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Conserved domains on  [gi|489248201|ref|WP_003156349|]
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MULTISPECIES: amino acid ABC transporter ATP-binding protein [Bacillus]

Protein Classification

amino acid ABC transporter ATP-binding protein( domain architecture ID 11438336)

amino acid ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ATP transporter complex responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of amino acid substrates including glutamine, glutamate, aspartate, and arginine, among others; some members of this architecture transport the osmoprotectant ectoine/hydroxyectoine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
1-242 1.70e-159

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


:

Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 441.36  E-value: 1.70e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasySRKDVHKLRQ 80
Cdd:COG1126    1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD---SKKDINKLRR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:COG1126   78 KVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIK 240
Cdd:COG1126  158 MLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237

                 ..
gi 489248201 241 QV 242
Cdd:COG1126  238 KV 239
 
Name Accession Description Interval E-value
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
1-242 1.70e-159

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 441.36  E-value: 1.70e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasySRKDVHKLRQ 80
Cdd:COG1126    1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD---SKKDINKLRR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:COG1126   78 KVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIK 240
Cdd:COG1126  158 MLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237

                 ..
gi 489248201 241 QV 242
Cdd:COG1126  238 KV 239
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
2-217 2.54e-127

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: 359.15  E-value: 2.54e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasySRKDVHKLRQQ 81
Cdd:cd03262    1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD---DKKNINELRQK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03262   78 VGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:cd03262  158 LFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
1-241 7.45e-110

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 316.31  E-value: 7.45e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAA---SYSRKDVHK 77
Cdd:PRK11264   3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslSQQKGLIRQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  78 LRQQTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:PRK11264  83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKK 237
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242

                 ....
gi 489248201 238 FIKQ 241
Cdd:PRK11264 243 FLEK 246
3a0107s01c2 TIGR00972
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...
2-239 1.94e-79

phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]


Pssm-ID: 273372 [Multi-domain]  Cd Length: 247  Bit Score: 239.12  E-value: 1.94e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAS-YSRK-DVHKLR 79
Cdd:TIGR00972   2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDiYDKKiDVVELR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   80 QQTAMVFQNYNLFkNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL----EHKADSYPITMSGGQQQRIGIARALA 155
Cdd:TIGR00972  82 RRVGMVFQKPNPF-PMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARALA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKqTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERT 235
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRT 239

                  ....
gi 489248201  236 KKFI 239
Cdd:TIGR00972 240 EDYI 243
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
17-168 1.49e-43

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: 144.33  E-value: 1.49e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasysRKDVHKLRQQTAMVFQNYNLFKNKT 96
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-----DDERKSLRKEIGYVFQDPQLFPRLT 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201   97 ALQNVTEAL-ITAQKKPKKEAEQIgmDLLRQVGLEHKAD----SYPITMSGGQQQRIGIARALAVDPHAILLDEPTS 168
Cdd:pfam00005  76 VRENLRLGLlLKGLSKREKDARAE--EALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
1-217 2.31e-42

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 143.32  E-value: 2.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLT----VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVH 76
Cdd:NF038007   1 MLNMQNAEKCYITKTiktkVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KlRQQTAMVFQNYNLFKNKTALQNVTEALITaQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:NF038007  81 R-RELIGYIFQSFNLIPHLSIFDNVALPLKY-RGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVS 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAfAREVADKVIFMADGRI 217
Cdd:NF038007 159 NPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
10-210 2.56e-28

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 106.16  E-value: 2.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  10 AFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVHK-----LRQQTAM 84
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDslpltVRDLVAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  85 -VFQNYNLFKNKTAL--QNVTEALitaqkkpkkeaEQIGMDLL--RQVGlehkadsypiTMSGGQQQRIGIARALAVDPH 159
Cdd:NF040873  81 gRWARRGLWRRLTRDdrAAVDDAL-----------ERVGLADLagRQLG----------ELSGGQRQRALLAQGLAQEAD 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREvADKVI 210
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCV 189
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
2-226 7.69e-15

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 72.85  E-value: 7.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLErPDDGIieiGDAKLNAASYSRKDVHK-LRQ 80
Cdd:NF000106  14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G-PDAGR---RPWRF*TWCANRRALRRtIG* 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQigmdLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:NF000106  90 HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADE----LLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAV 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:NF000106 166 LYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
GguA NF040905
sugar ABC transporter ATP-binding protein;
5-219 1.34e-14

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 72.51  E-value: 1.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   5 RHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL-----------------------NLLERPDDGIIEIg 61
Cdd:NF040905   5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvyphgsyegeilfdgevcrfkDIRDSEALGIVII- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  62 daklnaasysrkdvHklrQQTAMVFQ---NYNLF-KNKTAlqnvTEALITAQKKPKKEAEqigmdLLRQVGLEHKADSyP 137
Cdd:NF040905  84 --------------H---QELALIPYlsiAENIFlGNERA----KRGVIDWNETNRRARE-----LLAKVGLDESPDT-L 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 138 ITMSG-GQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:NF040905 137 VTDIGvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGR 216

                 ...
gi 489248201 217 IIE 219
Cdd:NF040905 217 TIE 219
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
2-226 7.33e-11

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 61.68  E-value: 7.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIE-----IGDAKLNAASYSR---- 72
Cdd:NF033858   2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdMADARHRRAVCPRiaym 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  73 -----KDVHklrqQTAMVFQNYNLFknktalqnvteALITAQKKPKKEAeQIGmDLLRQVGLEHKADSYPITMSGGQQQR 147
Cdd:NF033858  82 pqglgKNLY----PTLSVFENLDFF-----------GRLFGQDAAERRR-RID-ELLRATGLAPFADRPAGKLSGGMKQK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 148 IGIARALAVDPHAILLDEPTSALDP-------ELvagvlqvIKSIAEKQTTM--IIVThemAFAREVA--DKVIFMADGR 216
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTGVDPlsrrqfwEL-------IDRIRAERPGMsvLVAT---AYMEEAErfDWLVAMDAGR 214
                        250
                 ....*....|
gi 489248201 217 IIEQGTPEEL 226
Cdd:NF033858 215 VLATGTPAEL 224
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
2-226 6.76e-09

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 55.90  E-value: 6.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLN-LLERPDdgiieiGDAKLNAASYSRKDVhKLRQ 80
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTgLLPASE------GEAWLFGQPVDAGDI-ATRR 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVteaLITAQ--KKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:NF033858 340 RVGYMSQAFSLYGELTVRQNL---ELHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKP 416
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 159 HAILLDEPTSALDPelVA--GVLQVIKSIA-EKQTTMIIVTHEMAFArEVADKVIFMADGRIIEQGTPEEL 226
Cdd:NF033858 417 ELLILDEPTSGVDP--VArdMFWRLLIELSrEDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAAL 484
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
26-218 7.19e-09

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: 53.15  E-value: 7.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    26 SGEVTAIIGPSGSGKSTLLRCL-NLLERPDDGIIEIGDAKLnaasysrkdvhklrqqtamvfqnynlfknktalqnvtea 104
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDI--------------------------------------- 41
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   105 litaqkkpkkeaeqigMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQ---- 180
Cdd:smart00382  42 ----------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleel 105
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 489248201   181 --VIKSIAEKQTTMIIVTHEMAFAREVAdkVIFMADGRII 218
Cdd:smart00382 106 rlLLLLKSEKNLTVILTTNDEKDLGPAL--LRRRFDRRIV 143
Rad50_Sulf NF041034
DNA double-strand break repair ATPase Rad50;
147-223 9.96e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 468963 [Multi-domain]  Cd Length: 872  Bit Score: 40.08  E-value: 9.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 147 RIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFaREVADKVIFM---ADGRIIEQGTP 223
Cdd:NF041034 793 RLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHDEEL-KEISDYIISVekkGDSSKVKVGSY 871
 
Name Accession Description Interval E-value
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
1-242 1.70e-159

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 441.36  E-value: 1.70e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasySRKDVHKLRQ 80
Cdd:COG1126    1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD---SKKDINKLRR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:COG1126   78 KVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIK 240
Cdd:COG1126  158 MLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237

                 ..
gi 489248201 241 QV 242
Cdd:COG1126  238 KV 239
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
2-217 2.54e-127

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: 359.15  E-value: 2.54e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasySRKDVHKLRQQ 81
Cdd:cd03262    1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD---DKKNINELRQK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03262   78 VGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:cd03262  158 LFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
1-239 9.01e-119

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 339.47  E-value: 9.01e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIG----------DAKLNAASy 70
Cdd:COG4598    8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGgeeirlkpdrDGELVPAD- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  71 sRKDVHKLRQQTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGI 150
Cdd:COG4598   87 -RRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 151 ARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:COG4598  166 ARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245

                 ....*....
gi 489248201 231 QNERTKKFI 239
Cdd:COG4598  246 KSERLRQFL 254
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
1-241 7.45e-110

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 316.31  E-value: 7.45e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAA---SYSRKDVHK 77
Cdd:PRK11264   3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslSQQKGLIRQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  78 LRQQTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:PRK11264  83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKK 237
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242

                 ....
gi 489248201 238 FIKQ 241
Cdd:PRK11264 243 FLEK 246
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
1-242 9.30e-102

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 295.46  E-value: 9.30e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasySRKDVHKLRQ 80
Cdd:PRK09493   1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND---PKVDERLIRQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:PRK09493  78 EAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIK 240
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQ 237

                 ..
gi 489248201 241 QV 242
Cdd:PRK09493 238 HV 239
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1-247 1.11e-98

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 291.21  E-value: 1.11e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAF----KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasYSRKDVH 76
Cdd:COG1135    1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTA--LSERELR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KLRQQTAMVFQNYNLFKNKTALQNVTEALITAqKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:COG1135   79 AARRKIGMIFQHFNLLSSRTVAENVALPLEIA-GVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERT 235
Cdd:COG1135  158 NPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELT 237
                        250
                 ....*....|..
gi 489248201 236 KKFIKQVGEPAE 247
Cdd:COG1135  238 RRFLPTVLNDEL 249
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
1-231 1.34e-87

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: 259.44  E-value: 1.34e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKD----LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaaSYSRKDVH 76
Cdd:cd03258    1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLT--LLSGKELR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KLRQQTAMVFQNYNLFKNKTALQNVTEALITAqKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:cd03258   79 KARRRIGMIFQHFNLLSSRTVFENVALPLEIA-GVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:cd03258  158 NPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
1-239 1.76e-85

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: 254.13  E-value: 1.76e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsySRKDVHKLRQ 80
Cdd:COG1127    5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGL--SEKELYELRR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:COG1127   83 RIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPqNERTKKFI 239
Cdd:COG1127  163 LLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
2-240 3.27e-84

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 251.09  E-value: 3.27e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLN-AASYSRKDVHKLRQ 80
Cdd:COG4161    3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfSQKPSEKAIRLLRQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:COG4161   83 KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTpEELFDNPQNERTKKFIK 240
Cdd:COG4161  163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHYLS 241
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1-239 2.15e-82

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 250.40  E-value: 2.15e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnaasysrKDVHKL-- 78
Cdd:COG3842    5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG----------RDVTGLpp 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  79 -RQQTAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:COG3842   75 eKRNVGMVFQDYALFPHLTVAENVAFGL-RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTH--EMAFAreVADKVIFMADGRIIEQGTPEELFDNPQNER 234
Cdd:COG3842  154 PRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHdqEEALA--LADRIAVMNDGRIEQVGTPEEIYERPATRF 231

                 ....*
gi 489248201 235 TKKFI 239
Cdd:COG3842  232 VADFI 236
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-220 3.39e-81

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 242.64  E-value: 3.39e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKD----LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDVH 76
Cdd:COG1136    4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI--SSLSERELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KLRQQT-AMVFQNYNLFKNKTALQNVTEALItAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALA 155
Cdd:COG1136   82 RLRRRHiGFVFQFFNLLPELTALENVALPLL-LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFArEVADKVIFMADGRIIEQ 220
Cdd:COG1136  161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVTHDPELA-ARADRVIRLRDGRIVSD 225
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1-237 1.44e-79

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: 247.89  E-value: 1.44e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAF-----KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDV 75
Cdd:COG1123  260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDL--TKLSRRSL 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  76 HKLRQQTAMVFQNYN--LFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL-EHKADSYPITMSGGQQQRIGIAR 152
Cdd:COG1123  338 RELRRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:COG1123  418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELgLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497

                 ....*.
gi 489248201 232 NERTKK 237
Cdd:COG1123  498 HPYTRA 503
3a0107s01c2 TIGR00972
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...
2-239 1.94e-79

phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]


Pssm-ID: 273372 [Multi-domain]  Cd Length: 247  Bit Score: 239.12  E-value: 1.94e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAS-YSRK-DVHKLR 79
Cdd:TIGR00972   2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDiYDKKiDVVELR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   80 QQTAMVFQNYNLFkNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL----EHKADSYPITMSGGQQQRIGIARALA 155
Cdd:TIGR00972  82 RRVGMVFQKPNPF-PMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARALA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKqTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERT 235
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRT 239

                  ....
gi 489248201  236 KKFI 239
Cdd:TIGR00972 240 EDYI 243
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
2-240 7.94e-79

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 237.60  E-value: 7.94e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLN-AASYSRKDVHKLRQ 80
Cdd:PRK11124   3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfSKTPSDKAIRELRR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:PRK11124  83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTpEELFDNPQNERTKKFIK 240
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNYLS 241
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
2-217 2.05e-78

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: 235.46  E-value: 2.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKD----LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDvHK 77
Cdd:cd03255    1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELA-AF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  78 LRQQTAMVFQNYNLFKNKTALQNVTEALItAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:cd03255   80 RRRHIGFVFQSFNLLPDLTALENVELPLL-LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREvADKVIFMADGRI 217
Cdd:cd03255  159 PKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVTHDPELAEY-ADRIIELRDGKI 218
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
1-226 4.82e-78

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 235.72  E-value: 4.82e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFK-DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASysRKDVHKLR 79
Cdd:COG3638    2 MLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALR--GRALRRLR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQNYNLFKNKTALQNV-------TEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIAR 152
Cdd:COG3638   80 RRIGMIFQQFNLVPRLSVLTNVlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:COG3638  160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
1-248 1.34e-77

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 237.78  E-value: 1.34e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAF----KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDVH 76
Cdd:PRK11153   1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL--TALSEKELR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KLRQQTAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:PRK11153  79 KARRQIGMIFQHFNLLSSRTVFDNVALPL-ELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERT 235
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLT 237
                        250
                 ....*....|....*.
gi 489248201 236 KKFIK---QVGEPAEL 248
Cdd:PRK11153 238 REFIQstlHLDLPEDY 253
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
2-239 2.93e-77

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 236.97  E-value: 2.93e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasYSRKDVHKLRqq 81
Cdd:COG1118    3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL----FTNLPPRERR-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:COG1118   77 VGFVFQHYALFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 162 LLDEPTSALD----PELVAGVLQVIKSIaekQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKK 237
Cdd:COG1118  156 LLDEPFGALDakvrKELRRWLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVAR 232

                 ..
gi 489248201 238 FI 239
Cdd:COG1118  233 FL 234
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
2-240 3.27e-76

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 231.40  E-value: 3.27e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAS--------YSRK 73
Cdd:PRK10619   6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRdkdgqlkvADKN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  74 DVHKLRQQTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKA-DSYPITMSGGQQQRIGIAR 152
Cdd:PRK10619  86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIAR 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQN 232
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245

                 ....*...
gi 489248201 233 ERTKKFIK 240
Cdd:PRK10619 246 PRLQQFLK 253
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
2-231 8.25e-76

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: 229.31  E-value: 8.25e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDVHKLRQQ 81
Cdd:cd03261    1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDI--SGLSEAELYRLRRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03261   79 MGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF--DNPQ 231
Cdd:cd03261  159 LYDEPTAGLDPIASGVIDDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPL 231
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
1-219 5.80e-73

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 221.85  E-value: 5.80e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFK-DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASysRKDVHKLR 79
Cdd:COG2884    1 MIRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLK--RREIPYLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQNYNLFKNKTALQNVTEALItAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPH 159
Cdd:COG2884   79 RRIGVVFQDFRLLPDRTVYENVALPLR-VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIE 219
Cdd:COG2884  158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1-219 1.38e-72

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 222.27  E-value: 1.38e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAF----KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnaasysrKDVH 76
Cdd:COG1116    7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----------KPVT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KLRQQTAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:COG1116   77 GPGPDRGVVFQEPALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 157 DPHAILLDEPTSALDpELVAGVLQ--VIKSIAEKQTTMIIVTH---EMAFareVADKVIFMAD--GRIIE 219
Cdd:COG1116  156 DPEVLLMDEPFGALD-ALTRERLQdeLLRLWQETGKTVLFVTHdvdEAVF---LADRVVVLSArpGRIVE 221
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
1-246 1.58e-72

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 224.95  E-value: 1.58e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklrq 80
Cdd:COG3839    3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNI----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 qtAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:COG3839   78 --AMVFQSYALYPHMTVYENIAFPL-KLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHE----MAFarevADKVIFMADGRIIEQGTPEELFDNPQNERT 235
Cdd:COG3839  155 FLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDRPANLFV 230
                        250
                 ....*....|.
gi 489248201 236 KKFIkqvGEPA 246
Cdd:COG3839  231 AGFI---GSPP 238
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
2-226 2.54e-72

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 220.71  E-value: 2.54e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasysRKDVHKLRQQ 81
Cdd:COG1131    1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV------ARDPAEVRRR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNKTALQNVtEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:COG1131   75 IGYVPQEPALYPDLTVRENL-RFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:COG1131  154 ILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
2-221 1.46e-71

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: 217.77  E-value: 1.46e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklrqq 81
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNI------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 tAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03259   75 -GMVFQDYALFPHLTVAENIAFGL-KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03259  153 LLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
2-226 1.64e-71

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: 218.20  E-value: 1.64e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLL-----ERPDDGIIEIGDAKLNAasySRKDVH 76
Cdd:cd03260    1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYD---LDVDVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KLRQQTAMVFQNYNLFkNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL--EHKADSYPITMSGGQQQRIGIARAL 154
Cdd:cd03260   78 ELRRRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARAL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489248201 155 AVDPHAILLDEPTSALDPELVAGVLQVIKSIAeKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:cd03260  157 ANEPEVLLLDEPTSALDPISTAKIEELIAELK-KEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
2-239 2.18e-71

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 219.14  E-value: 2.18e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLL--ERPD---DGIIEIGDAKLNAASYsrkDVH 76
Cdd:COG1117   12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIYDPDV---DVV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KLRQQTAMVFQNYNLFkNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL----EHKADSYPITMSGGQQQRIGIAR 152
Cdd:COG1117   89 ELRRRVGMVFQKPNPF-PKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIAR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 153 ALAVDPHAILLDEPTSALDPelVAGvLQVIKSIAE--KQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:COG1117  168 ALAVEPEVLLMDEPTSALDP--IST-AKIEELILElkKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNP 244

                 ....*....
gi 489248201 231 QNERTKKFI 239
Cdd:COG1117  245 KDKRTEDYI 253
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
2-231 3.70e-71

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: 217.59  E-value: 3.70e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKD-LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasysRKDVHKLRQ 80
Cdd:COG1122    1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT-----KKNLRELRR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYN--LFkNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:COG1122   76 KVGLVFQNPDdqLF-APTVEEDVAFGP-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:COG1122  154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
2-216 3.86e-71

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: 215.51  E-value: 3.86e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysRKDVHKLRQQ 81
Cdd:cd03229    1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL---EDELPPLRRR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNKTALQNVTEALitaqkkpkkeaeqigmdllrqvglehkadsypitmSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03229   78 IGMVFQDFALFPHLTVLENIALGL-----------------------------------SGGQQQRVALARALAMDPDVL 122
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:cd03229  123 LLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
2-226 6.38e-71

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: 217.44  E-value: 6.38e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLT-VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaaSYSRKDVHKLRQ 80
Cdd:cd03256    1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDIN--KLKGKALRQLRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNV-------TEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARA 153
Cdd:cd03256   79 QIGMIFQQFNLIERLSVLENVlsgrlgrRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 154 LAVDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:cd03256  159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1-240 6.60e-67

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: 207.35  E-value: 6.60e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAF----KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVH 76
Cdd:COG1124    1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV-----TRRRRK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KLRQQTAMVFQNY--NLFKNKTALQNVTEALiTAQKKPKKEaEQIGmDLLRQVGL-EHKADSYPITMSGGQQQRIGIARA 153
Cdd:COG1124   76 AFRRRVQMVFQDPyaSLHPRHTVDRILAEPL-RIHGLPDRE-ERIA-ELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 154 LAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQN 232
Cdd:COG1124  153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232

                 ....*...
gi 489248201 233 ERTKKFIK 240
Cdd:COG1124  233 PYTRELLA 240
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
2-220 7.83e-67

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: 206.17  E-value: 7.83e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKD----LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdvhk 77
Cdd:cd03293    1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  78 lrqqtAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:cd03293   76 -----GYVFQQDALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVD 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 158 PHAILLDEPTSALDpELVAGVLQ--VIKSIAEKQTTMIIVTHEMAFAREVADKVIFMA--DGRIIEQ 220
Cdd:cd03293  150 PDVLLLDEPFSALD-ALTREQLQeeLLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSarPGRIVAE 215
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
1-228 1.89e-66

phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]


Pssm-ID: 131368 [Multi-domain]  Cd Length: 243  Bit Score: 206.00  E-value: 1.89e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    1 MIQVRHIRKAF-KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASysRKDVHKLR 79
Cdd:TIGR02315   1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLR--GKKLRKLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   80 QQTAMVFQNYNLFKNKTALQNVTEALITAQKKPK-------KEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIAR 152
Cdd:TIGR02315  79 RRIGMIFQHYNLIERLTVLENVLHGRLGYKPTWRsllgrfsEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201  153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFD 228
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINkEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
20-242 3.44e-66

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: 206.34  E-value: 3.44e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASysRKDVHKLRQQT-AMVFQNYNLFKNKTAL 98
Cdd:cd03294   43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMS--RKELRELRRKKiSMVFQSFALLPHRTVL 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  99 QNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPeLVAGV 178
Cdd:cd03294  121 ENVAFGL-EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP-LIRRE 198
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 179 LQ--VIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIKQV 242
Cdd:cd03294  199 MQdeLLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
2-239 1.16e-65

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: 203.72  E-value: 1.16e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKlrQQ 81
Cdd:cd03296    3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-----TDVPVQE--RN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNKTALQNVTEALIT---AQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03296   76 VGFVFQHYALFRHMTVFDNVAFGLRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDP----ELVAGVLQVIKsiaEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNER 234
Cdd:cd03296  156 KVLLLDEPFGALDAkvrkELRRWLRRLHD---ELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232

                 ....*
gi 489248201 235 TKKFI 239
Cdd:cd03296  233 VYSFL 237
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
1-239 1.31e-65

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 205.71  E-value: 1.31e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTV-LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKLR 79
Cdd:COG1125    1 MIEFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDI-----RDLDPVELR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQNYNLFKNKTALQNVteALI-TAQKKPKKEAEQIGMDLLRQVGLEHK--ADSYPITMSGGQQQRIGIARALAV 156
Cdd:COG1125   76 RRIGYVIQQIGLFPHMTVAENI--ATVpRLLGWDKERIRARVDELLELVGLDPEeyRDRYPHELSGGQQQRVGVARALAA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 157 DPHAILLDEPTSALDPeLVAGVLQV-IKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNER 234
Cdd:COG1125  154 DPPILLMDEPFGALDP-ITREQLQDeLLRLqRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDF 232

                 ....*
gi 489248201 235 TKKFI 239
Cdd:COG1125  233 VADFV 237
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
1-221 1.56e-65

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: 203.12  E-value: 1.56e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKD----LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVh 76
Cdd:cd03257    1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 kLRQQTAMVFQNYNLFKN--KTALQNVTEALITAQKKPKKEAEQ-IGMDLLRQVGL-EHKADSYPITMSGGQQQRIGIAR 152
Cdd:cd03257   80 -RRKEIQMVFQDPMSSLNprMTIGEQIAEPLRIHGKLSKKEARKeAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIAR 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03257  159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1-231 2.45e-64

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: 202.98  E-value: 2.45e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFK----DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRC-LNLLERP--DDGIIEIGDAKLnaASYSRK 73
Cdd:COG0444    1 LLEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAiLGLLPPPgiTSGEILFDGEDL--LKLSEK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  74 DVHKLR-QQTAMVFQN-YnlfknkTAL-------QNVTEALITAQKKPKKEAEQIGMDLLRQVGL---EHKADSYPITMS 141
Cdd:COG0444   79 ELRKIRgREIQMIFQDpM------TSLnpvmtvgDQIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 142 GGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQ 220
Cdd:COG0444  153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEE 232
                        250
                 ....*....|.
gi 489248201 221 GTPEELFDNPQ 231
Cdd:COG0444  233 GPVEELFENPR 243
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
1-228 5.94e-63

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: 197.19  E-value: 5.94e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDvhkLRQ 80
Cdd:COG1120    1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL--ASLSRRE---LAR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVteAL-----ITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALA 155
Cdd:COG1120   76 RIAYVPQEPPAPFGLTVRELV--ALgryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFD 228
Cdd:COG1120  154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
2-231 1.57e-61

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: 193.04  E-value: 1.57e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKL-RQ 80
Cdd:cd03219    1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-----TGLPPHEIaRL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTEALITAQK---------KPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIA 151
Cdd:cd03219   76 GIGRTFQIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 152 RALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:cd03219  156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
17-242 4.61e-61

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 196.86  E-value: 4.61e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAklNAASYSRKDVHKLRQQT-AMVFQNYNLFKNK 95
Cdd:COG4175   43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGE--DITKLSKKELRELRRKKmSMVFQHFALLPHR 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  96 TALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDP--- 172
Cdd:COG4175  121 TVLENVAFGL-EIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlir 199
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 173 -----ELVAgvLQviksiAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIKQV 242
Cdd:COG4175  200 remqdELLE--LQ-----AKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDV 267
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
2-239 4.91e-60

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: 189.37  E-value: 4.91e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnaasysrKDVHKL--- 78
Cdd:cd03300    1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG----------KDITNLpph 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  79 RQQTAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03300   71 KRPVNTVFQNYALFPHLTVFENIAFGL-RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKK 237
Cdd:cd03300  150 KVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVAD 229

                 ..
gi 489248201 238 FI 239
Cdd:cd03300  230 FI 231
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
1-231 5.15e-60

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: 189.86  E-value: 5.15e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKL-R 79
Cdd:COG0411    4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-----TGLPPHRIaR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQNYNLFKNKTALQNV--------TEALITA------QKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQ 145
Cdd:COG0411   79 LGIARTFQNPRLFPELTVLENVlvaaharlGRGLLAAllrlprARREEREARERAEELLERVGLADRADEPAGNLSYGQQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 146 QRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPE 224
Cdd:COG0411  159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238

                 ....*..
gi 489248201 225 ELFDNPQ 231
Cdd:COG0411  239 EVRADPR 245
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
3-216 7.68e-60

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: 188.06  E-value: 7.68e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   3 QVRHIRKAFKDLT--VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasysrKDVHKLRQ 80
Cdd:cd03225    1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK-----LSLKELRR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYN--LFKNktalqNVTEALITA---QKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALA 155
Cdd:cd03225   76 KVGLVFQNPDdqFFGP-----TVEEEVAFGlenLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:cd03225  151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1-231 3.03e-59

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: 195.12  E-value: 3.03e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAF--KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLErPDDGIIEiGDAKLNAASYSRKDVHKL 78
Cdd:COG1123    4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRIS-GEVLLDGRDLLELSEALR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  79 RQQTAMVFQNY-NLFKNKTALQNVTEALItAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:COG1123   82 GRRIGMVFQDPmTQLNPVTVGDQIAEALE-NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:COG1123  161 PDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
2-242 3.29e-59

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274496 [Multi-domain]  Cd Length: 353  Bit Score: 191.02  E-value: 3.29e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklrqq 81
Cdd:TIGR03265   5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDY------ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   82 tAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:TIGR03265  79 -GIVFQSYALFPNLTVADNIAYGL-KNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  162 LLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIK 240
Cdd:TIGR03265 157 LLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG 236

                  ..
gi 489248201  241 QV 242
Cdd:TIGR03265 237 EV 238
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
2-217 7.66e-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: 7.66e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIeigdaKLNAASYSRKDVHKLRQQ 81
Cdd:COG4619    1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI-----YLDGKPLSAMPPPEWRRQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNkTALQNVTEALITAQKKPKKEAEQigmDLLRQVGLEHKADSYPIT-MSGGQQQRIGIARALAVDPHA 160
Cdd:COG4619   76 VAYVPQEPALWGG-TVRDNLPFPFQLRERKFDRERAL---ELLERLGLPPDILDKPVErLSGGERQRLALIRALLLQPDV 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKS-IAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:COG4619  152 LLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
1-244 1.06e-57

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: 183.52  E-value: 1.06e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAklnaasYSRKDVHKLRQ 80
Cdd:COG4555    1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE------DVRKEPREARR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVtEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:COG4555   75 QIGVLPDERGLYDRLTVRENI-RYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKK-FI 239
Cdd:COG4555  154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDaFV 233

                 ....*
gi 489248201 240 KQVGE 244
Cdd:COG4555  234 ALIGS 238
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
2-241 1.00e-56

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: 180.96  E-value: 1.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLT-VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaklNAASYSRKDVHKLRQ 80
Cdd:cd03295    1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFI-----DGEDIREQDPVELRR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTeALITAQKKPKKEAEQIGMDLLRQVGLE--HKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03295   76 KIGYVIQQIGLFPHMTVEENIA-LVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKK 237
Cdd:cd03295  155 PLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAE 234

                 ....
gi 489248201 238 FIKQ 241
Cdd:cd03295  235 FVGA 238
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
1-216 3.43e-56

cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]


Pssm-ID: 131721 [Multi-domain]  Cd Length: 214  Bit Score: 178.60  E-value: 3.43e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    1 MIQVRHIRKAFK-DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaaSYSRKDVHKLR 79
Cdd:TIGR02673   1 MIEFHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVN--RLRGRQLPLLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   80 QQTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPH 159
Cdd:TIGR02673  79 RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVG-AALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201  160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
1-241 7.75e-56

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 178.41  E-value: 7.75e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVldGIDLEIKSGEVTAIIGPSGSGKSTLlrcLNLL---ERPDDGIIEIGDAKLNAASYSRKDVhk 77
Cdd:COG3840    1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTL---LNLIagfLPPDSGRILWNGQDLTALPPAERPV-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  78 lrqqtAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIgMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALaVD 157
Cdd:COG3840   74 -----SMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQV-EQALERVGLAGLLDRLPGQLSGGQRQRVALARCL-VR 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 158 PHAI-LLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERT 235
Cdd:COG3840  147 KRPIlLLDEPFSALDPALRQEMLDLVDELCrERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPAL 226

                 ....*.
gi 489248201 236 KKFIKQ 241
Cdd:COG3840  227 AAYLGI 232
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
1-225 1.37e-55

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: 178.01  E-value: 1.37e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKD----LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasYSRKDVH 76
Cdd:COG4181    8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA--LDEDARA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KLR-QQTAMVFQNYNLFKNKTALQNVteaLITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALA 155
Cdd:COG4181   86 RLRaRHVGFVFQSFQLLPTLTALENV---MLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489248201 156 VDPhAILL-DEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEE 225
Cdd:COG4181  163 TEP-AILFaDEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
2-231 1.58e-55

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 180.70  E-value: 1.58e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAF---------KDLTV--LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgDAKlNAASY 70
Cdd:COG4608    8 LEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILF-DGQ-DITGL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  71 SRKDVHKLRQQTAMVFQN-Y-NLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL--EHkADSYPITMSGGQQQ 146
Cdd:COG4608   86 SGRELRPLRRRMQMVFQDpYaSLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrpEH-ADRYPHEFSGGQRQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 147 RIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEE 225
Cdd:COG4608  165 RIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLqDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDE 244

                 ....*.
gi 489248201 226 LFDNPQ 231
Cdd:COG4608  245 LYARPL 250
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
15-231 4.49e-55

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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275314 [Multi-domain]  Cd Length: 277  Bit Score: 178.03  E-value: 4.49e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasYSRKDVHKLRQQTAMVFQN--YNLF 92
Cdd:TIGR04521  19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITA--KKKKKLKDLRKKVGLVFQFpeHQLF 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   93 KNkTALQNVtealitA-----QKKPKKEAEQIGMDLLRQVGLEHK-ADSYPITMSGGQQQRIGIARALAVDPHAILLDEP 166
Cdd:TIGR04521  97 EE-TVYKDI------AfgpknLGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEP 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201  167 TSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:TIGR04521 170 TAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
4-212 4.81e-54

putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 173.19  E-value: 4.81e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    4 VRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgDAKLNAASYSRKDVHKLRQQTA 83
Cdd:TIGR03608   1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYL-NGQETPPLNSKKASKFRREKLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   84 MVFQNYNLFKNKTALQNVTEALItAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILL 163
Cdd:TIGR03608  80 YLFQNFALIENETVEENLDLGLK-YKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 489248201  164 DEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFArEVADKVIFM 212
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
2-217 8.81e-54

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: 171.04  E-value: 8.81e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasysRKDVHKLRQQ 81
Cdd:cd03230    1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI------KKEPEEVKRR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNKTALQNvtealitaqkkpkkeaeqigmdllrqvglehkadsypITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03230   75 IGYLPEEPSLYENLTVREN-------------------------------------LKLSGGMKQRLALAQALLHDPELL 117
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:cd03230  118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
20-242 1.47e-53

glycine betaine/L-proline transport ATP binding subunit; This model describes 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 130254 [Multi-domain]  Cd Length: 363  Bit Score: 176.58  E-value: 1.47e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEI-GDAKLNAASYSRKDVHklRQQTAMVFQNYNLFKNKTAL 98
Cdd:TIGR01186  12 ADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIdGENIMKQSPVELREVR--RKKIGMVFQQFALFPHMTIL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   99 QNvTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPeLVAGV 178
Cdd:TIGR01186  90 QN-TSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDP-LIRDS 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201  179 LQ--VIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIKQV 242
Cdd:TIGR01186 168 MQdeLKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
2-239 1.92e-53

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 176.68  E-value: 1.92e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVHklrqq 81
Cdd:PRK09452  15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVN----- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 taMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:PRK09452  90 --TVFQSYALFPHMTVFENVAFGL-RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIaEKQT--TMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFI 239
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKAL-QRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFI 245
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
2-242 2.09e-53

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 176.04  E-value: 2.09e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIeigdaKLNAASYSRkdVHKLRQQ 81
Cdd:PRK10851   3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI-----RFHGTDVSR--LHARDRK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNKTALQNVTEAL--ITAQKKPKKEA-EQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:PRK10851  76 VGFVFQHYALFRHMTVFDNIAFGLtvLPRRERPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPelvagvlQVIKSI--------AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:PRK10851 156 QILLLDEPFGALDA-------QVRKELrrwlrqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
                        250
                 ....*....|..
gi 489248201 231 QNERTKKFIKQV 242
Cdd:PRK10851 229 ATRFVLEFMGEV 240
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
2-221 2.53e-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: 2.53e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklrqq 81
Cdd:cd03301    1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDI------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 tAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03301   75 -AMVFQNYALYPHMTVYDNIAFGL-KLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03301  153 LMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
2-239 1.41e-52

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: 170.21  E-value: 1.41e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLtVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIeigdaKLNAasysrKDVHKL--- 78
Cdd:cd03299    1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI-----LLNG-----KDITNLppe 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  79 RQQTAMVFQNYNLFKNKTALQNVTEALITaQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03299   70 KRDISYVPQNYALFPHMTVYKNIAYGLKK-RKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKK 237
Cdd:cd03299  149 KILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAE 228

                 ..
gi 489248201 238 FI 239
Cdd:cd03299  229 FL 230
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-235 4.81e-52

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 169.11  E-value: 4.81e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnaasysrKDVHKLRQ 80
Cdd:COG1121    6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----------KPPRRARR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLfkNK----TALQNVTEALITAQ---KKPKKEAEQIGMDLLRQVGLEHKADSyPI-TMSGGQQQRIGIAR 152
Cdd:COG1121   76 RIGYVPQRAEV--DWdfpiTVRDVVLMGRYGRRglfRRPSRADREAVDEALERVGLEDLADR-PIgELSGGQQQRVLLAR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMaDGRIIEQGTPEELFDNPQN 232
Cdd:COG1121  153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENL 231

                 ...
gi 489248201 233 ERT 235
Cdd:COG1121  232 SRA 234
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
1-230 8.80e-52

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: 171.82  E-value: 8.80e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRhIRKAFKDLTvLDgIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKL--NAASYSRKdVHKL 78
Cdd:COG4148    2 MLEVD-FRLRRGGFT-LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLP-PHRR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  79 RqqTAMVFQNYNLFKNKTALQNvteaLITAQKKPKKEAEQIGMD-LLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:COG4148   78 R--IGYVFQEARLFPHLSVRGN----LLYGRKRAPRAERRISFDeVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSS 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:COG4148  152 PRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
16-227 2.61e-51

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: 167.99  E-value: 2.61e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDakLNAASysRKDVHKLRQQTAMVFQN-YNLFKN 94
Cdd:TIGR04520  17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLD--EENLWEIRKKVGMVFQNpDNQFVG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   95 KT-------ALQNvtealitaQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:TIGR04520  93 ATveddvafGLEN--------LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEAT 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201  168 SALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELF 227
Cdd:TIGR04520 165 SMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIF 224
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
2-226 6.49e-51

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: 176.18  E-value: 6.49e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLT--VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDakLNAASYSRKDvhkLR 79
Cdd:COG2274  474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG--IDLRQIDPAS---LR 548
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQNYNLFkNKTALQNVTEAlitaqkKPKKEAEQIgMDLLRQVGLEHKADSYP-----------ITMSGGQQQRI 148
Cdd:COG2274  549 RQIGVVLQDVFLF-SGTIRENITLG------DPDATDEEI-IEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRL 620
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 149 GIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAeKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEEL 226
Cdd:COG2274  621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEEL 696
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
3-216 7.34e-51

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: 163.18  E-value: 7.34e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   3 QVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKLRQQT 82
Cdd:cd00267    1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI-----AKLPLEELRRRI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  83 AMVFQnynlfknktalqnvtealitaqkkpkkeaeqigmdllrqvglehkadsypitMSGGQQQRIGIARALAVDPHAIL 162
Cdd:cd00267   76 GYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489248201 163 LDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:cd00267  104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
3-221 1.03e-50

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: 163.76  E-value: 1.03e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   3 QVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDvhkLRQQT 82
Cdd:cd03214    1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL--ASLSPKE---LARKI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  83 AMVFQnynlfknktalqnvtealitaqkkpkkeaeqigmdLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAIL 162
Cdd:cd03214   76 AYVPQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 163 LDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03214  121 LDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
13-217 1.54e-50

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: 164.50  E-value: 1.54e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaaSYSRKDVHKLRQQTAMVFQNYNLF 92
Cdd:cd03292   13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGRAIPYLRRKIGVVFQDFRLL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  93 KNKTALQNVTEALITAQKKPKKEAEQIgMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDP 172
Cdd:cd03292   91 PDRNVYENVAFALEVTGVPPREIRKRV-PAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 489248201 173 ELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:cd03292  170 DTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
2-226 4.66e-50

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


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 171.87  E-value: 4.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAF--KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLrclNLLER---PDDGIIEIGDAKLnaASYSRKDvh 76
Cdd:COG4987  334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLL---ALLLRfldPQSGSITLGGVDL--RDLDEDD-- 406
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 kLRQQTAMVFQNYNLFkNKTALQNVTEAlitaqkKPKKEAEQIgMDLLRQVGLEHKADSYP-----------ITMSGGQQ 145
Cdd:COG4987  407 -LRRRIAVVPQRPHLF-DTTLRENLRLA------RPDATDEEL-WAALERVGLGDWLAALPdgldtwlgeggRRLSGGER 477
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 146 QRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMAfAREVADKVIFMADGRIIEQGTPEE 225
Cdd:COG4987  478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV-LLITHRLA-GLERMDRILVLEDGRIVEQGTHEE 555

                 .
gi 489248201 226 L 226
Cdd:COG4987  556 L 556
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
1-225 5.43e-50

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 164.13  E-value: 5.43e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDVHK--- 77
Cdd:COG4559    1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL--AAWSPWELARrra 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  78 -LRQQTAMVFQnynlFknkTALQNVteAL-ITAQKKPKKEAEQIGMDLLRQVGLEHKAD-SYPiTMSGGQQQRIGIARAL 154
Cdd:COG4559   79 vLPQHSSLAFP----F---TVEEVV--ALgRAPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVL 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 155 A-------VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEE 225
Cdd:COG4559  149 AqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
2-239 1.14e-49

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 163.16  E-value: 1.14e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLN-LLERPDDGIIEiGDAKLNAASYSRKDVHKLRQ 80
Cdd:PRK14247   4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNrLIELYPEARVS-GEVYLDGQDIFKMDVIELRR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTEAL-ITAQKKPKKEAEQIGMDLLRQVGL----EHKADSYPITMSGGQQQRIGIARALA 155
Cdd:PRK14247  83 RVQMVFQIPNPIPNLSIFENVALGLkLNRLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIaEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERT 235
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241

                 ....
gi 489248201 236 KKFI 239
Cdd:PRK14247 242 EKYV 245
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
1-216 1.29e-48

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: 159.91  E-value: 1.29e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAF-------KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEI--GDAKLNAASYS 71
Cdd:COG4778    4 LLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQAS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  72 RKDVHKLRQQT-AMVFQNYNLFKNKTALQNVTEALItAQKKPKKEAEQIGMDLLRQVGL-EHKADSYPITMSGGQQQRIG 149
Cdd:COG4778   84 PREILALRRRTiGYVSQFLRVIPRVSALDVVAEPLL-ERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVN 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 150 IARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:COG4778  163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
16-226 1.65e-48

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 168.03  E-value: 1.65e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLrclNLLER---PDDGIIEIGDakLNAASYSRKDvhkLRQQTAMVFQNYNLF 92
Cdd:COG1132  355 VLKDISLTIPPGETVALVGPSGSGKSTLV---NLLLRfydPTSGRILIDG--VDIRDLTLES---LRRQIGVVPQDTFLF 426
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  93 kNKTALQNVTEAlitaqkKPKKEAEQIgMDLLRQVGLEHKADSYP-----------ITMSGGQQQRIGIARALAVDPHAI 161
Cdd:COG1132  427 -SGTIRENIRYG------RPDATDEEV-EEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPIL 498
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAeKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEEL 226
Cdd:COG1132  499 ILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEEL 561
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
15-226 2.23e-48

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: 167.63  E-value: 2.23e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkDVHKLRQQTAMVFQNYNLFKN 94
Cdd:COG4988  351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL-----DPASWRRQIAWVPQNPYLFAG 425
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  95 kTALQNVTEAlitaqkKPKKEAEQIgMDLLRQVGLEHKADSYP-----------ITMSGGQQQRIGIARALAVDPHAILL 163
Cdd:COG4988  426 -TIRENLRLG------RPDASDEEL-EAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLL 497
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 164 DEPTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREvADKVIFMADGRIIEQGTPEEL 226
Cdd:COG4988  498 DEPTAHLDAETEAEILQALRRLAKGRTV-ILITHRLALLAQ-ADRILVLDDGRIVEQGTHEEL 558
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
8-246 3.42e-47

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: 163.70  E-value: 3.42e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   8 RKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRC-LNLLerPDDGIIEIGDAKLNAasYSRKDVHKLRQQTAMVF 86
Cdd:COG4172  293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLAlLRLI--PSEGEIRFDGQDLDG--LSRRALRPLRRRMQVVF 368
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  87 QN-YN-LFKNKTALQNVTEALITAQKKPKKEA-EQIGMDLLRQVGLEHKA-DSYPITMSGGQQQRIGIARALAVDPHAIL 162
Cdd:COG4172  369 QDpFGsLSPRMTVGQIIAEGLRVHGPGLSAAErRARVAEALEEVGLDPAArHRYPHEFSGGQRQRIAIARALILEPKLLV 448
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 163 LDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIKQ 241
Cdd:COG4172  449 LDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAA 528

                 ....*
gi 489248201 242 VGEPA 246
Cdd:COG4172  529 APLLE 533
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
1-239 5.20e-47

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 156.47  E-value: 5.20e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNlleRPDDGIIEI---GDAKLNAAS-YS-RKDV 75
Cdd:PRK14239   5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN---RMNDLNPEVtitGSIVYNGHNiYSpRTDT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  76 HKLRQQTAMVFQNYNLFKnKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL-----EHKADSyPITMSGGQQQRIGI 150
Cdd:PRK14239  82 VDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIwdevkDRLHDS-ALGLSGGQQQRVCI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 151 ARALAVDPHAILLDEPTSALDPeLVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDP-ISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238

                 ....*....
gi 489248201 231 QNERTKKFI 239
Cdd:PRK14239 239 KHKETEDYI 247
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
1-221 8.73e-47

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: 154.76  E-value: 8.73e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRhIRKAFKDLTvLDgIDLEIkSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasySRKDVHKLRQ 80
Cdd:cd03297    1 MLCVD-IEKRLPDFT-LK-IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD---SRKKINLPPQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 Q--TAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQigmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03297   74 QrkIGLVFQQYALFPHLNVRENLAFGLKRKRNREDRISVD---ELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQP 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03297  151 ELLLLDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
32-242 9.46e-47

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


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 158.04  E-value: 9.46e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   32 IIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVHklrqqtaMVFQNYNLFKNKTALQNVTEALiTAQKK 111
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHIN-------MVFQSYALFPHMTVEENVAFGL-KMRKV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  112 PKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEK-QT 190
Cdd:TIGR01187  73 PRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGI 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489248201  191 TMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIKQV 242
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
10-239 2.34e-46

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 155.64  E-value: 2.34e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  10 AFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAS-YSRKDVHKLRQQTAMVFQN 88
Cdd:PRK14271  30 GFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSiFNYRDVLEFRRRVGMLFQR 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  89 YNLFKnKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL----EHKADSYPITMSGGQQQRIGIARALAVDPHAILLD 164
Cdd:PRK14271 110 PNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 165 EPTSALDPELVAGVLQVIKSIAEKqTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFI 239
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
2-216 5.30e-46

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: 151.38  E-value: 5.30e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAF--KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkDVHKLR 79
Cdd:cd03228    1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL-----DLESLR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQNYNLFkNKTALQNVtealitaqkkpkkeaeqigmdllrqvglehkadsypitMSGGQQQRIGIARALAVDPH 159
Cdd:cd03228   76 KNIAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPP 116
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREvADKVIFMADGR 216
Cdd:cd03228  117 ILILDEATSALDPETEALILEALRALAKGKTV-IVIAHRLSTIRD-ADRIIVLDDGR 171
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
9-226 6.11e-46

daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]


Pssm-ID: 130256 [Multi-domain]  Cd Length: 302  Bit Score: 155.24  E-value: 6.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    9 KAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaklnaASYS-RKDVHKLRQQTAMVFQ 87
Cdd:TIGR01188   1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARV-------AGYDvVREPRKVRRSIGIVPQ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   88 NYNLFKNKTALQNVtEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:TIGR01188  74 YASVDEDLTGRENL-EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPT 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201  168 SALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:TIGR01188 153 TGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1-239 6.38e-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: 160.24  E-value: 6.38e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKD----LTVLDGIDLEIKSGEVTAIIGPSGSGKS-TLLRCLNLLerPDDGIIEIGDAKLNAASYSRKDV 75
Cdd:COG4172    6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLL--PDPAAHPSGSILFDGQDLLGLSE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  76 HKLRQ----QTAMVFQNynlfkNKTAL-------QNVTEALITAQKKPKKEAEQIGMDLLRQVGL---EHKADSYPITMS 141
Cdd:COG4172   84 RELRRirgnRIAMIFQE-----PMTSLnplhtigKQIAEVLRLHRGLSGAAARARALELLERVGIpdpERRLDAYPHQLS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 142 GGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQ 220
Cdd:COG4172  159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
                        250
                 ....*....|....*....
gi 489248201 221 GTPEELFDNPQNERTKKFI 239
Cdd:COG4172  239 GPTAELFAAPQHPYTRKLL 257
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
1-234 9.93e-46

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 154.08  E-value: 9.93e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLT-VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaaSYSRKDVHKLR 79
Cdd:PRK13639   1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI---KYDKKSLLEVR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQNYN--LFKnKTALQNVTEALITAqKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:PRK13639  78 KTVGIVFQNPDdqLFA-PTVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNER 234
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
2-226 1.90e-45

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: 151.50  E-value: 1.90e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDL--TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnaasYS-RKDVHKL 78
Cdd:cd03263    1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING-------YSiRTDRKAA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  79 RQQTAMVFQNYNLFKNKTALQNVteaLITAQKK--PKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:cd03263   74 RQSLGYCPQFDALFDELTVREHL---RFYARLKglPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIG 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAeKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:cd03263  151 GPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
1-225 2.05e-45

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 152.62  E-value: 2.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDVHK--- 77
Cdd:PRK13548   2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPL--ADWSPAELARrra 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  78 -LRQQTAMVFQnynlFknkTALQNVTEALITAQKkPKKEAEQIGMDLLRQVGLEHKAD-SYPiTMSGGQQQRIGIARALA 155
Cdd:PRK13548  80 vLPQHSSLSFP----F---TVEEVVAMGRAPHGL-SRAEDDALVAAALAQVDLAHLAGrDYP-QLSGGEQQRVQLARVLA 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 156 ------VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEE 225
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERgLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
2-245 4.40e-45

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 152.48  E-value: 4.40e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLT--VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASysrkdVHKLR 79
Cdd:PRK13635   6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET-----VWDVR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQNY-NLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:PRK13635  81 RQVGMVFQNPdNQFVGATVQDDVAFGL-ENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQT-TMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELF---------- 227
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFksghmlqeig 238
                        250
                 ....*....|....*....
gi 489248201 228 -DNPQNERTKKFIKQVGEP 245
Cdd:PRK13635 239 lDVPFSVKLKELLKRNGIL 257
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
21-221 5.90e-45

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: 149.95  E-value: 5.90e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  21 DLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklrqqtAMVFQNYNLFKNKTALQN 100
Cdd:cd03298   18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPV-------SMLFQENNLFAHLTVEQN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 101 VTEAL-----ITAQKKPKKEAeqigmdLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELV 175
Cdd:cd03298   91 VGLGLspglkLTAEDRQAIEV------ALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489248201 176 AGVLQ-VIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03298  165 AEMLDlVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
2-239 7.77e-45

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 151.15  E-value: 7.77e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLN-LLERPDDGIIEiGDAKLNAASYSRKDVH--KL 78
Cdd:PRK14267   5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrLLELNEEARVE-GEVRLFGRNIYSPDVDpiEV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  79 RQQTAMVFQNYNLFKNKTALQNVTEAL-ITAQKKPKKEAEQIGMDLLRQVGL----EHKADSYPITMSGGQQQRIGIARA 153
Cdd:PRK14267  84 RREVGMVFQYPNPFPHLTIYDNVAIGVkLNGLVKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 154 LAVDPHAILLDEPTSALDPELVAGVLQVIKSIaEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNE 233
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHE 242

                 ....*.
gi 489248201 234 RTKKFI 239
Cdd:PRK14267 243 LTEKYV 248
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
17-236 8.66e-45

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 152.81  E-value: 8.66e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdAKLNAASYSRKDVHKLRQQTAMVFQN-Y-NLFKN 94
Cdd:PRK11308  31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYY--QGQDLLKADPEAQKLLRQKIQIVFQNpYgSLNPR 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  95 KTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL--EHkADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDP 172
Cdd:PRK11308 109 KKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrpEH-YDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 173 ELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTK 236
Cdd:PRK11308 188 SVQAQVLNLMMDLqQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQ 252
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
8-231 1.39e-44

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 151.33  E-value: 1.39e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   8 RKAFKDltvldgIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnAASYSRKDVHKLRQQTAMVFQ 87
Cdd:PRK13634  20 RRALYD------VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVI-TAGKKNKKLKPLRKKVGIVFQ 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  88 --NYNLFKNktalqnvtealiTAQKK----------PKKEAEQIGMDLLRQVGLEHKA-DSYPITMSGGQQQRIGIARAL 154
Cdd:PRK13634  93 fpEHQLFEE------------TVEKDicfgpmnfgvSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 155 AVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
2-229 1.81e-44

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: 149.12  E-value: 1.81e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKL-NAASYSRkdvhkLRQ 80
Cdd:cd03224    1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItGLPPHER-----ARA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTalqnVTEALITAQKKPKKEAEQIGMD-------LLRQVgLEHKADsypiTMSGGQQQRIGIARA 153
Cdd:cd03224   76 GIGYVPEGRRIFPELT----VEENLLLGAYARRRAKRKARLErvyelfpRLKER-RKQLAG----TLSGGEQQMLAIARA 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 154 LAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDN 229
Cdd:cd03224  147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
2-230 2.33e-44

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 152.57  E-value: 2.33e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklrqq 81
Cdd:PRK11432   7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDI------ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 tAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:PRK11432  81 -CMVFQSYALFPHMSLGENVGYGL-KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
2-239 3.66e-44

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 149.60  E-value: 3.66e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKD---------LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSR 72
Cdd:COG4167    5 LEVRNLSKTFKYrtglfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  73 KDVHkLRqqtaMVFQNYNlfknkTAL---QNVTEAL-----ITAQKKPKKEAEQIgMDLLRQVGL--EHkADSYPITMSG 142
Cdd:COG4167   85 RCKH-IR----MIFQDPN-----TSLnprLNIGQILeeplrLNTDLTAEEREERI-FATLRLVGLlpEH-ANFYPHMLSS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 143 GQQQRIGIARALAVDPHAILLDEPTSALDPELVAgvlQVIKSIAEKQTTM----IIVTHEMAFAREVADKVIFMADGRII 218
Cdd:COG4167  153 GQKQRVALARALILQPKIIIADEALAALDMSVRS---QIINLMLELQEKLgisyIYVSQHLGIVKHISDKVLVMHQGEVV 229
                        250       260
                 ....*....|....*....|.
gi 489248201 219 EQGTPEELFDNPQNERTKKFI 239
Cdd:COG4167  230 EYGKTAEVFANPQHEVTKRLI 250
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
2-239 6.77e-44

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 148.65  E-value: 6.77e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKL-NAASYSRK-DVHKLR 79
Cdd:PRK14258   8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFfNQNIYERRvNLNRLR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQNYNLFKnKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL----EHKADSYPITMSGGQQQRIGIARALA 155
Cdd:PRK14258  88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMAD-----GRIIEQGTPEELFDN 229
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNS 246
                        250
                 ....*....|
gi 489248201 230 PQNERTKKFI 239
Cdd:PRK14258 247 PHDSRTREYV 256
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
17-168 1.49e-43

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: 144.33  E-value: 1.49e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasysRKDVHKLRQQTAMVFQNYNLFKNKT 96
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-----DDERKSLRKEIGYVFQDPQLFPRLT 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201   97 ALQNVTEAL-ITAQKKPKKEAEQIgmDLLRQVGLEHKAD----SYPITMSGGQQQRIGIARALAVDPHAILLDEPTS 168
Cdd:pfam00005  76 VRENLRLGLlLKGLSKREKDARAE--EALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
2-226 3.39e-43

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: 145.59  E-value: 3.39e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGiieigdaKLNAASYS-RKDVHKLRQ 80
Cdd:cd03265    1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG-------RATVAGHDvVREPREVRR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVteaLITA--QKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03265   74 RIGIVFQDLSVDDELTGWENL---YIHArlYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:cd03265  151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
4-217 1.34e-42

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 145.21  E-value: 1.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   4 VRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkdvhklRQQTA 83
Cdd:PRK11247  15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA----------REDTR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  84 MVFQNYNLFKNKTALQNVTEALitaQKKPKKEAEQIgmdlLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILL 163
Cdd:PRK11247  85 LMFQDARLLPWKKVIDNVGLGL---KGQWRDAALQA----LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 164 DEPTSALDPELVAGVLQVIKSIAEKQT-TMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-220 2.04e-42

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 145.00  E-value: 2.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAF----KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdvh 76
Cdd:COG4525    3 MLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 klrqqtAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:COG4525   79 ------GVVFQKDALLPWLNVLDNVAFGL-RLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 157 DPHAILLDEPTSALDP-------ELvagVLQViksIAEKQTTMIIVTHEMAFAREVADKVIFMAD--GRIIEQ 220
Cdd:COG4525  152 DPRFLLMDEPFGALDAltreqmqEL---LLDV---WQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVER 218
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
1-217 2.31e-42

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 143.32  E-value: 2.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLT----VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVH 76
Cdd:NF038007   1 MLNMQNAEKCYITKTiktkVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KlRQQTAMVFQNYNLFKNKTALQNVTEALITaQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:NF038007  81 R-RELIGYIFQSFNLIPHLSIFDNVALPLKY-RGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVS 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAfAREVADKVIFMADGRI 217
Cdd:NF038007 159 NPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
9-230 4.37e-42

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 145.76  E-value: 4.37e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   9 KAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSR-----------KDVHK 77
Cdd:PRK13631  34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHelitnpyskkiKNFKE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  78 LRQQTAMVFQ--NYNLFKNkTALQNVTEALItAQKKPKKEAEQIGMDLLRQVGLEHK-ADSYPITMSGGQQQRIGIARAL 154
Cdd:PRK13631 114 LRRRVSMVFQfpEYQLFKD-TIEKDIMFGPV-ALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGIL 191
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 155 AVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
1-205 5.18e-42

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: 142.23  E-value: 5.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasysRKDVHKLRQ 80
Cdd:COG4133    2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI------RDAREDYRR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVteALITAQKKPKKEAEQIgMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:COG4133   76 RLAYLGHADGLKPELTVRENL--RFWAALYGLRADREAI-DEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTH---EMAFAREV 205
Cdd:COG4133  153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqplELAAARVL 200
cbiO PRK13640
energy-coupling factor transporter ATPase;
2-243 1.56e-41

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 143.40  E-value: 1.56e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKD--LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDD---GIIEIGDAKLNAasysrKDVH 76
Cdd:PRK13640   6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTA-----KTVW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KLRQQTAMVFQNY-NLFKNKTALQNVTEALITAQKkPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALA 155
Cdd:PRK13640  81 DIREKVGIVFQNPdNQFVGATVGDDVAFGLENRAV-PRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFArEVADKVIFMADGRIIEQGTPEELFDNPQner 234
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE--- 235

                 ....*....
gi 489248201 235 tkkFIKQVG 243
Cdd:PRK13640 236 ---MLKEIG 241
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
1-226 3.78e-41

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 141.37  E-value: 3.78e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDakLNAASYSRKDVHK--- 77
Cdd:COG4604    1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDG--LDVATTPSRELAKrla 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  78 -LRQqtamvfqnynlfknktalQNVTEALIT------------AQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQ 144
Cdd:COG4604   79 iLRQ------------------ENHINSRLTvrelvafgrfpySKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQ 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 145 QQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTP 223
Cdd:COG4604  141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP 220

                 ...
gi 489248201 224 EEL 226
Cdd:COG4604  221 EEI 223
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
2-218 4.47e-41

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: 138.33  E-value: 4.47e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSrkdvHKLRQQ 81
Cdd:cd03216    1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR----DARRAG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQnynlfknktalqnvtealitaqkkpkkeaeqigmdllrqvglehkadsypitMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03216   77 IAMVYQ----------------------------------------------------LSVGERQMVEIARALARNARLL 104
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRII 218
Cdd:cd03216  105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1-226 7.08e-41

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 141.78  E-value: 7.08e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasysRKDVHKL-- 78
Cdd:COG4152    1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-----PEDRRRIgy 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  79 ----RqqtamvfqnyNLFKNKTalqnVTEALI-TAQKK--PKKEAEQIGMDLLRQVGLEHKADSyPI-TMSGGQQQRIGI 150
Cdd:COG4152   76 lpeeR----------GLYPKMK----VGEQLVyLARLKglSKAEAKRRADEWLERLGLGDRANK-KVeELSKGNQQKVQL 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 151 ARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:COG4152  141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
1-225 7.53e-41

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 147.95  E-value: 7.53e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAF----KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdAKLNAASYSRKDVH 76
Cdd:PRK10535   4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRV--AGQDVATLDADALA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KLRQQT-AMVFQNYNLFKNKTALQNVTEALITAqKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALA 155
Cdd:PRK10535  82 QLRREHfGFIFQRYHLLSHLTAAQNVEVPAVYA-GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEE 225
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQE 229
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
1-231 7.58e-41

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 140.16  E-value: 7.58e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnaasysrKDVHKL-- 78
Cdd:COG1137    3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG----------EDITHLpm 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  79 ----RQ------QTAMVFqnynlfKNKTALQNVtEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRI 148
Cdd:COG1137   73 hkraRLgigylpQEASIF------RKLTVEDNI-LAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 149 GIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEmafARE---VADKVIFMADGRIIEQGTPEE 225
Cdd:COG1137  146 EIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHN---VREtlgICDRAYIISEGKVLAEGTPEE 222

                 ....*.
gi 489248201 226 LFDNPQ 231
Cdd:COG1137  223 ILNNPL 228
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
2-221 8.09e-41

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: 139.27  E-value: 8.09e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnaaSYSRKDVHKLRQQ 81
Cdd:cd03268    1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG------KSYQKNIEALRRI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVfQNYNLFKNKTALQNVtEALITAQKKPKKEAEQIgmdlLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03268   75 GALI-EAPGFYPNLTARENL-RLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03268  149 ILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
22-242 8.26e-41

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 144.41  E-value: 8.26e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  22 LEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDakLNAASYSRKDVHKLR-QQTAMVFQNYNLFKNKTALQN 100
Cdd:PRK10070  49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDAELREVRrKKIAMVFQSFALMPHMTVLDN 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 101 VTEALITAqKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPeLVAGVLQ 180
Cdd:PRK10070 127 TAFGMELA-GINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP-LIRTEMQ 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 181 --VIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIKQV 242
Cdd:PRK10070 205 deLVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
2-230 1.22e-40

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: 139.60  E-value: 1.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKlRQQ 81
Cdd:cd03218    1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-----TKLPMHK-RAR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVF--QNYNLFKNKTALQNVTEALITaQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPH 159
Cdd:cd03218   75 LGIGYlpQEASIFRKLTVEENILAVLEI-RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEmafARE---VADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:cd03218  154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHN---VREtlsITDRAYIIYEGKVLAEGTPEEIAANE 224
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
11-221 1.24e-40

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: 138.82  E-value: 1.24e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  11 FKDLTV-------LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnaasysrKDVHKLRQQTA 83
Cdd:cd03235    2 VEDLTVsygghpvLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG----------KPLEKERKRIG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  84 MVFQNYNLFKNK--TALQNVTEAL---ITAQKKPKKEAEQIGMDLLRQVGLEHKADsYPI-TMSGGQQQRIGIARALAVD 157
Cdd:cd03235   72 YVPQRRSIDRDFpiSVRDVVLMGLyghKGLFRRLSKADKAKVDEALERVGLSELAD-RQIgELSGGQQQRVLLARALVQD 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMaDGRIIEQG 221
Cdd:cd03235  151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
17-239 1.62e-40

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 140.30  E-value: 1.62e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLErpD-------DGIIEIGDAKLNAasySRKDVHKLRQQTAMVFQNY 89
Cdd:PRK14243  26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLN--DlipgfrvEGKVTFHGKNLYA---PDVDPVEVRRRIGMVFQKP 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  90 NLFKnKTALQNVTEAlitaqkkPKKEAEQIGMD-----LLRQVGL----EHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:PRK14243 101 NPFP-KSIYDNIAYG-------ARINGYKGDMDelverSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEV 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEkQTTMIIVTHEMAFAREVADKVIFMA---------DGRIIEQGTPEELFDNPQ 231
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQ 251

                 ....*...
gi 489248201 232 NERTKKFI 239
Cdd:PRK14243 252 QQATRDYV 259
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
2-239 2.87e-40

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 142.09  E-value: 2.87e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasysrkDVHKLRQQ 81
Cdd:PRK11000   4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-------DVPPAERG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNKTALQNVTEALITAQKKpKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:PRK11000  77 VGMVFQSYALYPHLSVAENMSFGLKLAGAK-KEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 162 LLDEPTSALDPEL-VAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFI 239
Cdd:PRK11000 156 LLDEPLSNLDAALrVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI 234
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
2-229 3.15e-40

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 140.61  E-value: 3.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFK-----DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIE--IGDAKLNAASYSR-- 72
Cdd:PRK13651   3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTKEKek 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  73 ---------------KDVHKLRQQTAMVFQ--NYNLFKnktalQNVTEALITAQKK---PKKEAEQIGMDLLRQVGL-EH 131
Cdd:PRK13651  83 vleklviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFE-----QTIEKDIIFGPVSmgvSKEEAKKRAAKYIELVGLdES 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 132 KADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIF 211
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIF 237
                        250
                 ....*....|....*...
gi 489248201 212 MADGRIIEQGTPEELFDN 229
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSD 255
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
1-231 6.78e-40

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 138.59  E-value: 6.78e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIrkAFK----DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasysRKDVH 76
Cdd:PRK13632   7 MIKVENV--SFSypnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS-----KENLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KLRQQTAMVFQNY-NLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALA 155
Cdd:PRK13632  80 EIRKKIGIIFQNPdNQFIGATVEDDIAFGL-ENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQT-TMIIVTHEMafaREV--ADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDM---DEAilADKVIVFSEGKLIAQGKPKEILNNKE 234
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
13-239 9.67e-40

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 137.87  E-value: 9.67e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLN-LLERPDDGIIEIGDAKLNAASYSRKDVHKLRQQTAMVFQNYNL 91
Cdd:PRK14246  22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrLIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  92 FKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL----EHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489248201 168 SALDPELVAGVLQVIKSIaEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFI 239
Cdd:PRK14246 182 SMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
1-247 1.12e-39

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 137.84  E-value: 1.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLL----ERPDDGIIEIGDAKLNAASYSRkDVH 76
Cdd:PRK09984   4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRTVQREGRLAR-DIR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KLRQQTAMVFQNYNLFKNKTALQNV-------TEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIG 149
Cdd:PRK09984  83 KSRANTGYIFQQFNLVNRLSVLENVligalgsTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 150 IARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVT-HEMAFAREVADKVIFMADGRIIEQGTPEElFD 228
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDGSSQQ-FD 241
                        250
                 ....*....|....*....
gi 489248201 229 NPQNERTKKFIKQVGEPAE 247
Cdd:PRK09984 242 NERFDHLYRSINRVEENAK 260
cbiO PRK13646
energy-coupling factor transporter ATPase;
17-227 1.48e-39

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 138.37  E-value: 1.48e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASySRKDVHKLRQQTAMVFQ--NYNLFKN 94
Cdd:PRK13646  23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKT-KDKYIRPVRKRIGMVFQfpESQLFED 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  95 ktalqNVTEALITAQKK---PKKEAEQIGMDLLRQVGLEHKA-DSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSAL 170
Cdd:PRK13646 102 -----TVEREIIFGPKNfkmNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 171 DPELVAGVLQVIKSIAEKQT-TMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF 227
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENkTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-226 1.91e-39

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 142.46  E-value: 1.91e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYsrKDVHKLRq 80
Cdd:COG1129    4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSP--RDAQAAG- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 qTAMVFQNYNLFKNKTALQNV------TEALITAQKKPKKEAEQigmdLLRQVGLEHKADSyPI-TMSGGQQQRIGIARA 153
Cdd:COG1129   81 -IAIIHQELNLVPNLSVAENIflgrepRRGGLIDWRAMRRRARE----LLARLGLDIDPDT-PVgDLSVAQQQLVEIARA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 154 LAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:COG1129  155 LSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
15-218 3.33e-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: 135.08  E-value: 3.33e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkdvhKLRQQTAMVFQN--YNLF 92
Cdd:cd03226   14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK--------ERRKSIGYVMQDvdYQLF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  93 KNktalqNVTEALITAQKKPKKEAEQIGmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDP 172
Cdd:cd03226   86 TD-----SVREELLLGLKELDAGNEQAE-TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489248201 173 ELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRII 218
Cdd:cd03226  160 KNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
1-227 3.36e-39

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 137.29  E-value: 3.36e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLT-VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasYSRKDVHKLR 79
Cdd:PRK13636   5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID---YSRKGLMKLR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQ--NYNLFkNKTALQNVTEALITAQKkPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:PRK13636  82 ESVGMVFQdpDNQLF-SASVYQDVSFGAVNLKL-PEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF 227
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
1-227 4.31e-39

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: 135.98  E-value: 4.31e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGI-IEIGDAKLNAAsysrkDVHKLR 79
Cdd:COG1119    3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGE-----DVWELR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMV---FQNYNlfknkTALQNVTEALITA-------QKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIG 149
Cdd:COG1119   78 KRIGLVspaLQLRF-----PRDETVLDVVLSGffdsiglYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 150 IARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF 227
Cdd:COG1119  153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAaEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
16-202 4.80e-39

cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130234 [Multi-domain]  Cd Length: 190  Bit Score: 134.09  E-value: 4.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasYSRKDVHKLRQQTAMVFQNYN--LFK 93
Cdd:TIGR01166   7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLD---YSRKGLLERRQRVGLVFQDPDdqLFA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   94 nKTALQNVTEALITAQKKPKkEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPE 173
Cdd:TIGR01166  84 -ADVDQDVAFGPLNLGLSEA-EVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
                         170       180
                  ....*....|....*....|....*....
gi 489248201  174 LVAGVLQVIKSIAEKQTTMIIVTHEMAFA 202
Cdd:TIGR01166 162 GREQMLAILRRLRAEGMTVVISTHDVDLA 190
cbiO PRK13641
energy-coupling factor transporter ATPase;
17-231 6.73e-39

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 136.50  E-value: 6.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASySRKDVHKLRQQTAMVFQ--NYNLFKN 94
Cdd:PRK13641  23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPET-GNKNLKKLRKKVSLVFQfpEAQLFEN 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  95 kTALQNVtealitaQKKPK------KEAEQIGMDLLRQVGL-EHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:PRK13641 102 -TVLKDV-------EFGPKnfgfseDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 168 SALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
1-242 9.89e-39

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 138.43  E-value: 9.89e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasysrkDVHKLRQ 80
Cdd:PRK11607  19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-------HVPPYQR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:PRK11607  92 PINMMFQSYALFPHMTVEQNIAFGL-KQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 161 ILLDEPTSALDPELVAGV-LQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFI 239
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250

                 ...
gi 489248201 240 KQV 242
Cdd:PRK11607 251 GSV 253
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
21-226 1.03e-38

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 134.32  E-value: 1.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  21 DLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklrqqtAMVFQNYNLFKNKTALQN 100
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPV-------SMLFQENNLFSHLTVAQN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 101 VTEAL-----ITAQKKPKKEaeqigmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELV 175
Cdd:PRK10771  92 IGLGLnpglkLNAAQREKLH------AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489248201 176 AGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK10771 166 QEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
21-221 1.79e-38

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


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 133.45  E-value: 1.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   21 DLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklrqqtAMVFQNYNLFKNKTALQN 100
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPV-------SMLFQENNLFAHLTVRQN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  101 VTEALITAQKKPKKEAEQIgMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQ 180
Cdd:TIGR01277  91 IGLGLHPGLKLNAEQQEKV-VDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 489248201  181 VIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:TIGR01277 170 LVKQLCsERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
1-217 1.83e-38

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 133.46  E-value: 1.83e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAF-KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDVHKLR 79
Cdd:PRK10908   1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDI--TRLKNREVPFLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMdLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPH 159
Cdd:PRK10908  79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSA-ALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
1-235 2.20e-38

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 134.28  E-value: 2.20e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEI-----GDAKLNAASYSRKDv 75
Cdd:PRK11701   6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdgQLRDLYALSEAERR- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  76 HKLRQQTAMVFQN--YNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLE-HKADSYPITMSGGQQQRIGIAR 152
Cdd:PRK11701  85 RLLRTEWGFVHQHprDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQIAR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKS-IAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQ 244

                 ....
gi 489248201 232 NERT 235
Cdd:PRK11701 245 HPYT 248
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
1-231 3.39e-38

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: 133.18  E-value: 3.39e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKL-R 79
Cdd:COG0410    3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-----TGLPPHRIaR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQNYNLFKNKTalqnVTEALITAQKkPKKEAEQIGMDLLRQVGLehkadsYPI----------TMSGGQQQRIG 149
Cdd:COG0410   78 LGIGYVPEGRRIFPSLT----VEENLLLGAY-ARRDRAEVRADLERVYEL------FPRlkerrrqragTLSGGEQQMLA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 150 IARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDN 229
Cdd:COG0410  147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLAD 226

                 ..
gi 489248201 230 PQ 231
Cdd:COG0410  227 PE 228
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
1-227 4.23e-38

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


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 133.78  E-value: 4.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    1 MIQVRHIRKAFKD---------LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYS 71
Cdd:TIGR02769   2 LLEVRDVTHTYRTgglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDL--YQLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   72 RKDVHKLRQQTAMVFQN-YNLFK-NKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHK-ADSYPITMSGGQQQRI 148
Cdd:TIGR02769  80 RKQRRAFRRDVQLVFQDsPSAVNpRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEdADKLPRQLSGGQLQRI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  149 GIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF 227
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL 239
cbiO PRK13643
energy-coupling factor transporter ATPase;
20-227 5.86e-38

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 134.09  E-value: 5.86e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASySRKDVHKLRQQTAMVFQ--NYNLFKnKTA 97
Cdd:PRK13643  25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS-KQKEIKPVRKKVGVVFQfpESQLFE-ETV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  98 LQNVTealITAQK--KPKKEAEQIGMDLLRQVGLEHKA-DSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPEL 174
Cdd:PRK13643 103 LKDVA---FGPQNfgIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489248201 175 VAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF 227
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
2-226 8.49e-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: 132.35  E-value: 8.49e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKD-LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKLRQ 80
Cdd:cd03253    1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI-----REVTLDSLRR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFkNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSY----PITMSGGQQQRIGIARALAV 156
Cdd:cd03253   76 AIGVVPQDTVLF-NDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIvgerGLKLSGGEKQRVAIARAILK 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMafaREV--ADKVIFMADGRIIEQGTPEEL 226
Cdd:cd03253  155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTT-IVIAHRL---STIvnADKIIVLKDGRIVERGTHEEL 222
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
1-239 9.90e-38

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 132.97  E-value: 9.90e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEI-GDaklNAASYSRKDVHKLR 79
Cdd:PRK11831   7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGE---NIPAMSRSRLYTVR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPH 159
Cdd:PRK11831  84 KRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 160 AILLDEPTSALDPeLVAGVLqvIKSIAEKQ----TTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPqNERT 235
Cdd:PRK11831 164 LIMFDEPFVGQDP-ITMGVL--VKLISELNsalgVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRV 239

                 ....
gi 489248201 236 KKFI 239
Cdd:PRK11831 240 RQFL 243
cbiO PRK13649
energy-coupling factor transporter ATPase;
17-227 1.55e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 132.95  E-value: 1.55e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASySRKDVHKLRQQTAMVFQ--NYNLFKn 94
Cdd:PRK13649  23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTS-KNKDIKQIRKKVGLVFQfpESQLFE- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  95 KTALQNVTealITAQK--KPKKEAEQIGMDLLRQVGL-EHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD 171
Cdd:PRK13649 101 ETVLKDVA---FGPQNfgVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 172 PELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF 227
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
14-219 1.68e-37

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 132.50  E-value: 1.68e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  14 LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDVHKLRQQTAMVFQNYNLFK 93
Cdd:PRK10419  25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL--AKLNRAQRKAFRRDIQMVFQDSISAV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  94 N--KTALQNVTEAL--ITAQKKPKKEAEQigMDLLRQVGL--EHkADSYPITMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:PRK10419 103 NprKTVREIIREPLrhLLSLDKAERLARA--SEMLRAVDLddSV-LDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489248201 168 SALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIE 219
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFgTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1-225 3.90e-37

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 136.31  E-value: 3.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsySRKDVHKLRq 80
Cdd:COG3845    5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIR--SPRDAIALG- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 qTAMVFQNYNLFKNKTALQNV---TEALITAQKKPKKEAEQIgMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:COG3845   82 -IGMVHQHFMLVPNLTVAENIvlgLEPTKGGRLDRKAARARI-RELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEE 225
Cdd:COG3845  160 ARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
1-221 4.04e-37

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: 129.80  E-value: 4.04e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLT----VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdAKLNAAsysrKDVH 76
Cdd:cd03266    1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV--DGFDVV----KEPA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KLRQQTAMVFQNYNLFKNKTALQNVteaLITAQKKPKKEAEQIGM--DLLRQVGLEHKADSYPITMSGGQQQRIGIARAL 154
Cdd:cd03266   75 EARRRLGFVSDSTGLYDRLTARENL---EYFAGLYGLKGDELTARleELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 155 AVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03266  152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
17-215 6.49e-37

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: 129.89  E-value: 6.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdvhklrqqtAMVFQNYNLFKNKT 96
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR----------MVVFQNYSLLPWLT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   97 ALQNVTEALITAQKK-PKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPeLV 175
Cdd:TIGR01184  71 VRENIALAVDRVLPDlSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA-LT 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 489248201  176 AGVLQ--VIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADG 215
Cdd:TIGR01184 150 RGNLQeeLMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
2-221 6.58e-37

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: 129.32  E-value: 6.58e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdvhklrqq 81
Cdd:cd03269    1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNKTalqnVTEALI-TAQKK--PKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03269   72 IGYLPEERGLYPKMK----VIDQLVyLAQLKglKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03269  148 ELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1-230 1.02e-36

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 132.66  E-value: 1.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFK-DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklr 79
Cdd:PRK11650   3 GLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDI---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 qqtAMVFQNYNLFKNKTALQNVTEALITAqKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPH 159
Cdd:PRK11650  79 ---AMVFQNYALYPHMSVRENMAYGLKIR-GMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 160 AILLDEPTSALDPEL-VAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRiIEQ-GTPEELFDNP 230
Cdd:PRK11650 155 VFLFDEPLSNLDAKLrVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV-AEQiGTPVEVYEKP 226
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
20-230 1.08e-36

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: 132.54  E-value: 1.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasySRKDV----HKLRqqTAMVFQNYNLFKNK 95
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD---SRKGIflppEKRR--IGYVFQEARLFPHL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   96 TALQNvteaLITAQKKPKKEAEQIGMD-LLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPEL 174
Cdd:TIGR02142  91 SVRGN----LRYGMKRARPSERRISFErVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201  175 VAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:TIGR02142 167 KYEILPYLERLhAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
cbiO PRK13637
energy-coupling factor transporter ATPase;
17-229 1.92e-36

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 130.17  E-value: 1.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVhklRQQTAMVFQ--NYNLFKN 94
Cdd:PRK13637  23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDI---RKKVGLVFQypEYQLFEE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  95 KTA------LQNVTEALITAQKKPKKEAEQIGMDLlrqvglEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTS 168
Cdd:PRK13637 100 TIEkdiafgPINLGLSEEEIENRVKRAMNIVGLDY------EDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489248201 169 ALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDN 229
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
16-228 2.56e-36

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: 128.11  E-value: 2.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaaSYSRKdvhKLRQQTAMVFQNYNLFkNK 95
Cdd:cd03254   18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR--DISRK---SLRSMIGVVLQDTFLF-SG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  96 TALQNVTEA-LITAQKKPKKEAEQIGMDLL---RQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD 171
Cdd:cd03254   92 TIMENIRLGrPNATDEEVIEAAKEAGAHDFimkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 172 PELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFD 228
Cdd:cd03254  172 TETEKLIQEALEKLMKGRTS-IIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
13-226 2.68e-36

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: 128.43  E-value: 2.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTllrCLNLLER---PDDGIIEIGDAKLNaasysRKDVHKLRQQTAMVFQNY 89
Cdd:cd03249   15 DVPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERfydPTSGEILLDGVDIR-----DLNLRWLRSQIGLVSQEP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  90 NLFkNKTALQNVtealitAQKKPKKEAEQIgMDLLRQ-------VGLEHKADS----YPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03249   87 VLF-DGTIAENI------RYGKPDATDEEV-EEAAKKanihdfiMSLPDGYDTlvgeRGSQLSGGQKQRIAIARALLRNP 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREvADKVIFMADGRIIEQGTPEEL 226
Cdd:cd03249  159 KILLLDEATSALDAESEKLVQEALDRAMKGRTT-IVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL 224
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
12-245 2.99e-36

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 130.60  E-value: 2.99e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  12 KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL-NLLERPDDGIIEIGDAKLNAasySRKDVHKLRQQTAMVFQN-- 88
Cdd:PRK15079  32 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIiGLVKATDGEVAWLGKDLLGM---KDDEWRAVRSDIQMIFQDpl 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  89 YNLFKNKTALQNVTEALITAQKK-PKKEAEQIGMDLLRQVGL-EHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEP 166
Cdd:PRK15079 109 ASLNPRMTIGEIIAEPLRTYHPKlSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 167 TSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIKQVGEP 245
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVPIP 268
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
16-222 4.29e-36

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 127.62  E-value: 4.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKdvHKLR-QQTAMVFQNYNLFKN 94
Cdd:PRK11629  24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAK--AELRnQKLGFIYQFHHLLPD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  95 KTALQNVTEALITAQKKPKkEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPEL 174
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPA-EINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489248201 175 VAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVaDKVIFMADGRIIEQGT 222
Cdd:PRK11629 181 ADSIFQLLGELNRLQgTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELS 228
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
17-231 1.37e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 127.56  E-value: 1.37e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasysrKDVHKLRQQTAMVFQN-YNLFKNK 95
Cdd:PRK13648  25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD-----DNFEKLRKHIGIVFQNpDNQFVGS 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  96 TALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELV 175
Cdd:PRK13648 100 IVKYDVAFGL-ENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 176 AGVLQVIKSI-AEKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:PRK13648 179 QNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
13-227 1.44e-35

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


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 132.90  E-value: 1.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkDVHKLRQQTAMVFQNYNLF 92
Cdd:TIGR02204 352 DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQL-----DPAELRARMALVPQDPVLF 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   93 KNkTALQNV-------TEALITAQKKPKKEAEQIGmdllrqvGLEHKADSY----PITMSGGQQQRIGIARALAVDPHAI 161
Cdd:TIGR02204 427 AA-SVMENIrygrpdaTDEEVEAAARAAHAHEFIS-------ALPEGYDTYlgerGVTLSGGQRQRIAIARAILKDAPIL 498
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201  162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIvTHEMAFAREvADKVIFMADGRIIEQGTPEELF 227
Cdd:TIGR02204 499 LLDEATSALDAESEQLVQQALETLMKGRTTLII-AHRLATVLK-ADRIVVMDQGRIVAQGTHAELI 562
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
16-226 1.72e-35

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 132.64  E-value: 1.72e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLrclNLLER---PDDGIIEIGDAKLNAasYSRKDvhkLRQQTAMVFQNYNLF 92
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLL---QLLTRawdPQQGEILLNGQPIAD--YSEAA---LRQAISVVSQRVHLF 426
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  93 kNKTALQNVTEAlitaqkKPKKEAEQIgMDLLRQVGLEHKADSYP----------ITMSGGQQQRIGIARALAVDPHAIL 162
Cdd:PRK11160 427 -SATLRDNLLLA------APNASDEAL-IEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLL 498
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 163 LDEPTSALDPELVAGVLQVIKSIAeKQTTMIIVTHEMaFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK11160 499 LDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQEL 560
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
2-245 2.82e-35

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: 131.46  E-value: 2.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLE--RPDDGII--------------------- 58
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpskvge 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   59 -------EIGDAKLNAASYSRKDVHKLRQQTAMVFQ-NYNLFKNKTALQNVTEALITAQKkPKKEAEQIGMDLLRQVGLE 130
Cdd:TIGR03269  81 pcpvcggTLEPEEVDFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGY-EGKEAVGRAVDLIEMVQLS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  131 HKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPE---LVAGVLqvIKSIAEKQTTMIIVTHEMAFAREVAD 207
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtakLVHNAL--EEAVKASGISMVLTSHWPEVIEDLSD 237
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 489248201  208 KVIFMADGRIIEQGTPEELfdnpqnerTKKFIKQVGEP 245
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEV--------VAVFMEGVSEV 267
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
2-221 3.22e-35

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: 124.61  E-value: 3.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGeVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasysRKDVHKLRQQ 81
Cdd:cd03264    1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV------LKQPQKLRRR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNKTALQNVtEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03264   74 IGYLPQEFGVYPNFTVREFL-DYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03264  153 IVDEPTAGLDPEERIRFRNLLSELGEDRIV-ILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
16-228 3.24e-35

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: 125.42  E-value: 3.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLrclNLLER---PDDGIIEIGDakLNAASYSRKDvhkLRQQTAMVFQNYNLF 92
Cdd:cd03251   17 VLRDISLDIPAGETVALVGPSGSGKSTLV---NLIPRfydVDSGRILIDG--HDVRDYTLAS---LRRQIGLVSQDVFLF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  93 kNKTALQNVtealitAQKKPKKEAEQIgMDLLRQVGLEHKADSYP-----------ITMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03251   89 -NDTVAENI------AYGRPGATREEV-EEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPPIL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFD 228
Cdd:cd03251  161 ILDEATSALDTESERLVQAALERLMKNRTT-FVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
16-217 3.48e-35

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: 123.48  E-value: 3.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaaSYSRKDvhkLRQQTAMVFQNYNLFKNk 95
Cdd:cd03246   17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS--QWDPNE---LGDHVGYLPQDDELFSG- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  96 TALQNVtealitaqkkpkkeaeqigmdllrqvglehkadsypitMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELV 175
Cdd:cd03246   91 SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489248201 176 AGVLQVIKSIAEKQTTMIIVTHEMAFAREvADKVIFMADGRI 217
Cdd:cd03246  133 RALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
15-246 4.23e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 126.36  E-value: 4.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDG--IIEIGDAKLnaasysRKDVHKLRQQTAMVFQNYNlf 92
Cdd:PRK13633  24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGkvYVDGLDTSD------EENLWDIRNKAGMVFQNPD-- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  93 kNKTALQNVTEALITAQKKPKKEAEQIGM---DLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSA 169
Cdd:PRK13633  96 -NQIVATIVEEDVAFGPENLGIPPEEIRErvdESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 170 LDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFdnPQNERTKKF---IKQVGEP 245
Cdd:PRK13633 175 LDPSGRREVVNTIKELNKKYgITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF--KEVEMMKKIgldVPQVTEL 251

                 .
gi 489248201 246 A 246
Cdd:PRK13633 252 A 252
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
1-225 7.85e-35

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 123.75  E-value: 7.85e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLrcLNLLERPDDGIIEIGDAKLNAASYSRKDVHklRQ 80
Cdd:COG4136    1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLL--AAIAGTLSPAFSASGEVLLNGRRLTALPAE--QR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTEALitAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:COG4136   77 RIGILFQDDLLFPHLSVGENLAFAL--PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 161 ILLDEPTSALDPELVAGVLQ-VIKSIAEKQTTMIIVTHEMAFARevadkvifmADGRIIEQGTPEE 225
Cdd:COG4136  155 LLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEEDAP---------AAGRVLDLGNWQH 211
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
17-226 1.83e-34

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: 129.15  E-value: 1.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIE--IGDAKLNAASYSRKDVHKLRQQTAMVFQNYNLFKN 94
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEWVDMTKPGPDGRGRAKRYIGILHQEYDLYPH 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   95 KTALQNVTEALitAQKKPKKEAEQIGMDLLRQVGLEHKA-----DSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSA 169
Cdd:TIGR03269 380 RTVLDNLTEAI--GLELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201  170 LDPELVAGVLQVI-KSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:TIGR03269 458 MDPITKVDVTHSIlKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
16-212 3.17e-34

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


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 128.56  E-value: 3.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkDVHKLRQQTAMVFQNYNLFkNK 95
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA-----DADSWRDQIAWVPQHPFLF-AG 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   96 TALQNVTEALITAQKKPKKEA-EQIGMDLLRQV---GLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD 171
Cdd:TIGR02857 411 TIAENIRLARPDASDAEIREAlERAGLDEFVAAlpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 489248201  172 PELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREvADKVIFM 212
Cdd:TIGR02857 491 AETEAEVLEALRALAQGRTV-LLVTHRLALAAL-ADRIVVL 529
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-227 5.73e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 123.30  E-value: 5.73e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLT---VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHK 77
Cdd:PRK13650   4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL-----TEENVWD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  78 LRQQTAMVFQNY-NLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:PRK13650  79 IRHKIGMVFQNPdNQFVGATVEDDVAFGL-ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMafaREVA--DKVIFMADGRIIEQGTPEELF 227
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDL---DEVAlsDRVLVMKNGQVESTSTPRELF 228
cbiO PRK13645
energy-coupling factor transporter ATPase;
13-229 5.85e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 123.58  E-value: 5.85e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVHKLRQQTAMVFQ--NYN 90
Cdd:PRK13645  23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQfpEYQ 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  91 LFKNkTALQNVTEALITAQKKpKKEAEQIGMDLLRQVGL-EHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSA 169
Cdd:PRK13645 103 LFQE-TIEKDIAFGPVNLGEN-KQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 170 LDPELVAGVLQVIKSIAEKQTTMII-VTHEMAFAREVADKVIFMADGRIIEQGTPEELFDN 229
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIImVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
2-228 6.28e-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: 128.30  E-value: 6.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    2 IQVRHIRKAF--KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLrclNLLER---PDDGIIEIGDAKLnaASYSRKDvh 76
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLV---NLIPRfyePDSGQILLDGHDL--ADYTLAS-- 403
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   77 kLRQQTAMVFQNYNLFkNKTALQNVT-EALITAQKKPKKEAEQIG--MDLLRQV--GLEHKADSYPITMSGGQQQRIGIA 151
Cdd:TIGR02203 404 -LRRQVALVSQDVVLF-NDTIANNIAyGRTEQADRAEIERALAAAyaQDFVDKLplGLDTPIGENGVLLSGGQRQRLAIA 481
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201  152 RALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIvTHEMAfAREVADKVIFMADGRIIEQGTPEELFD 228
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVI-AHRLS-TIEKADRIVVMDDGRIVERGTHNELLA 556
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
16-228 1.46e-33

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: 121.44  E-value: 1.46e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkDVHKLRQQTAMVFQNYNLFkNK 95
Cdd:cd03252   17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA-----DPAWLRRQVGVVLQENVLF-NR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  96 TALQNVTEALITAQKKPKKEAEQIG--MDLLRQV--GLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD 171
Cdd:cd03252   91 SIRDNIALADPGMSMERVIEAAKLAgaHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 172 PELVAGVLQVIKSIAEKQtTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFD 228
Cdd:cd03252  171 YESEHAIMRNMHDICAGR-TVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
2-228 2.25e-33

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 121.77  E-value: 2.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLT-VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasysrKDVHKLRQ 80
Cdd:PRK13647   5 IEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA-----ENEKWVRS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYN--LFKNkTALQNVTEALITaQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:PRK13647  80 KVGLVFQDPDdqVFSS-TVWDDVAFGPVN-MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFD 228
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
1-230 2.93e-33

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 120.87  E-value: 2.93e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIeigdaKLNAASYSRKDVHKL-R 79
Cdd:PRK11300   5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI-----LLRGQHIEGLPGHQIaR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQNYNLFKNKTALQNvteaLITAQ-------------KKPK-KEAEQIGMDL----LRQVGLEHKADSYPITMS 141
Cdd:PRK11300  80 MGVVRTFQHVRLFREMTVIEN----LLVAQhqqlktglfsgllKTPAfRRAESEALDRaatwLERVGLLEHANRQAGNLA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 142 GGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQ 220
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
                        250
                 ....*....|
gi 489248201 221 GTPEELFDNP 230
Cdd:PRK11300 236 GTPEEIRNNP 245
cbiO PRK13644
energy-coupling factor transporter ATPase;
1-230 4.64e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 120.86  E-value: 4.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLT-VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdAKLNAASYSRkdVHKLR 79
Cdd:PRK13644   1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV--SGIDTGDFSK--LQGIR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQN-YNLFKNKTALQNVT---EALITAQKKPKKEAEQIgmdlLRQVGLEHKADSYPITMSGGQQQRIGIARALA 155
Cdd:PRK13644  77 KLVGIVFQNpETQFVGRTVEEDLAfgpENLCLPPIEIRKRVDRA----LAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAfAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
1-242 6.55e-33

phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]


Pssm-ID: 188208 [Multi-domain]  Cd Length: 253  Bit Score: 119.94  E-value: 6.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEI---GDAKLNAASYSRKDVHK 77
Cdd:TIGR02323   3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELELYQLSEAERRR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   78 L-RQQTAMVFQNY--NLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLE-HKADSYPITMSGGQQQRIGIARA 153
Cdd:TIGR02323  83 LmRTEWGFVHQNPrdGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQIARN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  154 LAVDPHAILLDEPTSALDPELVAGVLQVIKS-IAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQN 232
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDVSVQARLLDLLRGlVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQH 242
                         250
                  ....*....|
gi 489248201  233 ERTKKFIKQV 242
Cdd:TIGR02323 243 PYTQLLVSSI 252
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
2-236 8.71e-33

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 119.80  E-value: 8.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAfKDLTVLDGIDLEIKSGEVTAIIGPSGSGKStlLRCLNLLERPDDGIIEIG-----DAKLNAASysrkdvh 76
Cdd:PRK10418   5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAgrvllDGKPVAPC------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KLRQQT-AMVFQN----YNLFKNKTAlqnvtEALITAQKKPKKEAEQIGMDLLRQVGLEHKA---DSYPITMSGGQQQRI 148
Cdd:PRK10418  75 ALRGRKiATIMQNprsaFNPLHTMHT-----HARETCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRM 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 149 GIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTT-MIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF 227
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229

                 ....*....
gi 489248201 228 DNPQNERTK 236
Cdd:PRK10418 230 NAPKHAVTR 238
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
15-239 9.58e-33

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 124.43  E-value: 9.58e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  15 TVLDGIDLEIKSGEVTAIIGPSGSGKST----LLRCLNllerpDDGIIEIGDAKLNaaSYSRKDVHKLRQQTAMVFQNYN 90
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLH--NLNRRQLLPVRHRIQVVFQDPN 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  91 LFKNK--TALQNVTEALITAQKK-PKKEAEQIGMDLLRQVGLEhkADS---YPITMSGGQQQRIGIARALAVDPHAILLD 164
Cdd:PRK15134 373 SSLNPrlNVLQIIEEGLRVHQPTlSAAQREQQVIAVMEEVGLD--PETrhrYPAEFSGGQRQRIAIARALILKPSLIILD 450
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 165 EPTSALDPELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFI 239
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
2-228 3.12e-32

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 119.52  E-value: 3.12e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASysrkdvHKLRQQ 81
Cdd:PRK13537   8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA------RHARQR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNKTALQNVteaLITAQ--KKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPH 159
Cdd:PRK13537  82 VGVVPQFDNLDPDFTVRENL---LVFGRyfGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFD 228
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1-242 4.45e-32

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 117.81  E-value: 4.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKdvhKLRQ 80
Cdd:PRK11231   2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI--SMLSSR---QLAR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQnynlfknktalQNVTEALITAQK--------------KPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQ 146
Cdd:PRK11231  77 RLALLPQ-----------HHLTPEGITVRElvaygrspwlslwgRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQ 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 147 RIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
                        250
                 ....*....|....*.
gi 489248201 227 FdnpqnerTKKFIKQV 242
Cdd:PRK11231 226 M-------TPGLLRTV 234
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
8-221 5.72e-32

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: 116.99  E-value: 5.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   8 RKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLrclNLLE-RPDDGIIEIGDAKLNAASYSRkdvHKLRQQTAMVF 86
Cdd:cd03234   14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLL---DAISgRVEGGGTTSGQILFNGQPRKP---DQFQKCVAYVR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  87 QNYNLFKNKTALQNVTEALI------TAQKKPKKEAEQIGmdlLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:cd03234   88 QDDILLPGLTVRETLTYTAIlrlprkSSDAIRKKRVEDVL---LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKV 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEM---AFarEVADKVIFMADGRIIEQG 221
Cdd:cd03234  165 LILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPrsdLF--RLFDRILLLSSGEIVYSG 226
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
16-221 9.26e-32

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: 116.15  E-value: 9.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAklnaaSYSRKDVHKLRQQTAMVFQNYNLFK-- 93
Cdd:cd03245   19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT-----DIRQLDPADLRRNIGYVPQDVTLFYgt 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  94 ---NKT-ALQNVTEALIT-----------AQKKPKkeaeqiGMDLlrQVGlEHKADsypitMSGGQQQRIGIARALAVDP 158
Cdd:cd03245   94 lrdNITlGAPLADDERILraaelagvtdfVNKHPN------GLDL--QIG-ERGRG-----LSGGQRQAVALARALLNDP 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEkQTTMIIVTHEMAFArEVADKVIFMADGRIIEQG 221
Cdd:cd03245  160 PILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
17-247 1.11e-31

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 118.69  E-value: 1.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  17 LDGIDLEIKSGEVTAIIGPSGSGKS-TLLRCLNLLERPddgiieiGDAKLNAASYSRKDVHKL----RQQ-----TAMVF 86
Cdd:PRK11022  23 VDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP-------GRVMAEKLEFNGQDLQRIsekeRRNlvgaeVAMIF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  87 QN--YNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL---EHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:PRK11022  96 QDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQT-TMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIK 240
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLR 255

                 ....*..
gi 489248201 241 QVGEPAE 247
Cdd:PRK11022 256 ALPEFAQ 262
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
3-226 1.65e-31

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


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 115.70  E-value: 1.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    3 QVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNA-ASYSRkdvhkLRQQ 81
Cdd:TIGR03410   2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKlPPHER-----ARAG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   82 TAMVFQNYNLFKNKTALQNVtealitaqkkpkkeaeQIGMDLLRQVGLEHKADSY---PITM----------SGGQQQRI 148
Cdd:TIGR03410  77 IAYVPQGREIFPRLTVEENL----------------LTGLAALPRRSRKIPDEIYelfPVLKemlgrrggdlSGGQQQQL 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201  149 GIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:TIGR03410 141 AIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRaEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
1-219 4.58e-31

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 115.18  E-value: 4.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdvhklrq 80
Cdd:PRK11248   1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 qtAMVFQNYNLFKNKTALQNVTEALITAqKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:PRK11248  73 --GVVFQNEGLLPWRNVQDNVAFGLQLA-GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 161 ILLDEPTSALDP----ELVAGVLQVIKSIAeKQTTMIivTHEMAFAREVADKVIFMA--DGRIIE 219
Cdd:PRK11248 150 LLLDEPFGALDAftreQMQTLLLKLWQETG-KQVLLI--THDIEEAVFMATELVLLSpgPGRVVE 211
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
17-226 5.48e-31

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 120.07  E-value: 5.48e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  17 LDGIDLEIKSGEVTAIIGPSGSGKSTLlrcLNLLER---PDDGIIEIgDAkLNAASYSRKdvhKLRQQTAMVFQNYNLFk 93
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRvfdPQSGRILI-DG-TDIRTVTRA---SLRRNIAVVFQDAGLF- 421
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  94 NKTALQN------------VTEALITAQ------KKPKKEAEQIGmdllrQVGLEhkadsypitMSGGQQQRIGIARALA 155
Cdd:PRK13657 422 NRSIEDNirvgrpdatdeeMRAAAERAQahdfieRKPDGYDTVVG-----ERGRQ---------LSGGERQRLAIARALL 487
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIvTHEMAFAREvADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKGRTTFII-AHRLSTVRN-ADRILVFDNGRVVESGSFDEL 556
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
16-226 6.00e-31

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


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 120.23  E-value: 6.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkDVHKLRQQTAMVFQNYNLFkNK 95
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIA-----DPAWLRRQMGVVLQENVLF-SR 545
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   96 TALQNVT--------EALITAQKKPKKEAEQIGmdlLRQvGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:TIGR01846 546 SIRDNIAlcnpgapfEHVIHAAKLAGAHDFISE---LPQ-GYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEAT 621
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201  168 SALDPELVAGVLQVIKSIAeKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEEL 226
Cdd:TIGR01846 622 SALDYESEALIMRNMREIC-RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEEL 678
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
16-228 8.16e-31

type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274550 [Multi-domain]  Cd Length: 694  Bit Score: 119.97  E-value: 8.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDakLNAASYSRKDvhkLRQQTAMVFQNYNLFkNK 95
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDG--VDIRQIDPAD---LRRNIGYVPQDPRLF-YG 553
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   96 TALQNVT--------EALITAqkkpkkeAEQIGM-DLLRQ--VGLEHkadsyPIT-----MSGGQQQRIGIARALAVDPH 159
Cdd:TIGR03375 554 TLRDNIAlgapyaddEEILRA-------AELAGVtEFVRRhpDGLDM-----QIGergrsLSGGQRQAVALARALLRDPP 621
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201  160 AILLDEPTSALDPELVAGVLQVIKSIAEKQtTMIIVTHEMAFArEVADKVIFMADGRIIEQGTPEELFD 228
Cdd:TIGR03375 622 ILLLDEPTSAMDNRSEERFKDRLKRWLAGK-TLVLVTHRTSLL-DLVDRIIVMDNGRIVADGPKDQVLE 688
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
12-221 1.19e-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: 112.26  E-value: 1.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  12 KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNllERPDDGIIEiGDAKLNAASYSRKdvhKLRQQTAMVFQNYNL 91
Cdd:cd03213   20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA--GRRTGLGVS-GEVLINGRPLDKR---SFRKIIGYVPQDDIL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  92 FKNKTalqnVTEAL-ITAQkkpkkeaeqigmdlLRQVglehkadsypitmSGGQQQRIGIARALAVDPHAILLDEPTSAL 170
Cdd:cd03213   94 HPTLT----VRETLmFAAK--------------LRGL-------------SGGERKRVSIALELVSNPSLLFLDEPTSGL 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489248201 171 DPELVAGVLQVIKSIAEKQTTMIIVTHE-MAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03213  143 DSSSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
2-221 1.28e-30

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: 112.02  E-value: 1.28e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAF--KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRclnLLER---PDDGIIEIGDAKLNAASYSrkdvh 76
Cdd:cd03247    1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQ---LLTGdlkPQQGEITLDGVPVSDLEKA----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 kLRQQTAMVFQNYNLFkNKTALQNVTEALitaqkkpkkeaeqigmdllrqvglehkadsypitmSGGQQQRIGIARALAV 156
Cdd:cd03247   73 -LSSLISVLNQRPYLF-DTTLRNNLGRRF-----------------------------------SGGERQRLALARILLQ 115
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEKQtTMIIVTHEMAfAREVADKVIFMADGRIIEQG 221
Cdd:cd03247  116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK-TLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
galliderm_ABC TIGR03740
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ...
2-229 1.43e-30

gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.


Pssm-ID: 163452 [Multi-domain]  Cd Length: 223  Bit Score: 113.26  E-value: 1.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIeigdaKLNAASYSRKDVHKLrqq 81
Cdd:TIGR03740   1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEI-----IFDGHPWTRKDLHKI--- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   82 tAMVFQNYNLFKNKTALQNVtEALITAQKKPKKEAEQIgmdlLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:TIGR03740  73 -GSLIESPPLYENLTARENL-KVHTTLLGLPDSRIDEV----LNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLL 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201  162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTP------EELFDN 229
Cdd:TIGR03740 147 ILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKInksenlEKLFVE 220
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
1-230 2.19e-30

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 116.48  E-value: 2.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGD---AKLNAASYSRKdVHK 77
Cdd:PRK09536   3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvEALSARAASRR-VAS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  78 LRQQTAMVFQnynlFKNKTALQnVTEALITAQKKPKKEAEQIGMD-LLRQVGLEHKADSYPITMSGGQQQRIGIARALAV 156
Cdd:PRK09536  82 VPQDTSLSFE----FDVRQVVE-MGRTPHRSRFDTWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQ 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 157 DPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
13-230 2.97e-30

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 118.29  E-value: 2.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTllrCLNLLER---PDDGIIEIGDAKLnaasySRKDVHKLRQQTAMVFQNY 89
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNlyqPTGGQVLLDGVPL-----VQYDHHYLHRQVALVGQEP 564
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   90 NLFkNKTALQNVTEALitaQKKPKKE----AEQIGMDLLRQvGLEHKADS----YPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:TIGR00958 565 VLF-SGSVRENIAYGL---TDTPDEEimaaAKAANAHDFIM-EFPNGYDTevgeKGSQLSGGQKQRIAIARALVRKPRVL 639
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201  162 LLDEPTSALDPElVAGVLQVIKSIAEKqtTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:TIGR00958 640 ILDEATSALDAE-CEQLLQESRSRASR--TVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
9-234 3.84e-30

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 112.68  E-value: 3.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   9 KAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGD---AKLNAASYSRKDVHKLRQQtAMV 85
Cdd:PRK10895  11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDediSLLPLHARARRGIGYLPQE-ASI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  86 FQNYNLFKNKTALQNVTEALITAQKKPKKEaeqigmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDE 165
Cdd:PRK10895  90 FRRLSVYDNLMAVLQIRDDLSAEQREDRAN------ELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 166 PTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNER 234
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
16-225 4.58e-30

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: 117.16  E-value: 4.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaASYSRKDVHK----LRQQTAM----VFQ 87
Cdd:COG4618  347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL--SQWDREELGRhigyLPQDVELfdgtIAE 424
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  88 NYNLFKNKTAlQNVTEALITA------QKKPKKEAEQIGMDLLRqvglehkadsypitMSGGQQQRIGIARALAVDPHAI 161
Cdd:COG4618  425 NIARFGDADP-EKVVAAAKLAgvhemiLRLPDGYDTRIGEGGAR--------------LSGGQRQRIGLARALYGDPRLV 489
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAfAREVADKVIFMADGRIIEQGTPEE 225
Cdd:COG4618  490 VLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
1-230 5.29e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 112.97  E-value: 5.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFK-DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaklNAASYSRKDVHKLR 79
Cdd:PRK13652   3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLI-----RGEPITKENIREVR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQNYN--LFkNKTALQNVTEALITAQKKPKKEAEQIGmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:PRK13652  78 KFVGLVFQNPDdqIF-SPTVEQDIAFGPINLGLDEETVAHRVS-SALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
15-226 1.23e-29

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: 116.46  E-value: 1.23e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRclnLLER---PDDGIIEIGDAKLnaasysrKDV--HKLRQQTAMVFQNY 89
Cdd:COG5265  372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLAR---LLFRfydVTSGRILIDGQDI-------RDVtqASLRAAIGIVPQDT 441
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  90 NLFkNKTALQNV-------TEALITAQKKpkkeAEQIGmDLLRQV--GLEhkadsypiTM--------SGGQQQRIGIAR 152
Cdd:COG5265  442 VLF-NDTIAYNIaygrpdaSEEEVEAAAR----AAQIH-DFIESLpdGYD--------TRvgerglklSGGEKQRVAIAR 507
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMII------VTHemafarevADKVIFMADGRIIEQGTPEEL 226
Cdd:COG5265  508 TLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIahrlstIVD--------ADEILVLEAGRIVERGTHAEL 579
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
11-227 1.34e-29

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 112.02  E-value: 1.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  11 FKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaasYSRKDVHKLRQQTAMVFQN-- 88
Cdd:PRK13638  11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD---YSKRGLLALRQQVATVFQDpe 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  89 ----YNLFKNKTA--LQN--VTEALITaqkKPKKEAeqigMDLLRQVGLEHKadsyPIT-MSGGQQQRIGIARALAVDPH 159
Cdd:PRK13638  88 qqifYTDIDSDIAfsLRNlgVPEAEIT---RRVDEA----LTLVDAQHFRHQ----PIQcLSHGQKKRVAIAGALVLQAR 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELF 227
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
12-226 1.98e-29

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 115.71  E-value: 1.98e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  12 KDLTVL--DG------IDLEIKSGEVTAIIGPSGSGKSTLLrclNLLE--RPDDGIIEIGDAKLNAAsysrkDVHKLRQQ 81
Cdd:PRK11174 353 EDLEILspDGktlagpLNFTLPAGQRIALVGPSGAGKTSLL---NALLgfLPYQGSLKINGIELREL-----DPESWRKH 424
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNkTALQNVTEAlitaqkKPKKEAEQIgMDLLRQV-----------GLEHKADSYPITMSGGQQQRIGI 150
Cdd:PRK11174 425 LSWVGQNPQLPHG-TLRDNVLLG------NPDASDEQL-QQALENAwvseflpllpqGLDTPIGDQAAGLSVGQAQRLAL 496
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 151 ARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREVaDKVIFMADGRIIEQGTPEEL 226
Cdd:PRK11174 497 ARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTT-LMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAEL 570
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
2-228 2.10e-29

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 113.00  E-value: 2.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdvhklRQQ 81
Cdd:PRK13536  42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA------RAR 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNKTALQNVteaLITAQ--KKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPH 159
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENL---LVFGRyfGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFD 228
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
1-248 2.84e-29

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 114.80  E-value: 2.84e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFK----DLTVLDGIDLEIKSGEVTAIIGPSGSGKS-TLLRCLNLLERPDdGIIEIGDAKLNAASYSRKDV 75
Cdd:PRK15134   5 LLAIENLSVAFRqqqtVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPP-VVYPSGDIRFHGESLLHASE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  76 HKLRQ----QTAMVFQNYNLFKNktALQNVTEAL---ITAQKKPKKEAEQIGM-DLLRQVGLEHKA---DSYPITMSGGQ 144
Cdd:PRK15134  84 QTLRGvrgnKIAMIFQEPMVSLN--PLHTLEKQLyevLSLHRGMRREAARGEIlNCLDRVGIRQAAkrlTDYPHQLSGGE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 145 QQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTP 223
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRA 241
                        250       260
                 ....*....|....*....|....*..
gi 489248201 224 EELFDNPQNERTKKFI--KQVGEPAEL 248
Cdd:PRK15134 242 ATLFSAPTHPYTQKLLnsEPSGDPVPL 268
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
15-242 4.55e-29

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 114.76  E-value: 4.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPddGIIEIGDAKLNAasySRKDVHKLRQQTAMVFQNYNLFKN 94
Cdd:TIGR00955  39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLLNG---MPIDAKEMRAISAYVQQDDLFIPT 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   95 KTALqnvtEALI-TAQKK-----PKKEAEQIGMDLLRQVGLEHKADS---YPITM---SGGQQQRIGIARALAVDPHAIL 162
Cdd:TIGR00955 114 LTVR----EHLMfQAHLRmprrvTKKEKRERVDEVLQALGLRKCANTrigVPGRVkglSGGERKRLAFASELLTDPPLLF 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  163 LDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHE-MAFAREVADKVIFMADGRIIEQGTPEEL---FDN-----PQNE 233
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAvpfFSDlghpcPENY 269

                  ....*....
gi 489248201  234 RTKKFIKQV 242
Cdd:TIGR00955 270 NPADFYVQV 278
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
1-230 6.02e-29

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 111.35  E-value: 6.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFK----DLTVLDGIDLEIKSGEVTAIIGPSGSGKS-TLLRCLNLLERpdDGIIEiGDAKLNAA---SYSR 72
Cdd:PRK09473  12 LLDVKDLRVTFStpdgDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAA--NGRIG-GSATFNGReilNLPE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  73 KDVHKLR-QQTAMVFQNynlfkNKTAL-------QNVTEALITAQKKPKKEA--EQIGM-DLLRQVGLEHKADSYPITMS 141
Cdd:PRK09473  89 KELNKLRaEQISMIFQD-----PMTSLnpymrvgEQLMEVLMLHKGMSKAEAfeESVRMlDAVKMPEARKRMKMYPHEFS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 142 GGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQ 220
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 243
                        250
                 ....*....|
gi 489248201 221 GTPEELFDNP 230
Cdd:PRK09473 244 GNARDVFYQP 253
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
1-239 1.77e-28

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 108.72  E-value: 1.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVL---------DGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYS 71
Cdd:PRK15112   4 LLEVRNLSKTFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  72 RKDvhklrQQTAMVFQNynlfkNKTAL---QNVTEAL-----ITAQKKPKKEAEQIgMDLLRQVGL--EHkADSYPITMS 141
Cdd:PRK15112  84 YRS-----QRIRMIFQD-----PSTSLnprQRISQILdfplrLNTDLEPEQREKQI-IETLRQVGLlpDH-ASYYPHMLA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 142 GGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIEQ 220
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
                        250
                 ....*....|....*....
gi 489248201 221 GTPEELFDNPQNERTKKFI 239
Cdd:PRK15112 232 GSTADVLASPLHELTKRLI 250
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1-218 2.19e-28

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 108.25  E-value: 2.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTV-----LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDV 75
Cdd:COG1101    1 MLELKNLSKTFNPGTVnekraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-----TKLPE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  76 HKLRQQTAMVFQN------YNLfknkTALQNvteaLITAQKKPKKEAEQIGM---------DLLRQV--GLEHKADSyPI 138
Cdd:COG1101   76 YKRAKYIGRVFQDpmmgtaPSM----TIEEN----LALAYRRGKRRGLRRGLtkkrrelfrELLATLglGLENRLDT-KV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 139 -TMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:COG1101  147 gLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226

                 ..
gi 489248201 217 II 218
Cdd:COG1101  227 II 228
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
10-210 2.56e-28

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 106.16  E-value: 2.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  10 AFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVHK-----LRQQTAM 84
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDslpltVRDLVAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  85 -VFQNYNLFKNKTAL--QNVTEALitaqkkpkkeaEQIGMDLL--RQVGlehkadsypiTMSGGQQQRIGIARALAVDPH 159
Cdd:NF040873  81 gRWARRGLWRRLTRDdrAAVDDAL-----------ERVGLADLagRQLG----------ELSGGQRQRALLAQGLAQEAD 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREvADKVI 210
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCV 189
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
1-220 2.72e-28

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 107.17  E-value: 2.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAF----KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLerpDDGiiEIGDAKLNAASYSRKDVH 76
Cdd:PRK10584   6 IVEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGL---DDG--SSGEVSLVGQPLHQMDEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 ---KLR-QQTAMVFQNYNLFKNKTALQNVT-EALITAQKKpkKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIA 151
Cdd:PRK10584  81 araKLRaKHVGFVFQSFMLIPTLNALENVElPALLRGESS--RQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 152 RALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREvADKVIFMADGRIIEQ 220
Cdd:PRK10584 159 RAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1-219 4.96e-28

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 111.31  E-value: 4.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaKLNAASYSrkdvhklrQ 80
Cdd:COG0488  315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE-TVKIGYFD--------Q 385
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAmvfqnyNLFKNKTALQNVTEAlitAQKKPKKEAEQI-------GMDLLRQVGlehkadsypiTMSGGQQQRIGIARA 153
Cdd:COG0488  386 HQE------ELDPDKTVLDELRDG---APGGTEQEVRGYlgrflfsGDDAFKPVG----------VLSGGEKARLALAKL 446
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 154 LAVDPHAILLDEPTSALDPElvagVLQVIKS-IAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIE 219
Cdd:COG0488  447 LLSPPNVLLLDEPTNHLDIE----TLEALEEaLDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
cbiO PRK13642
energy-coupling factor transporter ATPase;
13-232 6.44e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 107.49  E-value: 6.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasysrKDVHKLRQQTAMVFQNY-NL 91
Cdd:PRK13642  19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA-----ENVWNLRRKIGMVFQNPdNQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  92 FKNKTALQNVTEALiTAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD 171
Cdd:PRK13642  94 FVGATVEDDVAFGM-ENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489248201 172 PELVAGVLQVIKSIAEK-QTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFDNPQN 232
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
15-226 1.41e-27

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


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 110.13  E-value: 1.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaaSYSRKDVHK----LRQQTAM----VF 86
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK--QWDRETFGKhigyLPQDVELfpgtVA 409
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   87 QNYNLFKNKTALQNVTEALITAQKKpkkeaEQIgmdllrqVGLEHKADSY----PITMSGGQQQRIGIARALAVDPHAIL 162
Cdd:TIGR01842 410 ENIARFGENADPEKIIEAAKLAGVH-----ELI-------LRLPDGYDTVigpgGATLSGGQRQRIALARALYGDPKLVV 477
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201  163 LDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAfAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEV 540
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1-229 3.08e-27

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 108.98  E-value: 3.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdVHKLrq 80
Cdd:PRK15439  11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK--AHQL-- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEqigmdLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:PRK15439  87 GIYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQ-----LLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDN 229
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
15-226 1.18e-26

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 103.91  E-value: 1.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNaaSYSRKDVHKlrqQTAMVFQNYNLFKN 94
Cdd:PRK10253  21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ--HYASKEVAR---RIGLLAQNATTPGD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  95 KTALQNVTEALITAQ---KKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD 171
Cdd:PRK10253  96 ITVQELVARGRYPHQplfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 172 PELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK10253 176 ISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
2-226 2.77e-26

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 106.64  E-value: 2.77e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAF--KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLrclNLLERPDDgiIEIGDAKLNAASYSRKDVHKLR 79
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIA---NLLTRFYD--IDEGEILLDGHDLRDYTLASLR 416
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTAMVFQNYNLFkNKTALQNVTEAlitaqKKPKKEAEQI--------GMDLLRQvgLEHKADSY----PITMSGGQQQR 147
Cdd:PRK11176 417 NQVALVSQNVHLF-NDTIANNIAYA-----RTEQYSREQIeeaarmayAMDFINK--MDNGLDTVigenGVLLSGGQRQR 488
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 148 IGIARALAVDPHAILLDEPTSALDPElVAGVLQVIKSIAEKQTTMIIVTHEMAfAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTE-SERAIQAALDELQKNRTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAEL 565
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
1-242 4.38e-26

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 106.09  E-value: 4.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKD----LTVLDGIDLEIKSGEVTAIIGPSGSGKS----TLLRCLN-----------LLERPDDGIIEIG 61
Cdd:PRK10261  12 VLAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEqagglvqcdkmLLRRRSRQVIELS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  62 DaklnaasYSRKDVHKLR-QQTAMVFQNYNLFKNK--TALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL-EHKA--DS 135
Cdd:PRK10261  92 E-------QSAAQMRHVRgADMAMIFQEPMTSLNPvfTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIpEAQTilSR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 136 YPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKsIAEKQTTM--IIVTHEMAFAREVADKVIFMA 213
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIK-VLQKEMSMgvIFITHDMGVVAEIADRVLVMY 243
                        250       260
                 ....*....|....*....|....*....
gi 489248201 214 DGRIIEQGTPEELFDNPQNERTKKFIKQV 242
Cdd:PRK10261 244 QGEAVETGSVEQIFHAPQHPYTRALLAAV 272
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
16-228 5.27e-26

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


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 105.98  E-value: 5.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEigdakLNAASYSRKDVHKLRQQTAMVFQNYNLF--- 92
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIL-----LNGFSLKDIDRHTLRQFINYLPQEPYIFsgs 563
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   93 ---------KNKTALQNVTEALITAQKKpkKEAEQIgmdllrQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILL 163
Cdd:TIGR01193 564 ilenlllgaKENVSQDEIWAACEIAEIK--DDIENM------PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLIL 635
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201  164 DEPTSALDPELVAGVLQVIKSIAEKqtTMIIVTHEMAFAREVaDKVIFMADGRIIEQGTPEELFD 228
Cdd:TIGR01193 636 DESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLD 697
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
13-217 6.24e-26

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: 101.01  E-value: 6.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTllrCLNLLER---PDDGIIEIGDAKLNAasYSRKDVHKlrqQTAMVFQNY 89
Cdd:cd03248   26 DTLVLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENfyqPQGGQVLLDGKPISQ--YEHKYLHS---KVSLVGQEP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  90 NLFkNKTALQNVTEALITAQKKPKKEAEQI----GMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDE 165
Cdd:cd03248   98 VLF-ARSLQDNIAYGLQSCSFECVKEAAQKahahSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDE 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489248201 166 PTSALDPELVAGVLQVIKSIAEKQTTMIIvTHEMAFArEVADKVIFMADGRI 217
Cdd:cd03248  177 ATSALDAESEQQVQQALYDWPERRTVLVI-AHRLSTV-ERADQILVLDGGRI 226
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
2-216 8.03e-26

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: 98.29  E-value: 8.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGdaklnaasySRKDVHKLRQq 81
Cdd:cd03221    1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------STVKIGYFEQ- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 tamvfqnynlfknktalqnvtealitaqkkpkkeaeqigmdllrqvglehkadsypitMSGGQQQRIGIARALAVDPHAI 161
Cdd:cd03221   71 ----------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 162 LLDEPTSALDPElvaGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:cd03221   93 LLDEPTNHLDLE---SIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
16-197 8.54e-26

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: 105.14  E-value: 8.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIeigdaKLNAASYSRKDVHKLRQQTAMVFQNYNLFkNK 95
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV-----TLDGVPVSSLDQDEVRRRVSVCAQDAHLF-DT 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   96 TALQNVteaLITAQKKPKKEAeqigMDLLRQVGLEHKADSYP-----------ITMSGGQQQRIGIARALAVDPHAILLD 164
Cdd:TIGR02868 424 TVRENL---RLARPDATDEEL----WAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLD 496
                         170       180       190
                  ....*....|....*....|....*....|...
gi 489248201  165 EPTSALDPELVAGVLQVIKSiAEKQTTMIIVTH 197
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
1-225 1.15e-25

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 100.54  E-value: 1.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFK----------------------DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGII 58
Cdd:COG1134    4 MIEVENVSKSYRlyhepsrslkelllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  59 EIgdaklnaasysRKDVhklrqqTAMV-----FQNyNLfknkTALQNVTeaLI-TAQKKPKKEAEQigmdLLRQV----G 128
Cdd:COG1134   84 EV-----------NGRV------SALLelgagFHP-EL----TGRENIY--LNgRLLGLSRKEIDE----KFDEIvefaE 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 129 LEHKADSyPI-TMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVAD 207
Cdd:COG1134  136 LGDFIDQ-PVkTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCD 214
                        250
                 ....*....|....*...
gi 489248201 208 KVIFMADGRIIEQGTPEE 225
Cdd:COG1134  215 RAIWLEKGRLVMDGDPEE 232
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
12-242 1.89e-25

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 104.55  E-value: 1.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  12 KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdVHKLRQQTAMVFQN--Y 89
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGK--LQALRRDIQFIFQDpyA 412
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  90 NLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGL--EHkADSYPITMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:PRK10261 413 SLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlpEH-AWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 168 SALDPELVAgvlQVIKSIAEKQTTM----IIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKKFIKQV 242
Cdd:PRK10261 492 SALDVSIRG---QIINLLLDLQRDFgiayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
12-224 3.24e-25

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 99.37  E-value: 3.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  12 KDLTV-------LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLnlLERPDDGIIEiGDAKLNAASYSRKDVHKlRQQT-- 82
Cdd:COG0396    4 KNLHVsvegkeiLKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MGHPKYEVTS-GSILLDGEDILELSPDE-RARAgi 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  83 AMVFQ---------NYNLFKnkTALQNVTEALITAQ---KKPKKEAEQIGMD---LLRQV--GLehkadsypitmSGGQQ 145
Cdd:COG0396   80 FLAFQypveipgvsVSNFLR--TALNARRGEELSAReflKLLKEKMKELGLDedfLDRYVneGF-----------SGGEK 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 146 QRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREV-ADKVIFMADGRIIEQGTPE 224
Cdd:COG0396  147 KRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIkPDFVHVLVDGRIVKSGGKE 226
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
4-218 6.97e-25

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 102.45  E-value: 6.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   4 VRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaklnaasysRKDVhklrqQTA 83
Cdd:COG0488    1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-----------PKGL-----RIG 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  84 MVFQNYNLFKNKTALQNVTEAL--ITAQKKPKKEAEQ----IGMDLLRQVGLEHK---ADSY------------------ 136
Cdd:COG0488   65 YLPQEPPLDDDLTVLDTVLDGDaeLRALEAELEELEAklaePDEDLERLAELQEEfeaLGGWeaearaeeilsglgfpee 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 137 ----PI-TMSGGQQQRIGIARALAVDPHAILLDEPTSALDpelvagvlqvIKSIA--EK-----QTTMIIVTHEMAFARE 204
Cdd:COG0488  145 dldrPVsELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----------LESIEwlEEflknyPGTVLVVSHDRYFLDR 214
                        250
                 ....*....|....
gi 489248201 205 VADKVIFMADGRII 218
Cdd:COG0488  215 VATRILELDRGKLT 228
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
11-223 7.96e-25

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: 97.95  E-value: 7.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  11 FKDLT---------VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKLRQQ 81
Cdd:cd03244    5 FKNVSlryrpnlppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI-----SKIGLHDLRSR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLF-----KNKTALQNVTE-----ALITAQKKPKKEAEQIGMDLLRQVGLEHkadsypitMSGGQQQRIGIA 151
Cdd:cd03244   80 ISIIPQDPVLFsgtirSNLDPFGEYSDeelwqALERVGLKEFVESLPGGLDTVVEEGGEN--------LSVGQRQLLCLA 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 152 RALAVDPHAILLDEPTSALDPELVAGVLQVIKSiAEKQTTMIIVTHE----MAFarevaDKVIFMADGRIIEQGTP 223
Cdd:cd03244  152 RALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRldtiIDS-----DRILVLDKGRVVEFDSP 221
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
10-197 1.20e-24

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 101.81  E-value: 1.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  10 AFKDLTV--------LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLL--------ERPDDGiieigdaklnaasysrk 73
Cdd:COG4178  364 ALEDLTLrtpdgrplLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwpygsgriARPAGA----------------- 426
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  74 dvhklrqqtAMVF---QNYnlfknktaLQNVT--EALI---TAQKKPKKEAEQIgmdlLRQVGLEHKADSY------PIT 139
Cdd:COG4178  427 ---------RVLFlpqRPY--------LPLGTlrEALLypaTAEAFSDAELREA----LEAVGLGHLAERLdeeadwDQV 485
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 140 MSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSiAEKQTTMIIVTH 197
Cdd:COG4178  486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
20-231 3.92e-24

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 98.79  E-value: 3.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasySRKDV----HKLRqqTAMVFQNYNLFKNK 95
Cdd:PRK11144  17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFD---AEKGIclppEKRR--IGYVFQDARLFPHY 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  96 TALQNVTEALitaQKKPKKEAEQIgMDLLrqvGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD-P-- 172
Cdd:PRK11144  92 KVRGNLRYGM---AKSMVAQFDKI-VALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPrk 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 173 -ELvagvLQVIKSIAEK-QTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:PRK11144 165 rEL----LPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
16-216 1.98e-23

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


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 93.69  E-value: 1.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLnllerpddgiieIGDAKLNAASYSrkdVHKlrqQTAMVFQNYNLFkNK 95
Cdd:cd03250   20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL------------LGELEKLSGSVS---VPG---SIAYVSQEPWIQ-NG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  96 TALQNVT----------EALITA-------QKKPKKEAEQIGmdllrQVGlehkadsypITMSGGQQQRIGIARALAVDP 158
Cdd:cd03250   81 TIRENILfgkpfdeeryEKVIKAcalepdlEILPDGDLTEIG-----EKG---------INLSGGQKQRISLARAVYSDA 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 159 HAILLDEPTSALDPELVAGVLQ-VIKSIAEKQTTMIIVTHEMAFAREvADKVIFMADGR 216
Cdd:cd03250  147 DIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
17-232 5.90e-23

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 93.75  E-value: 5.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL-NLLerPDDGIIEIGDAKLNAASYSRKDVHK--LRQQT----AM-VFQN 88
Cdd:COG4138   12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILLNGRPLSDWSAAELARHRayLSQQQsppfAMpVFQY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  89 YNLFKNKTALQNVTEALItaqkkpkkeaeqigMDLLRQVGLEHKADSyPIT-MSGGQQQRIGIARAL-----AVDPHA-- 160
Cdd:COG4138   90 LALHQPAGASSEAVEQLL--------------AQLAEALGLEDKLSR-PLTqLSGGEWQRVRLAAVLlqvwpTINPEGql 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDnPQN 232
Cdd:COG4138  155 LLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT-PEN 225
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1-215 7.05e-23

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 96.78  E-value: 7.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaklNAASYSRKDvHKLRQ 80
Cdd:PRK09700   5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI-----NNINYNKLD-HKLAA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 Q--TAMVFQNYNLFKNKTALQNV------TEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIAR 152
Cdd:PRK09700  79 QlgIGIIYQELSVIDELTVLENLyigrhlTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 153 ALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADG 215
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
14-197 1.11e-22

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: 91.65  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   14 LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDV-HKLRQQTAMvfqnynlf 92
Cdd:TIGR01189  13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENiLYLGHLPGL-------- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   93 KNK-TALQNVT---EALITAQKKPKkeaeqigmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTS 168
Cdd:TIGR01189  85 KPElSALENLHfwaAIHGGAQRTIE--------DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
                         170       180
                  ....*....|....*....|....*....
gi 489248201  169 ALDPELVAGVLQVIKSIAEKQTTMIIVTH 197
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLLTTH 185
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
1-218 1.34e-22

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: 96.05  E-value: 1.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLeRPD---DGIIEIGDAKLNAASYSRKDvhk 77
Cdd:TIGR02633   1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASNIRDTE--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   78 lRQQTAMVFQNYNLFKNKTALQNV---TEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPIT-MSGGQQQRIGIARA 153
Cdd:TIGR02633  77 -RAGIVIIHQELTLVPELSVAENIflgNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKA 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201  154 LAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRII 218
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
2-224 2.34e-21

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: 88.35  E-value: 2.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL--NLLERPDDGIIEIGDAKLNAAS-YSRKdvhkl 78
Cdd:cd03217    1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPpEERA----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  79 RQQTAMVFQNynlfknKTALQNVTEalitaqkkpkkeaeqigMDLLRQVGLehkadsypiTMSGGQQQRIGIARALAVDP 158
Cdd:cd03217   76 RLGIFLAFQY------PPEIPGVKN-----------------ADFLRYVNE---------GFSGGEKKRNEILQLLLLEP 123
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTH-EMAFAREVADKVIFMADGRIIEQGTPE 224
Cdd:cd03217  124 DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDKE 190
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1-218 2.66e-21

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 92.30  E-value: 2.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLeRPD---DGIIEIGDAKLNAASYsrKDVHk 77
Cdd:PRK13549   5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNI--RDTE- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  78 lRQQTAMVFQNYNLFKNKTALQNV------TEALITAQKKPKKEAEQigmdLLRQVGLEHKADSYPITMSGGQQQRIGIA 151
Cdd:PRK13549  81 -RAGIAIIHQELALVKELSVLENIflgneiTPGGIMDYDAMYLRAQK----LLAQLKLDINPATPVGNLGLGQQQLVEIA 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 152 RALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRII 218
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
12-221 2.91e-21

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: 88.36  E-value: 2.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  12 KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaklnaasysrkdvhkLRQQTAMVFQNYNL 91
Cdd:cd03220   33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-----------------RGRVSSLLGLGGGF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  92 FKNKTALQNVT-EALI---TAQKKPKKEAE-----QIGMDLLRQVGlehkadsypiTMSGGQQQRIGIARALAVDPHAIL 162
Cdd:cd03220   96 NPELTGRENIYlNGRLlglSRKEIDEKIDEiiefsELGDFIDLPVK----------TYSSGMKARLAFAIATALEPDILL 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 163 LDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03220  166 IDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
17-223 3.16e-21

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: 92.38  E-value: 3.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasysrkDVHKLRQQTAMVFQNYNLFKNKT 96
Cdd:TIGR01257  946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET------NLDAVRQSLGMCPQHNILFHHLT 1019
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    97 ALQNVteaLITAQKKPKKEAE-QIGMD-LLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPEL 174
Cdd:TIGR01257 1020 VAEHI---LFYAQLKGRSWEEaQLEMEaMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 489248201   175 VAGVLQVIKSIAEKQtTMIIVTHEMAFAREVADKVIFMADGRIIEQGTP 223
Cdd:TIGR01257 1097 RRSIWDLLLKYRSGR-TIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
15-226 3.40e-21

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 89.46  E-value: 3.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGD---AKLNAASYSRKdVHKLRQQTAmvfqnynl 91
Cdd:PRK10575  25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqplESWSSKAFARK-VAYLPQQLP-------- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  92 fknktALQNVT-EALITAQKKP-------------KKEAEQIGMdllrqVGLEHKADSYPITMSGGQQQRIGIARALAVD 157
Cdd:PRK10575  96 -----AAEGMTvRELVAIGRYPwhgalgrfgaadrEKVEEAISL-----VGLKPLAHRLVDSLSGGERQRAWIAMLVAQD 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
2-230 1.42e-20

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 90.16  E-value: 1.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLrclNLLERPDDgiIEIGDAKLNAASYSRKDVHKLRQQ 81
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLL---SLIQRHFD--VSEGDIRFHDIPLTKLQLDSWRSR 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYNLFKNKTAlQNVtealitAQKKPKKEAEQIGM---------DLLR-QVGLEHKADSYPITMSGGQQQRIGIA 151
Cdd:PRK10789 391 LAVVSQTPFLFSDTVA-NNI------ALGRPDATQQEIEHvarlasvhdDILRlPQGYDTEVGERGVMLSGGQKQRISIA 463
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 152 RALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQtTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFDNP 230
Cdd:PRK10789 464 RALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGR-TVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
hmuV PRK13547
heme ABC transporter ATP-binding protein;
1-238 1.53e-20

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 87.57  E-value: 1.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL--NLLE-RPDDGIIEIGDAKLNAASYSRKDVHK 77
Cdd:PRK13547   1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGgGAPRGARVTGDVTLNGEPLAAIDAPR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  78 LRQQTAMVFQnynlfKNKTALQNVTEALITAQKKPkkEAEQIGMDLLRQVGLE----HKADSYPI------TMSGGQQQR 147
Cdd:PRK13547  81 LARLRAVLPQ-----AAQPAFAFSAREIVLLGRYP--HARRAGALTHRDGEIAwqalALAGATALvgrdvtTLSGGELAR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 148 IGIARALA---------VDPHAILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:PRK13547 154 VQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLArDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
                        250       260
                 ....*....|....*....|.
gi 489248201 218 IEQGTPEELFDNPQNERTKKF 238
Cdd:PRK13547 234 VAHGAPADVLTPAHIARCYGF 254
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
4-221 1.61e-20

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: 87.00  E-value: 1.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   4 VRHI-RKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDaklnAASYSRKDVHkLRQQT 82
Cdd:cd03267   23 LKSLfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKKF-LRRIG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  83 AMVFQNYNLFKNKTALQnvTEALITA--QKKPKKEAEQIG--MDLLRqvgLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:cd03267   98 VVFGQKTQLWWDLPVID--SFYLLAAiyDLPPARFKKRLDelSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03267  173 EILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
5-249 3.07e-20

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 89.02  E-value: 3.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   5 RHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSrkdvHKLRQQTAM 84
Cdd:PRK10982   2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSK----EALENGISM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  85 VFQNYNLFKNKTALQNV------TEALITAQKKPKKEAEQIGMDLLRQVGLEHKAdsypITMSGGQQQRIGIARALAVDP 158
Cdd:PRK10982  78 VHQELNLVLQRSVMDNMwlgrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKV----ATLSVSQMQMIEIAKAFSYNA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELfDNPQ------- 231
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL-TMDKiiammvg 232
                        250
                 ....*....|....*...
gi 489248201 232 NERTKKFIKQVGEPAELV 249
Cdd:PRK10982 233 RSLTQRFPDKENKPGEVI 250
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
12-217 4.29e-20

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: 84.41  E-value: 4.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  12 KDLTV---LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaklNAASYSRKDVHKLRQQtAMVFqn 88
Cdd:cd03215    8 RGLSVkgaVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITL-----DGKPVTRRSPRDAIRA-GIAY-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  89 ynlfknktalqnVTEalitaqkKPKKEAEQIGMDLLRQVGLehkadsyPITMSGGQQQRIGIARALAVDPHAILLDEPTS 168
Cdd:cd03215   80 ------------VPE-------DRKREGLVLDLSVAENIAL-------SSLLSGGNQQKVVLARWLARDPRVLILDEPTR 133
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489248201 169 ALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:cd03215  134 GVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
12-187 7.56e-20

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: 83.83  E-value: 7.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  12 KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNllERPDDGIIEiGDAKLNAasysRKDVHKLRQQTAMVFQNYNL 91
Cdd:cd03232   18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGVIT-GEILING----RPLDKNFQRSTGYVEQQDVH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  92 FKNKTalqnVTEAL-ITAqkkpkkeaeqigmdLLRQVGLEHKadsypitmsggqqQRIGIARALAVDPHAILLDEPTSAL 170
Cdd:cd03232   91 SPNLT----VREALrFSA--------------LLRGLSVEQR-------------KRLTIGVELAAKPSILFLDEPTSGL 139
                        170
                 ....*....|....*..
gi 489248201 171 DPELVAGVLQVIKSIAE 187
Cdd:cd03232  140 DSQAAYNIVRFLKKLAD 156
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
1-210 7.97e-20

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 84.77  E-value: 7.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdvhkLRQ 80
Cdd:PRK10247   7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI-----YRQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFkNKTALQNVteaLITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPIT-MSGGQQQRIGIARALAVDPH 159
Cdd:PRK10247  82 QVSYCAQTPTLF-GDTVYDNL---IFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPK 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489248201 160 AILLDEPTSALDPELVAGVLQVIKSIA-EKQTTMIIVTHEmafAREV--ADKVI 210
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHD---KDEInhADKVI 208
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-229 1.86e-19

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 84.16  E-value: 1.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKdvhkLRQ 80
Cdd:PRK11614   5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI----MRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQvgLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:PRK11614  81 AVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDN 229
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
15-197 2.58e-19

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 83.47  E-value: 2.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL--NLLERPDDGIIEIGDAKLNaasysrkdvhklrqqtamvfqnynlf 92
Cdd:COG2401   44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFG-------------------------- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  93 KNKTALQNVtealitAQKKPKKEAeqigMDLLRQVGLehkADSY-----PITMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:COG2401   98 REASLIDAI------GRKGDFKDA----VELLNAVGL---SDAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
                        170       180       190
                 ....*....|....*....|....*....|...
gi 489248201 168 SALDPEL---VAGVLQviKSIAEKQTTMIIVTH 197
Cdd:COG2401  165 SHLDRQTakrVARNLQ--KLARRAGITLVVATH 195
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
13-197 8.67e-19

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 81.46  E-value: 8.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYsRKDVHKLRQQTAMvfqnynlf 92
Cdd:PRK13539  14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV-AEACHYLGHRNAM-------- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  93 knKTALqNVTEALITAQKKPKKEAEQIgMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDP 172
Cdd:PRK13539  85 --KPAL-TVAENLEFWAAFLGGEELDI-AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
                        170       180
                 ....*....|....*....|....*
gi 489248201 173 ELVAGVLQVIKSIAEKQTTMIIVTH 197
Cdd:PRK13539 161 AAVALFAELIRAHLAQGGIVIAATH 185
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1-235 9.49e-19

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 83.60  E-value: 9.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRK-------------AFKDL--------TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIE 59
Cdd:COG4586    1 IIEVENLSKtyrvyekepglkgALKGLfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  60 IgdaklnaASYS-RKDVHKLRQQTAMVF-------------QNYNLFKnktALQNVtealitaqkkPKKEAEQIgMDLLR 125
Cdd:COG4586   81 V-------LGYVpFKRRKEFARRIGVVFgqrsqlwwdlpaiDSFRLLK---AIYRI----------PDAEYKKR-LDELV 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 126 QV-GLEHKADSyPI-TMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSI-AEKQTTMIIVTHEMAFA 202
Cdd:COG4586  140 ELlDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDI 218
                        250       260       270
                 ....*....|....*....|....*....|...
gi 489248201 203 REVADKVIFMADGRIIEQGTPEELFDNPQNERT 235
Cdd:COG4586  219 EALCDRVIVIDHGRIIYDGSLEELKERFGPYKT 251
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
13-215 1.55e-18

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: 81.22  E-value: 1.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRKDVHKlRQQTAMVFQNYNLF 92
Cdd:cd03290   13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRN-RYSVAYAAQKPWLL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  93 kNKTALQNVTEALITAQKKPKKEAE----QIGMDLLrQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTS 168
Cdd:cd03290   92 -NATVEENITFGSPFNKQRYKAVTDacslQPDIDLL-PFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489248201 169 ALDPELVAGVLQ--VIKSIAEKQTTMIIVTHEMAFAREvADKVIFMADG 215
Cdd:cd03290  170 ALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
2-227 2.02e-18

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 84.00  E-value: 2.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAF-KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSrkdvhKLRQ 80
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS-----VLRQ 415
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQN-----YNLFKNKTALQNVTEALITAqkkpKKEAEQIGmDLLRQV--GLEHKADSYPITMSGGQQQRIGIARA 153
Cdd:PRK10790 416 GVAMVQQDpvvlaDTFLANVTLGRDISEEQVWQ----ALETVQLA-ELARSLpdGLYTPLGEQGNNLSVGQKQLLALARV 490
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 154 LAVDPHAILLDEPTSALDpelvAGVLQVIK---SIAEKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELF 227
Cdd:PRK10790 491 LVQTPQILILDEATANID----SGTEQAIQqalAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
23-243 2.70e-18

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: 80.92  E-value: 2.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  23 EIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaKLNAASYSRKDVhklrqqtamvfqnynlfknkTALQNVT 102
Cdd:cd03237   21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI---ELDTVSYKPQYI--------------------KADYEGT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 103 -EALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQV 181
Cdd:cd03237   78 vRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 182 IKSIAEK-QTTMIIVTHEMAFAREVADKVIFMaDGRIIEQGTPeelfDNPQNERT--KKFIKQVG 243
Cdd:cd03237  158 IRRFAENnEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGVA----NPPQSLRSgmNRFLKNLD 217
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
16-240 3.40e-18

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 82.26  E-value: 3.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRC-LNLLerPDDGII-----EIGDAKLNAASYS-RKDVhkLRQQTAMVFQN 88
Cdd:COG4170   22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAiCGIT--KDNWHVtadrfRWNGIDLLKLSPReRRKI--IGREIAMIFQE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  89 YN--LFKNKTALQNVTEALITAQKKPK-----KEAEQIGMDLLRQVGL-EHKA--DSYPITMSGGQQQRIGIARALAVDP 158
Cdd:COG4170   98 PSscLDPSAKIGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIkDHKDimNSYPHELTEGECQKVMIAMAIANQP 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDNPQNERTKK 237
Cdd:COG4170  178 RLLIADEPTNAMESTTQAQIFRLLARLNQLQgTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKA 257

                 ...
gi 489248201 238 FIK 240
Cdd:COG4170  258 LLR 260
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
18-202 3.91e-18

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 79.85  E-value: 3.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  18 DGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIeigdaklnaaSYSRKDVHKLRQQtamvFqNYNLF----- 92
Cdd:PRK13538  18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV----------LWQGEPIRRQRDE----Y-HQDLLylghq 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  93 ---KNK-TALQNvteaLITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARaLAVDPHAI-LLDEPT 167
Cdd:PRK13538  83 pgiKTElTALEN----LRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALAR-LWLTRAPLwILDEPF 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489248201 168 SALDpelVAGVLQVIKSIAE--KQTTMIIVT--HEMAFA 202
Cdd:PRK13538 158 TAID---KQGVARLEALLAQhaEQGGMVILTthQDLPVA 193
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
12-224 1.13e-17

FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273907 [Multi-domain]  Cd Length: 243  Bit Score: 79.23  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   12 KDLTV-------LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLnlLERPD----DGIIEIGDAKLNAAS---YSRKDVHk 77
Cdd:TIGR01978   4 KDLHVsvedkeiLKGVNLTVKKGEIHAIMGPNGSGKSTLSKTI--AGHPSyevtSGTILFKGQDLLELEpdeRARAGLF- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   78 lrqqtaMVFQN-------YNLFKNKTALQNVTEAlitAQKKPKKEAE-----QIGMDLLRQVGlEHKADSYPITMSGGQQ 145
Cdd:TIGR01978  81 ------LAFQYpeeipgvSNLEFLRSALNARRSA---RGEEPLDLLDfekllKEKLALLDMDE-EFLNRSVNEGFSGGEK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  146 QRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVA-DKVIFMADGRIIEQGTPE 224
Cdd:TIGR01978 151 KRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKpDYVHVLLDGRIVKSGDVE 230
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
5-219 1.29e-17

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 81.50  E-value: 1.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   5 RHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASysrkDVHKLRQQTAM 84
Cdd:PRK11288   8 DGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAS----TTAALAAGVAI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  85 VFQNYNLFKNKTALQNV------TEALITAQKKPKKEA----EQIGMDLLRQVGLEHkadsypitMSGGQQQRIGIARAL 154
Cdd:PRK11288  84 IYQELHLVPEMTVAENLylgqlpHKGGIVNRRLLNYEAreqlEHLGVDIDPDTPLKY--------LSIGQRQMVEIAKAL 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 155 AVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIE 219
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
23-225 1.41e-17

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 79.21  E-value: 1.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  23 EIKSGEVTAIIGPSGSGKSTLLRCL-NLLerPDDGIIEIGDAKLNAASYSRKDVHK--LRQQ----TAM-VFQNYNLFK- 93
Cdd:PRK03695  18 EVRAGEILHLVGPNGAGKSTLLARMaGLL--PGSGSIQFAGQPLEAWSAAELARHRayLSQQqtppFAMpVFQYLTLHQp 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  94 NKTALQNVTEALitaqkkpkkeaeqigMDLLRQVGLEHKADSYPITMSGGQQQRIGIARAL-----AVDPHA--ILLDEP 166
Cdd:PRK03695  96 DKTRTEAVASAL---------------NEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAGqlLLLDEP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 167 TSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEE 225
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
12-226 5.22e-17

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 79.68  E-value: 5.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  12 KDLTV---LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSrkdvHKLRQQTAMVFQN 88
Cdd:COG1129  260 EGLSVggvVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPR----DAIRAGIAYVPED 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  89 ---YNLFKNKTALQNVTealITAQKK--------PKKEAEQIGmDLLRQVGLehKADS--YPI-TMSGGQQQRIGIARAL 154
Cdd:COG1129  336 rkgEGLVLDLSIRENIT---LASLDRlsrgglldRRRERALAE-EYIKRLRI--KTPSpeQPVgNLSGGNQQKVVLAKWL 409
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 155 AVDPHAILLDEPTSALDpelV---AGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:COG1129  410 ATDPKVLILDEPTRGID---VgakAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
PLN03232 PLN03232
ABC transporter C family member; Provisional
17-244 6.87e-17

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 79.63  E-value: 6.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLrclnllerpddgiieigDAKLNAASYSRKDVHKLRQQTAMVFQNYNLFkNKT 96
Cdd:PLN03232  633 LSDINLEIPVGSLVAIVGGTGEGKTSLI-----------------SAMLGELSHAETSSVVIRGSVAYVPQVSWIF-NAT 694
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   97 ALQNVteaLITAQKKPKKEAEQIGMdllrqVGLEHKADSYP-----------ITMSGGQQQRIGIARALAVDPHAILLDE 165
Cdd:PLN03232  695 VRENI---LFGSDFESERYWRAIDV-----TALQHDLDLLPgrdlteigergVNISGGQKQRVSMARAVYSNSDIYIFDD 766
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201  166 PTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVaDKVIFMADGRIIEQGTPEELFDNpqNERTKKFIKQVGE 244
Cdd:PLN03232  767 PLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS--GSLFKKLMENAGK 842
PLN03211 PLN03211
ABC transporter G-25; Provisional
9-221 1.01e-16

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 79.15  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   9 KAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNllerpddGIIEIGDAKLNAASYSRKDVHKLRQQTAMVFQN 88
Cdd:PLN03211  76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALA-------GRIQGNNFTGTILANNRKPTKQILKRTGFVTQD 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  89 YNLFKNKTalqnVTEALI--TAQKKPKKEAEQ----IGMDLLRQVGLEH-----KADSYPITMSGGQQQRIGIARALAVD 157
Cdd:PLN03211 149 DILYPHLT----VRETLVfcSLLRLPKSLTKQekilVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLIN 224
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 158 PHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHE-MAFAREVADKVIFMADGRIIEQG 221
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
PLN03130 PLN03130
ABC transporter C family member; Provisional
17-229 1.13e-16

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 79.01  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLnLLERP--DDGIIEIgdaklnaasysrkdvhklRQQTAMVFQNYNLFkN 94
Cdd:PLN03130  633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAM-LGELPprSDASVVI------------------RGTVAYVPQVSWIF-N 692
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   95 KTALQNVteaLITAQKKPKKEAEQIgmdllRQVGLEHKADSYP-----------ITMSGGQQQRIGIARALAVDPHAILL 163
Cdd:PLN03130  693 ATVRDNI---LFGSPFDPERYERAI-----DVTALQHDLDLLPggdlteigergVNISGGQKQRVSMARAVYSNSDVYIF 764
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201  164 DEPTSALDPELVAGVLQviKSIAE--KQTTMIIVTHEMAFAREVaDKVIFMADGRIIEQGTPEELFDN 229
Cdd:PLN03130  765 DDPLSALDAHVGRQVFD--KCIKDelRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
14-197 1.17e-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: 75.61  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  14 LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYS-RKDVHKLRQQTAM-----VFQ 87
Cdd:cd03231   13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIkttlsVLE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  88 NYNLFKNKTALQNVTEALITaqkkpkkeaeqigMDLlrqVGLEHKADSYpitMSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:cd03231   93 NLRFWHADHSDEQVEEALAR-------------VGL---NGFEDRPVAQ---LSAGQQRRVALARLLLSGRPLWILDEPT 153
                        170       180       190
                 ....*....|....*....|....*....|
gi 489248201 168 SALDPELVAGVLQVIKSIAEKQTTMIIVTH 197
Cdd:cd03231  154 TALDKAGVARFAEAMAGHCARGGMVVLTTH 183
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
17-228 2.26e-16

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: 78.06  E-value: 2.26e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLnlLERPDdgiieigdaKLNAASYSRKDVHKLRQQTAMvfQNYNLFKN-- 94
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMD---------KVEGHVHMKGSVAYVPQQAWI--QNDSLRENil 720
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    95 ------KTALQNVTEA---LITAQKKPKKEAEQIGmdllrqvglehkadSYPITMSGGQQQRIGIARALAVDPHAILLDE 165
Cdd:TIGR00957  721 fgkalnEKYYQQVLEAcalLPDLEILPSGDRTEIG--------------EKGVNLSGGQKQRVSLARAVYSNADIYLFDD 786
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   166 PTSALDP-------ELVAGVLQVIKSiaekqTTMIIVTHEMAFAREVaDKVIFMADGRIIEQGTPEELFD 228
Cdd:TIGR00957  787 PLSAVDAhvgkhifEHVIGPEGVLKN-----KTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
13-215 3.24e-16

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 77.84  E-value: 3.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNllERPDDGIIEIGDAKLNA----ASYSR-------KDVHkLRQQ 81
Cdd:TIGR00956  775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGrpldSSFQRsigyvqqQDLH-LPTS 851
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    82 TamvfqnynlfknktalqnVTEALITA------QKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGG----QQQRIGIA 151
Cdd:TIGR00956  852 T------------------VRESLRFSaylrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIG 913
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201   152 RALAVDPHAIL-LDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHE-MAFAREVADKVIFMADG 215
Cdd:TIGR00956  914 VELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpSAILFEEFDRLLLLQKG 979
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
16-223 4.66e-16

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: 74.37  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasySRKDVHKLRQQTAMVFQNYNLFKNk 95
Cdd:cd03369   23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI-----STIPLEDLRSSLTIIPQDPTLFSG- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  96 talqnvtealiTAQKKPKKEAEQIGMDLLRQVGLEHKADSypitMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELV 175
Cdd:cd03369   97 -----------TIRSNLDPFDEYSDEEIYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATD 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489248201 176 AGVLQVIKSiAEKQTTMIIVTHEMafaREVA--DKVIFMADGRIIEQGTP 223
Cdd:cd03369  162 ALIQKTIRE-EFTNSTILTIAHRL---RTIIdyDKILVMDAGEVKEYDHP 207
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
7-221 5.18e-16

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: 73.84  E-value: 5.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   7 IRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLeRPDDGIIEiGDAKLNAASYsRKDVHKLRQQTAMVF 86
Cdd:cd03233   13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-TEGNVSVE-GDIHYNGIPY-KEFAEKYPGEIIYVS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  87 QNYNLFKNKTalqnVTEALITAqkkpkkeAEQIGMDLLRQVglehkadsypitmSGGQQQRIGIARALAVDPHAILLDEP 166
Cdd:cd03233   90 EEDVHFPTLT----VRETLDFA-------LRCKGNEFVRGI-------------SGGERKRVSIAEALVSRASVLCWDNS 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 167 TSALDPELVAGVLQVIKSIA--EKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQG 221
Cdd:cd03233  146 TRGLDSSTALEILKCIRTMAdvLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
ycf16 CHL00131
sulfate ABC transporter protein; Validated
1-224 5.19e-16

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 75.06  E-value: 5.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRClnLLERPDDGIIEiGDAKLNAASYSRKDVHKLRQ 80
Cdd:CHL00131   7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKV--IAGHPAYKILE-GDILFKGESILDLEPEERAH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTA-MVFQN---YNLFKNKTALQNVTEALITAQKKPKKEA---EQIGMDLLRQVGLEHKADSYPIT--MSGGQQQRIGIA 151
Cdd:CHL00131  84 LGIfLAFQYpieIPGVSNADFLRLAYNSKRKFQGLPELDPlefLEIINEKLKLVGMDPSFLSRNVNegFSGGEKKRNEIL 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201 152 RALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHemaFARE----VADKVIFMADGRIIEQGTPE 224
Cdd:CHL00131 164 QMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRLldyiKPDYVHVMQNGKIIKTGDAE 237
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
20-217 1.09e-15

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 75.86  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYsrkdvhKLRQQTAMVF-----QNYNLFKN 94
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST------AQRLARGLVYlpedrQSSGLYLD 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  95 KTALQNVTeALITAQK----KPKKEA---EQigmdLLRQVGLEHKADSYPI-TMSGGQQQRIGIARALAVDPHAILLDEP 166
Cdd:PRK15439 356 APLAWNVC-ALTHNRRgfwiKPARENavlER----YRRALNIKFNHAEQAArTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489248201 167 TSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
1-226 2.18e-15

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 75.04  E-value: 2.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEigdaklnaasYSRKDVH---- 76
Cdd:PRK10762   4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIL----------YLGKEVTfngp 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  77 KLRQQT--AMVFQNYNLFKNKTALQNV------TEALITAQ-KKPKKEAEQigmdLLRQVGLEHKADSYPITMSGGQQQR 147
Cdd:PRK10762  74 KSSQEAgiGIIHQELNLIPQLTIAENIflgrefVNRFGRIDwKKMYAEADK----LLARLNLRFSSDKLVGELSIGEQQM 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 148 IGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK10762 150 VEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
7-210 3.90e-15

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 74.07  E-value: 3.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   7 IRKAFKD--LTVLDGidlEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgDAKLnaaSYsrkdvhK---LRQQ 81
Cdd:PRK13409 346 LTKKLGDfsLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKI---SY------KpqyIKPD 412
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  82 TAMVFQNYnlfknktaLQNVTEALITAQKKPkkeaeqigmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAI 161
Cdd:PRK13409 413 YDGTVEDL--------LRSITDDLGSSYYKS---------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLY 475
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489248201 162 LLDEPTSALDPELVAGVLQVIKSIAE-KQTTMIIVTHEMAFAREVADKVI 210
Cdd:PRK13409 476 LLDEPSAHLDVEQRLAVAKAIRRIAEeREATALVVDHDIYMIDYISDRLM 525
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
15-197 7.35e-15

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: 69.88  E-value: 7.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNllerpddGIIEIGDAKLNaaSYSRKDVHKLRQQTAMVFQNynlfkn 94
Cdd:cd03223   15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALA-------GLWPWGSGRIG--MPEGEDLLFLPQRPYLPLGT------ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  95 ktalqnvtealitaqkkpkkeaeqigmdlLRQVGLehkadsYP--ITMSGGQQQRIGIARALAVDPHAILLDEPTSALDP 172
Cdd:cd03223   80 -----------------------------LREQLI------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
                        170       180
                 ....*....|....*....|....*
gi 489248201 173 ELVAGVLQVIKsiaEKQTTMIIVTH 197
Cdd:cd03223  125 ESEDRLYQLLK---ELGITVISVGH 146
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
2-226 7.69e-15

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 72.85  E-value: 7.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLErPDDGIieiGDAKLNAASYSRKDVHK-LRQ 80
Cdd:NF000106  14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G-PDAGR---RPWRF*TWCANRRALRRtIG* 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQigmdLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:NF000106  90 HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADE----LLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAV 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 161 ILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:NF000106 166 LYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
20-219 8.06e-15

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: 73.29  E-value: 8.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAASYSRkdvhkLRQQTAMVFQNYNLFKNktalq 99
Cdd:COG4615  351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREA-----YRQLFSAVFSDFHLFDR----- 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 100 nvteaLITAQKKPkkEAEQIgMDLLRQVGLEHK---ADSYPIT--MSGGQQQRIGIARALAVDPHAILLDEPTSALDP-- 172
Cdd:COG4615  421 -----LLGLDGEA--DPARA-RELLERLELDHKvsvEDGRFSTtdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPef 492
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489248201 173 ------ELvagvLQVIKsiaEKQTTMIIVTH-EMAFarEVADKVIFMADGRIIE 219
Cdd:COG4615  493 rrvfytEL----LPELK---ARGKTVIAISHdDRYF--DLADRVLKMDYGKLVE 537
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
15-234 1.29e-14

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 71.45  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkdvhkLRQQ-TAMVFQNYNLFK 93
Cdd:PRK15056  21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA---------LQKNlVAYVPQSEEVDW 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  94 NKTALqnVTEALITAQ-------KKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEP 166
Cdd:PRK15056  92 SFPVL--VEDVVMMGRyghmgwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 167 TSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIfMADGRIIEQGTPEELFDNPQNER 234
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTFTAENLEL 236
GguA NF040905
sugar ABC transporter ATP-binding protein;
5-219 1.34e-14

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 72.51  E-value: 1.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   5 RHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL-----------------------NLLERPDDGIIEIg 61
Cdd:NF040905   5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvyphgsyegeilfdgevcrfkDIRDSEALGIVII- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  62 daklnaasysrkdvHklrQQTAMVFQ---NYNLF-KNKTAlqnvTEALITAQKKPKKEAEqigmdLLRQVGLEHKADSyP 137
Cdd:NF040905  84 --------------H---QELALIPYlsiAENIFlGNERA----KRGVIDWNETNRRARE-----LLAKVGLDESPDT-L 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 138 ITMSG-GQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGR 216
Cdd:NF040905 137 VTDIGvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGR 216

                 ...
gi 489248201 217 IIE 219
Cdd:NF040905 217 TIE 219
PTZ00243 PTZ00243
ABC transporter; Provisional
16-231 1.49e-14

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 72.89  E-value: 1.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLrcLNLLErpddgIIEI--GDAKLNAASYSRKDVHKLRQQTAMVFQNYNLFk 93
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLL--LTFMR-----MVEVcgGEIRVNGREIGAYGLRELRRQFSMIPQDPVLF- 1396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   94 NKTALQNVTEALITAQKKPKKEAEQIGmdLLRQVGLEHKA-DSYPI----TMSGGQQQRIGIARA-LAVDPHAILLDEPT 167
Cdd:PTZ00243 1397 DGTVRQNVDPFLEASSAEVWAALELVG--LRERVASESEGiDSRVLeggsNYSVGQRQLMCMARAlLKKGSGFILMDEAT 1474
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201  168 SALDPELVAGVLQVIKSiAEKQTTMIIVTHEMafaREVA--DKVIFMADGRIIEQGTPEELFDNPQ 231
Cdd:PTZ00243 1475 ANIDPALDRQIQATVMS-AFSAYTVITIAHRL---HTVAqyDKIIVMDHGAVAEMGSPRELVMNRQ 1536
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
2-173 2.30e-14

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: 71.89  E-value: 2.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDA-KLNAASYSRKDvhklrq 80
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvKLAYVDQSRDA------ 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   81 qtamvfqnynLFKNKTALQNVTEalitaqkkpkkeaeqiGMDLLRQVGLEHKADSY-------------PI-TMSGGQQQ 146
Cdd:TIGR03719 397 ----------LDPNKTVWEEISG----------------GLDIIKLGKREIPSRAYvgrfnfkgsdqqkKVgQLSGGERN 450
                         170       180
                  ....*....|....*....|....*..
gi 489248201  147 RIGIARALAVDPHAILLDEPTSALDPE 173
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVE 477
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
16-240 3.17e-14

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 70.99  E-value: 3.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  16 VLDGIDLEIKSGEVTAIIGPSGSGKStllrclnLLERPDDGIIEiGDAKLNAASYSRKDVHKLR-----------QQTAM 84
Cdd:PRK15093  22 AVDRVSMTLTEGEIRGLVGESGSGKS-------LIAKAICGVTK-DNWRVTADRMRFDDIDLLRlsprerrklvgHNVSM 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  85 VFQNYNLFKNKTalQNVTEALITA-----------QKKPKKEAEQIgmDLLRQVGL-EHKA--DSYPITMSGGQQQRIGI 150
Cdd:PRK15093  94 IFQEPQSCLDPS--ERVGRQLMQNipgwtykgrwwQRFGWRKRRAI--ELLHRVGIkDHKDamRSFPYELTEGECQKVMI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 151 ARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDN 229
Cdd:PRK15093 170 AIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNnTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTT 249
                        250
                 ....*....|.
gi 489248201 230 PQNERTKKFIK 240
Cdd:PRK15093 250 PHHPYTQALIR 260
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
11-240 4.55e-14

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 71.60  E-value: 4.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   11 FKDLTvldgidLEIKSGEVTAIIGPSGSGKSTLLrclNLLER----PDDGIIEIGDAKLNAASYSRKDVHKLRQQTAMV- 85
Cdd:PTZ00265 1184 YKDLT------FSCDSKKTTAIVGETGSGKSTVM---SLLMRfydlKNDHHIVFKNEHTNDMTNEQDYQGDEEQNVGMKn 1254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   86 ------------FQNYNLFKNKTA------------LQNVTEALITAQKKP-----------KKEAEQIGMDLLRQV--- 127
Cdd:PTZ00265 1255 vnefsltkeggsGEDSTVFKNSGKilldgvdicdynLKDLRNLFSIVSQEPmlfnmsiyeniKFGKEDATREDVKRAckf 1334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  128 --------GLEHKADS----YPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDP---ELVAGVLQVIKSIAEKqtTM 192
Cdd:PTZ00265 1335 aaidefieSLPNKYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADK--TI 1412
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489248201  193 IIVTHEMAFAREVADKVIFMADGR----IIEQGTPEELFdNPQNERTKKFIK 240
Cdd:PTZ00265 1413 ITIAHRIASIKRSDKIVVFNNPDRtgsfVQAHGTHEELL-SVQDGVYKKYVK 1463
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
25-200 5.16e-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: 5.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  25 KSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEigdaklNAASYsrKDVHKLRQQTAMvfQNYnlfknktaLQNVTEA 104
Cdd:COG1245   97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD------EEPSW--DEVLKRFRGTEL--QDY--------FKKLANG 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 105 LITAQKKPK-----------------KEAEQIGM--DLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDE 165
Cdd:COG1245  159 EIKVAHKPQyvdlipkvfkgtvrellEKVDERGKldELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489248201 166 PTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMA 200
Cdd:COG1245  239 PSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLA 273
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
1-221 7.64e-14

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 69.05  E-value: 7.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL------------------NLLE-----RPDDGI 57
Cdd:PRK09580   1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagredyevtggtvefkgkDLLElspedRAGEGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  58 -------IEI-GDAKLNAASYSRKDVHKLRQQTAM-VFQNYNLFKNKTALQNVTEALITaqkkpkkeaeqigmdllRQVG 128
Cdd:PRK09580  81 fmafqypVEIpGVSNQFFLQTALNAVRSYRGQEPLdRFDFQDLMEEKIALLKMPEDLLT-----------------RSVN 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 129 lehkadsypITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVA-D 207
Cdd:PRK09580 144 ---------VGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpD 214
                        250
                 ....*....|....
gi 489248201 208 KVIFMADGRIIEQG 221
Cdd:PRK09580 215 YVHVLYQGRIVKSG 228
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
11-221 1.05e-13

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: 66.96  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  11 FKDLTV--LDGIDLEIKSGEVTAIIGPSGSGKSTLLRclnllerpdDGIIEIGDAKLNAA--SYSRkdvhklrQQTAMVF 86
Cdd:cd03238    3 VSGANVhnLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISFlpKFSR-------NKLIFID 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  87 QnynlfknktaLQNVTEalitaqkkpkkeaeqIGMDLLRqvgLEHKADsypiTMSGGQQQRIGIARALAVDPHAIL--LD 164
Cdd:cd03238   67 Q----------LQFLID---------------VGLGYLT---LGQKLS----TLSGGELQRVKLASELFSEPPGTLfiLD 114
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 165 EPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREvADKVIFMA------DGRIIEQG 221
Cdd:cd03238  115 EPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGpgsgksGGKVVFSG 176
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
7-210 1.10e-13

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: 69.81  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   7 IRKAFKD--LTVLDGidlEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEiGDAKLnaaSYSRKDVhklrqqtam 84
Cdd:COG1245  347 LTKSYGGfsLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKI---SYKPQYI--------- 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  85 vfqnynlfknkTALQNVT-EALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILL 163
Cdd:COG1245  411 -----------SPDYDGTvEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 479
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489248201 164 DEPTSALDPELVAGVLQVIKSIAEKQ-TTMIIVTHEMAFAREVADKVI 210
Cdd:COG1245  480 DEPSAHLDVEQRLAVAKAIRRFAENRgKTAMVVDHDIYLIDYISDRLM 527
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
20-219 1.46e-13

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 69.62  E-value: 1.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsysrkDVHKLRQQTAMVFQNYNLFknktalq 99
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE-----QPEDYRKLFSAVFTDFHLF------- 409
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 100 nvtEALITAQKKPKKEAeqIGMDLLRQVGLEHKADS-----YPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPEL 174
Cdd:PRK10522 410 ---DQLLGPEGKPANPA--LVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF 484
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489248201 175 VAGVLQV-IKSIAEKQTTMIIVTHEMAFArEVADKVIFMADGRIIE 219
Cdd:PRK10522 485 RREFYQVlLPLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQLSE 529
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
1-231 1.74e-13

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 67.83  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEigdaklnaasysrkDVHKLRq 80
Cdd:PRK09544   4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------------RNGKLR- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 qTAMVFQNYNLfkNKTALQNVTEALitaQKKPKKEAEQIgMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHA 160
Cdd:PRK09544  69 -IGYVPQKLYL--DTTLPLTVNRFL---RLRPGTKKEDI-LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 161 ILLDEPTSALDpelVAGVLQVIKSIAEKQTTM----IIVTHEMAFAREVADKVIFMaDGRIIEQGTPEELFDNPQ 231
Cdd:PRK09544 142 LVLDEPTQGVD---VNGQVALYDLIDQLRRELdcavLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE 212
PLN03130 PLN03130
ABC transporter C family member; Provisional
16-229 2.82e-13

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 69.00  E-value: 2.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDakLNAASYSRKDVHK---LRQQTAMVFQN---Y 89
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG--CDISKFGLMDLRKvlgIIPQAPVLFSGtvrF 1331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   90 NL--FkNKTALQNVTEALITAQKKpkkeaeqigmDLLRQ--VGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDE 165
Cdd:PLN03130 1332 NLdpF-NEHNDADLWESLERAHLK----------DVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201  166 PTSALDPELVAgVLQviKSIAE--KQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFDN 229
Cdd:PLN03130 1401 ATAAVDVRTDA-LIQ--KTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN 1462
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
14-226 5.68e-13

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 67.74  E-value: 5.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  14 LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAAsySRKDVHKL--------RQQTAMV 85
Cdd:COG3845  271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGL--SPRERRRLgvayipedRLGRGLV 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  86 fQNYNLFKNkTALQNVTEALITA-----QKKPKKEAEQI--GMDlLRQVGLEHKADSypitMSGGQQQRIGIARALAVDP 158
Cdd:COG3845  349 -PDMSVAEN-LILGRYRRPPFSRggfldRKAIRAFAEELieEFD-VRTPGPDTPARS----LSGGNQQKVILARELSRDP 421
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRII-----EQGTPEEL 226
Cdd:COG3845  422 KLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVgevpaAEATREEI 494
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
17-226 1.81e-12

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 66.58  E-value: 1.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNllerpDDGIIEIGDAKLNAASY--SRKDVHklrqqtamvfQNYNLFKN 94
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLT-----GDTTVTSGDATVAGKSIltNISDVH----------QNMGYCPQ 2019
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    95 KTALQNvteaLITAQKK----------PKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLD 164
Cdd:TIGR01257 2020 FDAIDD----LLTGREHlylyarlrgvPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLD 2095
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489248201   165 EPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:TIGR01257 2096 EPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
17-223 2.60e-12

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: 64.56  E-value: 2.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  17 LDGIDLEIKSGEVTAIIGPSGSGKSTLL---------RCLNL-LERPDDGIIEIGDAKL-----------------NAAS 69
Cdd:cd03271   11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLkKEQPGNHDRIEGLEHIdkvividqspigrtprsNPAT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  70 YSrKDVHKLRQqtamVF------QNYN------LFKNKTALQ----NVTEALITAQKKPKKEAEqigMDLLRQVGLEHKA 133
Cdd:cd03271   91 YT-GVFDEIRE----LFcevckgKRYNretlevRYKGKSIADvldmTVEEALEFFENIPKIARK---LQTLCDVGLGYIK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 134 DSYPI-TMSGGQQQRIGIARALA-VDPHAIL--LDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAReVADKV 209
Cdd:cd03271  163 LGQPAtTLSGGEAQRIKLAKELSkRSTGKTLyiLDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CADWI 241
                        250       260
                 ....*....|....*....|
gi 489248201 210 IFM------ADGRIIEQGTP 223
Cdd:cd03271  242 IDLgpeggdGGGQVVASGTP 261
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
2-225 3.55e-12

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 65.30  E-value: 3.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL-NLLErPDDGIIEIGDaklNAasysrkDVHKLRQ 80
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLvGELE-PDSGTVKWSE---NA------NIGYYAQ 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQN-YNLFK----------NKTALQNVTEALITAQKKPKKEAEQIgmdllrqvglehkadsypitmSGGQQQRIG 149
Cdd:PRK15064 390 DHAYDFENdLTLFDwmsqwrqegdDEQAVRGTLGRLLFSQDDIKKSVKVL---------------------SGGEKGRML 448
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 150 IARALAVDPHAILLDEPTSALDPElvagvlqVIKSIA---EK-QTTMIIVTHEMAFAREVADKVIFMADGRIIE-QGTPE 224
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPTNHMDME-------SIESLNmalEKyEGTLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYE 521

                 .
gi 489248201 225 E 225
Cdd:PRK15064 522 E 522
PLN03232 PLN03232
ABC transporter C family member; Provisional
16-242 3.78e-12

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 65.77  E-value: 3.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAklNAASYSRKDvhkLRQQTAMVFQNYNLFKNK 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDC--DVAKFGLTD---LRRVLSIIPQSPVLFSGT 1325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   96 TALQ----------NVTEALITAQKKPKKEAEQIGMDLLRQVGLEhkadsypiTMSGGQQQRIGIARALAVDPHAILLDE 165
Cdd:PLN03232 1326 VRFNidpfsehndaDLWEALERAHIKDVIDRNPFGLDAEVSEGGE--------NFSVGQRQLLSLARALLRRSKILVLDE 1397
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489248201  166 PTSALDPELVAGVLQVIKSiAEKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELFDNpqneRTKKFIKQV 242
Cdd:PLN03232 1398 ATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR----DTSAFFRMV 1468
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
10-210 4.13e-12

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 65.36  E-value: 4.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  10 AFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEI-GD-----------------------AKL 65
Cdd:PRK11147  12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDlivarlqqdpprnvegtvydfvaEGI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  66 NAASYSRKDVHKLRQQTAMVFQNYNLfkNKTA-LQNVTEALITAQKKPKkeaeqIgMDLLRQVGLEhkADSYPITMSGGQ 144
Cdd:PRK11147  92 EEQAEYLKRYHDISHLVETDPSEKNL--NELAkLQEQLDHHNLWQLENR-----I-NEVLAQLGLD--PDAALSSLSGGW 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 145 QQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIaekQTTMIIVTHEMAFAREVADKVI 210
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF---QGSIIFISHDRSFIRNMATRIV 224
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
2-203 4.22e-12

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 65.44  E-value: 4.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    2 IQVRHIRKAF---KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDA-------------KL 65
Cdd:PTZ00265  383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrsKI 462
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   66 NAAS------------------YSRKDVHKLRQQT------------------AMVFQNYNLFKNKTAlqnvTEALITAQ 109
Cdd:PTZ00265  463 GVVSqdpllfsnsiknnikyslYSLKDLEALSNYYnedgndsqenknkrnscrAKCAGDLNDMSNTTD----SNELIEMR 538
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  110 KKPKKEAEQIGMDLLRQVGLEHKADSYP-----------ITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGV 178
Cdd:PTZ00265  539 KNYQTIKDSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
                         250       260
                  ....*....|....*....|....*.
gi 489248201  179 LQVIKSIAEKQTTM-IIVTHEMAFAR 203
Cdd:PTZ00265  619 QKTINNLKGNENRItIIIAHRLSTIR 644
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
2-173 4.36e-12

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 65.14  E-value: 4.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGD-AKLNAASYSRKdvhklrq 80
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGEtVKLAYVDQSRD------- 397
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 qtamvfqnyNLFKNKTALQNVTEalitaqkkpkkeaeqiGMDLLRQVGLEHKADSY-------------PI-TMSGGQQQ 146
Cdd:PRK11819 398 ---------ALDPNKTVWEEISG----------------GLDIIKVGNREIPSRAYvgrfnfkggdqqkKVgVLSGGERN 452
                        170       180
                 ....*....|....*....|....*..
gi 489248201 147 RIGIARALAVDPHAILLDEPTSALDPE 173
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLDVE 479
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
16-206 7.26e-12

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: 64.57  E-value: 7.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLE-------RPDDGiIEIG----DAKLNAASYSRKDVHKLRQQTAM 84
Cdd:TIGR03719  20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDkdfngeaRPQPG-IKVGylpqEPQLDPTKTVRENVEEGVAEIKD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   85 VFQNYNLFKNKTALQNVT-EALITAQKKPKKEAE-QIGMDLLRQvgLEHKADSY-------PIT-MSGGQQQRIGIARAL 154
Cdd:TIGR03719  99 ALDRFNEISAKYAEPDADfDKLAAEQAELQEIIDaADAWDLDSQ--LEIAMDALrcppwdaDVTkLSGGERRRVALCRLL 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489248201  155 AVDPHAILLDEPTSALDPELVAGVLQVIKsiaEKQTTMIIVTHEMAFAREVA 206
Cdd:TIGR03719 177 LSKPDMLLLDEPTNHLDAESVAWLERHLQ---EYPGTVVAVTHDRYFLDNVA 225
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
13-197 9.96e-12

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 62.56  E-value: 9.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgDAKLNAASYSRKDVHKLRQQTAmvfqnynLF 92
Cdd:PRK13543  23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGDRSRFMAYLGHLPG-------LK 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  93 KNKTALQNVTEALITAQKKPKkeaeQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARaLAVDPHAI-LLDEPTSALD 171
Cdd:PRK13543  95 ADLSTLENLHFLCGLHGRRAK----QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLD 169
                        170       180
                 ....*....|....*....|....*.
gi 489248201 172 PELVAGVLQVIKSIAEKQTTMIIVTH 197
Cdd:PRK13543 170 LEGITLVNRMISAHLRGGGAALVTTH 195
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
25-200 1.16e-11

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: 62.77  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  25 KSGEVTAIIGPSGSGKSTLLRCL------NL---LERPD-DGIIEI--GDAKLNAASYSRKDVHKLRQQTAMVFQNYNLF 92
Cdd:cd03236   24 REGQVLGLVGPNGIGKSTALKILagklkpNLgkfDDPPDwDEILDEfrGSELQNYFTKLLEGDVKVIVKPQYVDLIPKAV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  93 KNKtalqnVTEALITAQKKPKKEaeqigmDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDP 172
Cdd:cd03236  104 KGK-----VGELLKKKDERGKLD------ELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
                        170       180
                 ....*....|....*....|....*...
gi 489248201 173 ELVAGVLQVIKSIAEKQTTMIIVTHEMA 200
Cdd:cd03236  173 KQRLNAARLIRELAEDDNYVLVVEHDLA 200
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
24-200 1.24e-11

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 64.06  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  24 IKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEigdaklnaASYSRKDVHKLRQQTAMvfQNYnlfknktaLQNVTE 103
Cdd:PRK13409  96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYE--------EEPSWDEVLKRFRGTEL--QNY--------FKKLYN 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 104 ALITAQKKPK-----------------KEAEQIGM--DLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLD 164
Cdd:PRK13409 158 GEIKVVHKPQyvdlipkvfkgkvrellKKVDERGKldEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489248201 165 EPTSALDPELVAGVLQVIKSIAEKQtTMIIVTHEMA 200
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAEGK-YVLVVEHDLA 272
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
7-247 2.41e-11

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 63.20  E-value: 2.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201     7 IRKAFKD-----LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL--NLlerpdDGIIEIGDAKLNAASYSRKDVHK-L 78
Cdd:TIGR00956   62 FRKLKKFrdtktFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasNT-----DGFHIGVEGVITYDGITPEEIKKhY 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    79 RQQTAMVFQNYNLFKNKTalqnVTEALITAQKKpkKEAEQIGMDLLRQVGLEHKADSYPIT------------------M 140
Cdd:TIGR00956  137 RGDVVYNAETDVHFPHLT----VGETLDFAARC--KTPQNRPDGVSREEYAKHIADVYMATyglshtrntkvgndfvrgV 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   141 SGGQQQRIGIARALAVDPHAILLDEPTSALDPelvAGVLQVIKSIAE-----KQTTMIIVTHEMAFAREVADKVIFMADG 215
Cdd:TIGR00956  211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDS---ATALEFIRALKTsanilDTTPLVAIYQCSQDAYELFDKVIVLYEG 287
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 489248201   216 RIIEQGTPEEL--------FDNPQNERTKKFIKQVGEPAE 247
Cdd:TIGR00956  288 YQIYFGPADKAkqyfekmgFKCPDRQTTADFLTSLTSPAE 327
PTZ00243 PTZ00243
ABC transporter; Provisional
16-217 2.53e-11

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 63.26  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNllerpddGIIEIGDAKLNAAsysrKDVHKLRQQ----TAMVFQNYNL 91
Cdd:PTZ00243  675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLL-------SQFEISEGRVWAE----RSIAYVPQQawimNATVRGNILF 743
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   92 FKNKTAlqnvtEALITAQKKPKKEAEqigmdlLRQV--GLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSA 169
Cdd:PTZ00243  744 FDEEDA-----ARLADAVRVSQLEAD------LAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489248201  170 LDPELVAGVLQ--VIKSIAEKqtTMIIVTHEM-AFARevADKVIFMADGRI 217
Cdd:PTZ00243  813 LDAHVGERVVEecFLGALAGK--TRVLATHQVhVVPR--ADYVVALGDGRV 859
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
121-226 4.65e-11

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: 62.34  E-value: 4.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  121 MDLLRQVGLEHKADSYPI-TMSGGQQQRIGIARAL---AVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVT 196
Cdd:TIGR00630 810 LQTLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIE 889
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489248201  197 HEMAFAReVADKVIFM------ADGRIIEQGTPEEL 226
Cdd:TIGR00630 890 HNLDVIK-TADYIIDLgpeggdGGGTVVASGTPEEV 924
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
17-212 5.33e-11

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: 59.30  E-value: 5.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLlerpddgiieigdaklnaasysrkdvhklrqqtAMVFQNYNLFKNKT 96
Cdd:cd03227   11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAIGL---------------------------------ALGGAQSATRRRSG 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  97 ALQNVTEALItaqkkpkkEAEQIGMDllrqvglehkadsypITMSGGQQQRIGIARALAVDPHA----ILLDEPTSALDP 172
Cdd:cd03227   58 VKAGCIVAAV--------SAELIFTR---------------LQLSGGEKELSALALILALASLKprplYILDEIDRGLDP 114
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 489248201 173 ELVAGVLQVIKSIAEKQTTMIIVTHEMAFArEVADKVIFM 212
Cdd:cd03227  115 RDGQALAEAILEHLVKGAQVIVITHLPELA-ELADKLIHI 153
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
23-210 6.48e-11

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: 59.51  E-value: 6.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  23 EIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIgdaklnaasysrkdvhklrqqtamvfqnynlfknktalqnvt 102
Cdd:cd03222   21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW------------------------------------------ 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 103 eALITAQKKPKKeaeqigmdllrqvglehkadsypITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVI 182
Cdd:cd03222   59 -DGITPVYKPQY-----------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
                        170       180
                 ....*....|....*....|....*....
gi 489248201 183 KSIAEK-QTTMIIVTHEMAFAREVADKVI 210
Cdd:cd03222  115 RRLSEEgKKTALVVEHDLAVLDYLSDRIH 143
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
2-226 7.33e-11

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 61.68  E-value: 7.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIE-----IGDAKLNAASYSR---- 72
Cdd:NF033858   2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdMADARHRRAVCPRiaym 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  73 -----KDVHklrqQTAMVFQNYNLFknktalqnvteALITAQKKPKKEAeQIGmDLLRQVGLEHKADSYPITMSGGQQQR 147
Cdd:NF033858  82 pqglgKNLY----PTLSVFENLDFF-----------GRLFGQDAAERRR-RID-ELLRATGLAPFADRPAGKLSGGMKQK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 148 IGIARALAVDPHAILLDEPTSALDP-------ELvagvlqvIKSIAEKQTTM--IIVThemAFAREVA--DKVIFMADGR 216
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTGVDPlsrrqfwEL-------IDRIRAERPGMsvLVAT---AYMEEAErfDWLVAMDAGR 214
                        250
                 ....*....|
gi 489248201 217 IIEQGTPEEL 226
Cdd:NF033858 215 VLATGTPAEL 224
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
16-227 1.27e-10

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: 59.92  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  16 VLDGIDLEIKSGEVTAIIGPSGSGKSTL-LRCLNLLERPDDGIIeigdakLNAASYSRKDVHKLRQQTAMVFQNYNLF-- 92
Cdd:cd03288   36 VLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFDGKIV------IDGIDISKLPLHTLRSRLSIILQDPILFsg 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  93 --------KNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHkadsypitMSGGQQQRIGIARALAVDPHAILLD 164
Cdd:cd03288  110 sirfnldpECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGEN--------FSVGQRQLFCLARAFVRKSSILIMD 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489248201 165 EPTSALDPElVAGVLQVIKSIAEKQTTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELF 227
Cdd:cd03288  182 EATASIDMA-TENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
17-217 1.87e-10

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 60.22  E-value: 1.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCL-NLLERPDDGIIEIGDAKLNaasySRKDVHKLRQQTAMVFQN---YNLF 92
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVD----IRNPAQAIRAGIAMVPEDrkrHGIV 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   93 KNKTALQNVTEALI---TAQKKPKKEAEQIGMDL-LRQVGLEHKADSYPIT-MSGGQQQRIGIARALAVDPHAILLDEPT 167
Cdd:TIGR02633 352 PILGVGKNITLSVLksfCFKMRIDAAAELQIIGSaIQRLKVKTASPFLPIGrLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 489248201  168 SALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
16-234 3.66e-10

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: 58.71  E-value: 3.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEigdaKLNAASYSrkdvhklrQQTAMVFQNynlfknk 95
Cdd:cd03291   52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK----HSGRISFS--------SQFSWIMPG------- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  96 TALQNVTEALITAQKKPKK--EAEQIGMDLLRqvgLEHKaDSYP-----ITMSGGQQQRIGIARALAVDPHAILLDEPTS 168
Cdd:cd03291  113 TIKENIIFGVSYDEYRYKSvvKACQLEEDITK---FPEK-DNTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFG 188
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 169 ALDPELVAGVLQ--VIKSIAEKqtTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELfdnpQNER 234
Cdd:cd03291  189 YLDVFTEKEIFEscVCKLMANK--TRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSEL----QSLR 249
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
16-226 4.92e-10

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 59.57  E-value: 4.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDakLNAASYSrkdVHKLRQQTAMVFQNYNLFKNK 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--LNIAKIG---LHDLRFKITIIPQDPVLFSGS 1375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    96 TAL----------QNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHkadsypitMSGGQQQRIGIARALAVDPHAILLDE 165
Cdd:TIGR00957 1376 LRMnldpfsqysdEEVWWALELAHLKTFVSALPDKLDHECAEGGEN--------LSVGQRQLVCLARALLRKTKILVLDE 1447
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201   166 PTSALDPELVAGVLQVIKSIAEKQTTMIIvTHE----MAFARevadkVIFMADGRIIEQGTPEEL 226
Cdd:TIGR00957 1448 ATAAVDLETDNLIQSTIRTQFEDCTVLTI-AHRlntiMDYTR-----VIVLDKGEVAEFGAPSNL 1506
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
29-210 8.87e-10

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: 56.85  E-value: 8.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  29 VTAIIGPSGSGKSTLLRCLNLL---ERPDDGIIEIGDAKLNAASYSRKDVH---KLRQQTAM-VFQNYNLFKNktalqnv 101
Cdd:cd03240   24 LTLIVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKLIREGEVRAQVKlafENANGKKYtITRSLAILEN------- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 102 teALITAQkkpkkeaEQIGMDLLRQVGlehkadsypiTMSGGQQQ------RIGIARALAVDPHAILLDEPTSALDPELV 175
Cdd:cd03240   97 --VIFCHQ-------GESNWPLLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENI 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 489248201 176 AGVL-QVIKSI-AEKQTTMIIVTHEMAFaREVADKVI 210
Cdd:cd03240  158 EESLaEIIEERkSQKNFQLIVITHDEEL-VDAADHIY 193
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
1-198 1.19e-09

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 56.50  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLnaasysRKDVHKLRQ 80
Cdd:PRK13540   1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI------KKDLCTYQK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVTEALITAqkkpkkeAEQIGMD-LLRQVGLEHKADsYPI-TMSGGQQQRIGIARALAVDP 158
Cdd:PRK13540  75 QLCFVGHRSGINPYLTLRENCLYDIHFS-------PGAVGITeLCRLFSLEHLID-YPCgLLSSGQKRQVALLRLWMSKA 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 489248201 159 HAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHE 198
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
16-234 1.27e-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: 58.38  E-value: 1.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    16 VLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEigdaKLNAASYSrkdvhklrQQTAMVFQNynlfknk 95
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK----HSGRISFS--------PQTSWIMPG------- 501
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    96 TALQNVTEALITAQKKPKK--EAEQIGMDLlrqvGLEHKADSYP-----ITMSGGQQQRIGIARALAVDPHAILLDEPTS 168
Cdd:TIGR01271  502 TIKDNIIFGLSYDEYRYTSviKACQLEEDI----ALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFT 577
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201   169 ALDPELVAGVLQ--VIKSIAEKqtTMIIVTHEMAFAREvADKVIFMADGRIIEQGTPEELfdnpQNER 234
Cdd:TIGR01271  578 HLDVVTEKEIFEscLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL----QAKR 638
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
2-243 2.28e-09

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


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 56.93  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKaFKDLTvldgIDLeikSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGI-IEIGDAklnaasYSRKDVHKLRQ 80
Cdd:COG3593    6 IKIKNFRS-IKDLS----IEL---SDDLTVLVGENNSGKSSILEALRLLLGPSSSRkFDEEDF------YLGDDPDLPEI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNY-----NLFKNKTALQNVTEALITAQKKPKKEAEQI-------------------------GMDLLRQVGLE 130
Cdd:COG3593   72 EIELTFGSLlsrllRLLLKEEDKEELEEALEELNEELKEALKALnellseylkelldgldlelelsldeLEDLLKSLSLR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 131 -HKADSYPITMSG-GQQQRIGIA--RALA-----VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAF 201
Cdd:COG3593  152 iEDGKELPLDRLGsGFQRLILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHL 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 489248201 202 AREV-ADKVIFMADGRIIEQGTpeELFDNPQNERtKKFIKQVG 243
Cdd:COG3593  232 LSEVpLENIRRLRRDSGGTTST--KLIDLDDEDL-RKLLRYLG 271
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
12-219 2.82e-09

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 56.72  E-value: 2.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  12 KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERpddgiIEIGDAKLNAASYS-RKDVHKLRQQTAMVFQNY- 89
Cdd:PRK09700 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK-----RAGGEIRLNGKDISpRSPLDAVKKGMAYITESRr 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  90 --NLFKNKTALQNVTEAL------------ITAQKKPKKEAEQIGMDLLRQVgleHKADSYPITMSGGQQQRIGIARALA 155
Cdd:PRK09700 349 dnGFFPNFSIAQNMAISRslkdggykgamgLFHEVDEQRTAENQRELLALKC---HSVNQNITELSGGNQQKVLISKWLC 425
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489248201 156 VDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIE 219
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
9-198 3.02e-09

ATPase/GTPase, AAA15 family [General function prediction only];


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 56.21  E-value: 3.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   9 KAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLL-------ERPDDGIIE-------------------IGD 62
Cdd:COG1106   11 RSFKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEALYFLrnlvlnsSQPGDKLVEpflldsesknepsefeilfLLD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  63 AKLNAA--SYSRKDVHK--------LRQQTAMVFQN-YNLFKNKTALQNVTEALITAQKKPKKEAEQIgMDLLRQVGLE- 130
Cdd:COG1106   91 GVRYEYgfELDKERIISewlyflstAAQLNVPLLSPlYDWFDNNISLDTSSDGLTLLLKEDESLKEEL-LELLKIADPGi 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 131 ---------------------HKADSYPIT---MSGGQQQRIGIARALA---VDPHAILLDEPTSALDPELVAGVLQVIK 183
Cdd:COG1106  170 edieveeeeiedlverklifkHKGGNVPLPlseESDGTKRLLALAGALLdalAKGGVLLIDEIEASLHPSLLRKLLKLFL 249
                        250
                 ....*....|....*.
gi 489248201 184 SIAEKQTT-MIIVTHE 198
Cdd:COG1106  250 DLANKNNAqLIFTTHS 265
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
140-226 3.81e-09

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 56.55  E-value: 3.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 140 MSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI-- 217
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRIsg 475
                         90
                 ....*....|..
gi 489248201 218 ---IEQGTPEEL 226
Cdd:PRK10762 476 eftREQATQEKL 487
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
2-226 6.76e-09

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 55.90  E-value: 6.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLN-LLERPDdgiieiGDAKLNAASYSRKDVhKLRQ 80
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTgLLPASE------GEAWLFGQPVDAGDI-ATRR 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  81 QTAMVFQNYNLFKNKTALQNVteaLITAQ--KKPKKEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDP 158
Cdd:NF033858 340 RVGYMSQAFSLYGELTVRQNL---ELHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKP 416
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489248201 159 HAILLDEPTSALDPelVA--GVLQVIKSIA-EKQTTMIIVTHEMAFArEVADKVIFMADGRIIEQGTPEEL 226
Cdd:NF033858 417 ELLILDEPTSGVDP--VArdMFWRLLIELSrEDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAAL 484
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
26-218 7.19e-09

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: 53.15  E-value: 7.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    26 SGEVTAIIGPSGSGKSTLLRCL-NLLERPDDGIIEIGDAKLnaasysrkdvhklrqqtamvfqnynlfknktalqnvtea 104
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDI--------------------------------------- 41
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   105 litaqkkpkkeaeqigMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQ---- 180
Cdd:smart00382  42 ----------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleel 105
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 489248201   181 --VIKSIAEKQTTMIIVTHEMAFAREVAdkVIFMADGRII 218
Cdd:smart00382 106 rlLLLLKSEKNLTVILTTNDEKDLGPAL--LRRRFDRRIV 143
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
139-241 9.13e-09

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 55.61  E-value: 9.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  139 TMSGGQQQRIGIARALAVDPHAI--LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHE---MAFAREVAD----KV 209
Cdd:PRK00635  476 TLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLADRIIDigpgAG 555
                          90       100       110
                  ....*....|....*....|....*....|..
gi 489248201  210 IFmaDGRIIEQGTPEElFDNPQNERTKKFIKQ 241
Cdd:PRK00635  556 IF--GGEVLFNGSPRE-FLAKSDSLTAKYLRQ 584
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
20-217 1.28e-08

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 54.92  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  20 IDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLNAasysRKDVHKLRQ---------------QTAM 84
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI----RSPRDAIRAgimlcpedrkaegiiPVHS 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  85 VFQNYNLFKNKtalQNVTEALITAQKKPKKEAEQigmdLLRQVGLEHKADSYPI-TMSGGQQQRIGIARALAVDPHAILL 163
Cdd:PRK11288 348 VADNINISARR---HHLRAGCLINNRWEAENADR----FIRSLNIKTPSREQLImNLSGGNQQKAILGRWLSEDMKVILL 420
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489248201 164 DEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
2-197 1.29e-08

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


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 54.23  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRkAFKDLTvldgIDLEIKSGeVTAIIGPSGSGKSTLLRCLNL-LERPDDGIIEIGDAKLN------------AA 68
Cdd:COG3950    6 LTIENFR-GFEDLE----IDFDNPPR-LTVLVGENGSGKTTLLEAIALaLSGLLSRLDDVKFRKLLirngefgdsaklIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  69 SYS--R-------KDVHKLRQQTAMVFQNY-NLFKNKTALQNVTEALITAQKKPKKEAE--------------------- 117
Cdd:COG3950   80 YYGtsRllldgplKKLERLKEEYFSRLDGYdSLLDEDSNLREFLEWLREYLEDLENKLSdeldekleavrealnkllpdf 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 118 ---QIGMDLLRQVGLEHKADSYPIT-MSGGQQQRIGIA-----RALAVDPHA---------ILLDEPTSALDPELVAGVL 179
Cdd:COG3950  160 kdiRIDRDPGRLVILDKNGEELPLNqLSDGERSLLALVgdlarRLAELNPALenplegegiVLIDEIDLHLHPKWQRRIL 239
                        250
                 ....*....|....*...
gi 489248201 180 QVIKSIAEKqTTMIIVTH 197
Cdd:COG3950  240 PDLRKIFPN-IQFIVTTH 256
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
139-217 1.56e-08

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 54.74  E-value: 1.56e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489248201 139 TMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
2-217 2.33e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 53.87  E-value: 2.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRKAFKDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRC------------LNLLERPDDGIIEIGDAKLNAAs 69
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndLTLFGRRRGSGETIWDIKKHIG- 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  70 YSRKDVHkLRQQTAMVFQNYNL---FKNKTALQNVTEALitaQKKPKKEAEQIGMDllrqvglEHKADSYPITMSGGQQQ 146
Cdd:PRK10938 340 YVSSSLH-LDYRVSTSVRNVILsgfFDSIGIYQAVSDRQ---QKLAQQWLDILGID-------KRTADAPFHSLSWGQQR 408
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 147 RIGIARALAVDPHAILLDEPTSALDP---ELVAGVLQVIksIAEKQTTMIIVTHEMAFARE-VADKVIFMADGRI 217
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVL--ISEGETQLLFVSHHAEDAPAcITHRLEFVPDGDI 481
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
17-229 2.86e-08

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 53.74  E-value: 2.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  17 LDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEI-GDAKLNAASYSRKDvhKLRQQTAMVFQNYNLFKNK 95
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAALIAISSGLNG--QLTGIENIELKGLMMGLTK 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  96 TALQNVTEALItaqkkpkkEAEQIGMDLLRQVGlehkadsypiTMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELV 175
Cdd:PRK13545 118 EKIKEIIPEII--------EFADIGKFIYQPVK----------TYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489248201 176 AGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFDN 229
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
PLN03140 PLN03140
ABC transporter G family member; Provisional
14-215 3.08e-08

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 54.08  E-value: 3.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   14 LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLnlLERPDDGIIEiGDAKLnaASYSRKdvhklrQQTAMVFQNYNLFK 93
Cdd:PLN03140  893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVL--AGRKTGGYIE-GDIRI--SGFPKK------QETFARISGYCEQN 961
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   94 NKTALQ-NVTEALITAQ--KKPKKEAEQIGMDLLRQV----GLEHKADS---YP-IT-MSGGQQQRIGIARALAVDPHAI 161
Cdd:PLN03140  962 DIHSPQvTVRESLIYSAflRLPKEVSKEEKMMFVDEVmelvELDNLKDAivgLPgVTgLSTEQRKRLTIAVELVANPSII 1041
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489248201  162 LLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAF-AREVADKVIFMADG 215
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRG 1096
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
13-217 3.34e-08

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 53.80  E-value: 3.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  13 DLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGdAKLNAASYsrkDVHKLrqqtamvfqnyNLF 92
Cdd:PRK11147 331 GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-TKLEVAYF---DQHRA-----------ELD 395
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  93 KNKTALQNVTEAlitaqkkpKKEAEQIGMDllRQV------GLEH-KADSYPI-TMSGGQQQRIGIARALAVDPHAILLD 164
Cdd:PRK11147 396 PEKTVMDNLAEG--------KQEVMVNGRP--RHVlgylqdFLFHpKRAMTPVkALSGGERNRLLLARLFLKPSNLLILD 465
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 165 EPTSALDPElvagVLQVIKS-IAEKQTTMIIVTHEMAFA-REVADKVIFMADGRI 217
Cdd:PRK11147 466 EPTNDLDVE----TLELLEElLDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKI 516
PLN03073 PLN03073
ABC transporter F family; Provisional
11-217 3.85e-08

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 53.71  E-value: 3.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  11 FKDLTVldGIDLEIKsgevTAIIGPSGSGKSTLLRCLNLLERPDDGIIeIGDAKLNAASYSRKDVHKLRQQTAMVFQNYN 90
Cdd:PLN03073 525 FKNLNF--GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKVRMAVFSQHHVDGLDLSSNPLLYMMR 597
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  91 LFKNktalqnVTEALITAQkkpkkeaeqigmdlLRQVGLEHKADSYPI-TMSGGQQQRIGIARALAVDPHAILLDEPTSA 169
Cdd:PLN03073 598 CFPG------VPEQKLRAH--------------LGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNH 657
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489248201 170 LDPELVAGVLQvikSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:PLN03073 658 LDLDAVEALIQ---GLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
21-226 1.39e-07

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 51.55  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  21 DLEIKSGEVTAIIGPSGSGKSTLLRCLNllerpDDGIIEIGDAKLNAASYSRKDVHKLRQQTAMVFQnynlfKNKTALQN 100
Cdd:PRK10938  23 SLTLNAGDSWAFVGANGSGKSALARALA-----GELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQ-----RNNTDMLS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 101 VTE---ALITAQ------KKPKKEAEqigmdLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD 171
Cdd:PRK10938  93 PGEddtGRTTAEiiqdevKDPARCEQ-----LAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 172 PELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEEL 226
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
PLN03073 PLN03073
ABC transporter F family; Provisional
139-236 1.55e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 51.78  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 139 TMSGGQQQRIGIARALAVDPHAILLDEPTSALDpelVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRII 218
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLV 420
                         90
                 ....*....|....*...
gi 489248201 219 EQGTPEELFDNPQNERTK 236
Cdd:PLN03073 421 TYKGDYDTFERTREEQLK 438
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
17-221 1.97e-07

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: 50.33  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  17 LDGIDLEIKSGEVTAIIGPSGSGKSTLL---------------------RCLNLLERPD-DGI------IEIgDAKLNAa 68
Cdd:cd03270   11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDvDSIeglspaIAI-DQKTTS- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  69 sysrkdvHKLRQQTAMVFQNYNLFKNKTALQNVTEALitaqkkpkkeaeqigmDLLRQVGLEHKADSYPI-TMSGGQQQR 147
Cdd:cd03270   89 -------RNPRSTVGTVTEIYDYLRLLFARVGIRERL----------------GFLVDVGLGYLTLSRSApTLSGGEAQR 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 148 IGIARALAVDPHAIL--LDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREvADKVIFMA------DGRIIE 219
Cdd:cd03270  146 IRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVIDIGpgagvhGGEIVA 224

                 ..
gi 489248201 220 QG 221
Cdd:cd03270  225 QG 226
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
115-241 2.21e-07

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 51.37  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  115 EAEQIGMD---------LLRQVGLEHKADSYPI-TMSGGQQQRIGIA-RALAVDPHAIL--LDEPTSALDPELVAGVLQV 181
Cdd:PRK00635  775 EAEKFFLDepsihekihALCSLGLDYLPLGRPLsSLSGGEIQRLKLAyELLAPSKKPTLyvLDEPTTGLHTHDIKALIYV 854
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201  182 IKSIAEKQTTMIIVTHEMAFAReVADKVIFMA------DGRIIEQGTPEELF--DNPQNERTKKFIKQ 241
Cdd:PRK00635  855 LQSLTHQGHTVVIIEHNMHVVK-VADYVLELGpeggnlGGYLLASCSPEELIhlHTPTAKALRPYLSS 921
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
121-247 2.89e-07

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 50.80  E-value: 2.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 121 MDLLRQVGLehkadSYpI-------TMSGGQQQRIGIARALA--VDPHAI-LLDEPTSALDPELVAGVLQVIKSIAEKQT 190
Cdd:COG0178  807 LQTLQDVGL-----GY-IklgqpatTLSGGEAQRVKLASELSkrSTGKTLyILDEPTTGLHFHDIRKLLEVLHRLVDKGN 880
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489248201 191 TMIIVTHEMAFAReVADKVIfmaD---------GRIIEQGTPEELFDNPQNErTKKFIKQVGEPAE 247
Cdd:COG0178  881 TVVVIEHNLDVIK-TADWII---DlgpeggdggGEIVAEGTPEEVAKVKASY-TGRYLKEYLEAAR 941
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
1-206 4.55e-07

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 50.12  E-value: 4.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   1 MIQVRhirKAF-KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGiieigDAKLnAASYSrkdVHKLR 79
Cdd:PRK11819   9 MNRVS---KVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-----EARP-APGIK---VGYLP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  80 QQTamvfqnyNLFKNKTALQNVTEALitAQKKPK-KEAEQIG---------MDLL--RQVGLEHKADSY----------- 136
Cdd:PRK11819  77 QEP-------QLDPEKTVRENVEEGV--AEVKAAlDRFNEIYaayaepdadFDALaaEQGELQEIIDAAdawdldsqlei 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 137 ------------PIT-MSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGvLQviKSIAEKQTTMIIVTHEMAFAR 203
Cdd:PRK11819 148 amdalrcppwdaKVTkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAW-LE--QFLHDYPGTVVAVTHDRYFLD 224

                 ...
gi 489248201 204 EVA 206
Cdd:PRK11819 225 NVA 227
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
2-197 4.96e-07

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 48.85  E-value: 4.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   2 IQVRHIRkAFKDLTVldgIDLEiksGEVTAIIGPSGSGKSTLLRCLNL-------------------------------- 49
Cdd:COG0419    5 LRLENFR-SYRDTET---IDFD---DGLNLIVGPNGAGKSTILEAIRYalygkarsrsklrsdlinvgseeasvelefeh 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  50 ------LERPDDGIIEIgdakLNAASYSRKDVhkLRQqtamVFQNYNLFKNKTALQNVTEALiTAQKKPKKEAEQIGMDL 123
Cdd:COG0419   78 ggkryrIERRQGEFAEF----LEAKPSERKEA--LKR----LLGLEIYEELKERLKELEEAL-ESALEELAELQKLKQEI 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201 124 LRQV-GLEHKAdsypiTMSGGQQQRIGIARALavdphAILLDepTSALDPELVAGVLQVIKSIAekqttmiIVTH 197
Cdd:COG0419  147 LAQLsGLDPIE-----TLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEELA-------IITH 202
uvrA PRK00349
excinuclease ABC subunit UvrA;
121-242 6.15e-07

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 50.07  E-value: 6.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 121 MDLLRQVGLehkadSY------PITMSGGQQQRIGIARALA---------VdphailLDEPTSALDPELVAGVLQVIKSI 185
Cdd:PRK00349 811 LQTLVDVGL-----GYiklgqpATTLSGGEAQRVKLAKELSkrstgktlyI------LDEPTTGLHFEDIRKLLEVLHRL 879
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 186 AEKQTTMIIVTHEMafarevaDkVIFMAD-------------GRIIEQGTPEELFDNPqNERTKKFIKQV 242
Cdd:PRK00349 880 VDKGNTVVVIEHNL-------D-VIKTADwiidlgpeggdggGEIVATGTPEEVAKVE-ASYTGRYLKPV 940
PLN03140 PLN03140
ABC transporter G family member; Provisional
14-242 8.11e-07

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 49.84  E-value: 8.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   14 LTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLrcLNLLERPDDGIIEIGDAKLN------------AASYSRKDVH----- 76
Cdd:PLN03140  178 LTILKDASGIIKPSRMTLLLGPPSSGKTTLL--LALAGKLDPSLKVSGEITYNgyrlnefvprktSAYISQNDVHvgvmt 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   77 ------------------------KLRQQTAMVF--QNYNLFKNKTALQNVTEALITaqkkpKKEAEQIGMDLLRQ--VG 128
Cdd:PLN03140  256 vketldfsarcqgvgtrydllselARREKDAGIFpeAEVDLFMKATAMEGVKSSLIT-----DYTLKILGLDICKDtiVG 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  129 lehkaDSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAE--KQTTMIIVTHEMAFAREVA 206
Cdd:PLN03140  331 -----DEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHltEATVLMSLLQPAPETFDLF 405
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 489248201  207 DKVIFMADGRIIEQGTPE---ELFDN-----PQNERTKKFIKQV 242
Cdd:PLN03140  406 DDIILLSEGQIVYQGPRDhilEFFEScgfkcPERKGTADFLQEV 449
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
15-247 9.67e-07

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 49.52  E-value: 9.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDdgiieiGDAKLNAASYSRKDVHKLRQQTAMVFQNYNLFKN 94
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE------GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSG 1306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    95 kTALQNVTEALITAQKKPKKEAEQIGM-DLLRQV--GLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALD 171
Cdd:TIGR01271 1307 -TFRKNLDPYEQWSDEEIWKVAEEVGLkSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   172 PElvagVLQVIKSIAeKQT----TMIIVTHEMAFAREVadKVIFMADGRIIEQgtpeelFDNPQ---NERTkkFIKQVGE 244
Cdd:TIGR01271 1386 PV----TLQIIRKTL-KQSfsncTVILSEHRVEALLEC--QQFLVIEGSSVKQ------YDSIQkllNETS--LFKQAMS 1450

                   ...
gi 489248201   245 PAE 247
Cdd:TIGR01271 1451 AAD 1453
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
15-172 1.55e-06

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: 47.93  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  15 TVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDdgiieiGDAKLNAASYSRKDVHKLRQQTAMVFQNYNLFKN 94
Cdd:cd03289   18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE------GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  95 kTALQNVTEALITAQKKPKKEAEqigmdllrQVGLEHKADSYP-----------ITMSGGQQQRIGIARALAVDPHAILL 163
Cdd:cd03289   92 -TFRKNLDPYGKWSDEEIWKVAE--------EVGLKSVIEQFPgqldfvlvdggCVLSHGHKQLMCLARSVLSKAKILLL 162

                 ....*....
gi 489248201 164 DEPTSALDP 172
Cdd:cd03289  163 DEPSAHLDP 171
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
140-217 2.43e-06

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 48.00  E-value: 2.43e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 140 MSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRI 217
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
23-197 4.46e-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: 47.44  E-value: 4.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   23 EIKSGEVTAIIGPSGSGKSTLLRCLN--------LLERPDDGIIEIgdakLNAASYsrKDVHKLRQQTAMVFQNYNLFKN 94
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFY----VPQRPY--MTLGTLRDQIIYPDSSEDMKRR 547
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   95 KTALQNVTEALitaqkkpkkEAEQIGMDLLRQVGLEHKADsYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPEL 174
Cdd:TIGR00954 548 GLSDKDLEQIL---------DNVQLTHILEREGGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
                         170       180
                  ....*....|....*....|...
gi 489248201  175 VAGVLQVIKsiaEKQTTMIIVTH 197
Cdd:TIGR00954 618 EGYMYRLCR---EFGITLFSVSH 637
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
124-231 5.17e-06

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: 47.32  E-value: 5.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  124 LRQVGLEHKADSYPI-TMSGGQQQRIGIARALAVDPHAIL--LDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMA 200
Cdd:TIGR00630 472 LIDVGLDYLSLSRAAgTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED 551
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 489248201  201 FAREvADKVIFMA------DGRIIEQGTPEELFDNPQ 231
Cdd:TIGR00630 552 TIRA-ADYVIDIGpgagehGGEVVASGTPEEILANPD 587
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
98-197 9.05e-06

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


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 45.84  E-value: 9.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   98 LQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPIT---MSGGQQQRIGIARALAVDPHA---ILLDEPTSALD 171
Cdd:pfam13304 192 LKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPafeLSDGTKRLLALLAALLSALPKgglLLIDEPESGLH 271
                          90       100
                  ....*....|....*....|....*.
gi 489248201  172 PELVAGVLQVIKSIAEKQTTMIIVTH 197
Cdd:pfam13304 272 PKLLRRLLELLKELSRNGAQLILTTH 297
AAA_29 pfam13555
P-loop containing region of AAA domain;
18-69 9.59e-06

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 42.20  E-value: 9.59e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489248201   18 DGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDdgiieiGDAKLNAAS 69
Cdd:pfam13555  13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPA------KRARFNKAA 58
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
123-229 7.29e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 43.62  E-value: 7.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 123 LLRQVGLEHKADSYPIT-MSGGQQQRIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIaekQTTMIIVTHEMAF 201
Cdd:PRK10636 132 LLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY---QGTLILISHDRDF 208
                         90       100
                 ....*....|....*....|....*...
gi 489248201 202 AREVADKVIFmadgriIEQGTPEELFDN 229
Cdd:PRK10636 209 LDPIVDKIIH------IEQQSLFEYTGN 230
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
12-240 8.56e-05

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 42.88  E-value: 8.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  12 KDLTVLDGIDLEIKSGEVTAIIGPSGSGKSTLLRCLNLLERPDDGIIE-IGDAKLNAAsysrkdvhklrqqtamvfqNYN 90
Cdd:PRK13546  35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDrNGEVSVIAI-------------------SAG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  91 LFKNKTALQNVTEALITAQKKPKkEAEQIGMDLLRQVGLEHKADSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSAL 170
Cdd:PRK13546  96 LSGQLTGIENIEFKMLCMGFKRK-EIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVG 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 171 DPELVAGVLQVIKSIAEKQTTMIIVTHEMAFAREVADKVIFMADGRIIEQGTPEELFdnPQNErtkKFIK 240
Cdd:PRK13546 175 DQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL--PKYE---AFLN 239
COG4637 COG4637
Predicted ATPase [General function prediction only];
1-50 8.58e-05

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 43.00  E-value: 8.58e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489248201   1 MIQVRHIR--KAFKDLTVldgiDLeiksGEVTAIIGPSGSGKSTLLRCLNLL 50
Cdd:COG4637    1 MITRIRIKnfKSLRDLEL----PL----GPLTVLIGANGSGKSNLLDALRFL 44
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
29-62 1.53e-04

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


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 41.99  E-value: 1.53e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 489248201   29 VTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGD 62
Cdd:pfam13304   1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTD 34
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
147-214 2.64e-04

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 41.80  E-value: 2.64e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 147 RIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKsiaEKQTTMIIVTHEMAFAREVADKvifMAD 214
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLN---ERNSTMIIISHDRHFLNSVCTH---MAD 224
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
94-215 4.53e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 41.35  E-value: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201   94 NKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLehkadSYPI------TMSGGQQQRIGIARALAVDPHAI--LLDE 165
Cdd:PRK00635 1341 DVTFLKKFLLTIHDDEEPSIIQDLLNRLTFIDKVGL-----SYITlgqeqdTLSDGEHYRLHLAKKISSNLTDIiyLLED 1415
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 489248201  166 PTSALDPELVAGVLQVIKSIAEKQTTmIIVTHEMAFAREVADKVIFMADG 215
Cdd:PRK00635 1416 PLSGLHPQDAPTLLQLIKELVTNNNT-VIATDRSGSLAEHADHLIHLGPG 1464
Rad50_Sulf NF041034
DNA double-strand break repair ATPase Rad50;
147-223 9.96e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 468963 [Multi-domain]  Cd Length: 872  Bit Score: 40.08  E-value: 9.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201 147 RIGIARALAVDPHAILLDEPTSALDPELVAGVLQVIKSIAEKQTTMIIVTHEMAFaREVADKVIFM---ADGRIIEQGTP 223
Cdd:NF041034 793 RLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHDEEL-KEISDYIISVekkGDSSKVKVGSY 871
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
17-43 1.30e-03

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 39.62  E-value: 1.30e-03
                         10        20
                 ....*....|....*....|....*..
gi 489248201  17 LDGIDLEIKSGEVTAIIGPSGSGKSTL 43
Cdd:COG0178   16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
29-173 3.87e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 37.16  E-value: 3.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  29 VTAIIGPSGSGKSTLLRCLNLLERPDDGIIEIGDAKLN--AASYSRKDVHKLRQQTAM-VFQNYNLFknkTALQNVTEAL 105
Cdd:PRK13541  28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINniAKPYCTYIGHNLGLKLEMtVFENLKFW---SEIYNSAETL 104
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489248201 106 ITAQKKPKKEaeqigmDLLrqvglehkaDSYPITMSGGQQQRIGIARALAVDPHAILLDEPTSALDPE 173
Cdd:PRK13541 105 YAAIHYFKLH------DLL---------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
7-56 4.17e-03

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 38.25  E-value: 4.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489248201   7 IRKAFKDLTVLDGIDLEIKsgeVTAIIGPSGSGKSTLLR--CLNLLERPDDG 56
Cdd:COG5635  163 LLERIESLKRLELLEAKKK---RLLILGEPGSGKTTLLRylALELAERYLDA 211
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
18-74 4.19e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 37.38  E-value: 4.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201  18 DGIDlEIK---SGEVTAIIGPSGSGKSTLlrcLNLLerpddgiieIGDAKLNAASYSRKD 74
Cdd:cd01854   74 EGLD-ELRellKGKTSVLVGQSGVGKSTL---LNAL---------LPELVLATGEISEKL 120
AAA_22 pfam13401
AAA domain;
29-60 6.64e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 35.78  E-value: 6.64e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 489248201   29 VTAIIGPSGSGKSTLLRCL-NLLERPDDGIIEI 60
Cdd:pfam13401   7 ILVLTGESGTGKTTLLRRLlEQLPEVRDSVVFV 39
AAA_23 pfam13476
AAA domain;
2-138 9.95e-03

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 35.93  E-value: 9.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489248201    2 IQVRHIRKaFKDLTvldgIDLeikSGEVTAIIGPSGSGKSTLLRCLNL--------LERPDDGIIEIGDAKLNaasysrk 73
Cdd:pfam13476   1 LTIENFRS-FRDQT----IDF---SKGLTLITGPNGSGKTTILDAIKLalygktsrLKRKSGGGFVKGDIRIG------- 65
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489248201   74 DVHKLRQQTAMVFQNYNLFKNKTALQNVTEALITAQKKPKKEAEQIGMDLLRQVGLEHKADSYPI 138
Cdd:pfam13476  66 LEGKGKAYVEITFENNDGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKII 130
 
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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