 227 PLSYLEK 233
Cdd:PRK11264 240 TRQFLEK 246
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
27-214 5.33e-48

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: 157.46  E-value: 5.33e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  27 GEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKK-EVRQQQQQMGMVFQHYNLLENLKIYDNVALPLKL 105
Cdd:cd03297   23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLPPQQRKIGLVFQQYALFPHLNVRENLAFGLKR 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 106 lKEKQPEKI--ERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEF 183
Cdd:cd03297  103 -KRNREDRIsvDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNL 181
                        170       180       190
                 ....*....|....*....|....*....|.
gi 488289759 184 RPTIFFVSHELETVKRLCNRILVMEKGQLIG 214
Cdd:cd03297  182 NIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
1-213 6.21e-48

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 157.99  E-value: 6.21e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHalKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVrqQQQQM 80
Cdd:COG3840    1 MLRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL---TALPP--AERPV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVAL---P-LKlLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:COG3840   74 SMLFQENNLFPHLTVAQNIGLglrPgLK-LTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG3840  153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
2-215 1.06e-47

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: 157.21  E-value: 1.06e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqqQMG 81
Cdd:cd03219    1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA----RLG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MV--FQHYNLLENLKIYDNVALPLKLLK-------------EKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIAR 146
Cdd:cd03219   77 IGrtFQIPRLFPELTVLENVMVAAQARTgsglllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 147 ALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:cd03219  157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGI-TVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
6-215 2.35e-47

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 156.51  E-value: 2.35e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   6 NVSKVYQE----THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFS---KKEVRQQQq 78
Cdd:PRK11629  10 NLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNQK- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  79 qMGMVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIER---LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK11629  89 -LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRaleMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLV 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLcNRILVMEKGQLIGE 215
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
17-162 3.31e-47

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: 153.19  E-value: 3.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQMGMVFQHYNLLENLKIY 96
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLR---KEIGYVFQDPQLFPRLTVR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759   97 DNVALPL---KLLKEKQPEKIERLLTFVDMAHKAE----AYPAQLSGGEKQRVSIARALSRNPKWLLCDEATS 162
Cdd:pfam00005  78 ENLRLGLllkGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
1-221 1.23e-46

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: 155.20  E-value: 1.23e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqqQM 80
Cdd:COG0411    4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA----RL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMV--FQHYNLLENLKIYDNVALP-------------LKLLKEKQPE-----KIERLLTFVDMAHKAEAYPAQLSGGEKQ 140
Cdd:COG0411   80 GIArtFQNPRLFPELTVLENVLVAaharlgrgllaalLRLPRARREEreareRAEELLERVGLADRADEPAGNLSYGQQR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 141 RVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GE 215
Cdd:COG0411  160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIaegtpAE 239

                 ....*.
gi 488289759 216 FLNNPQ 221
Cdd:COG0411  240 VRADPR 245
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
3-213 1.39e-46

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: 152.59  E-value: 1.39e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   3 ELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQMGM 82
Cdd:cd03214    1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---RKIAY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  83 VFQhynllenlkiydnvalplkllkekqpekierLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATS 162
Cdd:cd03214   78 VPQ-------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488289759 163 SLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03214  127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-210 2.76e-46

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 154.63  E-value: 2.76e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVY----QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrqq 76
Cdd:COG4525    3 MLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 qqqmGMVFQHYNLLENLKIYDNVALPLKL--LKEKQPEKI-ERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:COG4525   79 ----GVVFQKDALLPWLNVLDNVAFGLRLrgVPKAERRARaEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKG 210
Cdd:COG4525  155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
1-215 8.20e-46

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 152.34  E-value: 8.20e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVY-QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQ 79
Cdd:PRK10908   1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLENLKIYDNVALPLkLLKEKQPEKIER----LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK10908  81 IGMIFQDHHLLMDRTVYDNVAIPL-IIAGASGDDIRRrvsaALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 156 LCDEATSSLDEENTESVVRLLhkthQEFRP---TIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLF----EEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
9-222 9.74e-46

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: 159.46  E-value: 9.74e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   9 KVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLmeQPSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVFQH- 86
Cdd:COG4172  294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLaLLRL--IPSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDp 371
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  87 YNLLeN--LKIYDNVALPLKLL-----KEKQPEKIERLLTFV----DMAHKaeaYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:COG4172  372 FGSL-SprMTVGQIIAEGLRVHgpglsAAERRARVAEALEEVgldpAARHR---YPHEFSGGQRQRIAIARALILEPKLL 447
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 156 LCDEATSSLDeentESV----VRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQ 222
Cdd:COG4172  448 VLDEPTSALD----VSVqaqiLDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVeqgptEQVFDAPQH 519
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
2-224 2.21e-45

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: 151.33  E-value: 2.21e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHaLKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrqqqQQMG 81
Cdd:cd03299    1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK-----RDIS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIERLLT---FVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:cd03299   75 YVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEiaeMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQYE 224
Cdd:cd03299  155 EPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIqvgkpEEVFKKPKNEF 225
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
2-215 2.09e-44

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: 156.46  E-value: 2.09e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVY-QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqM 80
Cdd:COG4988  337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ---I 413
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLL-----ENLKIYDNVAlplkllkekQPEKIERLLTFVDMAHKAEAYP-----------AQLSGGEKQRVSI 144
Cdd:COG4988  414 AWVPQNPYLFagtirENLRLGRPDA---------SDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLAL 484
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEfRpTIFFVSHELETVKRlCNRILVMEKGQLIGE 215
Cdd:COG4988  485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG-R-TVILITHRLALLAQ-ADRILVLDDGRIVEQ 552
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
2-215 7.36e-44

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: 145.26  E-value: 7.36e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQqqMG 81
Cdd:cd03216    1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAG--IA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQhynllenlkiydnvalplkllkekqpekierlltfvdmahkaeaypaqLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:cd03216   79 MVYQ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPT 110
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488289759 162 SSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:cd03216  111 AALTPAEVERLFKVIRRLRAQGV-AVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
2-222 1.05e-43

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 147.88  E-value: 1.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLM--EQPS---EGEIRIDGRNVqtFSKK----E 72
Cdd:COG1117   12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDI--YDPDvdvvE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  73 VRqqqQQMGMVFQHYNLLeNLKIYDNVALPLKLLKEKQP----EKIERLLTFV----DMAHKAEAYPAQLSGGEKQRVSI 144
Cdd:COG1117   90 LR---RRVGMVFQKPNPF-PKSIYDNVAYGLRLHGIKSKseldEIVEESLRKAalwdEVKDRLKKSALGLSGGQQQRLCI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRLCNRILVMEKGQLIgEF------LN 218
Cdd:COG1117  166 ARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELV-EFgpteqiFT 242

                 ....
gi 488289759 219 NPQQ 222
Cdd:COG1117  243 NPKD 246
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
2-213 1.74e-43

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: 146.11  E-value: 1.74e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskkEVRQQQQQ 79
Cdd:cd03263    1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAARQS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLENLKIYDNVAL--PLKLLKEKQ-PEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:cd03263   77 LGYCPQFDALFDELTVREHLRFyaRLKGLPKSEiKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEfrPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03263  157 LDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLR 211
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
6-215 2.17e-43

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 147.53  E-value: 2.17e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   6 NVSKVYQE-----THA----LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:PRK10419   8 GLSHHYAHgglsgKHQhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVFQHYNLLENLK--IYDNVALPLKLL----KEKQPEKIERLLTFVDMAHK-AEAYPAQLSGGEKQRVSIARALS 149
Cdd:PRK10419  88 RRDIQMVFQDSISAVNPRktVREIIREPLRHLlsldKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALA 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 150 RNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
2-227 2.43e-43

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 150.10  E-value: 2.43e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQMG 81
Cdd:PRK09452  15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-----HVPAENRHVN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIERL---LTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:PRK09452  90 TVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVmeaLRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLigEFLNNPQQYEEEP 227
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI--EQDGTPREIYEEP 236
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-216 2.73e-43

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 152.48  E-value: 2.73e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVrqQQQQM 80
Cdd:COG1129    4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDA--QAAGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVAL---PLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:COG1129   82 AIIHQELNLVPNLSVAENIFLgrePRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGEF 216
Cdd:COG1129  162 LILDEPTASLTEREVERLFRIIRRLKAQGV-AIIYISHRLDEVFEIADRVTVLRDGRLVGTG 222
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
2-221 1.23e-42

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 145.11  E-value: 1.23e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNV----------QTFSKK 71
Cdd:PRK10619   6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlKVADKN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  72 EVRQQQQQMGMVFQHYNLLENLKIYDNV-ALPLKLL---KEKQPEKIERLLTFVDMAHKAEA-YPAQLSGGEKQRVSIAR 146
Cdd:PRK10619  86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLglsKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIAR 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 147 ALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQL-----IGEFLNNPQ 221
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIeeegaPEQLFGNPQ 244
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
19-213 2.99e-42

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: 146.78  E-value: 2.99e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  19 NIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQ-----TFSKKEVRQqqqqMGMVFQHYNLLENL 93
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdsargIFLPPHRRR----IGYVFQEARLFPHL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  94 KIYDNVALPLK-LLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESV 172
Cdd:COG4148   93 SVRGNLLYGRKrAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 488289759 173 VRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG4148  173 LPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
2-213 3.25e-42

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: 150.69  E-value: 3.25e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQ 79
Cdd:COG4987  334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR---RR 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHY-----NLLENLKIydnvALPlkllkEKQPEKIERLLTFVDMAHKAEAYP-----------AQLSGGEKQRVS 143
Cdd:COG4987  411 IAVVPQRPhlfdtTLRENLRL----ARP-----DATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLA 481
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 144 IARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEfRpTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:COG4987  482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG-R-TVLLITHRLAGLER-MDRILVLEDGRIV 548
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1-215 3.54e-42

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 149.41  E-value: 3.54e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqQQQM 80
Cdd:COG3845    5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAI--ALGI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVAL---PLKLLKEKQPEKIERLLTF-------VDmahkAEAYPAQLSGGEKQRVSIARALSR 150
Cdd:COG3845   83 GMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELserygldVD----PDAKVEDLSVGEQQRVEILKALYR 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:COG3845  159 GARILILDEPTAVLTPQEADELFEILRRLAAEGK-SIIFITHKLREVMAIADRVTVLRRGKVVGT 222
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
2-212 3.64e-42

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: 141.20  E-value: 3.64e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHA--LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQ 79
Cdd:cd03246    1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG---DH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLENlKIYDNValplkllkekqpekierlltfvdmahkaeaypaqLSGGEKQRVSIARALSRNPKWLLCDE 159
Cdd:cd03246   78 VGYLPQDDELFSG-SIAENI----------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488289759 160 ATSSLDEENTESVVRLLhKTHQEFRPTIFFVSHELETVKRlCNRILVMEKGQL 212
Cdd:cd03246  123 PNSHLDVEGERALNQAI-AALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
17-220 1.85e-41

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: 141.06  E-value: 1.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkevRQQQQQMgMVFQHYNLLENLKIY 96
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-------EPGPDRM-VVFQNYSLLPWLTVR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   97 DNVALPLK-----LLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTES 171
Cdd:TIGR01184  73 ENIALAVDrvlpdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488289759  172 VVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKG--QLIGEFLNNP 220
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGpaANIGQILEVP 203
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
2-213 5.71e-41

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: 139.55  E-value: 5.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQEThalkNIHFSVQL--GEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqTFSKKEVRQqqqq 79
Cdd:cd03298    1 VRLDKIRFSYGEQ----PMHFDLTFaqGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRP---- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLENLKIYDNVAL---PLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:cd03298   72 VSMLFQENNLFAHLTVEQNVGLglsPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03298  152 LDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
2-213 6.30e-41

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 143.32  E-value: 6.30e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevrqQQQQMG 81
Cdd:PRK11432   7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI-----QQRDIC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIERL---LTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:PRK11432  82 MVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVkeaLELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
14-237 7.34e-41

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: 142.94  E-value: 7.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   14 THALKnIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKK-EVRQQQQQMGMVFQHYNLLEN 92
Cdd:TIGR02142  11 DFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGYVFQEARLFPH 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   93 LKIYDNVALPLKLLKEKQ----PEKIERLLtfvDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEEN 168
Cdd:TIGR02142  90 LSVRGNLRYGMKRARPSErrisFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  169 TESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGEflNNPQQYEEEP-LSYLEKVERS 237
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA--GPIAEVWASPdLPWLAREDQG 234
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
2-215 8.74e-41

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 140.92  E-value: 8.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRnvqTFSKKEVRQQQQQ 79
Cdd:PRK13635   6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVRRQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHY-NLLENLKIYDNVALPLKLLKEKQPEKIERL---LTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK13635  83 VGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVdqaLRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRlCNRILVMEKGQLIGE 215
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
2-213 1.30e-40

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: 138.90  E-value: 1.30e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETH-ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQM 80
Cdd:cd03254    3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLR---SMI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLL-----ENLKIYDNVAlplKLLKEKQPEKIERLLTFVDmaHKAEAYPAQ-------LSGGEKQRVSIARAL 148
Cdd:cd03254   80 GVVLQDTFLFsgtimENIRLGRPNA---TDEEVIEAAKEAGAHDFIM--KLPNGYDTVlgenggnLSQGERQLLAIARAM 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 149 SRNPKWLLCDEATSSLDEEnTESVV-----RLLHKThqefrpTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:cd03254  155 LRDPKILILDEATSNIDTE-TEKLIqealeKLMKGR------TSIIIAHRLSTIKN-ADKILVLDDGKII 216
cbiO PRK13637
energy-coupling factor transporter ATPase;
2-234 2.58e-40

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 139.80  E-value: 2.58e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqTFSKKEVRQQ 76
Cdd:PRK13637   3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVFQH--YNLLENlKIYDNVALPLKLLKEKQPEKIERL--------LTFVDMAHKAeayPAQLSGGEKQRVSIAR 146
Cdd:PRK13637  82 RKKVGLVFQYpeYQLFEE-TIEKDIAFGPINLGLSEEEIENRVkramnivgLDYEDYKDKS---PFELSGGQKRRVAIAG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 147 ALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLigEFLNNPQQYEEE 226
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC--ELQGTPREVFKE 235

                 ....*...
gi 488289759 227 pLSYLEKV 234
Cdd:PRK13637 236 -VETLESI 242
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
2-213 4.74e-40

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: 137.34  E-value: 4.74e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQ 79
Cdd:cd03245    3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLR---RN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLeNLKIYDNVALPLKLLKEkqpEKIERLLTFVDMAHKAEAYP-----------AQLSGGEKQRVSIARAL 148
Cdd:cd03245   80 IGYVPQDVTLF-YGTLRDNITLGAPLADD---ERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARAL 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 149 SRNPKWLLCDEATSSLDEENTEsvvRLLHKTHQEFRP-TIFFVSHELeTVKRLCNRILVMEKGQLI 213
Cdd:cd03245  156 LNDPPILLLDEPTSAMDMNSEE---RLKERLRQLLGDkTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
2-213 4.98e-40

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: 137.62  E-value: 4.98e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQ--ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQ 79
Cdd:cd03252    1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLR---RQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHyNLLENLKIYDNVALPLKLLKEKQPEKIERLLTFVDMAHK-AEAYP-------AQLSGGEKQRVSIARALSRN 151
Cdd:cd03252   78 VGVVLQE-NVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISElPEGYDtivgeqgAGLSGGQRQRIAIARALIHN 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 152 PKWLLCDEATSSLDEENTESVVRLLHKTHQEfrPTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:cd03252  157 PRILIFDEATSALDYESEHAIMRNMHDICAG--RTVIIIAHRLSTVKN-ADRIIVMEKGRIV 215
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
2-215 7.01e-40

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: 136.73  E-value: 7.01e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfsKKEVRQQQQQMG 81
Cdd:cd03265    1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV----VREPREVRRRIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:cd03265   77 IVFQDLSVDDELTGWENLYIHARLYgvpGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:cd03265  157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
1-229 1.41e-39

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 140.36  E-value: 1.41e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQM 80
Cdd:PRK11607  19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVPPYQRPI 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVALPLK---LLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:PRK11607  94 NMMFQSYALFPHMTVEQNIAFGLKqdkLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 158 DEATSSLDEENTE----SVVRLLHKTHQefrpTIFFVSHELETVKRLCNRILVMEKGQL--IGEflnnPQQYEEEPLS 229
Cdd:PRK11607 174 DEPMGALDKKLRDrmqlEVVDILERVGV----TCVMVTHDQEEAMTMAGRIAIMNRGKFvqIGE----PEEIYEHPTT 243
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
14-213 1.67e-39

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: 135.46  E-value: 1.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  14 THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskkevRQQQQQMGMVFQH--YNLLE 91
Cdd:cd03226   13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERRKSIGYVMQDvdYQLFT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  92 NlKIYDNVALPLKLLKEKqPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTES 171
Cdd:cd03226   87 D-SVREELLLGLKELDAG-NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488289759 172 VVRLLhKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03226  165 VGELI-RELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
1-227 1.87e-39

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 143.71  E-value: 1.87e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQ- 75
Cdd:PRK10535   4 LLELKDIRRSYPsgeeQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQl 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  76 QQQQMGMVFQHYNLLENLKIYDNVALPL---KLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:PRK10535  84 RREHFGFIFQRYHLLSHLTAAQNVEVPAvyaGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHElETVKRLCNRILVMEKGQLIGeflNNPQQYEEEP 227
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHD-PQVAAQAERVIEIRDGEIVR---NPPAQEKVNV 233
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-222 9.34e-39

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 135.63  E-value: 9.34e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVY---QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGrnvQTFSKKEVRQQQ 77
Cdd:PRK13650   4 IIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVWDIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  78 QQMGMVFQHY-NLLENLKIYDNVA-------LPLKLLKEKqpekIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALS 149
Cdd:PRK13650  81 HKIGMVFQNPdNQFVGATVEDDVAfglenkgIPHEEMKER----VNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 150 RNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKrLCNRILVMEKGQLigEFLNNPQQ 222
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV--ESTSTPRE 226
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
1-213 1.04e-38

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: 134.44  E-value: 1.04e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEG-EIRIDGRnvqTFSKKEVRQQQQQ 79
Cdd:COG1119    3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGE---RRGGEDVWELRKR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMV--FQHYNLLENLKI--------YDNVALPLKLlKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALS 149
Cdd:COG1119   80 IGLVspALQLRFPRDETVldvvlsgfFDSIGLYREP-TDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 150 RNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG1119  159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
1-221 1.93e-38

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 134.73  E-value: 1.93e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGrnvQTFSKKEVRQQQQ 78
Cdd:PRK13632   7 MIKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG---ITISKENLKEIRK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  79 QMGMVFQHY-NLLENLKIYDNVALPL---KLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:PRK13632  84 KIGIIFQNPdNQFIGATVEDDIAFGLenkKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKrLCNRILVMEKGQLIG-----EFLNNPQ 221
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAqgkpkEILNNKE 234
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
2-213 2.00e-38

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: 133.51  E-value: 2.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETH--ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqq 79
Cdd:cd03251    1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHyNLLENLKIYDNVALPLKllkEKQPEKIErlltfvDMAHKAEAYP-----------------AQLSGGEKQRV 142
Cdd:cd03251   78 IGLVSQD-VFLFNDTVAENIAYGRP---GATREEVE------EAARAANAHEfimelpegydtvigergVKLSGGQRQRI 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 143 SIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKThQEFRpTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:cd03251  148 AIARALLKDPPILILDEATSALDTESERLVQAALERL-MKNR-TTFVIAHRLSTIEN-ADRIVVLEDGKIV 215
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
1-231 2.19e-38

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 134.37  E-value: 2.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLM---EQPSEGEIRIDGRNVQTFSK--KEVRQ 75
Cdd:PRK09984   4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlaRDIRK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  76 QQQQMGMVFQHYNLLENLKIYDNVALP-----------LKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSI 144
Cdd:PRK09984  84 SRANTGYIFQQFNLVNRLSVLENVLIGalgstpfwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIgeFLNNPQQYE 224
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVF--YDGSSQQFD 241

                 ....*..
gi 488289759 225 EEPLSYL 231
Cdd:PRK09984 242 NERFDHL 248
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
2-213 4.42e-38

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: 132.74  E-value: 4.42e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQ-ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQM 80
Cdd:cd03253    1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLR---RAI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHyNLLENLKIYDNVAL--PlkllkEKQPEKIERLLTFVDMAHKAEAYPAQ-----------LSGGEKQRVSIARA 147
Cdd:cd03253   78 GVVPQD-TVLFNDTIGYNIRYgrP-----DATDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARA 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 148 LSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEfRPTIfFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:cd03253  152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSKG-RTTI-VIAHRLSTIVN-ADKIIVLKDGRIV 214
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
16-220 5.46e-38

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 136.70  E-value: 5.46e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQ-QQQQMGMVFQHYNLLENLK 94
Cdd:PRK10070  43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvRRKKIAMVFQSFALMPHMT 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  95 IYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD----EE 167
Cdd:PRK10070 123 VLDNTAFGMELAginAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTE 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 168 NTESVVRLLHKtHQEfrpTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNP 220
Cdd:PRK10070 203 MQDELVKLQAK-HQR---TIVFISHDLDEAMRIGDRIAIMQNGEVVqvgtpDEILNNP 256
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
2-216 1.26e-37

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: 131.08  E-value: 1.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETH--ALKNIHFSVQLGEIVGIVGKSGSGKSTL-LRLLNLMEqPSEGEIRIDGRNVQTFSKKEVRqqqQ 78
Cdd:cd03244    3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLlLALFRLVE-LSSGSILIDGVDISKIGLHDLR---S 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  79 QMGMVFQHYNLL-----ENLKIYD-------NVALPLKLLKE---KQPEKIErlltfvdmaHKAEAYPAQLSGGEKQRVS 143
Cdd:cd03244   79 RISIIPQDPVLFsgtirSNLDPFGeysdeelWQALERVGLKEfveSLPGGLD---------TVVEEGGENLSVGQRQLLC 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 144 IARALSRNPKWLLCDEATSSLDEENTESVVRLLhktHQEFR-PTIFFVSHELETVKRlCNRILVMEKGQLIgEF 216
Cdd:cd03244  150 LARALLRKSKILVLDEATASVDPETDALIQKTI---REAFKdCTVLTIAHRLDTIID-SDRILVLDKGRVV-EF 218
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
2-222 1.28e-37

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 132.27  E-value: 1.28e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVY---------QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskKE 72
Cdd:COG4167    5 LEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY---GD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  73 VRQQQQQMGMVFQHYN--LLENLKIYDNVALPLKL---LKEKQ-PEKIERLLTFVDM-AHKAEAYPAQLSGGEKQRVSIA 145
Cdd:COG4167   82 YKYRCKHIRMIFQDPNtsLNPRLNIGQILEEPLRLntdLTAEErEERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 146 RALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNP 220
Cdd:COG4167  162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVeygktAEVFANP 241

                 ..
gi 488289759 221 QQ 222
Cdd:COG4167  242 QH 243
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
2-213 1.65e-37

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: 131.12  E-value: 1.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVY---QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqq 78
Cdd:cd03249    1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  79 qMGMVFQHYNLLENlKIYDNVALPLKLLKEKQPEKIerlltfvdmAHKAEAYP-----------------AQLSGGEKQR 141
Cdd:cd03249   79 -IGLVSQEPVLFDG-TIAENIRYGKPDATDEEVEEA---------AKKANIHDfimslpdgydtlvgergSQLSGGQKQR 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 142 VSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:cd03249  148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
1-200 3.02e-37

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: 129.52  E-value: 3.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskKEVRQQQQQM 80
Cdd:COG4133    2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR----DAREDYRRRL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFqHYNLL-ENLKIYDNVALPLKLLKEKQP-EKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:COG4133   78 AYLG-HADGLkPELTVRENLRFWAALYGLRADrEAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 488289759 159 EATSSLDEENTESVVRLLHKtHQEFRPTIFFVSH---ELETVKRL 200
Cdd:COG4133  157 EPFTALDAAGVALLAELIAA-HLARGGAVLLTTHqplELAAARVL 200
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
2-213 1.84e-36

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: 127.69  E-value: 1.84e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGeIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfsKKEVRQQQQQMG 81
Cdd:cd03264    1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLRRRIG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVALpLKLLKE----KQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:cd03264   76 YLPQEFGVYPNFTVREFLDY-IAWLKGipskEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEfrpTIFFVS-HELETVKRLCNRILVMEKGQLI 213
Cdd:cd03264  155 DEPTAGLDPEERIRFRNLLSELGED---RIVILStHIVEDVESLCNQVAVLNKGKLV 208
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
6-214 3.01e-36

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 128.64  E-value: 3.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   6 NVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIrIDGRNVQTFSKKEVRqqqqqmgMVFQ 85
Cdd:PRK11247  17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTR-------LMFQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  86 HYNLLENLKIYDNVALPlklLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:PRK11247  89 DARLLPWKKVIDNVGLG---LKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488289759 166 E----ENTESVVRLLhkthQEFRPTIFFVSHELETVKRLCNRILVMEKGQlIG 214
Cdd:PRK11247 166 AltriEMQDLIESLW----QQHGFTVLLVTHDVSEAVAMADRVLLIEEGK-IG 213
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
4-210 3.29e-36

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 131.31  E-value: 3.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   4 LVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQMGMV 83
Cdd:PRK11000   6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-----DVPPAERGVGMV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  84 FQHYNLLENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEA 160
Cdd:PRK11000  81 FQSYALYPHLSVAENMSFGLKLAGAKKEEinqRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 161 TSSLDeenteSVVRL-----LHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKG 210
Cdd:PRK11000 161 LSNLD-----AALRVqmrieISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAG 210
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
1-211 3.63e-36

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: 127.55  E-value: 3.63e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVY-------QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQT-FSKKE 72
Cdd:COG4778    4 LLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVdLAQAS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  73 VRQ----QQQQMGMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHK-AEAYPAQLSGGEKQRVSI 144
Cdd:COG4778   84 PREilalRRRTIGYVSQFLRVIPRVSALDVVAEPLLERgvdREEARARARELLARLNLPERlWDLPPATFSGGEQQRVNI 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:COG4778  164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGT-AIIGIFHDEEVREAVADRVVDVTPFS 229
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
15-210 3.95e-36

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 130.08  E-value: 3.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  15 HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVFQH-YNLLE-N 92
Cdd:PRK11308  29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpYGSLNpR 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  93 LKIYDNVALPL----KLLKEKQPEKIERLLTFVDM-AHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:PRK11308 109 KKVGQILEEPLlintSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVS 188
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488289759 168 NTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVM------EKG 210
Cdd:PRK11308 189 VQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMylgrcvEKG 237
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
12-222 5.27e-36

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: 133.27  E-value: 5.27e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  12 QETHALKNIHFSVQLGEIVGIVGKSGSGKS-TLLRLLNLMEQPS---EGEIRIDGRNVQTFSKKEVRQ-QQQQMGMVFQh 86
Cdd:COG4172   21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDLLGLSERELRRiRGNRIAMIFQ- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  87 ynllE-----N--LKIYDNVALPLKL---LKEKQP-EKIERLLTFV---DMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:COG4172  100 ----EpmtslNplHTIGKQIAEVLRLhrgLSGAAArARALELLERVgipDPERRLDAYPHQLSGGQRQRVMIAMALANEP 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQ 222
Cdd:COG4172  176 DLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVeqgptAELFAAPQH 250
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
16-216 2.62e-35

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 132.01  E-value: 2.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQMGMVFQHYNLLeNLKI 95
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLR---RNIAVVFQDAGLF-NRSI 425
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  96 YDNvalpLKLLKEKQpekierllTFVDMAHKAEAYPA--------------------QLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK13657 426 EDN----IRVGRPDA--------TDEEMRAAAERAQAhdfierkpdgydtvvgergrQLSGGERQRLAIARALLKDPPIL 493
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 156 LCDEATSSLDEEnTESVVRLLHKTHQEFRpTIFFVSHELETVkRLCNRILVMEKGQLI--GEF 216
Cdd:PRK13657 494 ILDEATSALDVE-TEAKVKAALDELMKGR-TTFIIAHRLSTV-RNADRILVFDNGRVVesGSF 553
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
1-215 4.47e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 125.96  E-value: 4.47e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQE-THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtFSKKEVRQQQQQ 79
Cdd:PRK13639   1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVRKT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHY-NLLENLKIYDNVA---LPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK13639  80 VGIVFQNPdDQLFAPTVEEDVAfgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEfRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
1-210 5.35e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 125.63  E-value: 5.35e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQ--ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqq 78
Cdd:PRK13648   7 IIVFKNVSFQYQsdASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH-- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  79 qMGMVFQH--YNLLENLKIYD------NVALPLKLLKEKQPEKIERlltfVDMAHKAEAYPAQLSGGEKQRVSIARALSR 150
Cdd:PRK13648  85 -IGIVFQNpdNQFVGSIVKYDvafgleNHAVPYDEMHRRVSEALKQ----VDMLERADYEPNALSGGQKQRVAIAGVLAL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHEL-ETVKrlCNRILVMEKG 210
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLsEAME--ADHVIVMNKG 218
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
2-216 5.61e-35

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


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 123.87  E-value: 5.61e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKevrqqQQQMG 81
Cdd:cd03268    1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA-----LRRIG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVALPLKLLKEKQpEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:cd03268   76 ALIEAPGFYPNLTARENLRLLARLLGIRK-KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 162 SSLDEENTESVVRLLHKtHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGEF 216
Cdd:cd03268  155 NGLDPDGIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
1-213 8.39e-35

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 124.88  E-value: 8.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevRQQQQQM 80
Cdd:PRK13548   2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP---AELARRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVAL---PLKLLKEKQPEKIERLLTFVDMAHKAE-AYPaQLSGGEKQRVSIARAL------SR 150
Cdd:PRK13548  79 AVLPQHSSLSFPFTVEEVVAMgraPHGLSRAEDDALVAAALAQVDLAHLAGrDYP-QLSGGEQQRVQLARVLaqlwepDG 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
9-229 3.54e-34

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 128.28  E-value: 3.54e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   9 KVYQETHALKNIHFSVQLGEIVGIVGKSGSGKST----LLRLLNlmeqpSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVF 84
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVF 368
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  85 QHYN--LLENLKIYDNVALPLK-----LLKEKQPEKIERLLTFVDM-AHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:PRK15134 369 QDPNssLNPRLNVLQIIEEGLRvhqptLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLII 448
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE-----FLNNPQQ-YEEEPLS 229
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQgdcerVFAAPQQeYTRQLLA 527
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
14-213 6.20e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 123.03  E-value: 6.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  14 THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtFSKKEVRQQQQQMGMVFQHY-NLLEN 92
Cdd:PRK13636  19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKLRESVGMVFQDPdNQLFS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  93 LKIYDNV---ALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENT 169
Cdd:PRK13636  98 ASVYQDVsfgAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 488289759 170 ESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
2-213 9.68e-34

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: 127.53  E-value: 9.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqq 79
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQ--- 407
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   80 MGMVFQHYNLLeNLKIYDNVALplKLLKEKQPEKIER------LLTFVDMAHKAEAYP-----AQLSGGEKQRVSIARAL 148
Cdd:TIGR02203 408 VALVSQDVVLF-NDTIANNIAY--GRTEQADRAEIERalaaayAQDFVDKLPLGLDTPigengVLLSGGQRQRLAIARAL 484
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759  149 SRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEfRPTIfFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQG-RTTL-VIAHRLSTIEK-ADRIVVMDDGRIV 546
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
1-213 1.03e-33

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 121.76  E-value: 1.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevRQQQQQM 80
Cdd:COG4559    1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSP---WELARRR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVAL---PLKLLKEKQPEKIERLLTFVDMAHKAE-AYPaQLSGGEKQRVSIARAL-------S 149
Cdd:COG4559   78 AVLPQHSSLAFPFTVEEVVALgraPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLaqlwepvD 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 150 RNPKWLLCDEATSSLDEENTESVVRLLHK-THQEFrpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG4559  157 GGPRWLFLDEPTSALDLAHQHAVLRLARQlARRGG--GVVAVLHDLNLAAQYADRILLLHQGRLV 219
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
2-213 1.24e-33

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 121.49  E-value: 1.24e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLM-----EQPSEGEIRIDGRNVqtFSKK----E 72
Cdd:PRK14267   5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--YSPDvdpiE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  73 VRQQqqqMGMVFQHYNLLENLKIYDNVALPLKL-----LKEKQPEKIERLLT----FVDMAHKAEAYPAQLSGGEKQRVS 143
Cdd:PRK14267  83 VRRE---VGMVFQYPNPFPHLTIYDNVAIGVKLnglvkSKKELDERVEWALKkaalWDEVKDRLNDYPSNLSGGQRQRLV 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 144 IARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLI 227
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
12-212 1.25e-33

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 121.04  E-value: 1.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  12 QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQ-QQQQMGMVFQHYNLL 90
Cdd:PRK10584  21 HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlRAKHVGFVFQSFMLI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  91 ENLKIYDNVALPLKLLKEKQPEKIER---LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:PRK10584 101 PTLNALENVELPALLRGESSRQSRNGakaLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 488289759 168 NTESVVRLLHKTHQEFRPTIFFVSHELETVKRlCNRILVMEKGQL 212
Cdd:PRK10584 181 TGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1-214 1.63e-33

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 123.80  E-value: 1.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQ-ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrqqqQQ 79
Cdd:PRK11650   3 GLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-----RD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLENLKIYDNVALPLKLLKEKQPEKIERlltfVDMAHKA---EAY----PAQLSGGEKQRVSIARALSRNP 152
Cdd:PRK11650  78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEER----VAEAARIlelEPLldrkPRELSGGQRQRVAMGRAIVREP 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 153 KWLLCDEATSSLDeentesvVRL-------LHKTHQEFRPTIFFVSH-ELETVKrLCNRILVMEKGQL--IG 214
Cdd:PRK11650 154 AVFLFDEPLSNLD-------AKLrvqmrleIQRLHRRLKTTSLYVTHdQVEAMT-LADRVVVMNGGVAeqIG 217
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
1-195 2.13e-33

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 120.96  E-value: 2.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrqqqqqm 80
Cdd:PRK11248   1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:PRK11248  73 GVVFQNEGLLPWRNVQDNVAFGLQLAgveKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELE 195
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIE 190
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
1-215 2.27e-33

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: 119.78  E-value: 2.27e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQ----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskKEVRQQ 76
Cdd:cd03266    1 MITADALTKRFRdvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAEA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVFQHYNLLENLKIYDNVALPLKL--LKEKQPE-KIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:cd03266   77 RRRLGFVSDSTGLYDRLTARENLEYFAGLygLKGDELTaRLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLhKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:cd03266  157 VLLLDEPTTGLDVMATRALREFI-RQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
16-212 2.38e-33

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: 118.69  E-value: 2.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqmGMVF-----QHYNLL 90
Cdd:cd03215   15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRA----GIAYvpedrKREGLV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  91 ENLKIYDNVALPlkllkekqpekierlltfvdmahkaeaypAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTE 170
Cdd:cd03215   91 LDLSVAENIALS-----------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488289759 171 SVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:cd03215  142 EIYRLIRELADAGK-AVLLISSELDELLGLCDRILVMYEGRI 182
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
2-213 2.55e-33

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: 126.47  E-value: 2.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHA-LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqM 80
Cdd:COG5265  358 VRFENVSFGYDPERPiLKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA---I 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHyNLLENLKIYDNVAL--PlkllkEKQPEKIER------LLTFVdmAHKAEAYPAQ-------LSGGEKQRVSIA 145
Cdd:COG5265  435 GIVPQD-TVLFNDTIAYNIAYgrP-----DASEEEVEAaaraaqIHDFI--ESLPDGYDTRvgerglkLSGGEKQRVAIA 506
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 146 RALSRNPKWLLCDEATSSLD---EENTESVVRLLHKTHqefrpTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:COG5265  507 RTLLKNPPILIFDEATSALDsrtERAIQAALREVARGR-----TTLVIAHRLSTIVD-ADEILVLEAGRIV 571
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
2-222 5.30e-33

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 120.02  E-value: 5.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLM-----EQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:PRK14247   4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRRR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQqmgMVFQHYNLLENLKIYDNVALPLKL---------LKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARA 147
Cdd:PRK14247  84 VQ---MVFQIPNPIPNLSIFENVALGLKLnrlvkskkeLQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 148 LSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQQ 222
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVewgptREVFTNPRH 238
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
2-207 9.08e-33

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: 124.32  E-value: 9.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    2 IELVNVSKVYQ-ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQM 80
Cdd:TIGR02857 322 LEFSGVSVAYPgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWR---DQI 398
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   81 GMVFQHYNLLENlKIYDNVALPlklLKEKQPEKIERLLTFVDMAHKAEAYP-----------AQLSGGEKQRVSIARALS 149
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLA---RPDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFL 474
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759  150 RNPKWLLCDEATSSLDEEnTESVV----RLLHKTHqefrpTIFFVSHELETVkRLCNRILVM 207
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAE-TEAEVlealRALAQGR-----TVLLVTHRLALA-ALADRIVVL 529
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
2-213 9.62e-33

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: 118.15  E-value: 9.62e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskkevrQQQQQMG 81
Cdd:cd03269    1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-------AARNRIG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLKIYDNVAL--PLKLLKEKQPEK-IERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:cd03269   74 YLPEERGLYPKMKVIDQLVYlaQLKGLKKEEARRrIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03269  154 EPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRAV 207
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
3-213 1.56e-32

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 119.00  E-value: 1.56e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   3 ELVNVSKVY---QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRnVQTFSKKEVR----Q 75
Cdd:PRK14246   9 DVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK-VLYFGKDIFQidaiK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  76 QQQQMGMVFQHYNLLENLKIYDNVALPLKL--LKEKQP------EKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARA 147
Cdd:PRK14246  88 LRKEVGMVFQQPNPFPHLSIYDNIAYPLKShgIKEKREikkiveECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARA 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 148 LSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELV 231
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
16-221 2.00e-32

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 120.20  E-value: 2.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLMEQpSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVFQH--YNLLEN 92
Cdd:PRK15079  36 AVDGVTLRLYEGETLGVVGESGCGKSTFARaIIGLVKA-TDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPR 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  93 LKIYDNVALPL-----KLLKEKQPEKIERLLTFVDM-AHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDE 166
Cdd:PRK15079 115 MTIGEIIAEPLrtyhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 167 ENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQ 221
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVelgtyDEVYHNPL 254
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
2-212 3.38e-32

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: 117.19  E-value: 3.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQ---ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqq 78
Cdd:cd03248   12 VKFQNVTFAYPtrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  79 qMGMVFQHYNLLENlKIYDNVALPLkllkekQPEKIERLLTFVDMAHKAEAYP--------------AQLSGGEKQRVSI 144
Cdd:cd03248   90 -VSLVGQEPVLFAR-SLQDNIAYGL------QSCSFECVKEAAQKAHAHSFISelasgydtevgekgSQLSGGQKQRVAI 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQefRPTIFFVSHELETVKRlCNRILVMEKGQL 212
Cdd:cd03248  162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
cbiO PRK13644
energy-coupling factor transporter ATPase;
1-215 4.51e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 118.17  E-value: 4.51e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQE-THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSK-KEVRqqqQ 78
Cdd:PRK13644   1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIR---K 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  79 QMGMVFQH-------YNLLENLKI-YDNVALPlkllkekqPEKIERLltfVDMA---HKAEAY----PAQLSGGEKQRVS 143
Cdd:PRK13644  78 LVGIVFQNpetqfvgRTVEEDLAFgPENLCLP--------PIEIRKR---VDRAlaeIGLEKYrhrsPKTLSGGQGQCVA 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 144 IARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVkRLCNRILVMEKGQLIGE 215
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEEL-HDADRIIVMDRGKIVLE 216
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
2-213 6.16e-32

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 122.24  E-value: 6.16e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQ 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR---QA 415
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLL-----ENLKIydnvALPlkllkEKQPEKIERLLTFVDMAHKAEAYPA----------QLSGGEKQRVSI 144
Cdd:PRK11160 416 ISVVSQRVHLFsatlrDNLLL----AAP-----NASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGI 486
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEfrPTIFFVSHELETVKRLcNRILVMEKGQLI 213
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN--KTVLMITHRLTGLEQF-DRICVMDNGQII 552
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
2-211 1.82e-31

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: 115.22  E-value: 1.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkevRQQQQQ-- 79
Cdd:cd03224    1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT-------GLPPHEra 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 ---MGMVFQHYNLLENLKIYDNVALPLKLL-KEKQPEKIERLLT-FVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:cd03224   74 ragIGYVPEGRRIFPELTVEENLLLGAYARrRAKRKARLERVYElFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 155 LLCDEATSSLdeenTESVVRLLHKTHQEFRP---TIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:cd03224  154 LLLDEPSEGL----APKIVEEIFEAIRELRDegvTILLVEQNARFALEIADRAYVLERGR 209
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
2-213 3.13e-31

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 120.51  E-value: 3.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQ--ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQ 79
Cdd:PRK11176 342 IEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLR---NQ 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLeNLKIYDNVALPLKllKEKQPEKIERLLTfvdMAHKAEAYP--------------AQLSGGEKQRVSIA 145
Cdd:PRK11176 419 VALVSQNVHLF-NDTIANNIAYART--EQYSREQIEEAAR---MAYAMDFINkmdngldtvigengVLLSGGQRQRIAIA 492
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 146 RALSRNPKWLLCDEATSSLDeenTESvVRLLHKTHQEFRP--TIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:PRK11176 493 RALLRDSPILILDEATSALD---TES-ERAIQAALDELQKnrTSLVIAHRLSTIEK-ADEILVVEDGEIV 557
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
1-213 4.55e-31

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 114.79  E-value: 4.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVY----------------------QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEI 58
Cdd:COG1134    4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  59 RIDGRNVQTFSkkevrqqqqqMGMVFqHYNL--LENlkIYDNVALpLKLLKEKQPEKIER------LLTFVDMAHKaeAY 130
Cdd:COG1134   84 EVNGRVSALLE----------LGAGF-HPELtgREN--IYLNGRL-LGLSRKEIDEKFDEivefaeLGDFIDQPVK--TY 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 131 paqlSGGEKQRVSIARALSRNPKWLLCDEATSSLDEentesvvRLLHKTHQEFR------PTIFFVSHELETVKRLCNRI 204
Cdd:COG1134  148 ----SSGMRARLAFAVATAVDPDILLVDEVLAVGDA-------AFQKKCLARIRelresgRTVIFVSHSMGAVRRLCDRA 216

                 ....*....
gi 488289759 205 LVMEKGQLI 213
Cdd:COG1134  217 IWLEKGRLV 225
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
1-212 5.76e-31

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 113.91  E-value: 5.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQetHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevrqQQQQM 80
Cdd:PRK10771   1 MLKLTDITWLYH--HLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP-----SRRPV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVAL---P-LKLlKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:PRK10771  74 SMLFQENNLFSHLTVAQNIGLglnPgLKL-NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILL 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
3-216 9.63e-31

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 118.48  E-value: 9.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   3 ELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVrqQQQQMGM 82
Cdd:PRK11288   6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAA--LAAGVAI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  83 VFQHYNLLENLKIYDNV---ALP-------LKLLKEKQPEKIERLLTFVDmahkAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:PRK11288  84 IYQELHLVPEMTVAENLylgQLPhkggivnRRLLNYEAREQLEHLGVDID----PDTPLKYLSIGQRQMVEIAKALARNA 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGEF 216
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGR-VILYVSHRMEEIFALCDAITVFKDGRYVATF 222
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1-213 1.50e-30

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 114.44  E-value: 1.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkevRQQQQQM 80
Cdd:COG4152    1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PEDRRRI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GmvfqhYnLLE------NLKIYDNVA--LPLKLLKEKQ-PEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRN 151
Cdd:COG4152   74 G-----Y-LPEerglypKMKVGEQLVylARLKGLSKAEaKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 152 PKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG4152  148 PELLILDEPFSGLDPVNVELLKDVIRELAAKGT-TVIFSSHQMELVEELCDRIVIINKGRKV 208
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
2-215 1.81e-30

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 114.52  E-value: 1.81e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskkEVRQQQQQMG 81
Cdd:PRK13537   8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS----RARHARQRVG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNL------LENLKIYDN-VALPLKLLKEKQPEkierLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:PRK13537  84 VVPQFDNLdpdftvRENLLVFGRyFGLSAAAARALVPP----LLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 155 LLCDEATSSLDEENT----ESVVRLLHKTHqefrpTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK13537 160 LVLDEPTTGLDPQARhlmwERLRSLLARGK-----TILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
1-165 2.32e-30

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 111.80  E-value: 2.32e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLL--NLMEQPS-EGEIRIDGRNVQTfskkeVRQQQ 77
Cdd:COG4136    1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagTLSPAFSaSGEVLLNGRRLTA-----LPAEQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  78 QQMGMVFQ------HYNLLENLKIydnvALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRN 151
Cdd:COG4136   76 RRIGILFQddllfpHLSVGENLAF----ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
                        170
                 ....*....|....
gi 488289759 152 PKWLLCDEATSSLD 165
Cdd:COG4136  152 PRALLLDEPFSKLD 165
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
17-213 2.81e-30

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: 111.10  E-value: 2.81e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLN--LMEQPSEGEIRIDGRNVqtfSKKEVRQQqqqMGMVFQHYNLLENLK 94
Cdd:cd03213   25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL---DKRSFRKI---IGYVPQDDILHPTLT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  95 IYDNVALPLKLlkekqpekierlltfvdmahkaeaypAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVR 174
Cdd:cd03213   99 VRETLMFAAKL--------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 488289759 175 LLHKTHQEFRpTIFFVSHEL-ETVKRLCNRILVMEKGQLI 213
Cdd:cd03213  153 LLRRLADTGR-TIICSIHQPsSEIFELFDKLLLLSQGRVI 191
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1-225 3.05e-30

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 117.09  E-value: 3.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIdGRNVQT--FSkkevrQQQQ 78
Cdd:COG0488  315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIgyFD-----QHQE 388
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  79 QmgmvfqhynLLENLKIYDNVAlplKLLKEKQPEKI----ERLLTFVDMAHKaeaYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:COG0488  389 E---------LDPDKTVLDELR---DGAPGGTEQEVrgylGRFLFSGDDAFK---PVGVLSGGEKARLALAKLLLSPPNV 453
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 155 LLCDEATSSLDEENTESVVRLLhkthQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIgEFLNNPQQYEE 225
Cdd:COG0488  454 LLLDEPTNHLDIETLEALEEAL----DDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR-EYPGGYDDYLE 519
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
1-215 3.13e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 113.26  E-value: 3.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVY------QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGrnVQTFSKKEVR 74
Cdd:PRK13633   4 MIKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  75 QQQQQMGMVFQHY-NLLENLKIYDNVAL-P--LKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSR 150
Cdd:PRK13633  82 DIRNKAGMVFQNPdNQIVATIVEEDVAFgPenLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRlCNRILVMEKGQLIGE 215
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVME 225
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
6-226 3.29e-30

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 112.56  E-value: 3.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   6 NVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLM-----EQPSEGEIRIDGRNVQTfSKKEVRQQQQQM 80
Cdd:PRK14239  10 DLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYS-PRTDTVDLRKEI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLEnLKIYDNVALPLKL--LKEKQ--PEKIERLL----TFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:PRK14239  89 GMVFQQPNPFP-MSIYENVVYGLRLkgIKDKQvlDEAVEKSLkgasIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRLCNRILVMEKGQLIgEFLN------NPQQYEEE 226
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLI-EYNDtkqmfmNPKHKETE 244
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
2-215 3.45e-30

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 114.54  E-value: 3.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfsKKEVRQQQQQMG 81
Cdd:PRK13536  42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLARARIG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNL------LENLKIYDNValpLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK13536 118 VVPQFDNLdleftvRENLLVFGRY---FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 156 LCDEATSSLDEENT----ESVVRLLHKTHqefrpTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK13536 195 ILDEPTTGLDPHARhliwERLRSLLARGK-----TILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
cbiO PRK13640
energy-coupling factor transporter ATPase;
2-213 4.37e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 112.97  E-value: 4.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETH--ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLN---LMEQPSEGEIRIDGRNVQTFSKKEVRQQ 76
Cdd:PRK13640   6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINgllLPDDNPNSKITVDGITLTAKTVWDIREK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 qqqMGMVFQHY-NLLENLKIYDNVALPLKLLKEKQPEKIE---RLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:PRK13640  86 ---VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKivrDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKrLCNRILVMEKGQLI 213
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLL 222
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
2-214 5.35e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 113.19  E-value: 5.35e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSK-KEVRQ 75
Cdd:PRK13634   3 ITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnKKLKP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  76 QQQQMGMVFQ--HYNLLENLKIYD------NVALPlkllKEKQPEKIERLLTFVDMAHKA-EAYPAQLSGGEKQRVSIAR 146
Cdd:PRK13634  83 LRKKVGIVFQfpEHQLFEETVEKDicfgpmNFGVS----EEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAG 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 147 ALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIG 214
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
2-213 5.81e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 113.26  E-value: 5.81e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSK------ 70
Cdd:PRK13651   3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkekek 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  71 ---------------KEVRQQQQQMGMVFQ--HYNLLENLKIYDNVALPLKLLKEKQpEKIERLLTFVDMAHKAEAY--- 130
Cdd:PRK13651  83 vleklviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKE-EAKKRAAKYIELVGLDESYlqr 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 131 -PAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEK 209
Cdd:PRK13651 162 sPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKD 240

                 ....
gi 488289759 210 GQLI 213
Cdd:PRK13651 241 GKII 244
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
2-211 5.92e-30

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: 108.69  E-value: 5.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDgrnvqtfskkevrqqqqqmg 81
Cdd:cd03221    1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 mvfqhynllENLKIydnvalplkllkekqpekierlltfvdmahkaeAYPAQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:cd03221   61 ---------STVKI---------------------------------GYFEQLSGGEKMRLALAKLLLENPNLLLLDEPT 98
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 488289759 162 SSLDEENTESVVRLLhkthQEFRPTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:cd03221   99 NHLDLESIEALEEAL----KEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
cbiO PRK13642
energy-coupling factor transporter ATPase;
1-215 9.30e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 112.11  E-value: 9.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQ---ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGrnvQTFSKKEVRQQQ 77
Cdd:PRK13642   4 ILEVENLVFKYEkesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  78 QQMGMVFQHY-NLLENLKIYDNVALPLK---LLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:PRK13642  81 RKIGMVFQNPdNQFVGATVEDDVAFGMEnqgIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRlCNRILVMEKGQLIGE 215
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKE 221
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
16-211 1.36e-29

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 112.90  E-value: 1.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  16 ALKNIHFSVQLGEIVGIVGKSGSGKS-TLLRLLNLMEQPS--EGEIRIDGRNVQTFSKKEV-RQQQQQMGMVFQH--YNL 89
Cdd:PRK09473  31 AVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFNGREILNLPEKELnKLRAEQISMIFQDpmTSL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  90 LENLKIYDNVALPLKLLK-----EKQPEKIeRLLTFVDM--AHK-AEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLHKgmskaEAFEESV-RMLDAVKMpeARKrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 488289759 162 SSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
8-213 1.39e-29

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 116.11  E-value: 1.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   8 SKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVFQ-- 85
Cdd:PRK10261 331 NRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQdp 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  86 HYNLLENLKIYDNVALPLK----LLKEKQPEKIERLLTFVDM-AHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEA 160
Cdd:PRK10261 411 YASLDPRQTVGDSIMEPLRvhglLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488289759 161 TSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
1-193 3.38e-29

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 109.42  E-value: 3.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqM 80
Cdd:PRK10247   7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ---V 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENlKIYDNVALPLKLLKEK-QPEKIERLLTFVDMA-HKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:PRK10247  84 SYCAQTPTLFGD-TVYDNLIFPWQIRNQQpDPAIFLDDLERFALPdTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488289759 159 EATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHE 193
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
20-213 5.33e-29

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 111.50  E-value: 5.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  20 IHFSVQLGE-------------IVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRN-VQTFSKKEVRQQQQQMGMVFQ 85
Cdd:PRK11144   4 LNFKQQLGDlcltvnltlpaqgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEKGICLPPEKRRIGYVFQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  86 ------HYNLLENLKiYDnvalplklLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDE 159
Cdd:PRK11144  84 darlfpHYKVRGNLR-YG--------MAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDE 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488289759 160 ATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
2-213 6.04e-29

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 108.39  E-value: 6.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVY----------------------QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIR 59
Cdd:cd03220    1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  60 IDGRNVQTFSkkevrqqqqqMGMVFQhynllENLKIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQL---SG 136
Cdd:cd03220   81 VRGRVSSLLG----------LGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVktySS 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 137 GEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03220  146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIR 221
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
2-230 7.83e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 109.44  E-value: 7.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQE-THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQM 80
Cdd:PRK13647   5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR---SKV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHY-NLLENLKIYDNVA---LPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:PRK13647  82 GLVFQDPdDQVFSSTVWDDVAfgpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGE----FLNNPQQYEEEPLSY 230
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEgdksLLTDEDIVEQAGLRL 238
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
2-236 1.08e-28

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: 112.97  E-value: 1.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQ--PSEGEI----------------RIDGR 63
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpSKVGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   64 NVQT--------------FSKKEVRQQQQQMGMVFQH-YNLLENLKIYDNVALPLKLLKEKQPEKIER---LLTFVDMAH 125
Cdd:TIGR03269  81 PCPVcggtlepeevdfwnLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRavdLIEMVQLSH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  126 KAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRIL 205
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
                         250       260       270
                  ....*....|....*....|....*....|.
gi 488289759  206 VMEKGQLIGEflNNPQQYEEEPLSYLEKVER 236
Cdd:TIGR03269 241 WLENGEIKEE--GTPDEVVAVFMEGVSEVEK 269
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
16-215 1.15e-28

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 110.22  E-value: 1.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  16 ALKNIHFSVQLGEIVGIVGKSGSGKS-TLLRLLNLMEQP---SEGEIRIDGRNVQTFSKKEVRQ-QQQQMGMVFQH---- 86
Cdd:PRK11022  22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKERRNlVGAEVAMIFQDpmts 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  87 --------YNLLENLKIYDNVALplkllKEKQPEKIErLLTFV---DMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK11022 102 lnpcytvgFQIMEAIKVHQGGNK-----KTRRQRAID-LLNQVgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
2-212 1.23e-28

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: 112.92  E-value: 1.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevRQQQQQ 79
Cdd:COG4618  331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR---EELGRH 407
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLENlKIYDNVALplklLKEKQPEKIerlltfVDMAHKAEA----------Y-------PAQLSGGEKQRV 142
Cdd:COG4618  408 IGYLPQDVELFDG-TIAENIAR----FGDADPEKV------VAAAKLAGVhemilrlpdgYdtrigegGARLSGGQRQRI 476
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 143 SIARALSRNPKWLLCDEATSSLDEENTESVVRLLhkthQEFRP---TIFFVSHELeTVKRLCNRILVMEKGQL 212
Cdd:COG4618  477 GLARALYGDPRLVVLDEPNSNLDDEGEAALAAAI----RALKArgaTVVVITHRP-SLLAAVDKLLVLRDGRV 544
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
11-213 2.37e-28

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: 107.42  E-value: 2.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  11 YQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqqQMGMVF-QHYNL 89
Cdd:cd03267   31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR----RIGVVFgQKTQL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  90 LENLKIYDNVALpLK----LLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:cd03267  107 WWDLPVIDSFYL-LAaiydLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488289759 166 EENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03267  186 VVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
2-220 2.47e-28

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 108.20  E-value: 2.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQpSEGEIRIDGRnVQTFSKK------EVRQ 75
Cdd:PRK14258   8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGR-VEFFNQNiyerrvNLNR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  76 QQQQMGMVFQHYNLLEnLKIYDNVALPLKLL----KEKQPEKIERLLTFVDM----AHKAEAYPAQLSGGEKQRVSIARA 147
Cdd:PRK14258  86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVgwrpKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 148 LSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLC----------NRILVMEKGQLIGEFL 217
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSdftaffkgneNRIGQLVEFGLTKKIF 244

                 ...
gi 488289759 218 NNP 220
Cdd:PRK14258 245 NSP 247
cbiO PRK13641
energy-coupling factor transporter ATPase;
2-213 2.55e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 108.38  E-value: 2.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNV--QTfSKKEVR 74
Cdd:PRK13641   3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpET-GNKNLK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  75 QQQQQMGMVFQ--HYNLLENLKIYDNVALPLKL------LKEKQPEKIERLLTFVDMAHKAeayPAQLSGGEKQRVSIAR 146
Cdd:PRK13641  82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFgfsedeAKEKALKWLKKVGLSEDLISKS---PFELSGGQMRRVAIAG 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 147 ALSRNPKWLLCDEATSSLDEENTESVVRLLhKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLF-KDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
2-159 2.93e-28

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: 106.86  E-value: 2.93e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVrQQQQQMG 81
Cdd:cd03218    1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI---TKLPM-HKRARLG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVF--QHYNLLENLKIYDNVALPL---KLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:cd03218   77 IGYlpQEASIFRKLTVEENILAVLeirGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156

                 ...
gi 488289759 157 CDE 159
Cdd:cd03218  157 LDE 159
cbiO PRK13649
energy-coupling factor transporter ATPase;
2-213 3.30e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 107.91  E-value: 3.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSK-KEVRQ 75
Cdd:PRK13649   3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  76 QQQQMGMVFQ--HYNLLENLKIYDNVALPLKL-LKEKQPEKIER-LLTFVDMAHKA-EAYPAQLSGGEKQRVSIARALSR 150
Cdd:PRK13649  83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFgVSQEEAEALAReKLALVGISESLfEKNPFELSGGQMRRVAIAGILAM 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGM-TIVLVTHLMDDVANYADFVYVLEKGKLV 224
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
1-215 4.09e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 107.58  E-value: 4.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQ-ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVRQQQQQ 79
Cdd:PRK13652   3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREVRKF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYN-LLENLKIYDNVA---LPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK13652  80 VGLVFQNPDdQIFSPTVEQDIAfgpINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
cbiO PRK13646
energy-coupling factor transporter ATPase;
2-215 4.85e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 107.94  E-value: 4.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSK-KEVRQ 75
Cdd:PRK13646   3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdKYIRP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  76 QQQQMGMVFQhynLLENLKIYDNVALPL-------KLLKEKQPEKIERLLTFVDMAHKA-EAYPAQLSGGEKQRVSIARA 147
Cdd:PRK13646  83 VRKRIGMVFQ---FPESQLFEDTVEREIifgpknfKMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSI 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 148 LSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQ 227
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
1-227 5.15e-28

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 107.16  E-value: 5.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQM 80
Cdd:PRK11831   7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVALPLK--------LLKEKQPEKIERlltfVDMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:PRK11831  87 SMLFQSGALFTDMNVFDNVAYPLRehtqlpapLLHSTVMMKLEA----VGLRGAAKLMPSELSGGMARRAALARAIALEP 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 153 KWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGEflNNPQQYEEEP 227
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAH--GSAQALQANP 235
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
1-213 5.29e-28

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: 111.05  E-value: 5.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    1 MIELVNVSKVYQET-----HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRID-GRNVQTFSKKEVR 74
Cdd:TIGR03269 279 IIKVRNVSKRYISVdrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPD 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   75 QQ---QQQMGMVFQHYNLLENLKIYDNV--ALPLKLLKEKQPEKIERLLTFVDMAHKA-----EAYPAQLSGGEKQRVSI 144
Cdd:TIGR03269 359 GRgraKRYIGILHQEYDLYPHRTVLDNLteAIGLELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVAL 438
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759  145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
2-226 7.14e-28

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 111.35  E-value: 7.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    2 IELVNVSKVY---QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqq 78
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ-- 556
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   79 qMGMVFQHyNLLENLKIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKAE--------AYPAQLSGGEKQRVSIARALSR 150
Cdd:TIGR00958 557 -VALVGQE-PVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPngydtevgEKGSQLSGGQKQRIAIARALVR 634
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759  151 NPKWLLCDEATSSLDEEntesVVRLLHKTHQEFRPTIFFVSHELETVKRlCNRILVMEKGQLiGEFLNNPQQYEEE 226
Cdd:TIGR00958 635 KPRVLILDEATSALDAE----CEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSV-VEMGTHKQLMEDQ 704
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
2-215 1.82e-27

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: 103.55  E-value: 1.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVY--QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFsKKEVRqqqQQ 79
Cdd:cd03247    1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALS---SL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLeNLKIYDNVAlplkllkekqpekierlltfvdmahkaeaypAQLSGGEKQRVSIARALSRNPKWLLCDE 159
Cdd:cd03247   77 ISVLNQRPYLF-DTTLRNNLG-------------------------------RRFSGGERQRLALARILLQDAPIVLLDE 124
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 160 ATSSLDEENTESVVRLLHKTHQEfrPTIFFVSHELETVKRLcNRILVMEKGQLIGE 215
Cdd:cd03247  125 PTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
1-213 2.13e-27

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 105.17  E-value: 2.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLL----RLLNlmeqPSEGEIRIDGRNVQTFSKKEVrqq 76
Cdd:COG4604    1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLsmisRLLP----PDSGEVLVDGLDVATTPSREL--- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVFQHYNLLENLKIYDNVAL---PL---KLLKEKQpEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSR 150
Cdd:COG4604   74 AKRLAILRQENHINSRLTVRELVAFgrfPYskgRLTAEDR-EIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG4604  153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVV 215
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
2-213 4.58e-27

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: 103.26  E-value: 4.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQE--THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqq 79
Cdd:cd03369    7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS--- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLE-----NLKIYDnvalplkllkEKQPEKIERLLtfvdmahKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:cd03369   84 LTIIPQDPTLFSgtirsNLDPFD----------EYSDEEIYGAL-------RVSEGGLNLSQGQRQLLCLARALLKRPRV 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEfrPTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:cd03369  147 LVLDEATASIDYATDALIQKTIREEFTN--STILTIAHRLRTIID-YDKILVMDAGEVK 202
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1-213 6.00e-27

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 104.40  E-value: 6.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqTFSKKEVRq 75
Cdd:COG1101    1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEYKR- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  76 qQQQMGMVFQhyNLL----ENLKIYDNVALPLK----------LLKEKQPEKIERLLTF-VDMAHKAEAYPAQLSGGEKQ 140
Cdd:COG1101   79 -AKYIGRVFQ--DPMmgtaPSMTIEENLALAYRrgkrrglrrgLTKKRRELFRELLATLgLGLENRLDTKVGLLSGGQRQ 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 141 RVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG1101  156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1-213 6.32e-27

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 105.55  E-value: 6.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQ---------------------ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIR 59
Cdd:COG4586    1 IIEVENLSKTYRvyekepglkgalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  60 IDGRNVQtfskKEVRQQQQQMGMVF-QHYNLLENLKIYDNvalpLKLLKE--KQPEKI--ERLLTFVDMAHKAEAY--PA 132
Cdd:COG4586   81 VLGYVPF----KRRKEFARRIGVVFgQRSQLWWDLPAIDS----FRLLKAiyRIPDAEykKRLDELVELLDLGELLdtPV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 133 -QLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:COG4586  153 rQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGR 232

                 ..
gi 488289759 212 LI 213
Cdd:COG4586  233 II 234
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1-210 7.66e-27

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 107.83  E-value: 7.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevrQQQQQM 80
Cdd:PRK15439  11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP----AKAHQL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 G--MVFQHYNLLENLKIYDNVALPLKlLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:PRK15439  87 GiyLVPQEPLLFPNLSVKENILFGLP-KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 159 EATSSLDEENTESVVR----LLHKTHqefrpTIFFVSHELETVKRLCNRILVMEKG 210
Cdd:PRK15439 166 EPTASLTPAETERLFSrireLLAQGV-----GIVFISHKLPEIRQLADRISVMRDG 216
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1-214 2.37e-26

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 106.41  E-value: 2.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrQQQQQM 80
Cdd:PRK09700   5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL--AAQLGI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVALPLKLLKE----------KQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSR 150
Cdd:PRK09700  83 GIIYQELSVIDELTVLENLYIGRHLTKKvcgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIG 214
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDGSSVC 225
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
1-221 3.21e-26

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: 101.60  E-value: 3.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLMeQPSEGEIRIDGRNVQTFSKKEVRQqqqq 79
Cdd:COG0410    3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLL-PPRSGSIRFDGEDITGLPPHRIAR---- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVF--QHYNLLENLKIYDNVALPLKLLKEKQPEK--IERLLT-FVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:COG0410   78 LGIGYvpEGRRIFPSLTVEENLLLGAYARRDRAEVRadLERVYElFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 155 LLCDEATSSL-----DEenTESVVRLLHKTHQefrpTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQ 221
Cdd:COG0410  158 LLLDEPSLGLaplivEE--IFEIIRRLNREGV----TILLVEQNARFALEIADRAYVLERGRIVlegtaAELLADPE 228
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
1-159 3.50e-26

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 101.64  E-value: 3.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevrQQQQQM 80
Cdd:COG1137    3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPM----HKRARL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVF--QHYNLLENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:COG1137   79 GIGYlpQEASIFRKLTVEDNILAVLELRklsKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158

                 ....
gi 488289759 156 LCDE 159
Cdd:COG1137  159 LLDE 162
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
12-211 3.53e-26

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 105.94  E-value: 3.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  12 QETHALKNIHFSVQLGEIVGIVGKSGSGKS-TLLRLLNLMEQPS----EGEIRIDGRNVQTFSKKEVRQ-QQQQMGMVFQ 85
Cdd:PRK15134  20 TVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGvRGNKIAMIFQ 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  86 H----YNLLENL--KIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKAE---AYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:PRK15134 100 EpmvsLNPLHTLekQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKrltDYPHQLSGGERQRVMIAMALLTRPELLI 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
12-213 3.72e-26

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 106.09  E-value: 3.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  12 QETHALKNIHFSVQLGEIVGIVGKSGSGKS-TLLRLLNLMEQpSEGEIRIDG-----RNVQTFSKKEVRQQQQQ------ 79
Cdd:PRK10261  27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKmllrrRSRQVIELSEQSAAQMRhvrgad 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLENL------KIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKAEA---YPAQLSGGEKQRVSIARALSR 150
Cdd:PRK10261 106 MAMIFQEPMTSLNPvftvgeQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIlsrYPHQLSGGMRQRVMIAMALSC 185
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
cbiO PRK13645
energy-coupling factor transporter ATPase;
2-213 4.32e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 102.78  E-value: 4.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKK--EVR 74
Cdd:PRK13645   7 IILDNVSYTYAkktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  75 QQQQQMGMVFQ--HYNLLENlKIYDNVAL-PLKLLKEKQP--EKIERLLTFVDMAHK-AEAYPAQLSGGEKQRVSIARAL 148
Cdd:PRK13645  87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFgPVNLGENKQEayKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGII 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
1-210 6.47e-26

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 104.15  E-value: 6.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVrqqQQQM 80
Cdd:PRK09536   3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA---SRRV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVAL---P----LKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:PRK09536  80 ASVPQDTSLSFEFDVRQVVEMgrtPhrsrFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 154 WLLCDEATSSLD---EENTESVVRLLHKTHQefrpTIFFVSHELETVKRLCNRILVMEKG 210
Cdd:PRK09536 160 VLLLDEPTASLDinhQVRTLELVRRLVDDGK----TAVAAIHDLDLAARYCDELVLLADG 215
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
1-213 8.86e-26

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 101.40  E-value: 8.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVY---------QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqTFSKK 71
Cdd:PRK15112   4 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  72 EVRQQQqqMGMVFQ--HYNLLENLKIYDNVALPLKLLKEKQPE----KIERLLTFVDM-AHKAEAYPAQLSGGEKQRVSI 144
Cdd:PRK15112  83 SYRSQR--IRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEqrekQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
17-213 2.85e-25

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 103.39  E-value: 2.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLnLMEQPSEGEIRIDGrnvQTFSKKEVRQQQQQMGMVFQHYNLLENlKIY 96
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNAL-LGFLPYQGSLKING---IELRELDPESWRKHLSWVGQNPQLPHG-TLR 440
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  97 DNVALPLKLLKEkqpEKIERLLT------FVDMAHKAEAYP-----AQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:PRK11174 441 DNVLLGNPDASD---EQLQQALEnawvseFLPLLPQGLDTPigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488289759 166 EENTESVVRLLHKTHQefRPTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:PRK11174 518 AHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIV 562
cbiO PRK13643
energy-coupling factor transporter ATPase;
1-213 3.59e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 100.19  E-value: 3.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQ-----ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSK-KEVR 74
Cdd:PRK13643   1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqKEIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  75 QQQQQMGMVFQ--HYNLLENLKIYDNVALPLKL-LKEKQPEKI-ERLLTFVDMAHKA-EAYPAQLSGGEKQRVSIARALS 149
Cdd:PRK13643  81 PVRKKVGVVFQfpESQLFEETVLKDVAFGPQNFgIPKEKAEKIaAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 150 RNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHII 223
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
16-216 9.90e-25

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 101.64  E-value: 9.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqqQMGMVF-----QHYNLL 90
Cdd:COG3845  273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERR----RLGVAYipedrLGRGLV 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  91 ENLKIYDNVAL------PL--------KLLKEKQPEKIERLltfvDMAHKAEAYPA-QLSGGEKQRVSIARALSRNPKWL 155
Cdd:COG3845  349 PDMSVAENLILgryrrpPFsrggfldrKAIRAFAEELIEEF----DVRTPGPDTPArSLSGGNQQKVILARELSRDPKLL 424
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 156 LCDEATSSLDEENTESVvrllhktHQEFRP------TIFFVSHELETVKRLCNRILVMEKGQLIGEF 216
Cdd:COG3845  425 IAAQPTRGLDVGAIEFI-------HQRLLElrdagaAVLLISEDLDEILALSDRIAVMYEGRIVGEV 484
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
16-213 2.01e-24

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: 101.35  E-value: 2.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQ---QMGMVFQHyNLLEN 92
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINylpQEPYIFSG-SILEN 567
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   93 LKIYDNVALplkllkekQPEKIERLLTFVDMAHKAEAYP-----------AQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:TIGR01193 568 LLLGAKENV--------SQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILDEST 639
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 488289759  162 SSLDEENTESVV-RLLHKTHQefrpTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:TIGR01193 640 SNLDTITEKKIVnNLLNLQDK----TIIFVAHRLSVAKQ-SDKIIVLDHGKII 687
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
6-226 2.84e-24

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 100.52  E-value: 2.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   6 NVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIridgrnvqtfskkeVRQQQQQMGMVFQ 85
Cdd:COG0488    3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------------SIPKGLRIGYLPQ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  86 HYNLLENLKIYDNVALPLKLLKE--KQPEKIERLLTFV--DMAHKAE-----------AYPAQ----------------- 133
Cdd:COG0488   69 EPPLDDDLTVLDTVLDGDAELRAleAELEELEAKLAEPdeDLERLAElqeefealggwEAEARaeeilsglgfpeedldr 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 134 ----LSGGEKQRVSIARALSRNPKWLLCDEATSSLDeenTESVVRL---LhkthQEFRPTIFFVSHE---LETVkrlCNR 203
Cdd:COG0488  149 pvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEWLeefL----KNYPGTVLVVSHDryfLDRV---ATR 218
                        250       260
                 ....*....|....*....|...
gi 488289759 204 ILVMEKGQLIgEFLNNPQQYEEE 226
Cdd:COG0488  219 ILELDRGKLT-LYPGNYSAYLEQ 240
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
14-215 3.96e-24

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 96.78  E-value: 3.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  14 THALKNIHFSVQ-------------LGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKK----EVRQQ 76
Cdd:PRK10575  11 TFALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafarKVAYL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVfqhynllENLKIYDNVAL-------PLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALS 149
Cdd:PRK10575  91 PQQLPAA-------EGMTVRELVAIgrypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 150 RNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQ 229
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
2-226 5.50e-24

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 96.39  E-value: 5.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQ--PS---EGEIRIDGRNV--QTFSKKEVR 74
Cdd:PRK14243  11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyaPDVDPVEVR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  75 QQqqqMGMVFQHYNLLENlKIYDNVALPLKLL--KEKQPEKIERLLT----FVDMAHKAEAYPAQLSGGEKQRVSIARAL 148
Cdd:PRK14243  91 RR---IGMVFQKPNPFPK-SIYDNIAYGARINgyKGDMDELVERSLRqaalWDEVKDKLKQSGLSLSGGQQQRLCIARAI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRLCN-----RILVMEKGQLIGEFL------ 217
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDmtaffNVELTEGGGRYGYLVefdrte 244
                        250
                 ....*....|..
gi 488289759 218 ---NNPQQYEEE 226
Cdd:PRK14243 245 kifNSPQQQATR 256
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
1-215 9.10e-24

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 98.92  E-value: 9.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrQQQQQM 80
Cdd:PRK10762   4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS--SQEAGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVALPL-------KLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:PRK10762  82 GIIHQELNLIPQLTIAENIFLGRefvnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELKSQGR-GIVYISHRLKEIFEICDDVTVFRDGQFIAE 222
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
15-213 9.20e-24

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 97.28  E-value: 9.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  15 HALKNIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLME---QPSEGEIRIDGRNVQTFSKKEVRQ-QQQQMGMVFQHYN- 88
Cdd:COG4170   21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKdnwHVTADRFRWNGIDLLKLSPRERRKiIGREIAMIFQEPSs 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  89 -LLENLKIYDNV--ALPLKLLKEK-------QPEKIERLLTFVDMA-HKA--EAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:COG4170  101 cLDPSAKIGDQLieAIPSWTFKGKwwqrfkwRKKRAIELLHRVGIKdHKDimNSYPHELTEGECQKVMIAMAIANQPRLL 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 156 LCDEATSSLdEENTES-VVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG4170  181 IADEPTNAM-ESTTQAqIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
2-213 1.15e-23

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 99.02  E-value: 1.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETH-ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqM 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG---V 417
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENlKIYDNVALPlkllKEKQPEKIERLLTFVDMAHKAEAYPA-----------QLSGGEKQRVSIARALS 149
Cdd:PRK10790 418 AMVQQDPVVLAD-TFLANVTLG----RDISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLV 492
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 150 RNPKWLLCDEATSSLDEENTESVVRLLHKTHQefRPTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAV 553
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1-214 1.86e-23

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 98.08  E-value: 1.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMeQPS---EGEIRIDGRNVQTFSKKEVrqQQ 77
Cdd:PRK13549   5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNIRDT--ER 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  78 QQMGMVFQHYNLLENLKIYDNVALPLKLLK------EKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRN 151
Cdd:PRK13549  82 AGIAIIHQELALVKELSVLENIFLGNEITPggimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 152 PKWLLCDEATSSLDEENTESVVRLLH--KTHQefrPTIFFVSHELETVKRLCNRILVMEKGQLIG 214
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRdlKAHG---IACIYISHKLNEVKAISDTICVIRDGRHIG 223
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
6-221 2.11e-23

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 94.58  E-value: 2.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   6 NVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEvrQQQQQMGMVFQ 85
Cdd:PRK10895   8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYLPQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  86 HYNLLENLKIYDNVALPLK----LLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:PRK10895  86 EASIFRRLSVYDNLMAVLQirddLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 162 SSLDEENTESVVRLLhkthQEFRPT---IFFVSHELETVKRLCNRILVMEKGQLIG-----EFLNNPQ 221
Cdd:PRK10895 166 AGVDPISVIDIKRII----EHLRDSglgVLITDHNVRETLAVCERAYIVSQGHLIAhgtptEILQDEH 229
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
6-213 6.96e-23

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 93.45  E-value: 6.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   6 NVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGR-----NVQTFSKKEVRQ-QQQQ 79
Cdd:PRK11701  11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRlLRTE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQH------------YNLLENL-----KIYDNV-ALPLKLLK--EKQPEKIERLltfvdmahkaeayPAQLSGGEK 139
Cdd:PRK11701  91 WGFVHQHprdglrmqvsagGNIGERLmavgaRHYGDIrATAGDWLErvEIDAARIDDL-------------PTTFSGGMQ 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 140 QRVSIARALSRNPKWLLCDEATSSLDeentESV-VRLLHKTHQ---EFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLD----VSVqARLLDLLRGlvrELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
17-211 9.96e-23

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 96.03  E-value: 9.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRidgrnvqtfskkevRQQQQQMGMVFQH-YNLLENLKi 95
Cdd:COG4178  379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA--------------RPAGARVLFLPQRpYLPLGTLR- 443
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  96 yDNVALPlKLLKEKQPEKIERLLTFVDMAHKAE------AYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENT 169
Cdd:COG4178  444 -EALLYP-ATAEAFSDAELREALEAVGLGHLAErldeeaDWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENE 521
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488289759 170 ESVVRLLHKTHQEfrPTIFFVSHElETVKRLCNRILVMEKGQ 211
Cdd:COG4178  522 AALYQLLREELPG--TTVISVGHR-STLAAFHDRVLELTGDG 560
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
15-216 1.20e-22

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 95.47  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  15 HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqmGMVF-----QHYNL 89
Cdd:COG1129  266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRA----GIAYvpedrKGEGL 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  90 LENLKIYDNVALP-------LKLLKEKQPEKI-ERLLTFVDM-AHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEA 160
Cdd:COG1129  342 VLDLSIRENITLAsldrlsrGGLLDRRRERALaEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 161 TSSLD----EEntesVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGEF 216
Cdd:COG1129  422 TRGIDvgakAE----IYRLIRELAAEGK-AVIVISSELPELLGLSDRILVMREGRIVGEL 476
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
8-213 1.20e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 94.15  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   8 SKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRI----------DGRNVQTFSKKEVR--- 74
Cdd:PRK13631  33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKIKnfk 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  75 QQQQQMGMVFQ--HYNLLENLKIYDNVALPLKLlKEKQPEKIERLLTFVDMAHKAEAY----PAQLSGGEKQRVSIARAL 148
Cdd:PRK13631 113 ELRRRVSMVFQfpEYQLFKDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDSYlersPFGLSGGQKRRVAIAGIL 191
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 149 SRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMDKGKIL 255
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
17-213 1.77e-22

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: 91.56  E-value: 1.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSE---GEIRIDGRNVqtfSKKEVrqqQQQMGMVFQHYNLLENL 93
Cdd:cd03234   23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR---KPDQF---QKCVAYVRQDDILLPGL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  94 KIYD------NVALPlKLLKEKQPEKIERLLTFVDMAHK--AEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:cd03234   97 TVREtltytaILRLP-RKSSDAIRKKRVEDVLLRDLALTriGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 166 EENTESVVRLLHKT-----------HQEfRPTIFfvsheletvkRLCNRILVMEKGQLI 213
Cdd:cd03234  176 SFTALNLVSTLSQLarrnriviltiHQP-RSDLF----------RLFDRILLLSSGEIV 223
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
1-214 1.15e-21

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: 92.97  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPS--EGEIRIDGRNVQTFSKKEVrqQQQ 78
Cdd:TIGR02633   1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDT--ERA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   79 QMGMVFQHYNLLENLKIYDNVAL----PLKLLKEKQPEKIER---LLTFVDMAHKAEAYP-AQLSGGEKQRVSIARALSR 150
Cdd:TIGR02633  79 GIVIIHQELTLVPELSVAENIFLgneiTLPGGRMAYNAMYLRaknLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNK 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759  151 NPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIfFVSHELETVKRLCNRILVMEKGQLIG 214
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACV-YISHKLNEVKAVCDTICVIRDGQHVA 221
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1-215 1.24e-21

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 90.07  E-value: 1.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVrqqQQQM 80
Cdd:PRK11231   2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL---ARRL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVA------LPL-KLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPK 153
Cdd:PRK11231  79 ALLPQHHLTPEGITVRELVAygrspwLSLwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
15-222 3.42e-21

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 91.65  E-value: 3.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   15 HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLL------NLMEQPSegeIRIDGRNVQtfsKKEVRQQQ---QQMGMVFQ 85
Cdd:TIGR00955  39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrspkGVKGSGS---VLLNGMPID---AKEMRAISayvQQDDLFIP 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   86 HYNLLENLKIYDNVALPLKLLKEKQPEKIERLLT---FVDMAHKAEAYPAQ---LSGGEKQRVSIARALSRNPKWLLCDE 159
Cdd:TIGR00955 113 TLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQalgLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDE 192
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759  160 ATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIgeFLNNPQQ 222
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVA--YLGSPDQ 253
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
4-213 3.90e-21

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 91.33  E-value: 3.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   4 LVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVrqQQQQMGMV 83
Cdd:PRK10982   1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA--LENGISMV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  84 FQHYNLLENLKIYDNVAL---PLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:PRK10982  79 HQELNLVLQRSVMDNMWLgryPTKGMfvdQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 158 DEATSSLDEENTESVVRLLHKThQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
2-167 4.62e-21

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: 87.03  E-value: 4.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQMG 81
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHENI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   82 MVFQHYN-------LLENLKIYDNVALPLKLlkekqpeKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARA-LSRNPK 153
Cdd:TIGR01189  76 LYLGHLPglkpelsALENLHFWAAIHGGAQR-------TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLwLSRRPL 148
                         170
                  ....*....|....
gi 488289759  154 WLLcDEATSSLDEE 167
Cdd:TIGR01189 149 WIL-DEPTTALDKA 161
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
11-213 5.93e-21

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 88.53  E-value: 5.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  11 YQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtFSKKEVRQQQQQMGMVFQHYN-L 89
Cdd:PRK13638  11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQVATVFQDPEqQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  90 LENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDmAHKAEAYPAQ-LSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:PRK13638  90 IFYTDIDSDIAFSLRNLGVPEAEitrRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488289759 166 EENTESVVRLLHKTHQEFRPTIfFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHVI-ISSHDIDLIYEISDAVYVLRQGQIL 215
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
2-200 1.01e-20

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 86.94  E-value: 1.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLL--NLMEQPSEGEIRIDgrnVQTFSKKEVrqqqqq 79
Cdd:COG2401   31 LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVP---DNQFGREAS------ 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 mgmvfqhynLLENLKIYDNVALPLKLLkekqpekierlltfvDMAHKAEAY-----PAQLSGGEKQRVSIARALSRNPKW 154
Cdd:COG2401  102 ---------LIDAIGRKGDFKDAVELL---------------NAVGLSDAVlwlrrFKELSTGQKFRFRLALLLAERPKL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRL 200
Cdd:COG2401  158 LVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDL 203
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
18-225 1.06e-20

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 90.47  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   18 KNIHFSVQLGEIVGIVGKSGSGKST----LLRLLNL--------------------MEQPSE------------------ 55
Cdd:PTZ00265 1185 KDLTFSCDSKKTTAIVGETGSGKSTvmslLMRFYDLkndhhivfknehtndmtneqDYQGDEeqnvgmknvnefsltkeg 1264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   56 ------------GEIRIDGRNVQTFSKKEVRQqqqqMGMVFQHYNLLENLKIYDNValplKLLKEKQP-EKIERLLTFVD 122
Cdd:PTZ00265 1265 gsgedstvfknsGKILLDGVDICDYNLKDLRN----LFSIVSQEPMLFNMSIYENI----KFGKEDATrEDVKRACKFAA 1336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  123 MAHKAEAYPAQ-----------LSGGEKQRVSIARALSRNPKWLLCDEATSSLDeENTEsvvRLLHKTHQEFR----PTI 187
Cdd:PTZ00265 1337 IDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSE---KLIEKTIVDIKdkadKTI 1412
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 488289759  188 FFVSHELETVKRlCNRILVMEKGQLIGEFLNNPQQYEE 225
Cdd:PTZ00265 1413 ITIAHRIASIKR-SDKIVVFNNPDRTGSFVQAHGTHEE 1449
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
16-220 1.77e-20

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 86.97  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevrQQQQQMGMV--FQHYNL---- 89
Cdd:PRK11300  20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG----HQIARMGVVrtFQHVRLfrem 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  90 --LENLKI----YDNVALPLKLLK-----EKQPEKIERL---LTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK11300  96 tvIENLLVaqhqQLKTGLFSGLLKtpafrRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIG-----EFLNNP 220
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAngtpeEIRNNP 245
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
18-215 2.10e-20

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 86.96  E-value: 2.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  18 KNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVrqqQQQMGMVFQHYNLLENLKIYD 97
Cdd:PRK10253  24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV---ARRIGLLAQNATTPGDITVQE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  98 NVA---LPLKLL----KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTE 170
Cdd:PRK10253 101 LVArgrYPHQPLftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 488289759 171 SVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQ 225
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
5-215 2.95e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 86.69  E-value: 2.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   5 VNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEG-----EIRIDGRNVqtFSKKEVRQQQQQ 79
Cdd:PRK14271  25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFRRR 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  80 MGMVFQHYNLLEnLKIYDNVA--------LPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRN 151
Cdd:PRK14271 103 VGMLFQRPNPFP-MSIMDNVLagvrahklVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 152 PKWLLCDEATSSLDEENTESVVRLLHKTHQefRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
16-194 9.89e-20

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: 87.42  E-value: 9.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQ---QQMGMVFqHYNLLEN 92
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVsvcAQDAHLF-DTTVREN 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   93 LKIydnvALPlkllkEKQPEKIERLLTFVDMAHKAEAYP-----------AQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:TIGR02868 429 LRL----ARP-----DATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPT 499
                         170       180       190
                  ....*....|....*....|....*....|...
gi 488289759  162 SSLDEENTESVVRLLHKTHQEFrpTIFFVSHEL 194
Cdd:TIGR02868 500 EHLDAETADELLEDLLAALSGR--TVVLITHHL 530
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
17-209 1.23e-19

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: 82.59  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNvqtfskkevrqqqqQMGMVFQH-Ynllenlki 95
Cdd:cd03223   17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE--------------DLLFLPQRpY-------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  96 ydnvaLPLKLLKEkqpekierlltfvdmahkAEAYP--AQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVV 173
Cdd:cd03223   75 -----LPLGTLRE------------------QLIYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488289759 174 RLLhkthQEFRPTIFFVSHElETVKRLCNRILVMEK 209
Cdd:cd03223  132 QLL----KELGITVISVGHR-PSLWKFHDRVLDLDG 162
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
2-216 1.55e-19

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 87.31  E-value: 1.55e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759     2 IELVNVSKVYQE--THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQ- 78
Cdd:TIGR00957 1285 VEFRNYCLRYREdlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITi 1364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    79 --QMGMVFQHyNLLENLKIYDN-------VALPLKLLK---EKQPEKIErlltfvdmaHKAEAYPAQLSGGEKQRVSIAR 146
Cdd:TIGR00957 1365 ipQDPVLFSG-SLRMNLDPFSQysdeevwWALELAHLKtfvSALPDKLD---------HECAEGGENLSVGQRQLVCLAR 1434
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   147 ALSRNPKWLLCDEATSSLDEEnTESVVRLLHKTHQEfRPTIFFVSHELETVKRLcNRILVMEKGQlIGEF 216
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLE-TDNLIQSTIRTQFE-DCTVLTIAHRLNTIMDY-TRVIVLDKGE-VAEF 1500
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-215 1.67e-19

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 83.77  E-value: 1.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFskKEVRQQQQQM 80
Cdd:PRK11614   5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW--QTAKIMREAV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVALPLKLLKEKQ-PEKIERLLTFVDMAHKAEAYPA-QLSGGEKQRVSIARALSRNPKWLLCD 158
Cdd:PRK11614  83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQfQERIKWVYELFPRLHERRIQRAgTMSGGEQQMLAIGRALMSQPRLLLLD 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 159 EATSSLdeenTESVVRLLHKTHQEFRP---TIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK11614 163 EPSLGL----APIIIQQIFDTIEQLREqgmTIFLVEQNANQALKLADRGYVLENGHVVLE 218
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
1-197 3.90e-19

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 83.24  E-value: 3.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRidgrnvqtfskkevRQQQQQM 80
Cdd:PRK09544   4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------------RNGKLRI 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQhynllenlKIYDNVALPL------KLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:PRK09544  70 GYVPQ--------KLYLDTTLPLtvnrflRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETV 197
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
17-182 8.58e-19

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 81.46  E-value: 8.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNvQTFSKkeVRQQQQQMGmvfqHYNLL-ENLKI 95
Cdd:PRK13539  18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-IDDPD--VAEACHYLG----HRNAMkPALTV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  96 YDNVALPLKLLKEKQPEkIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARAL-SRNPKWLLcDEATSSLDEENTESVVR 174
Cdd:PRK13539  91 AENLEFWAAFLGGEELD-IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLvSNRPIWIL-DEPTAALDAAAVALFAE 168

                 ....*...
gi 488289759 175 LLhKTHQE 182
Cdd:PRK13539 169 LI-RAHLA 175
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
2-210 8.73e-19

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 85.08  E-value: 8.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    2 IELVNVSKVY---QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRI-DGRNVQTFSKKEVRQQq 77
Cdd:PTZ00265  383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK- 461
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   78 qqMGMVFQHYNLLENlKIYDNVALPLKLLKE------------------------------------------------- 108
Cdd:PTZ00265  462 --IGVVSQDPLLFSN-SIKNNIKYSLYSLKDlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemr 538
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  109 KQPEKIERLlTFVDMAHKA------EAYP-----------AQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTES 171
Cdd:PTZ00265  539 KNYQTIKDS-EVVDVSKKVlihdfvSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 488289759  172 VVRLLHKTH-QEFRPTIfFVSHELETVkRLCNRILVM---EKG 210
Cdd:PTZ00265  618 VQKTINNLKgNENRITI-IIAHRLSTI-RYANTIFVLsnrERG 658
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
4-238 1.82e-18

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: 83.83  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    4 LVNVSKVYQET-HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRI-DGRNV-------QTFSKKEVR 74
Cdd:TIGR03719   7 MNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKVgylpqepQLDPTKTVR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   75 qQQQQMGM-----VFQHYNllenlKIYDNVALPL----KLLKE--KQPEKIE-----RLLTFVDMAHKA------EAYPA 132
Cdd:TIGR03719  87 -ENVEEGVaeikdALDRFN-----EISAKYAEPDadfdKLAAEqaELQEIIDaadawDLDSQLEIAMDAlrcppwDADVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  133 QLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHkthqEFRPTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ----EYPGTVVAVTHDRYFLDNVAGWILELDRGRG 236
                         250       260
                  ....*....|....*....|....*.
gi 488289759  213 IgeflnnPqqYEEEPLSYLEKVERSL 238
Cdd:TIGR03719 237 I------P--WEGNYSSWLEQKQKRL 254
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
8-211 5.99e-18

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: 79.05  E-value: 5.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   8 SKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLnLME-QPSEGEIRIDGR-----------------NVQtfs 69
Cdd:cd03250   12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGElEKLSGSVSVPGSiayvsqepwiqngtireNIL--- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  70 kkevrqqqqqMGMVFQH--YN-------LLENLKIydnvaLPLKLLKEkqpekI-ERLLTfvdmahkaeaypaqLSGGEK 139
Cdd:cd03250   88 ----------FGKPFDEerYEkvikacaLEPDLEI-----LPDGDLTE-----IgEKGIN--------------LSGGQK 133
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 140 QRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRlCNRILVMEKGQ 211
Cdd:cd03250  134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
PLN03232 PLN03232
ABC transporter C family member; Provisional
17-240 6.40e-18

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 82.33  E-value: 6.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQ---QMGMVFQ---HYNLl 90
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSiipQSPVLFSgtvRFNI- 1330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   91 ENLKIYDNVALPLKLLKEKQPEKIERLLTFVDmahkAEAYPA--QLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEEn 168
Cdd:PLN03232 1331 DPFSEHNDADLWEALERAHIKDVIDRNPFGLD----AEVSEGgeNFSVGQRQLLSLARALLRRSKILVLDEATASVDVR- 1405
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759  169 TESvvrLLHKT-HQEFRP-TIFFVSHELETVKRlCNRILVMEKGQLIgEFlNNPQQYEEEPLSYLEKVERSLRP 240
Cdd:PLN03232 1406 TDS---LIQRTiREEFKScTMLVIAHRLNTIID-CDKILVLSSGQVL-EY-DSPQELLSRDTSAFFRMVHSTGP 1473
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
16-213 7.19e-18

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 82.07  E-value: 7.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQMGMVFQHYNLLENlKI 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR---SRLAVVSQTPFLFSD-TV 405
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  96 YDNVALPLKLLKEKQPEKIERLLTF-VDMAHKAEAYPAQ-------LSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:PRK10789 406 ANNIALGRPDATQQEIEHVARLASVhDDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSAVDGR 485
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488289759 168 nTESvvRLLHKTHQ--EFRpTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:PRK10789 486 -TEH--QILHNLRQwgEGR-TVIISAHRLSALTE-ASEILVMQHGHIA 528
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
15-212 9.85e-18

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 81.48  E-value: 9.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  15 HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQmgmvfqhynlLENLK 94
Cdd:PRK13545  38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTG----------IENIE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  95 IYdnvALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVR 174
Cdd:PRK13545 108 LK---GLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 488289759 175 LLHKtHQEFRPTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:PRK13545 185 KMNE-FKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
19-182 1.06e-17

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 78.31  E-value: 1.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  19 NIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQMGMVFQHYN-----L--LE 91
Cdd:PRK13538  19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR-----RQRDEYHQDLLYLGHQPgikteLtaLE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  92 NLKIYdnvalpLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIAR-ALSRNPKWLLcDEATSSLDEENTE 170
Cdd:PRK13538  94 NLRFY------QRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARlWLTRAPLWIL-DEPFTAIDKQGVA 166
                        170       180
                 ....*....|....*....|...
gi 488289759 171 SVVRLL--H---------KTHQE 182
Cdd:PRK13538 167 RLEALLaqHaeqggmvilTTHQD 189
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
16-199 1.23e-17

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 78.04  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFskkeVRQQQQ-------------QMGm 82
Cdd:NF040873   7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAY----VPQRSEvpdslpltvrdlvAMG- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  83 VFQHYNLLENLKIYDNVAlplkllkekqpekIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATS 162
Cdd:NF040873  82 RWARRGLWRRLTRDDRAA-------------VDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 488289759 163 SLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKR 199
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGA-TVVVVTHDLELVRR 184
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
2-213 1.30e-17

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 79.11  E-value: 1.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSkvyqETHALKNIHFSVQLGEIVGIVGKSGSGKSTLL-RLLNLMeqPSEGEIRIDGRNVQTFSKKEVRQQ---- 76
Cdd:COG4138    1 LQLNDVA----VAGRLGPISAQVNAGELIHLIGPNGAGKSTLLaRMAGLL--PGQGEILLNGRPLSDWSAAELARHrayl 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 -QQQM---GM-VFQHYNLlenlkiydnvALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARAL--- 148
Cdd:COG4138   75 sQQQSppfAMpVFQYLAL----------HQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqv 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 149 --SRNP--KWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:COG4138  145 wpTINPegQLLLLDEPMNSLDVAQQAALDRLLRELCQQGI-TVVMSSHDLNHTLRHADRVWLLKQGKLV 212
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
27-208 1.93e-17

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: 78.60  E-value: 1.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  27 GEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNV----QTFS-KKEVRQQQQQMGMVFQHYNLlenlKIYDN-VA 100
Cdd:cd03237   25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpQYIKaDYEGTVRDLLSSITKDFYTH----PYFKTeIA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 101 LPLKLlkekqpEKI-ERLLTfvdmahkaeaypaQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKT 179
Cdd:cd03237  101 KPLQI------EQIlDREVP-------------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRF 161
                        170       180
                 ....*....|....*....|....*....
gi 488289759 180 HQEFRPTIFFVSHELETVKRLCNRILVME 208
Cdd:cd03237  162 AENNEKTAFVVEHDIIMIDYLADRLIVFE 190
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
6-212 3.28e-17

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: 80.44  E-value: 3.28e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759     6 NVSKVYQETH--ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfSKKEVRQQqqqMGMV 83
Cdd:TIGR01257  933 NLVKIFEPSGrpAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQS---LGMC 1008
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    84 FQHYNLLENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEA 160
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEaqlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 488289759   161 TSSLDEENTESVVRLLHKtHQEFRpTIFFVSHELETVKRLCNRILVMEKGQL 212
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLK-YRSGR-TIIMSTHHMDEADLLGDRIAIISQGRL 1138
PTZ00243 PTZ00243
ABC transporter; Provisional
17-210 3.45e-17

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 80.21  E-value: 3.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQMGMVFQHYNLLENlkiy 96
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELR---RQFSMIPQDPVLFDG---- 1398
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   97 dNVALPLKLLKEKQPEKIERLLTFVDM----AHKAEAYPAQL-------SGGEKQRVSIARA-LSRNPKWLLCDEATSSL 164
Cdd:PTZ00243 1399 -TVRQNVDPFLEASSAEVWAALELVGLrervASESEGIDSRVleggsnySVGQRQLMCMARAlLKKGSGFILMDEATANI 1477
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 488289759  165 D---EENTESVVRLLHKTHqefrpTIFFVSHELETVKRlCNRILVMEKG 210
Cdd:PTZ00243 1478 DpalDRQIQATVMSAFSAY-----TVITIAHRLHTVAQ-YDKIIVMDHG 1520
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
2-212 7.42e-17

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 78.86  E-value: 7.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETH-ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRqqqQQM 80
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYR---KLF 399
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNvalplkllKEKQPEKIERLLTFVDMAHKAE-----AYPAQLSGGEKQRVSIARALSRNPKWL 155
Cdd:PRK10522 400 SAVFTDFHLFDQLLGPEG--------KPANPALVEKWLERLKMAHKLEledgrISNLKLSKGQKKRLALLLALAEERDIL 471
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 156 LCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHElETVKRLCNRILVMEKGQL 212
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
2-213 9.68e-17

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 77.23  E-value: 9.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETH-ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQ---QQ 77
Cdd:PRK15056   7 IVVNDVTVTWRNGHtALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAyvpQS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  78 QQMGMVFQhyNLLENLKI---YDNVALpLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:PRK15056  87 EEVDWSFP--VLVEDVVMmgrYGHMGW-LRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 155 LLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRIlVMEKGQLI 213
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYT-VMVKGTVL 220
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
22-213 1.29e-16

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 76.12  E-value: 1.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  22 FSVQLGEIVGIVGKSGSGKSTLL-RLLNLMeqPSEGEIRIDGRNVQTFSKKEVRQQ-----QQQM---GM-VFQHYNLle 91
Cdd:PRK03695  17 AEVRAGEILHLVGPNGAGKSTLLaRMAGLL--PGSGSIQFAGQPLEAWSAAELARHraylsQQQTppfAMpVFQYLTL-- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  92 nlkiydnvALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARAL-----SRNP--KWLLCDEATSSL 164
Cdd:PRK03695  93 --------HQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSL 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488289759 165 DEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGI-AVVMSSHDLNHTLRHADRVWLLKQGKLL 212
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
22-165 2.07e-16

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: 74.84  E-value: 2.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  22 FSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQtfskkEVRQQQQQMGMVFQHYN-------LLENLK 94
Cdd:cd03231   21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD-----FQRDSIARGLLYLGHAPgikttlsVLENLR 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759  95 IYDNVAlplkllkekQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARA-LSRNPKWLLcDEATSSLD 165
Cdd:cd03231   96 FWHADH---------SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLlLSGRPLWIL-DEPTTALD 157
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
18-215 2.11e-16

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 77.78  E-value: 2.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  18 KNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGrnvQTFSKKEVRQQQQQmGMVF-----QHYNLLEN 92
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG---KEINALSTAQRLAR-GLVYlpedrQSSGLYLD 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  93 LKIYDNVA------LPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQ-LSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:PRK15439 356 APLAWNVCalthnrRGFWIKPARENAVLERYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 488289759 166 EENTESVVRLLHKTHQEfRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGA 484
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
2-225 2.47e-16

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 77.67  E-value: 2.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIdGRNVqtfskkevrqqqqQMG 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-------------KLA 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   82 MVFQHYNLLENLK-IYDNVALPLKLLKekqpekierlLTFVDMAHKA------------EAYPAQLSGGEKQRVSIARAL 148
Cdd:TIGR03719 389 YVDQSRDALDPNKtVWEEISGGLDIIK----------LGKREIPSRAyvgrfnfkgsdqQKKVGQLSGGERNRVHLAKTL 458
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759  149 SRNPKWLLCDEATSSLDEENtesvVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGEFLNNPQQYEE 225
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVET----LRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEWFEGNFSEYEE 531
PLN03130 PLN03130
ABC transporter C family member; Provisional
17-213 2.55e-16

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 77.86  E-value: 2.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQqqqMGMVFQ---------HY 87
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV---LGIIPQapvlfsgtvRF 1331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   88 NLlENLKIYDNVALPLKLLKEKQPEKIERLLTFVDmAHKAEAyPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDee 167
Cdd:PLN03130 1332 NL-DPFNEHNDADLWESLERAHLKDVIRRNSLGLD-AEVSEA-GENFSVGQRQLLSLARALLRRSKILVLDEATAAVD-- 1406
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488289759  168 ntesvVR---LLHKT-HQEFRP-TIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:PLN03130 1407 -----VRtdaLIQKTiREEFKScTMLIIAHRLNTIID-CDRILVLDAGRVV 1451
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
4-192 2.57e-16

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 77.47  E-value: 2.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   4 LVNVSKVY-QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRI-DGRNV-------QTFSKKEVR 74
Cdd:PRK11819   9 MNRVSKVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKVgylpqepQLDPEKTVR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  75 QQ-QQQMGMVFQHYNLLEnlKIYDNVALPL----KLLKE--KQPEKIER-----LLTFVDMAHKA------EAYPAQLSG 136
Cdd:PRK11819  89 ENvEEGVAEVKAALDRFN--EIYAAYAEPDadfdALAAEqgELQEIIDAadawdLDSQLEIAMDAlrcppwDAKVTKLSG 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 137 GEKQRVSIARALSRNPKWLLCDEATSSLDeenTESVVRLLHktH-QEFRPTIFFVSH 192
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLEQ--FlHDYPGTVVAVTH 218
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
20-229 5.34e-16

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 76.49  E-value: 5.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  20 IHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKE-VRQ-------QQQQMGMVfQHYNLLE 91
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaIRAgimlcpeDRKAEGII-PVHSVAD 350
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  92 NLKIY------------------DNVALPLKLLKEKQPEkIERLLTFvdmahkaeaypaqLSGGEKQRVSIARALSRNPK 153
Cdd:PRK11288 351 NINISarrhhlragclinnrweaENADRFIRSLNIKTPS-REQLIMN-------------LSGGNQQKAILGRWLSEDMK 416
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGEfLNNPQQYEEEPLS 229
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIYELAAQGV-AVLFVSSDLPEVLGVADRIVVMREGRIAGE-LAREQATERQALS 490
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
20-176 7.02e-16

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 73.73  E-value: 7.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  20 IHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVFQHYNLLENLKIydnv 99
Cdd:PRK13543  30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHF---- 105
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 100 alpLKLLKEKQPEKIE-RLLTFVDMAHKAEAYPAQLSGGEKQRVSIARA-LSRNPKWLLcDEATSSLDEENTESVVRLL 176
Cdd:PRK13543 106 ---LCGLHGRRAKQMPgSALAIVGLAGYEDTLVRQLSAGQKKRLALARLwLSPAPLWLL-DEPYANLDLEGITLVNRMI 180
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
17-216 7.45e-16

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 76.20  E-value: 7.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKkevrQQQQQMGMVF-----QHYNLLE 91
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSP----QDGLANGIVYisedrKRDGLVL 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  92 NLKIYDNVALP-LKLLKE-----KQPEKIERLLTFVDMAH----KAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:PRK10762 344 GMSVKENMSLTaLRYFSRaggslKHADEQQAVSDFIRLFNiktpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488289759 162 SSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGEF 216
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAEGL-SIILVSSEMPEVLGMSDRILVMHEGRISGEF 477
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
2-126 8.50e-16

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 75.99  E-value: 8.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETH-----ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVRQQ 76
Cdd:COG4615  328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAY 404
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMGMVFQHYNLLENLkiydnvalpLKLLKEKQPEKIERLLTFVDMAHK 126
Cdd:COG4615  405 RQLFSAVFSDFHLFDRL---------LGLDGEADPARARELLERLELDHK 445
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
16-213 8.61e-16

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 75.22  E-value: 8.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQP----SEGEIRIDGRNVQTFSKKEVRQQ-QQQMGMVFQH---- 86
Cdd:PRK15093  22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKLvGHNVSMIFQEpqsc 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  87 --------YNLLENLKIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKA--EAYPAQLSGGEKQRVSIARALSRNPKWLL 156
Cdd:PRK15093 102 ldpservgRQLMQNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDamRSFPYELTEGECQKVMIAIALANQPRLLI 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 157 CDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:PRK15093 182 ADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
18-221 1.23e-15

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 73.58  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  18 KNIHFSVQLGEIVGIVGKSGSGKS-TLLRLLNLME---QPSEGEIRIDGRNV--QTFSKKEVRQQQQQMGMVFQ-----H 86
Cdd:PRK10418  20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKPVapCALRGRKIATIMQNPRSAFNplhtmH 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  87 YNLLENLK---IYDNVALPLKLLKEKQPEKIERLLtfvdmahkaEAYPAQLSGGEKQRVSIARAL-SRNPkWLLCDEATS 162
Cdd:PRK10418 100 THARETCLalgKPADDATLTAALEAVGLENAARVL---------KLYPFEMSGGMLQRMMIALALlCEAP-FIIADEPTT 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 163 SLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI-----GEFLNNPQ 221
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVeqgdvETLFNAPK 233
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
18-230 1.53e-15

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 75.21  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  18 KNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKE--------VRQQQQQMGMvFQHYNL 89
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkkgmayITESRRDNGF-FPNFSI 358
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  90 LENLKIYDNVAL-----PLKLLKEKQPEKI---ERLLTFVDmAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:PRK09700 359 AQNMAISRSLKDggykgAMGLFHEVDEQRTaenQRELLALK-CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 162 SSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIGEFLNNPQQYEEEPLSY 230
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMAW 505
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
2-212 1.55e-15

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: 73.74  E-value: 1.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQE--THALKNIHFSVQLGEIVGIVGKSGSGKSTL----LRLLNlmeqpSEGEIRIDGRNVQTFSKKEVRq 75
Cdd:cd03289    3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVPLQKWR- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  76 qqQQMGMVFQ-----------------HYNLLENLKIYDNVAlpLKLLKEKQPEKIErlLTFVDMAHkaeaypaQLSGGE 138
Cdd:cd03289   77 --KAFGVIPQkvfifsgtfrknldpygKWSDEEIWKVAEEVG--LKSVIEQFPGQLD--FVLVDGGC-------VLSHGH 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 139 KQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRlCNRILVMEKGQL 212
Cdd:cd03289  144 KQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADC--TVILSEHRIEAMLE-CQRFLVIEENKV 214
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1-239 2.12e-15

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 74.99  E-value: 2.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskkevRQQQ--- 77
Cdd:PRK11147   3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVA------RLQQdpp 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  78 -QQMGMVF-------QHynLLENLKIYDNValpLKLLKEKQPEK----IERLLTFVDMAH-----------------KAE 128
Cdd:PRK11147  77 rNVEGTVYdfvaegiEE--QAEYLKRYHDI---SHLVETDPSEKnlneLAKLQEQLDHHNlwqlenrinevlaqlglDPD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 129 AYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLhkthQEFRPTIFFVSHELETVKRLCNRILVME 208
Cdd:PRK11147 152 AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL----KTFQGSIIFISHDRSFIRNMATRIVDLD 227
                        250       260       270
                 ....*....|....*....|....*....|.
gi 488289759 209 KGQLIgeflNNPQQYEEeplsYLEKVERSLR 239
Cdd:PRK11147 228 RGKLV----SYPGNYDQ----YLLEKEEALR 250
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
1-193 2.34e-15

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 71.90  E-value: 2.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfsKKEVRQQQQQM 80
Cdd:PRK13540   1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  81 GMVFQHYNLLENLKIYDNVALPLKLlkEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEA 160
Cdd:PRK13540  77 CFVGHRSGINPYLTLRENCLYDIHF--SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
                        170       180       190
                 ....*....|....*....|....*....|...
gi 488289759 161 TSSLDEENTESVVRLLhKTHQEFRPTIFFVSHE 193
Cdd:PRK13540 155 LVALDELSLLTIITKI-QEHRAKGGAVLLTSHQ 186
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
19-219 7.12e-15

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: 73.32  E-value: 7.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   19 NIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLMEQPSEGEIRIDGRNVQTFSKKE--------VRQQQQQMGMVFQ---H 86
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQairagiamVPEDRKRHGIVPIlgvG 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   87 YNLleNLKIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKAEAYP-AQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:TIGR02633 358 KNI--TLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488289759  166 EENTESVVRLLHKTHQEfRPTIFFVSHELETVKRLCNRILVMEKGQLIGEFLNN 219
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNH 488
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
19-219 1.20e-14

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 72.65  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  19 NIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLMEQPSEGEIRIDGRNVQTFSKKEVrqQQQQMGMVFQ---HYNLLENLK 94
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKIRNPQQA--IAQGIAMVPEdrkRDGIVPVMG 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  95 IYDNVALPL-----------KLLKEKQPEK-IERLLtfVDMAHkAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATS 162
Cdd:PRK13549 358 VGKNITLAAldrftggsridDAAELKTILEsIQRLK--VKTAS-PELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488289759 163 SLDEENTESVVRLLHKTHQEfRPTIFFVSHELETVKRLCNRILVMEKGQLIGEFLNN 219
Cdd:PRK13549 435 GIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINH 490
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
27-208 2.09e-14

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 71.76  E-value: 2.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  27 GEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDgrnvQTFSKKEVRQQQQQMGMVFQhynLLENLK-------IYDNV 99
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----LKISYKPQYIKPDYDGTVED---LLRSITddlgssyYKSEI 437
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 100 ALPLKLlkekqpekiERLLtfvdmahkaEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKT 179
Cdd:PRK13409 438 IKPLQL---------ERLL---------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRI 499
                        170       180
                 ....*....|....*....|....*....
gi 488289759 180 HQEFRPTIFFVSHELETVKRLCNRILVME 208
Cdd:PRK13409 500 AEEREATALVVDHDIYMIDYISDRLMVFE 528
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
23-208 4.61e-14

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: 70.97  E-value: 4.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  23 SVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIR---------------IDGRnVQTFSKKEVRQQqqqmgmvfqhy 87
Cdd:COG1245  362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkisykpqyispdYDGT-VEEFLRSANTDD----------- 429
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  88 nlLENLKIYDNVALPLKLlkekqpekiERLLtfvdmahkaEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:COG1245  430 --FGSSYYKTEIIKPLGL---------EKLL---------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 488289759 168 NTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVME 208
Cdd:COG1245  490 QRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE 530
GguA NF040905
sugar ABC transporter ATP-binding protein;
1-213 9.97e-14

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 69.82  E-value: 9.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLnlmeqpS--------EGEIRIDGrNVQTFskKE 72
Cdd:NF040905   1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVL------SgvyphgsyEGEILFDG-EVCRF--KD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  73 VRQQQQQmGMVFQHYNL--LENLKIYDNVALPLKLLK------EKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSI 144
Cdd:NF040905  72 IRDSEAL-GIVIIHQELalIPYLSIAENIFLGNERAKrgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEI 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 145 ARALSRNPKWLLCDEATSSLDEENTESVVRLLHkthqEFRP---TIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLL----ELKAqgiTSIIISHKLNEIRRVADSITVLRDGRTI 218
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
2-225 1.05e-13

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 69.92  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRidgrnvqtFSKKevrqqqQQMG 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK--------WSEN------ANIG 385
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQ-HYNLLEN-LKIYDNVAlplkllKEKQPEKIE--------RLLTFVDMAHKAeayPAQLSGGEKQRVSIARALSRN 151
Cdd:PRK15064 386 YYAQdHAYDFENdLTLFDWMS------QWRQEGDDEqavrgtlgRLLFSQDDIKKS---VKVLSGGEKGRMLFGKLMMQK 456
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289759 152 PKWLLCDEATSSLDEENTESVVRLLHKthqeFRPTIFFVSHELETVKRLCNRILVMEKGQLIgEFLNNpqqYEE 225
Cdd:PRK15064 457 PNVLVMDEPTNHMDMESIESLNMALEK----YEGTLIFVSHDREFVSSLATRIIEITPDGVV-DFSGT---YEE 522
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1-210 1.58e-13

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 69.66  E-value: 1.58e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759     1 MIELVNVSKVYQETH--ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskkEVRQQQQ 78
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDVHQ 2012
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    79 QMGMVFQHYNLLENLKIYDNVALPLKlLKEKQPEKIERLLTF----VDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKW 154
Cdd:TIGR01257 2013 NMGYCPQFDAIDDLLTGREHLYLYAR-LRGVPAEEIEKVANWsiqsLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 488289759   155 LLCDEATSSLDEENTESVVRLLHKTHQEFRPTIfFVSHELETVKRLCNRILVMEKG 210
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREGRAVV-LTSHSMEECEALCTRLAIMVKG 2146
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
17-208 3.36e-13

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: 68.78  E-value: 3.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    17 LKNIHFSVQLGEIVGIVGKSGSGKSTL----LRLLNlmeqpSEGEIRIDGRNVQTFSkkeVRQQQQQMGMV--------- 83
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLlsalLRLLS-----TEGEIQIDGVSWNSVT---LQTWRKAFGVIpqkvfifsg 1306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    84 --------FQHYNLLENLKIYDNVAlpLKLLKEKQPEKIERLLtfVDMAHkaeaypaQLSGGEKQRVSIARALSRNPKWL 155
Cdd:TIGR01271 1307 tfrknldpYEQWSDEEIWKVAEEVG--LKSVIEQFPDKLDFVL--VDGGY-------VLSNGHKQLMCLARSILSKAKIL 1375
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 488289759   156 LCDEATSSLDEENTESVVRLLHKTHQEFrpTIFFVSHELETVKRlCNRILVME 208
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSFSNC--TVILSEHRVEALLE-CQQFLVIE 1425
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
15-225 4.01e-13

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 66.76  E-value: 4.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  15 HALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGrnvqtfskkevrqqqqQMGMVFQHYNLLENLK 94
Cdd:PRK13546  38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAISAGLSGQLT 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  95 IYDNVALPL-------KLLKEKQPEKIErlltFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:PRK13546 102 GIENIEFKMlcmgfkrKEIKAMTPKIIE----FSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 168 NTESVVRLLHKtHQEFRPTIFFVSHELETVKRLCNRILVMEKGQL--IGEFLNNPQQYEE 225
Cdd:PRK13546 178 FAQKCLDKIYE-FKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLkdYGELDDVLPKYEA 236
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
17-213 4.07e-13

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: 65.75  E-value: 4.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPS---EGEIRIDGRNvqtfSKKEVRQQQQQMGMVFQHynllenl 93
Cdd:cd03233   23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP----YKEFAEKYPGEIIYVSEE------- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  94 kiyDNvalplkllkeKQPE-KIERLLTFVDMAhKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENT-ES 171
Cdd:cd03233   92 ---DV----------HFPTlTVRETLDFALRC-KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAlEI 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488289759 172 VVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLI 213
Cdd:cd03233  158 LKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
27-208 1.39e-12

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: 63.75  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  27 GEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTfskkevrqqqqqmgmvfqhynllenlkiydnvalplkll 106
Cdd:cd03222   25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVY--------------------------------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 107 kekQPEKIErlltfvdmahkaeaypaqLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPT 186
Cdd:cd03222   66 ---KPQYID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKT 124
                        170       180
                 ....*....|....*....|..
gi 488289759 187 IFFVSHELETVKRLCNRILVME 208
Cdd:cd03222  125 ALVVEHDLAVLDYLSDRIHVFE 146
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
17-210 1.41e-12

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


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 64.19  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPS--EGEIRIDGR-NVQTFskkevrqqQQQMGMVFQHYNLLENL 93
Cdd:cd03232   23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRpLDKNF--------QRSTGYVEQQDVHSPNL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  94 KIYDNvalplkllkekqpekierlLTFvdmahkaEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVV 173
Cdd:cd03232   95 TVREA-------------------LRF-------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 488289759 174 RLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKG 210
Cdd:cd03232  149 RFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRG 185
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
2-225 2.55e-12

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 65.53  E-value: 2.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIdGRNVqtfskkevrqqqqQMG 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-------------KLA 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  82 MVFQHYNLLENLK-IYDNVALPLKLLKEKQPEKIERlltfvdmahkaeAYPA--------------QLSGGEKQRVSIAR 146
Cdd:PRK11819 391 YVDQSRDALDPNKtVWEEISGGLDIIKVGNREIPSR------------AYVGrfnfkggdqqkkvgVLSGGERNRLHLAK 458
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 147 ALSRNPKWLLCDEATSSLDEENtesvVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEkgqliGE-----FLNNPQ 221
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDVET----LRALEEALLEFPGCAVVISHDRWFLDRIATHILAFE-----GDsqvewFEGNFQ 529

                 ....
gi 488289759 222 QYEE 225
Cdd:PRK11819 530 EYEE 533
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
17-178 3.17e-12

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: 63.31  E-value: 3.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLlnLMEQPS----EGEIRIDGRNvqtfskkevrqqqqqmgmvfqhynlLEN 92
Cdd:cd03217   16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKT--IMGHPKyevtEGEILFKGED-------------------------ITD 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  93 LKIYDNVALPLKLLKEKQPE----KIERLLTFVDMAhkaeaypaqLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEEN 168
Cdd:cd03217   69 LPPEERARLGIFLAFQYPPEipgvKNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
                        170
                 ....*....|
gi 488289759 169 TESVVRLLHK 178
Cdd:cd03217  140 LRLVAEVINK 149
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
16-211 5.02e-12

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 65.15  E-value: 5.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  16 ALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIR-----IDGRNVQTfsKKEVrqqqqqmGMVFQHYNLL 90
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIAT--RRRV-------GYMSQAFSLY 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  91 ENLKIYDNVALPLKLL---KEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:NF033858 352 GELTVRQNLELHARLFhlpAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488289759 168 NTESVVRLLHKTHQEFRPTIFFVSH---ELEtvkRlCNRILVMEKGQ 211
Cdd:NF033858 432 ARDMFWRLLIELSREDGVTIFISTHfmnEAE---R-CDRISLMHAGR 474
PLN03211 PLN03211
ABC transporter G-25; Provisional
12-211 6.25e-12

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 64.52  E-value: 6.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  12 QETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPS--EGEIRIDGRnvqtfskKEVRQQQQQMGMVFQ---- 85
Cdd:PLN03211  79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNR-------KPTKQILKRTGFVTQddil 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  86 --HYNLLENLKIYDNVALPLKLLKEKQPEKIERLLTFVDMAhKAE------AYPAQLSGGEKQRVSIARALSRNPKWLLC 157
Cdd:PLN03211 152 ypHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLT-KCEntiignSFIRGISGGERKRVSIAHEMLINPSLLIL 230
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
27-204 2.78e-11

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: 59.69  E-value: 2.78e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    27 GEIVGIVGKSGSGKSTLLRLL-NLMEQPSEGEIRIDGrnvqtfskkevrqqqqqmgmvfqhynllenlkiydnvalplkl 105
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDG------------------------------------------- 38
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   106 lkekqpEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENT-----ESVVRLLHKTH 180
Cdd:smart00382  39 ------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELRLLLLLK 112
                          170       180
                   ....*....|....*....|....
gi 488289759   181 QEFRPTIFFVSHELETVKRLCNRI 204
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPALLRR 136
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
23-207 1.47e-10

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: 59.30  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  23 SVQLGEIVGIVGKSGSGKSTLLRLL------NLMEQPSEGEIR--ID---GRNVQTFSKKeVRQQQQQMGMVFQHYNLLE 91
Cdd:cd03236   22 VPREGQVLGLVGPNGIGKSTALKILagklkpNLGKFDDPPDWDeiLDefrGSELQNYFTK-LLEGDVKVIVKPQYVDLIP 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  92 NlKIYDNVALPLKLLKEKqpEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTES 171
Cdd:cd03236  101 K-AVKGKVGELLKKKDER--GKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488289759 172 VVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVM 207
Cdd:cd03236  178 AARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL 212
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
17-210 2.41e-10

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: 58.50  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLrLLNLME-QPSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVFQHYNLLENLKI 95
Cdd:cd03290   17 LSNINIRIPTGQLTMIVGQVGCGKSSLL-LAILGEmQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNATV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  96 YDNVALPLKLLKEKQPEKIER--------LLTFVDMAHKAEAyPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:cd03290   96 EENITFGSPFNKQRYKAVTDAcslqpdidLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488289759 168 NT-----ESVVRLLhkthQEFRPTIFFVSHELETVKRlCNRILVMEKG 210
Cdd:cd03290  175 LSdhlmqEGILKFL----QDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
PLN03130 PLN03130
ABC transporter C family member; Provisional
13-165 2.78e-10

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 60.14  E-value: 2.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   13 ETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLnLMEQP--SEGEIRIDGRNVQTfskkevrqqqQQMGMVFqhynll 90
Cdd:PLN03130  629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM-LGELPprSDASVVIRGTVAYV----------PQVSWIF------ 691
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   91 eNLKIYDNVALPLKLlkekQPEKIERLLTFVDMAHKAEAYPA-----------QLSGGEKQRVSIARALSRNPKWLLCDE 159
Cdd:PLN03130  692 -NATVRDNILFGSPF----DPERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDD 766

                  ....*.
gi 488289759  160 ATSSLD 165
Cdd:PLN03130  767 PLSALD 772
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
1-214 3.41e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 59.36  E-value: 3.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQEThaLKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKE-------- 72
Cdd:PRK10982 250 ILEVRNLTSLRQPS--IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfal 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  73 VRQQQQQMGMVFQ---HYN-LLENLKIYDNvalPLKLLKEKqpeKIERLLTFV--DMAHKAEAYPAQ---LSGGEKQRVS 143
Cdd:PRK10982 328 VTEERRSTGIYAYldiGFNsLISNIRNYKN---KVGLLDNS---RMKSDTQWVidSMRVKTPGHRTQigsLSGGNQQKVI 401
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488289759 144 IARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQLIG 214
Cdd:PRK10982 402 IGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLVAG 471
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
17-211 2.91e-09

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: 56.02  E-value: 2.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRnvQTFSKK------EVRQQQQQMGMVFQHYNLL 90
Cdd:cd03291   53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSSQfswimpGTIKENIIFGVSYDEYRYK 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  91 ENLKiydnvALPLKLLKEKQPEKIERLLtfvdmahkAEAyPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD----E 166
Cdd:cd03291  131 SVVK-----ACQLEEDITKFPEKDNTVL--------GEG-GITLSGGQRARISLARAVYKDADLYLLDSPFGYLDvfteK 196
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 488289759 167 ENTESVVRLLHKTHqefrpTIFFVSHELETVKRlCNRILVMEKGQ 211
Cdd:cd03291  197 EIFESCVCKLMANK-----TRILVTSKMEHLKK-ADKILILHEGS 235
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
17-213 4.29e-09

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: 55.30  E-value: 4.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVRQQQQQMGMVFQ---------HY 87
Cdd:cd03288   37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI---SKLPLHTLRSRLSIILQdpilfsgsiRF 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  88 NLLENLKIYDNV---ALP---LKLLKEKQPEKIERLLTfvdmaHKAEAYpaqlSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:cd03288  114 NLDPECKCTDDRlweALEiaqLKNMVKSLPGGLDAVVT-----EGGENF----SVGQRQLFCLARAFVRKSSILIMDEAT 184
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488289759 162 SSLDEEnTESVVRLLHKTHQEFRpTIFFVSHELETVKRlCNRILVMEKGQLI 213
Cdd:cd03288  185 ASIDMA-TENILQKVVMTAFADR-TVVTIAHRVSTILD-ADLVLVLSRGILV 233
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
27-194 5.86e-09

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: 55.56  E-value: 5.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  27 GEIVGIVGKSGSGKSTLLRLL---------NLMEQPSEGEI--RIDGRNVQTF----SKKEVR-----QQQQQMGMVFQH 86
Cdd:COG1245   99 GKVTGILGPNGIGKSTALKILsgelkpnlgDYDEEPSWDEVlkRFRGTELQDYfkklANGEIKvahkpQYVDLIPKVFKG 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  87 yNLLENLKIYDNvalplkllKEKQPEKIERLltfvDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDE 166
Cdd:COG1245  179 -TVRELLEKVDE--------RGKLDELAEKL----GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
                        170       180
                 ....*....|....*....|....*...
gi 488289759 167 ENTESVVRLLHKTHQEFRPtIFFVSHEL 194
Cdd:COG1245  246 YQRLNVARLIRELAEEGKY-VLVVEHDL 272
PLN03073 PLN03073
ABC transporter F family; Provisional
18-193 6.12e-09

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 55.64  E-value: 6.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  18 KNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIridgrnvqtFSKKEVRqqqqqMGMVFQHYnlLENLKIYD 97
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV---------FRSAKVR-----MAVFSQHH--VDGLDLSS 589
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  98 NVALPLKLLKEKQPEKIER--LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRL 175
Cdd:PLN03073 590 NPLLYMMRCFPGVPEQKLRahLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQG 669
                        170
                 ....*....|....*...
gi 488289759 176 LhkthQEFRPTIFFVSHE 193
Cdd:PLN03073 670 L----VLFQGGVLMVSHD 683
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
14-210 6.75e-09

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 55.69  E-value: 6.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    14 THALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRnvQTFSKKE------VRQQQQQMGMVFQHY 87
Cdd:TIGR01271  439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSPQTswimpgTIKDNIIFGLSYDEY 516
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    88 NLLENLKiydnvALPLKLLKEKQPEKIERLLTFVDMAhkaeaypaqLSGGEKQRVSIARALSRNPKWLLCDEATSSLD-- 165
Cdd:TIGR01271  517 RYTSVIK-----ACQLEEDIALFPEKDKTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFTHLDvv 582
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 488289759   166 --EENTESVVRLLHKTHqefrpTIFFVSHELETVKRlCNRILVMEKG 210
Cdd:TIGR01271  583 teKEIFESCLCKLMSNK-----TRILVTSKLEHLKK-ADKILLLHEG 623
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
17-179 9.01e-09

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 55.50  E-value: 9.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLN---LMEQPSEGEIRIDGRNVQ-TFSKKEVRQQQQQMGMvfQHYNLLEN 92
Cdd:TIGR00956  779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervTTGVITGGDRLVNGRPLDsSFQRSIGYVQQQDLHL--PTSTVRES 856
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    93 LKIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKAEAY---PAQ-LSGGEKQRVSIARALSRNPKWLL-CDEATSSLDEE 167
Cdd:TIGR00956  857 LRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQ 936
                          170
                   ....*....|..
gi 488289759   168 NTESVVRLLHKT 179
Cdd:TIGR00956  937 TAWSICKLMRKL 948
PLN03232 PLN03232
ABC transporter C family member; Provisional
17-200 9.25e-09

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 55.37  E-value: 9.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLnLMEQPSEGEIRIDGRNVQTFSKkevrqqqqQMGMVFqhynlleNLKIY 96
Cdd:PLN03232  633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAM-LGELSHAETSSVVIRGSVAYVP--------QVSWIF-------NATVR 696
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   97 DNVALPLKLlkekQPEKIERLLTFVDMAHKAEAYPAQ-----------LSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:PLN03232  697 ENILFGSDF----ESERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 488289759  166 EentesvvrllHKTHQEFRPTIffvSHELETVKRL 200
Cdd:PLN03232  773 A----------HVAHQVFDSCM---KDELKGKTRV 794
hmuV PRK13547
heme ABC transporter ATP-binding protein;
17-215 1.07e-08

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 54.45  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLL--NLMEQPS------EGEIRIDGRNV------QTFSKKEVRQQQQQMGM 82
Cdd:PRK13547  17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGGGAprgarvTGDVTLNGEPLaaidapRLARLRAVLPQAAQPAF 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  83 VFQHYNLLeNLKIYDNvALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALS---------RNPK 153
Cdd:PRK13547  97 AFSAREIV-LLGRYPH-ARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPR 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 154 WLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
2-165 1.75e-08

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 54.36  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVqtfSKKEVRQQQ---- 77
Cdd:NF033858   2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM---ADARHRRAVcpri 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  78 ----QQMGMvfqhyNLLENLKIYDNVALPLKLLKEKQPE---KIERLLTFVDMAHKAEAyPA-QLSGGEKQRVSIARALS 149
Cdd:NF033858  79 aympQGLGK-----NLYPTLSVFENLDFFGRLFGQDAAErrrRIDELLRATGLAPFADR-PAgKLSGGMKQKLGLCCALI 152
                        170
                 ....*....|....*.
gi 488289759 150 RNPKWLLCDEATSSLD 165
Cdd:NF033858 153 HDPDLLILDEPTTGVD 168
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
17-165 1.96e-08

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: 54.57  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLR-LLNLMEQpSEGEIRIDGrnvqtfSKKEVRQQQqqmgmvfqhynLLENLKI 95
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKG------SVAYVPQQA-----------WIQNDSL 715
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    96 YDNVALPLKLLKEKQPEKIERLLTFVDMahkaEAYPA-----------QLSGGEKQRVSIARALSRNPKWLLCDEATSSL 164
Cdd:TIGR00957  716 RENILFGKALNEKYYQQVLEACALLPDL----EILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791

                   .
gi 488289759   165 D 165
Cdd:TIGR00957  792 D 792
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
29-176 2.37e-08

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 52.57  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  29 IVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDGRNVQTFSKKEVRQQQQQMGMVFQhYNLLENLK----IYDNValplk 104
Cdd:PRK13541  28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLE-MTVFENLKfwseIYNSA----- 101
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 105 llkekqpEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLL 176
Cdd:PRK13541 102 -------ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
27-165 5.40e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 52.89  E-value: 5.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  27 GEIVGIVGKSGSGKSTLLRLL---------NLMEQPSEGEI--RIDGRNVQTF----SKKEVR-----QQQQQMGMVFQH 86
Cdd:PRK13409  99 GKVTGILGPNGIGKTTAVKILsgelipnlgDYEEEPSWDEVlkRFRGTELQNYfkklYNGEIKvvhkpQYVDLIPKVFKG 178
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759  87 yNLLENLKIYDNvalplkllKEKQPEKIERLltfvDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLD 165
Cdd:PRK13409 179 -KVRELLKKVDE--------RGKLDEVVERL----GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
7-193 1.06e-07

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 52.09  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   7 VSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIdgrnvqtfsKKEVRqqqqqMGMVFQH 86
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGIK-----LGYFAQH 383
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  87 YnlLENLKIYDNvalPLKLLKEKQPEKIERLLT-----FVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:PRK10636 384 Q--LEFLRADES---PLQHLARLAPQELEQKLRdylggFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
                        170       180       190
                 ....*....|....*....|....*....|..
gi 488289759 162 SSLDEENTESVVRLLhkthQEFRPTIFFVSHE 193
Cdd:PRK10636 459 NHLDLDMRQALTEAL----IDFEGALVVVSHD 486
ycf16 CHL00131
sulfate ABC transporter protein; Validated
1-213 1.40e-07

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 50.80  E-value: 1.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLlnLMEQPS----EGEIRIDGRNVQTFSKKEvrqq 76
Cdd:CHL00131   7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKV--IAGHPAykilEGDILFKGESILDLEPEE---- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 QQQMG--MVFQH------YNLLENLKIYDNVALPLKLLKEKQP----EKIERLLTFVDMAHK------AEAYpaqlSGGE 138
Cdd:CHL00131  81 RAHLGifLAFQYpieipgVSNADFLRLAYNSKRKFQGLPELDPleflEIINEKLKLVGMDPSflsrnvNEGF----SGGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 139 KQRVSIARALSRNPKWLLCDEATSSLD----EENTESVVRLLHKTHqefrpTIFFVSHeletVKRLCNRIL-----VMEK 209
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDidalKIIAEGINKLMTSEN-----SIILITH----YQRLLDYIKpdyvhVMQN 227

                 ....
gi 488289759 210 GQLI 213
Cdd:CHL00131 228 GKII 231
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
2-180 2.78e-07

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 49.62  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVsKVYQETHalkNIHFSvqlGEIVGIVGKSGSGKSTLLRLLNL---MEQPSEGEIRIDGRNVQ--------TFSK 70
Cdd:COG0419    5 LRLENF-RSYRDTE---TIDFD---DGLNLIVGPNGAGKSTILEAIRYalyGKARSRSKLRSDLINVGseeasvelEFEH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  71 KE-----VRQQQQQMGMVFQHYNLLE-------NLKIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKAEAY------PA 132
Cdd:COG0419   78 GGkryriERRQGEFAEFLEAKPSERKealkrllGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQlsgldpIE 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488289759 133 QLSGGEKQRVSIARALSrnpkwLLCDeaTSSLDEENTESVVRLLHK----TH 180
Cdd:COG0419  158 TLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEElaiiTH 202
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
5-211 3.42e-07

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: 48.86  E-value: 3.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   5 VNVSKVYQetHALKNIHFSVQLGEIVGIVGKSGSGKSTLLrllnLMEQPSEGEIRIDGrNVQTFSKkevrqqqQQMGMVF 84
Cdd:cd03238    1 LTVSGANV--HNLQNLDVSIPLNVLVVVTGVSGSGKSTLV----NEGLYASGKARLIS-FLPKFSR-------NKLIFID 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  85 QHYNLLENLKIYdnvaLPLkllkekqpekiERLLtfvdmahkaeaypAQLSGGEKQRVSIARALSRNPK--WLLCDEATS 162
Cdd:cd03238   67 QLQFLIDVGLGY----LTL-----------GQKL-------------STLSGGELQRVKLASELFSEPPgtLFILDEPST 118
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488289759 163 SLDEENT----ESVVRLLHKTHqefrpTIFFVSHELETVKRlCNRILVMEKGQ 211
Cdd:cd03238  119 GLHQQDInqllEVIKGLIDLGN-----TVILIEHNLDVLSS-ADWIIDFGPGS 165
PTZ00243 PTZ00243
ABC transporter; Provisional
17-174 3.88e-07

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 50.55  E-value: 3.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRllNLMeqpSEGEIRiDGRNVQTFSKKEVRQQQQQMgmvfqhynlleNLKIY 96
Cdd:PTZ00243  676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQ--SLL---SQFEIS-EGRVWAERSIAYVPQQAWIM-----------NATVR 738
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   97 DNVALplkllkeKQPEKIERLLTFVDMAhKAEAYPAQL---------------SGGEKQRVSIARALSRNPKWLLCDEAT 161
Cdd:PTZ00243  739 GNILF-------FDEEDAARLADAVRVS-QLEADLAQLgggleteigekgvnlSGGQKARVSLARAVYANRDVYLLDDPL 810
                         170
                  ....*....|...
gi 488289759  162 SSLDEENTESVVR 174
Cdd:PTZ00243  811 SALDAHVGERVVE 823
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
3-193 6.11e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 49.56  E-value: 6.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   3 ELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPSEGEIRIDgrnvqtfSKKEVrqqqqqmgM 82
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-------TKLEV--------A 385
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  83 VF-QHYNLLENLK-IYDNVAlplkllKEKQPEKI---ER-----LLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNP 152
Cdd:PRK11147 386 YFdQHRAELDPEKtVMDNLA------EGKQEVMVngrPRhvlgyLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPS 459
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 488289759 153 KWLLCDEATSSLDEENTEsvvrLLHKTHQEFRPTIFFVSHE 193
Cdd:PRK11147 460 NLLILDEPTNDLDVETLE----LLEELLDSYQGTVLLVSHD 496
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
134-192 5.75e-06

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


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 46.67  E-value: 5.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759  134 LSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLhkthQEFRPTIFFVSH 192
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
GguA NF040905
sugar ABC transporter ATP-binding protein;
10-216 6.13e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 46.71  E-value: 6.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  10 VYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLlrllnLME-------QPSEGEIRIDGRNVQTFSKKE--------VR 74
Cdd:NF040905 269 LHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTEL-----AMSvfgrsygRNISGTVFKDGKEVDVSTVSDaidaglayVT 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  75 QQQQQMGMvfqhyNLLENLKiyDNVALP-LKLLKEKqpekierllTFVDmAHK----AEAYPA--------------QLS 135
Cdd:NF040905 344 EDRKGYGL-----NLIDDIK--RNITLAnLGKVSRR---------GVID-ENEeikvAEEYRKkmniktpsvfqkvgNLS 406
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 136 GGEKQRVSIARALSRNPKWLLCDEATSSLD-----EENTesVVRLLHKTHQefrpTIFFVSHELETVKRLCNRILVMEKG 210
Cdd:NF040905 407 GGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgakyEIYT--IINELAAEGK----GVIVISSELPELLGMCDRIYVMNEG 480

                 ....*.
gi 488289759 211 QLIGEF 216
Cdd:NF040905 481 RITGEL 486
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
17-213 6.34e-06

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 46.64  E-value: 6.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNL----MEQPSEGEIRIDGrnvqtFSKKEVRQQQQ-------QMGMVFQ 85
Cdd:TIGR00956   77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDG-----ITPEEIKKHYRgdvvynaETDVHFP 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759    86 HYNLLENLkiyDNVALplklLKEKQ--PEKIERLltfVDMAHKAEAYPAQL------------------SGGEKQRVSIA 145
Cdd:TIGR00956  152 HLTVGETL---DFAAR----CKTPQnrPDGVSRE---EYAKHIADVYMATYglshtrntkvgndfvrgvSGGERKRVSIA 221
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   146 RALSRNPKWLLCDEATSSLDEENTESVVRLLhKTHQEFRPTIFFVS--HELETVKRLCNRILVMEKGQLI 213
Cdd:TIGR00956  222 EASLGGAKIQCWDNATRGLDSATALEFIRAL-KTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQI 290
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
14-198 1.44e-05

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: 44.56  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  14 THALKNIHFSVQLGEIVGIVGKSGSGKSTLL---------------------RLLNLMEQPS----EG---EIRIDgrnv 65
Cdd:cd03270    8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDvdsiEGlspAIAID---- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  66 QTFSKKEVRqqqQQMGMVFQHYNLLENLkiYDNVALplkllkekqpekIERL-------LTFVDMAHKAEAypaqLSGGE 138
Cdd:cd03270   84 QKTTSRNPR---STVGTVTEIYDYLRLL--FARVGI------------RERLgflvdvgLGYLTLSRSAPT----LSGGE 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 139 KQRVSIARALSRNPKWLL--CDEATSSLDEENTESVVRLLHKThQEFRPTIFFVSHELETVK 198
Cdd:cd03270  143 AQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIR 203
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
14-217 1.72e-05

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 45.59  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   14 THALKNIHFSVQLGEIVGIVGKSGSGKSTLLR------LLNLMEQPSEGEIRIDG----------RNVQTFSKK------ 71
Cdd:PRK00635  608 KHNLKDLTISLPLGRLTVVTGVSGSGKSSLINdtlvpaVEEFIEQGFCSNLSIQWgaisrlvhitRDLPGRSQRsiplty 687
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   72 -----EVRQ---QQ---QQMGMVFQHYNL------------LENLKIYDN---VALPLKLLKEKQPEKIE------RLLT 119
Cdd:PRK00635  688 ikafdDLRElfaEQprsKRLGLTKSHFSFntplgacaecqgLGSITTTDNrtsIPCPSCLGKRFLPQVLEvrykgkNIAD 767
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  120 FVDM-AHKAEAY----P-----------------------AQLSGGEKQRVSIARAL---SRNPKWLLCDEATSSLDEEN 168
Cdd:PRK00635  768 ILEMtAYEAEKFfldePsihekihalcslgldylplgrplSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHD 847
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488289759  169 TESVVRLLHK-THQEFrpTIFFVSHELETVKrLCNRILVM--EKGQLIGEFL 217
Cdd:PRK00635  848 IKALIYVLQSlTHQGH--TVVIIEHNMHVVK-VADYVLELgpEGGNLGGYLL 896
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
32-200 2.10e-05

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


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 44.14  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  32 IVGKSGSGKSTLLRLLNLM---EQPSEGEIRIDGRNVqtFSKKEVRqqqQQMGMVFQH-----YNLLENLKIYDNVALPl 103
Cdd:cd03240   27 IVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKL--IREGEVR---AQVKLAFENangkkYTITRSLAILENVIFC- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 104 kllkeKQpEKIERLLtfVDMahkaeayPAQLSGGEKQ------RVSIARALSRNPKWLLCDEATSSLDEEN-TESVVRLL 176
Cdd:cd03240  101 -----HQ-GESNWPL--LDM-------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEII 165
                        170       180
                 ....*....|....*....|....
gi 488289759 177 HKTHQEFRPTIFFVSHELETVKRL 200
Cdd:cd03240  166 EERKSQKNFQLIVITHDEELVDAA 189
PLN03140 PLN03140
ABC transporter G family member; Provisional
17-179 2.79e-05

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 44.84  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLMEQPS--EGEIRIDG--RNVQTFSKkeVRQQQQQMGMVFQHYNLLEN 92
Cdd:PLN03140  896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfpKKQETFAR--ISGYCEQNDIHSPQVTVRES 973
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   93 LKIYDNVALPLKLLKEKQPEKIERLLTFVDMAHKAEA---YPA--QLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEE 167
Cdd:PLN03140  974 LIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAivgLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
                         170
                  ....*....|..
gi 488289759  168 NTESVVRLLHKT 179
Cdd:PLN03140 1054 AAAIVMRTVRNT 1065
PLN03073 PLN03073
ABC transporter F family; Provisional
27-214 3.88e-05

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 44.47  E-value: 3.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  27 GEIVGIVGKSGSGKSTLLRLLNL--------------MEQPSEGE--------IRIDGRNVQTFsKKEVRQQQQQMGMVF 84
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMAMhaidgipkncqilhVEQEVVGDdttalqcvLNTDIERTQLL-EEEAQLVAQQRELEF 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  85 QHYNLLENLKIYDNVAlplKLLKEKQPEKIERLLTFVDmAHKAEAYPA------------------QLSGGEKQRVSIAR 146
Cdd:PLN03073 282 ETETGKGKGANKDGVD---KDAVSQRLEEIYKRLELID-AYTAEARAAsilaglsftpemqvkatkTFSGGWRMRIALAR 357
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289759 147 ALSRNPKWLLCDEATSSLDEEntesVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKGQLIG 214
Cdd:PLN03073 358 ALFIEPDLLLLDEPTNHLDLH----AVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVT 421
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
32-200 4.08e-05

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: 42.73  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  32 IVGKSGSGKSTLLRLLNLMEqpsegeiridgrnvqtfskkevrqqqqqmGMVFQHYNLLENLKIYDNVALplkllkekqp 111
Cdd:cd03227   26 ITGPNGSGKSTILDAIGLAL-----------------------------GGAQSATRRRSGVKAGCIVAA---------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759 112 EKIERLLTFVdmahkaeaypaQLSGGEKQRVSIARAL---SRNPKWLLC-DEATSSLDEENTESVVRLLHKTHQEFRpTI 187
Cdd:cd03227   67 VSAELIFTRL-----------QLSGGEKELSALALILalaSLKPRPLYIlDEIDRGLDPRDGQALAEAILEHLVKGA-QV 134
                        170
                 ....*....|...
gi 488289759 188 FFVSHELETVKRL 200
Cdd:cd03227  135 IVITHLPELAELA 147
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
1-165 5.77e-05

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 43.24  E-value: 5.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   1 MIELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLNLME--QPSEGEIRIDGRNVQTFSKKEvrQQQQ 78
Cdd:PRK09580   1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED--RAGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  79 QMGMVFQHYNLLENL--KIYDNVALPlKLLKEKQPEKIERlLTFVD-MAHKAE--AYPAQL---------SGGEKQRVSI 144
Cdd:PRK09580  79 GIFMAFQYPVEIPGVsnQFFLQTALN-AVRSYRGQEPLDR-FDFQDlMEEKIAllKMPEDLltrsvnvgfSGGEKKRNDI 156
                        170       180
                 ....*....|....*....|.
gi 488289759 145 ARALSRNPKWLLCDEATSSLD 165
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLD 177
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
2-195 1.42e-04

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 42.31  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759   2 IELVNVSKVYQETHALKNIHFSVQLGEIVGIVGKSGSGKSTLLRLlnlmeqpsegeirIDGRNVQTFSKKEV---RQQ-- 76
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSL-------------ITGDHPQGYSNDLTlfgRRRgs 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  77 -------QQQMGMVFQHYNL----------------LENLKIYDNVAlplkllkEKQPEKIERLLTFVDM-AHKAEAYPA 132
Cdd:PRK10938 328 getiwdiKKHIGYVSSSLHLdyrvstsvrnvilsgfFDSIGIYQAVS-------DRQQKLAQQWLDILGIdKRTADAPFH 400
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289759 133 QLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTESVVRLLHKTHQEFRPTIFFVSHELE 195
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAE 463
SbcC_Walker_B pfam13558
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ...
132-178 1.53e-04

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


Pssm-ID: 463921 [Multi-domain]  Cd Length: 90  Bit Score: 39.53  E-value: 1.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  132 AQLSGGEKQR---VSIARALS--------RNPKWLLC--DEATSSLDEENTESVVRLLHK 178
Cdd:pfam13558  31 GGLSGGEKQLlayLPLAAALAaqygsaegRPPAPRLVflDEAFAKLDEENIRTALELLRA 90
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
15-198 2.27e-04

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: 41.45  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  15 HALKNIHFSVQLGEIVGIVGKSGSGKSTLL---------RLLNL-MEQPSEGE-----------IRID----GR----NV 65
Cdd:cd03271    9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLkKEQPGNHDrieglehidkvIVIDqspiGRtprsNP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  66 QTFSK--KEVRQqqqqmgmVF------QHYN--LLE----NLKIYDNVALPLK---LLKEKQPEKIERLLTFVD--MAHK 126
Cdd:cd03271   89 ATYTGvfDEIRE-------LFcevckgKRYNreTLEvrykGKSIADVLDMTVEealEFFENIPKIARKLQTLCDvgLGYI 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488289759 127 AEAYPA-QLSGGEKQRVSIARALSRNPK----WLLcDEATSSLdeeNTESVVRLLHKTHQ--EFRPTIFFVSHELETVK 198
Cdd:cd03271  162 KLGQPAtTLSGGEAQRIKLAKELSKRSTgktlYIL-DEPTTGL---HFHDVKKLLEVLQRlvDKGNTVVVIEHNLDVIK 236
uvrA PRK00349
excinuclease ABC subunit UvrA;
1-44 2.42e-04

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 41.98  E-value: 2.42e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488289759   1 MIELVNVSKvyqetHALKNIHFSVQLGEIVGIVGKSGSGKSTLL 44
Cdd:PRK00349 614 FLKLKGARE-----NNLKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
1-44 2.52e-04

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 41.92  E-value: 2.52e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 488289759    1 MIELVNVSKvyqetHALKNIHFSVQLGEIVGIVGKSGSGKSTLL 44
Cdd:TIGR00630 613 FLTLKGARE-----NNLKNITVSIPLGLFTCITGVSGSGKSTLI 651
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
20-211 3.00e-04

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 40.72  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  20 IHFS-VQLGEIVGIVGKSGSGKSTLLrllNLMEQPSEGEIRIDGRNVQTFS-----KKEVR-----QQQQQMGMVFQHYN 88
Cdd:cd03279   20 IDFTgLDNNGLFLICGPTGAGKSTIL---DAITYALYGKTPRYGRQENLRSvfapgEDTAEvsftfQLGGKKYRVERSRG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  89 LleNLKIYDNVA-LPlkllkekQPEkIERLLTfvdmahkaEAYpAQLSGGEKQRVSIARALS----------RNPKWLLC 157
Cdd:cd03279   97 L--DYDQFTRIVlLP-------QGE-FDRFLA--------RPV-STLSGGETFLASLSLALAlsevlqnrggARLEALFI 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488289759 158 DEATSSLDEENTESVVRLLHKTHQEFRpTIFFVSHELETVKRLCNRILVMEKGQ 211
Cdd:cd03279  158 DEGFGTLDPEALEAVATALELIRTENR-MVGVISHVEELKERIPQRLEVIKTPG 210
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
17-224 3.28e-04

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 41.31  E-value: 3.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  17 LKNIHFSVQLGEIVGIVGKSGSGKSTLLRLLnlmeqpsEGEIRIDGRNV---QTFSKKEVRQQQQQMGMVFQHYnLLENL 93
Cdd:PRK10636  17 LDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYtfpGNWQLAWVNQETPALPQPALEY-VIDGD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  94 KIYDNVALPLKLLKEKQP--------------------EKIERLLTFVDMAHKAEAYPAQ-LSGGEKQRVSIARALSRNP 152
Cdd:PRK10636  89 REYRQLEAQLHDANERNDghaiatihgkldaidawtirSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALICRS 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289759 153 KWLLCDEATSSLDEEntesVVRLLHKTHQEFRPTIFFVSHELETVKRLCNRILVMEKgQLIGEFLNNPQQYE 224
Cdd:PRK10636 169 DLLLLDEPTNHLDLD----AVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ-QSLFEYTGNYSSFE 235
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
91-215 5.36e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 40.49  E-value: 5.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289759  91 ENLKIydnVALPLKLLKEKQPEKIERLLTFVDMAHKAEAYPAQLSGGEKQRVSIARALSRNPKWLLCDEATSSLDEENTE 170
Cdd:NF000106 105 ENLYM---IGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRN 181
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 488289759 171 SVVRLLHKTHQEfRPTIFFVSHELETVKRLCNRILVMEKGQLIGE 215
Cdd:NF000106 182 EVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-43 4.73e-03

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 38.08  E-value: 4.73e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 488289759   1 MIELVNVSKvyqetHALKNIHFSVQLGEIVGIVGKSGSGKSTL 43
Cdd:COG0178  610 FLTIKGARE-----NNLKNVDVEIPLGVLTCVTGVSGSGKSTL 647
MobB pfam03205
Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.
29-47 5.23e-03

Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.


Pssm-ID: 427196 [Multi-domain]  Cd Length: 133  Bit Score: 35.99  E-value: 5.23e-03
                          10        20
                  ....*....|....*....|
gi 488289759   29 IVGIVGKSGSGKSTLL-RLL 47
Cdd:pfam03205   1 ILGIVGWSGSGKTTLLeKLI 20
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
14-43 5.92e-03

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 37.69  E-value: 5.92e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 488289759   14 THALKNIHFSVQLGEIVGIVGKSGSGKSTL 43
Cdd:TIGR00630   9 EHNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
 
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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