|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-217 |
1.23e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 228.02 E-value: 1.23e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-----PGKAKNKITVLLQ 80
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 81 ENTIPNSLKVEELIAFFQSISDNPLTN-----QEVQEHLQFkEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPT 155
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEareriDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 156 AGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHE 217
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-205 |
5.77e-67 |
|
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: 206.48 E-value: 5.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-----PGKAKNKITVLLQ 80
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKdikkePEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 81 ENTIPNSLKVEELIaffqsisdnpltnqevqehlqfkedqyqqfadKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDT 160
Cdd:cd03230 81 EPSLYENLTVRENL--------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081348506 161 STRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:cd03230 129 ESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-233 |
1.21e-58 |
|
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: 187.76 E-value: 1.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPG-----KAKNKITVLL 79
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrkeprEARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 80 QENTIPNSLKVEELIAFFQSISDNPLTN-----QEVQEHLQFKEDQYQQfADKLSGGQRRLLAFVLCLIDKPKILFLDEP 154
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEElkkriEELIELLGLEEFLDRR-VGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348506 155 TAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHEEKEKQvtLPSSFVSIV 233
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEN--LEDAFVALI 236
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-217 |
9.52e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 164.88 E-value: 9.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-GKAKNKITVLL 79
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPpRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 80 QENTIPNS--LKVEELIA--------FFQSISDNplTNQEVQEHLQ------FKEDQYQQfadkLSGGQRR--LLAfvLC 141
Cdd:COG1121 82 QRAEVDWDfpITVRDVVLmgrygrrgLFRRPSRA--DREAVDEALErvgledLADRPIGE----LSGGQQQrvLLA--RA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348506 142 LIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHE 217
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPE 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-206 |
1.49e-49 |
|
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: 163.44 E-value: 1.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKG--KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-----PGKAKNKITVL 78
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 79 LQENTIPNSLKVEELIAFF---QSISDNplTNQEVQEHLqFKEDQYQQFADK----LSGGQRRLLAFVLCLIDKPKILFL 151
Cdd:cd03263 81 PQFDALFDELTVREHLRFYarlKGLPKS--EIKEEVELL-LRVLGLTDKANKrartLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 152 DEPTAGMDTSTRQRFWEIVNDLKKsGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-211 |
1.39e-48 |
|
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: 161.35 E-value: 1.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN------KITVLLQ-------EN 82
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlrelrrKVGLVFQnpddqlfAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 83 TipnslkVEELIAFfqsisdnPLTN---------QEVQEHLQF--KEDQYQQFADKLSGGQRRLLAF--VLCLidKPKIL 149
Cdd:COG1122 92 T------VEEDVAF-------GPENlglpreeirERVEEALELvgLEHLADRPPHELSGGQKQRVAIagVLAM--EPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 150 FLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-204 |
8.16e-48 |
|
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: 158.78 E-value: 8.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN------KITVLLQEntiPNS-- 87
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlkelrrKVGLVFQN---PDDqf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 88 --LKVEELIAFfqSISDNPLTNQEVQEHLQFKEDQY--QQFADK----LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMD 159
Cdd:cd03225 89 fgPTVEEEVAF--GLENLGLPEEEIEERVEEALELVglEGLRDRspftLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081348506 160 TSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGK 204
Cdd:cd03225 167 PAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-204 |
2.06e-45 |
|
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: 150.86 E-value: 2.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 7 QVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNkitvllqentipn 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 87 SLKVEELIAF-FQsisdnpltnqevqehlqfkedqyqqfadkLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQR 165
Cdd:cd00267 68 LEELRRRIGYvPQ-----------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRER 118
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081348506 166 FWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGK 204
Cdd:cd00267 119 LLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-211 |
1.31e-44 |
|
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: 151.73 E-value: 1.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGK-------AKnKITV 77
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAslsrrelAR-RIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 78 LLQENTIPNSLKVEELIA--------FFQSISDNplTNQEVQEHLQ------FKEDQYQQfadkLSGGQRRLLAFVLCLI 143
Cdd:COG1120 80 VPQEPPAPFGLTVRELVAlgryphlgLFGRPSAE--DREAVEEALErtglehLADRPVDE----LSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348506 144 DKPKILFLDEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-204 |
1.48e-43 |
|
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: 147.63 E-value: 1.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGK-----AKNKITVLL 79
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRdaredYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 80 QENTIPNSLKVEELIAFFQSISDNPLTNQEVQEHL-QFK-EDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAG 157
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREAIDEALeAVGlAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081348506 158 MDTSTRQRFWEIVNDLKKSGVTILYSSHyiEEVEHTADRILVLHQGK 204
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTH--QPLELAAARVLDLGDFK 206
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-211 |
1.88e-43 |
|
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: 149.03 E-value: 1.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 2 SETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP--GKAKNKITVL- 78
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitGLPPHRIARLg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 79 ----LQENTIPNSLKVEE-----------------LIAFFQSISDNPLTNQEVQEHLQF--KEDQYQQFADKLSGGQRRL 135
Cdd:COG0411 81 iartFQNPRLFPELTVLEnvlvaaharlgrgllaaLLRLPRARREEREARERAEELLERvgLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348506 136 LAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKK-SGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-219 |
1.91e-43 |
|
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: 148.35 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP--GKAKNKITVL----- 78
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitGLPPHEIARLgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 79 LQENTIPNSLKVEE------------LIAFFQSISDNPLTNQEVQEHLQF-----KEDQYqqfADKLSGGQRRLLAFVLC 141
Cdd:cd03219 81 FQIPRLFPELTVLEnvmvaaqartgsGLLLARARREEREARERAEELLERvgladLADRP---AGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348506 142 LIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHEEK 219
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-216 |
2.18e-43 |
|
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: 148.20 E-value: 2.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-----GKAKN-- 73
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitglsEKELYel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 74 --KITVLLQENTIPNSLKVEELIAFfqsisdnPLtnqevQEHLQFKEDQYQQ-------------FADK----LSGGQRR 134
Cdd:COG1127 81 rrRIGMLFQGGALFDSLTVFENVAF-------PL-----REHTDLSEAEIRElvleklelvglpgAADKmpseLSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 135 LLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYA 213
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEE 228
|
...
gi 1081348506 214 MRH 216
Cdd:COG1127 229 LLA 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-206 |
1.66e-42 |
|
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: 145.05 E-value: 1.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK----PGKAKNKITVLLQE 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKsyqkNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 82 NTIPNSLKVEELIAFFQSISDNPLTN-QEVQEHLQFKEDQYQQFAdKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDT 160
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRiDEVLDVVGLKDSAKKKVK-GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1081348506 161 STRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:cd03268 160 DGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-205 |
2.05e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 144.57 E-value: 2.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN------KITVLL 79
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 80 QENTI-PNSlkVEELIAFFQSISDNPLTNQEVQ---EHLQFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPT 155
Cdd:COG4619 81 QEPALwGGT--VRDNLPFPFQLRERKFDRERALellERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 156 AGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:COG4619 159 SALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-216 |
2.81e-42 |
|
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: 145.34 E-value: 2.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP---------GKAKNKIT 76
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisglseaelYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 77 VLLQENTIPNSLKVEELIAFfqsisdnPLtnqevQEHLQFKEDQYQQ-------------FADK----LSGGQRRLLAFV 139
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF-------PL-----REHTRLSEEEIREivlekleavglrgAEDLypaeLSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348506 140 LCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRH 216
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-211 |
4.94e-42 |
|
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: 144.05 E-value: 4.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG-----KPGKAKNKITVLLQ 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvrEPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 81 ENTIPNSLKVEELIAFFQSISDNP--LTNQEVQEHLQFKEdqYQQFADKL----SGGQRRLLAFVLCLIDKPKILFLDEP 154
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPgaERRERIDELLDFVG--LLEAADRLvktySGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348506 155 TAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-211 |
7.68e-42 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 144.87 E-value: 7.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN------KITVLL 79
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSpwelarRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 80 QENTIPNSLKVEELIAF--FQSISDNPLTNQEVQEHLQ------FKEDQYQQfadkLSGG--QRRLLAFVLCLI-----D 144
Cdd:COG4559 82 QHSSLAFPFTVEEVVALgrAPHGSSAAQDRQIVREALAlvglahLAGRSYQT----LSGGeqQRVQLARVLAQLwepvdG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081348506 145 KPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSG---VTILY----SSHYieevehtADRILVLHQGKLIRDTTP 211
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARRGggvVAVLHdlnlAAQY-------ADRILLLHQGRLVAQGTP 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-208 |
1.47e-41 |
|
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: 142.72 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGdCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG-----KPGKAKNKITVLLQ 80
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 81 ENTIPNSLKVEEL---IAFFQSISDN--PLTNQEVQEHLQFkEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPT 155
Cdd:cd03264 80 EFGVYPNFTVREFldyIAWLKGIPSKevKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 156 AGMDTSTRQRFWEIVNDLKKSGVTILySSHYIEEVEHTADRILVLHQGKLIRD 208
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGEDRIVIL-STHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
17-200 |
1.21e-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: 140.36 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-GKAKNKITVLLQENTIPNS--LKVEEL 93
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPlEKERKRIGYVPQRRSIDRDfpISVRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 94 IA--------FFQSISDnpLTNQEVQEHLQF-----KEDqyQQFaDKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDT 160
Cdd:cd03235 91 VLmglyghkgLFRRLSK--ADKAKVDEALERvglseLAD--RQI-GELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1081348506 161 STRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVL 200
Cdd:cd03235 166 KTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-204 |
5.61e-40 |
|
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: 137.32 E-value: 5.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP--------GKAKNKITV 77
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdledelPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 78 LLQENTIPNSLKVEELIAFfqsisdnpltnqevqehlqfkedqyqqfadKLSGGQRRLLAFVLCLIDKPKILFLDEPTAG 157
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081348506 158 MDTSTRQRFWEIVNDLKK-SGVTILYSSHYIEEVEHTADRILVLHQGK 204
Cdd:cd03229 131 LDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
21-282 |
7.24e-40 |
|
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: 140.99 E-value: 7.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG-----KPGKAKNKITVLLQENTIPNSLKVEE--- 92
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvvrEPRKVRRSIGIVPQYASVDEDLTGREnle 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 93 LIAFFQSISDNpLTNQEVQEHLQFKEDQYqqFADKL----SGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWE 168
Cdd:TIGR01188 89 MMGRLYGLPKD-EAEERAEELLELFELGE--AADRPvgtySGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 169 IVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIR------------DTTPYAMRHEEKEKQVTLPSSFVSIVHGL 236
Cdd:TIGR01188 166 YIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAegtpeelkrrlgKDTLESRPRDIQSLKVEVSMLIAELGETG 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1081348506 237 EDIYEVTEKRDVISFMTKDIEK----VWQSLEEEGCGISDIEIQNKTLLD 282
Cdd:TIGR01188 246 LGLLAVTVDSDRIKILVPDGDEtvpeIVEAAIRNGIRIRSISTERPSLDD 295
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-206 |
7.28e-40 |
|
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: 138.79 E-value: 7.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGK----TILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNKITVLLQ 80
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 81 ENTI------PNS-----LKVEELIA---FFQSISDNPLTNQEVQ----EHLQFKEDQYQQFADKLSGGQRRLLAFVLCL 142
Cdd:cd03257 81 RKEIqmvfqdPMSslnprMTIGEQIAeplRIHGKLSKKEARKEAVllllVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 143 IDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-211 |
7.83e-39 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 136.83 E-value: 7.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 4 TVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK------PGKAKNKITV 77
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwsPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 78 LLQENTIPNSLKVEELIAFfqSISDNPLTNQEVQEHLQ----------FKEDQYQQfadkLSGG--QRRLLAFVLCLI-- 143
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAM--GRAPHGLSRAEDDALVAaalaqvdlahLAGRDYPQ----LSGGeqQRVQLARVLAQLwe 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348506 144 --DKPKILFLDEPTAGMDTSTRQRFWEIVNDL-KKSGVT---ILY----SSHYieevehtADRILVLHQGKLIRDTTP 211
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAvivVLHdlnlAARY-------ADRIVLLHQGRLVADGTP 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-208 |
1.56e-38 |
|
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: 133.71 E-value: 1.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 7 QVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-----GKAKNK-ITVLLQ 80
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslsPKELARkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 81 entIPNSLKVEELIaffqsisdnpltnqevqehlqfkedqyQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDT 160
Cdd:cd03214 81 ---ALELLGLAHLA---------------------------DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1081348506 161 STRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLIRD 208
Cdd:cd03214 131 AHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-206 |
1.84e-38 |
|
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: 134.72 E-value: 1.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP--GKAKNKITVLLQENT 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPldIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 84 IPNSLKVEELIAFFQSISDnpLTNQEVQ-------EHLQFKEDQYQQFaDKLSGGQRRLLAFVLCLIDKPKILFLDEPTA 156
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKG--LKKEEARrridewlERLELSEYANKRV-EELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1081348506 157 GMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-228 |
5.21e-38 |
|
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: 135.27 E-value: 5.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK---PGKAKN------KITVLLQ-------E 81
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRditAKKKKKlkdlrkKVGLVFQfpehqlfE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 82 NTipnslkVEELIAFfqsisdNP----LTNQEVQE-------HLQFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILF 150
Cdd:TIGR04521 98 ET------VYKDIAF------GPknlgLSEEEAEErvkealeLVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 151 LDEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAM-RHEE--KEKQVTLP 226
Cdd:TIGR04521 166 LDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVfSDVDelEKIGLDVP 245
|
..
gi 1081348506 227 SS 228
Cdd:TIGR04521 246 EI 247
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-229 |
2.92e-37 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 132.40 E-value: 2.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-------GKAKNKITV 77
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDithlpmhERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 78 LLQENTIPNSLKVEE-LIAFFQSISDNPLTNQEVQEHLQFKEDQYQQFADK----LSGGQRRLLAFVLCLIDKPKILFLD 152
Cdd:TIGR04406 81 LPQEASIFRKLTVEEnIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNkamsLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348506 153 EPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHEEKEKQVTLPSSF 229
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLGEQF 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-225 |
1.13e-36 |
|
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: 130.36 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-------GKAKNKITVL 78
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 79 LQENTIPNSLKVEE-LIAFFQSIsdnPLTNQEVQEHLQFKEDQYQ------QFADKLSGGQRRLLAFVLCLIDKPKILFL 151
Cdd:cd03218 81 PQEASIFRKLTVEEnILAVLEIR---GLSKKEREEKLEELLEEFHithlrkSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081348506 152 DEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHEEKEKQVTL 225
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYL 231
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-251 |
1.14e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 132.15 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP--GKAKNKITVLLQEN 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPldPEDRRRIGYLPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 83 TIPNSLKVEELIAFFQSISDnpLTNQEVQEHLQ--FK----EDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTA 156
Cdd:COG4152 81 GLYPKMKVGEQLVYLARLKG--LSKAEAKRRADewLErlglGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 157 GMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHEEKEKQVTL-PSSFVSIVHG 235
Cdd:COG4152 159 GLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLeADGDAGWLRA 238
|
250
....*....|....*.
gi 1081348506 236 LEDIYEVTEKRDVISF 251
Cdd:COG4152 239 LPGVTVVEEDGDGAEL 254
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-206 |
1.27e-36 |
|
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: 128.32 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGkaknkitvllqenTIP 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV-------------SFA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 86 NSLKVEEL-IAFFqsisdnpltnqevqehlqfkedqYQqfadkLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQ 164
Cdd:cd03216 68 SPRDARRAgIAMV-----------------------YQ-----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1081348506 165 RFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:cd03216 120 RLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-204 |
3.77e-36 |
|
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: 127.11 E-value: 3.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKA------KNKITVLLQENTIpnslk 89
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDldleslRKNIAYVPQDPFL----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 90 veeliaFFQSISDNpLtnqevqehlqfkedqyqqfadkLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEI 169
Cdd:cd03228 88 ------FSGTIREN-I----------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEA 138
|
170 180 190
....*....|....*....|....*....|....*
gi 1081348506 170 VNDLKKsGVTILYSSHYIEEVEHtADRILVLHQGK 204
Cdd:cd03228 139 LRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-206 |
4.83e-36 |
|
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: 128.64 E-value: 4.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKR--IKGKTI--LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG-----KPGKAKNKIT 76
Cdd:cd03266 2 ITADALTKRfrDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 77 VLLQENTIPNSLKVEELIAFFQSISDNPLTNQ-----EVQEHLQFKEdqyqqFADK----LSGGQRRLLAFVLCLIDKPK 147
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELtarleELADRLGMEE-----LLDRrvggFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348506 148 ILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-211 |
6.83e-36 |
|
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: 134.65 E-value: 6.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKR-----IKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNKI 75
Cdd:COG1123 256 AAEPLLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 TVLLQENTI------PNS-----LKVEELIAFfqsisdnPLTN----------QEVQEHLQF---KEDQYQQFADKLSGG 131
Cdd:COG1123 336 SLRELRRRVqmvfqdPYSslnprMTVGDIIAE-------PLRLhgllsraerrERVAELLERvglPPDLADRYPHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 132 QRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLIRDTT 210
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
.
gi 1081348506 211 P 211
Cdd:COG1123 489 T 489
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-215 |
1.67e-35 |
|
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: 128.00 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 10 SLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN------KITVLLQEnt 83
Cdd:COG1124 10 SYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRrkafrrRVQMVFQD-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 84 iP-NSL----KVEELIAFFQSISDNPLTNQEVQEHLQ---FKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPT 155
Cdd:COG1124 88 -PyASLhprhTVDRILAEPLRIHGLPDREERIAELLEqvgLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 156 AGMDTSTRQRFWEIVNDLKK-SGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMR 215
Cdd:COG1124 167 SALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-214 |
4.14e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 128.38 E-value: 4.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-----GKAKNKI 75
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPvpsraRHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 TVLLQ-ENTIPNSLKVEELIAFFQSISDNPLTNQE-VQEHLQFKedQYQQFAD----KLSGGQRRLLAFVLCLIDKPKIL 149
Cdd:PRK13537 83 GVVPQfDNLDPDFTVRENLLVFGRYFGLSAAAARAlVPPLLEFA--KLENKADakvgELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 150 FLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAM 214
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-218 |
6.14e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 128.80 E-value: 6.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-----GKAKNKI 75
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPvparaRLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 TVLLQENTIPNSLKVEE-LIAFFQSISDNPLTNQEV-QEHLQFK--EDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFL 151
Cdd:PRK13536 117 GVVPQFDNLDLEFTVREnLLVFGRYFGMSTREIEAViPSLLEFArlESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348506 152 DEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHEE 218
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-211 |
1.51e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 125.55 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 4 TVIQVTSLGKRIK-GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-----GKAKNK--- 74
Cdd:COG3638 1 PMLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtalrGRALRRlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 75 -ITVLLQENTIPNSLKVEE--LIA------FFQSISdNPLTNQEVQEHLQFKE-----DQYQQFADKLSGGQRRLLAFVL 140
Cdd:COG3638 81 rIGMIFQQFNLVPRLSVLTnvLAGrlgrtsTWRSLL-GLFPPEDRERALEALErvglaDKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348506 141 CLIDKPKILFLDEPTAGMD-TSTRQrfweIVNDLKK----SGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:COG3638 160 ALVQEPKLILADEPVASLDpKTARQ----VMDLLRRiareDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPP 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-217 |
2.01e-34 |
|
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: 124.47 E-value: 2.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-------GKAKNKITVLLQENTIPNSLKVEE 92
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDitglpphERARAGIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 93 ---LIAFFQSISDNPLTNQEVQEHLQFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEI 169
Cdd:cd03224 95 nllLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081348506 170 VNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHE 217
Cdd:cd03224 175 IRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-209 |
2.31e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 124.39 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKR-IKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-GKAKN--------K 74
Cdd:COG2884 1 MIRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlSRLKRreipylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 75 ITVLLQE-NTIPNsLKVEELIAFfqsisdnPLTNQEVQEHLQFK-----------EDQYQQFADKLSGGQRRLLAFVLCL 142
Cdd:COG2884 81 IGVVFQDfRLLPD-RTVYENVAL-------PLRVTGKSRKEIRRrvrevldlvglSDKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348506 143 IDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDT 209
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
17-218 |
3.58e-34 |
|
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: 131.11 E-value: 3.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKA------KNKITVLLQENTIpnslkv 90
Cdd:COG2274 487 SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQidpaslRRQIGVVLQDVFL------ 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 91 eeliaFFQSISDN------PLTNQEVQEHLQ------FKE---DQYQQ----FADKLSGGQRRLLAFVLCLIDKPKILFL 151
Cdd:COG2274 561 -----FSGTIRENitlgdpDATDEEIIEAARlaglhdFIEalpMGYDTvvgeGGSNLSGGQRQRLAIARALLRNPRILIL 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348506 152 DEPTAGMDTSTRQRFWEIVNDLKKsGVTILYSSHYIEEVEHtADRILVLHQGKLIRDTTpyamrHEE 218
Cdd:COG2274 636 DEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGT-----HEE 695
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-206 |
1.16e-33 |
|
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: 122.24 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP----GKAKNKITVLLQE 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 82 NTIPNSLKVEELIAFfqsisdnPLTNQEV---QEHLQFKE--------DQYQQFADKLSGGQRRLLAFVLCLIDKPKILF 150
Cdd:cd03259 81 YALFPHLTVAENIAF-------GLKLRGVpkaEIRARVREllelvgleGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348506 151 LDEPTAGMDTSTRQRFW-EIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:cd03259 154 LDEPLSALDAKLREELReELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-211 |
4.17e-33 |
|
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: 121.52 E-value: 4.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIK-GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPG---------KAKNKI 75
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgkalrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 TVLLQENTIPNSLKVEELI--------AFFQSISdNPLTNQEVQEHLQFKE-----DQYQQFADKLSGGQRRLLAFVLCL 142
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgrrSTWRSLF-GLFPKEEKQRALAALErvgllDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 143 IDKPKILFLDEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPP 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
17-208 |
4.86e-33 |
|
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: 121.34 E-value: 4.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQV--LIDGKPGKA-----KNKITVL---LQENtIPN 86
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrLFGERRGGEdvwelRKRIGLVspaLQLR-FPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 87 SLKVEELI--AFFQSI--SDNPLTNQEVQ-----EHLQFKEDQYQQFADkLSGGQRRLlafVLC---LIDKPKILFLDEP 154
Cdd:COG1119 94 DETVLDVVlsGFFDSIglYREPTDEQRERarellELLGLAHLADRPFGT-LSQGEQRR---VLIaraLVKDPELLILDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 155 TAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRD 208
Cdd:COG1119 170 TAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-205 |
5.66e-33 |
|
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: 120.59 E-value: 5.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-----GKA----KNKITVLLQENTIPNS 87
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrGRAipylRRKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 88 LKVEELIAFFQSISDNP--LTNQEVQEHLQFK--EDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTR 163
Cdd:cd03292 93 RNVYENVAFALEVTGVPprEIRKRVPAALELVglSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1081348506 164 QRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:cd03292 173 WEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-211 |
6.29e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 120.90 E-value: 6.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 3 ETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-------GKAKNKI 75
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithlpmhKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 TVLLQENTIPNSLKVEE-LIAFFQSIsdnPLTNQEVQEHLqfkEDQYQQF---------ADKLSGGQRRLLAFVLCLIDK 145
Cdd:COG1137 81 GYLPQEASIFRKLTVEDnILAVLELR---KLSKKEREERL---EELLEEFgithlrkskAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348506 146 PKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTP 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-211 |
7.28e-33 |
|
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: 126.17 E-value: 7.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 3 ETVIQVTSLGKRIKG--KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPS---SGQVLIDGK------PGKA 71
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRdllelsEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 72 KNKITVLLQE-NTIPNSLKVEELIAFFQSISDNPLTN--QEVQEHLQF--KEDQYQQFADKLSGGQRRLLAFVLCLIDKP 146
Cdd:COG1123 82 GRRIGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEarARVLELLEAvgLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348506 147 KILFLDEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-200 |
7.50e-33 |
|
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: 120.27 E-value: 7.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKR----IKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN-KITVLLQ 80
Cdd:cd03293 1 LEVRNVSKTygggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGpDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 81 ENTIPNSLKVEELIAF---FQSISDnpltnQEVQEHLQ--FKEDQYQQFADK----LSGGQRRLLAFVLCLIDKPKILFL 151
Cdd:cd03293 81 QDALLPWLTVLDNVALgleLQGVPK-----AEARERAEelLELVGLSGFENAyphqLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1081348506 152 DEPTAGMDTSTRQRFW-EIVNDLKKSGVTILYSSHYIEEVEHTADRILVL 200
Cdd:cd03293 156 DEPFSALDALTREQLQeELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-205 |
8.34e-33 |
|
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: 119.90 E-value: 8.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKG----KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-------GKAK-- 72
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDisklsekELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 73 -NKITVLLQE-NTIPNsLKVEELIAFFQSISDNPLTNQEVQ-----EHLQFkEDQYQQFADKLSGGQRRLLAFVLCLIDK 145
Cdd:cd03255 81 rRHIGFVFQSfNLLPD-LTALENVELPLLLAGVPKKERRERaeellERVGL-GDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 146 PKILFLDEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYiEEVEHTADRILVLHQGKL 205
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-208 |
8.79e-33 |
|
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: 120.51 E-value: 8.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-PGKAKNK----ITVLL-QENTIPNSLKVE 91
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKRRKKflrrIGVVFgQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 92 ELIAFFQSISDNP-----LTNQEVQEHLQFKEDQYQQfADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRF 166
Cdd:cd03267 114 DSFYLLAAIYDLPparfkKRLDELSELLDLEELLDTP-VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081348506 167 WEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRD 208
Cdd:cd03267 193 RNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-206 |
1.39e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.13 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 2 SETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK------PGKAKNK- 74
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsPRDAQAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 75 ITVLLQE-NTIPNsLKVEELIAFFQSISDNPLTN--------QEVQEHLQFKEDQYQQFADkLSGGQRRLLAFVLCLIDK 145
Cdd:COG1129 81 IAIIHQElNLVPN-LSVAENIFLGREPRRGGLIDwramrrraRELLARLGLDIDPDTPVGD-LSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 146 PKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-211 |
1.91e-32 |
|
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: 119.71 E-value: 1.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRI-KGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG---------KPGKAKNK 74
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtditklrgkKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 75 ITVLLQE-NTIPNSLKVEELI-------AFFQSISdNPLTNQEVQEHLQFKE-----DQYQQFADKLSGGQRRLLAFVLC 141
Cdd:TIGR02315 81 IGMIFQHyNLIERLTVLENVLhgrlgykPTWRSLL-GRFSEEDKERALSALErvglaDKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 142 LIDKPKILFLDEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAP 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-211 |
5.03e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.77 E-value: 5.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG--------KPGKAKNKITVLLQ-------EN 82
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvKLSDIRKKVGLVFQypeyqlfEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 83 TIpnslkvEELIAFFQS---ISDNPLTNQeVQEHLQFKEDQYQQFADK----LSGGQRRLLAFVLCLIDKPKILFLDEPT 155
Cdd:PRK13637 100 TI------EKDIAFGPInlgLSEEEIENR-VKRAMNIVGLDYEDYKDKspfeLSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348506 156 AGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-205 |
6.42e-32 |
|
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: 116.55 E-value: 6.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKG--KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG------KPGKAKNKITV 77
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisqwDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 78 LLQEntipnslkvEELiaFFQSISDNpltnqevqehlqfkedqyqqfadKLSGGQRRLLAFVLCLIDKPKILFLDEPTAG 157
Cdd:cd03246 81 LPQD---------DEL--FSGSIAEN-----------------------ILSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081348506 158 MDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEhTADRILVLHQGKL 205
Cdd:cd03246 127 LDVEGERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-212 |
7.73e-32 |
|
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: 117.72 E-value: 7.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP----GKAKNKITVLLQE 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 82 NTIPNSLKVEELIAFFQSISDNP--LTNQEVQEHLQF--KEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAG 157
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPkaEIKERVAEALDLvqLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348506 158 MDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPY 212
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPE 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-156 |
1.59e-31 |
|
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: 114.67 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN------KITVLLQENTIPNSLKVEELI 94
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDErkslrkEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 95 AFFQSISDNPLTNQEVQ-----EHLQFKEDQYQ---QFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTA 156
Cdd:pfam00005 81 RLGLLLKGLSKREKDARaeealEKLGLGDLADRpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-206 |
1.84e-31 |
|
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: 116.90 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCI-----LGDKKPSSGQVLIDGKPGKAKN------- 73
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 74 -KITVLLQE-NTIPNSlkVEELIAF---FQSISDNPLTNQEVQEHLQ----FKEDQYQQFADKLSGGQRRLLAFVLCLID 144
Cdd:cd03260 81 rRVGMVFQKpNPFPGS--IYDNVAYglrLHGIKLKEELDERVEEALRkaalWDEVKDRLHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 145 KPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSgVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-212 |
2.43e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 119.43 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPgkaknkITVLLQ 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD------VTGLPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 81 E----NTI-------PNsLKVEELIAFfqsisdnPLTN---------QEVQE-----HLQFKEDQYqqfADKLSGGQR-- 133
Cdd:COG3842 75 EkrnvGMVfqdyalfPH-LTVAENVAF-------GLRMrgvpkaeirARVAEllelvGLEGLADRY---PHQLSGGQQqr 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 134 ----RLLAFvlclidKPKILFLDEPTAGMDTSTRQRF-WEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRD 208
Cdd:COG3842 144 valaRALAP------EPRVLLLDEPLSALDAKLREEMrEELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQV 217
|
....
gi 1081348506 209 TTPY 212
Cdd:COG3842 218 GTPE 221
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-212 |
4.04e-31 |
|
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: 115.79 E-value: 4.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKA------KNKITVLLQENTIpnslk 89
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDisrkslRSMIGVVLQDTFL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 90 veeliaFFQSISDN-----PLTNQEVQEHLQfKEDQYQQFADK---------------LSGGQRRLLAFVLCLIDKPKIL 149
Cdd:cd03254 89 ------FSGTIMENirlgrPNATDEEVIEAA-KEAGAHDFIMKlpngydtvlgenggnLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 150 FLDEPTAGMDTSTRQRFWEIVNDLKKsGVTILYSSHYIEEVEHtADRILVLHQGKLIRDTTPY 212
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHD 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
24-206 |
5.46e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 115.62 E-value: 5.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 24 ISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK------PgkAKNKITVLLQENTIPNSLKVEELIAFf 97
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalpP--AERPVSMLFQENNLFPHLTVAQNIGL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 98 qSISDN-PLTNQE------------VQEHLQFKEDQyqqfadkLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQ 164
Cdd:COG3840 95 -GLRPGlKLTAEQraqveqalervgLAGLLDRLPGQ-------LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081348506 165 RFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:COG3840 167 EMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-200 |
6.01e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 116.34 E-value: 6.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKR----IKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN-KI 75
Cdd:COG1116 3 AAAPALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGpDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 TVLLQENTIPNSLKVEELIAFFQSISDNPLT--NQEVQEHLqfkeDQY--QQFADK----LSGGQRRLLAFVLCLIDKPK 147
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGLELRGVPKAerRERARELL----ELVglAGFEDAyphqLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1081348506 148 ILFLDEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVL 200
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-206 |
6.72e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 118.33 E-value: 6.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSetvIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPgkakNKITVLLQ 80
Cdd:COG1118 1 MS---IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD----LFTNLPPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 81 ENTI----------PNsLKVEELIAFFqsISDNPLTNQE----VQEHLqfKEDQYQQFADK----LSGGQR------RLL 136
Cdd:COG1118 74 ERRVgfvfqhyalfPH-MTVAENIAFG--LRVRPPSKAEirarVEELL--ELVQLEGLADRypsqLSGGQRqrvalaRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081348506 137 AfVlclidKPKILFLDEPTAGMDTSTRQ--RFW--EIvndLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:COG1118 149 A-V-----EPEVLLLDEPFGALDAKVRKelRRWlrRL---HDELGGTTVFVTHDQEEALELADRVVVMNQGRIE 213
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-211 |
7.48e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 115.95 E-value: 7.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-----PGK--AKnKITVL 78
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattPSRelAK-RLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 79 LQENTIPNSLKVEELIAF--FqsisdnP-----LT---NQEVQEHLQFK--EDQYQQFADKLSGGQRR--LLAFVLCliD 144
Cdd:COG4604 81 RQENHINSRLTVRELVAFgrF------PyskgrLTaedREIIDEAIAYLdlEDLADRYLDELSGGQRQraFIAMVLA--Q 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 145 KPKILFLDEPTAGMD----TSTRQRFWEIVNDLKKSGVTIL----YSSHYieevehtADRILVLHQGKLIRDTTP 211
Cdd:COG4604 153 DTDYVLLDEPLNNLDmkhsVQMMKLLRRLADELGKTVVIVLhdinFASCY-------ADHIVAMKDGRVVAQGTP 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-222 |
8.12e-31 |
|
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: 115.08 E-value: 8.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP--GKAKNKIT----VLLQE--NTIPNsLKVE 91
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDitGLPPHRIArlgiGYVPEgrRIFPS-LTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 92 E-LIAFFQSISDNPLTNQEVQEHLQF----KEDQYQQfADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRF 166
Cdd:COG0410 97 EnLLLGAYARRDRAEVRADLERVYELfprlKERRRQR-AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348506 167 WEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHEEKEKQ 222
Cdd:COG0410 176 FEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVRE 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-206 |
1.21e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 120.17 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 4 TVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVlidgKPGKaKNKITVLLQENT 83
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----KLGE-TVKIGYFDQHQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 84 ipnSLKVEE-LIAFFQSISDNpLTNQEVQEHLQ---FKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMD 159
Cdd:COG0488 389 ---ELDPDKtVLDELRDGAPG-GTEQEVRGYLGrflFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1081348506 160 TSTRqrfwEIVND-LKK-SGvTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:COG0488 465 IETL----EALEEaLDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-280 |
1.59e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 116.73 E-value: 1.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-PGKAKNK----ITVLL-QENT----IP--NSL 88
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvPFKRRKEfarrIGVVFgQRSQlwwdLPaiDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 89 kveELIAFFQSISDNPLTN--QEVQEHLQFkEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRF 166
Cdd:COG4586 118 ---RLLKAIYRIPDAEYKKrlDELVELLDL-GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 167 WEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHE-EKEKQVTL----PSSFVSIVHGLEdIY 240
Cdd:COG4586 194 REFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERfGPYKTIVLelaePVPPLELPRGGE-VI 272
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1081348506 241 EVTEKRDVISFMTKD-IEKVWQSLEEEgCGISDIEIQNKTL 280
Cdd:COG4586 273 EREGNRVRLEVDPREsLAEVLARLLAR-YPVRDLTIEEPPI 312
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-218 |
3.36e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 114.32 E-value: 3.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP--GKAKNKITVL 78
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 79 LQENTIPNslkveelIAFFQSISdnPLTNQEVQEHLQ---------FKEDQYQQ--------------------FADK-- 127
Cdd:PRK11300 81 GVVRTFQH-------VRLFREMT--VIENLLVAQHQQlktglfsglLKTPAFRRaesealdraatwlervglleHANRqa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 128 --LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGK 204
Cdd:PRK11300 152 gnLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
250
....*....|....
gi 1081348506 205 LIRDTTPYAMRHEE 218
Cdd:PRK11300 232 PLANGTPEEIRNNP 245
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-211 |
4.33e-30 |
|
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: 113.59 E-value: 4.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN----KITVLLQE 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPvqerNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 82 NTIPNSLKVEELIAF---FQSISDNP---LTNQEVQEHLQFKedQYQQFADK----LSGGQRRLLAFVLCLIDKPKILFL 151
Cdd:cd03296 83 YALFRHMTVFDNVAFglrVKPRSERPpeaEIRAKVHELLKLV--QLDWLADRypaqLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081348506 152 DEPTAGMDTSTRQ--RFW--EIVNDLkksGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:cd03296 161 DEPFGALDAKVRKelRRWlrRLHDEL---HVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-206 |
5.78e-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: 112.88 E-value: 5.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN--KITVLLQENT 83
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDlhKIGSLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 84 IPNSLKVEE---LIAFFQSISDnpltnQEVQEHLQFK--EDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGM 158
Cdd:TIGR03740 81 LYENLTAREnlkVHTTLLGLPD-----SRIDEVLNIVdlTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081348506 159 DTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:TIGR03740 156 DPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
17-211 |
6.40e-30 |
|
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: 118.32 E-value: 6.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKA------KNKITVLLQENTIpnslkv 90
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDldpaswRRQIAWVPQNPYL------ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 91 eeliaFFQSISDNPL------TNQEVQEHLQ------FKEDQYQQFADK-------LSGGQRRLLAFVLCLIDKPKILFL 151
Cdd:COG4988 423 -----FAGTIRENLRlgrpdaSDEELEAALEaagldeFVAALPDGLDTPlgeggrgLSGGQAQRLALARALLRDAPLLLL 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 152 DEPTAGMDTSTRQRFWEIVNDLKKsGVTILYSSHYIEEVEHtADRILVLHQGKLIRDTTP 211
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTH 555
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-206 |
6.90e-30 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 111.49 E-value: 6.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPS--SGQVLIDGKPGKA---KNKITVLLQENTIPNSLKV 90
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKrsfRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 91 EELIAFfqsisdnpltnqevQEHLQfkedqyqqfadKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIV 170
Cdd:cd03213 100 RETLMF--------------AAKLR-----------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1081348506 171 NDLKKSGVTILYSSHYI-EEVEHTADRILVLHQGKLI 206
Cdd:cd03213 155 RRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-205 |
1.62e-29 |
|
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: 110.21 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 3 ETVIQVtslgKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNKITVL---- 78
Cdd:cd03215 2 EPVLEV----RGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 79 -------LQENTIPNslkveeliaffQSISDNPLTNQEvqehlqfkedqyqqfadkLSGG--QRRLLAfvLCLIDKPKIL 149
Cdd:cd03215 78 ayvpedrKREGLVLD-----------LSVAENIALSSL------------------LSGGnqQKVVLA--RWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348506 150 FLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-209 |
5.08e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 110.13 E-value: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 3 ETVIQVTSLGKRIK-GK---TILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP--GKAKNKIT 76
Cdd:COG1136 2 SPLLELRNLTKSYGtGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDisSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 77 VLLQE---------NTIPNsLKVEELIAFFQSISDNPLT--NQEVQE-----HLqfkEDQYQQFADKLSGGQRRLLAFVL 140
Cdd:COG1136 82 RLRRRhigfvfqffNLLPE-LTALENVALPLLLAGVSRKerRERAREllervGL---GDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 141 CLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYiEEVEHTADRILVLHQGKLIRDT 209
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSDE 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
10-229 |
1.56e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 109.60 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 10 SLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-------GKAKNKITVLLQEN 82
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisllplhARARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 83 TIPNSLKV-EELIAFFQSISDnpLTNQEVQE---------HLQFKEDQYQQfadKLSGGQRRLLAFVLCLIDKPKILFLD 152
Cdd:PRK10895 88 SIFRRLSVyDNLMAVLQIRDD--LSAEQREDranelmeefHIEHLRDSMGQ---SLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348506 153 EPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHEEKEKQVTLPSSF 229
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGEDF 239
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-211 |
1.67e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.17 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNKI------TVLLQENTIPNSL- 88
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllevrkTVGIVFQNPDDQLf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 89 --KVEELIAFfqsisdNP----LTNQEVQEHLQ--FKEDQYQQFADK----LSGGQRRLLAFVLCLIDKPKILFLDEPTA 156
Cdd:PRK13639 93 apTVEEDVAF------GPlnlgLSKEEVEKRVKeaLKAVGMEGFENKpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 157 GMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
13-206 |
2.57e-28 |
|
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: 108.15 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 13 KRIKGKTIleDISFEINqGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP----------GKAKNKITVLLQEN 82
Cdd:cd03297 8 KRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlPPQQRKIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 83 TIPNSLKVEELIAF-FQSISDNPLTNQEVQ-------EHLQfkedqyQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEP 154
Cdd:cd03297 85 ALFPHLNVRENLAFgLKRKRNREDRISVDElldllglDHLL------NRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 155 TAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-223 |
4.14e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.56 E-value: 4.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKA------KNKITVLLQENTIPNSLKVE 91
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlssrqlARRLALLPQHHLTPEGITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 92 ELIAFFQS--------ISDNplTNQEVQEHLQfkEDQYQQFADK----LSGGQRR--LLAFVLCLiDKPkILFLDEPTAG 157
Cdd:PRK11231 95 ELVAYGRSpwlslwgrLSAE--DNARVNQAME--QTRINHLADRrltdLSGGQRQraFLAMVLAQ-DTP-VVLLDEPTTY 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348506 158 MDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHEEKEKQV 223
Cdd:PRK11231 169 LDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTV 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-205 |
5.17e-28 |
|
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: 107.23 E-value: 5.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-GKAKNKITVLLQE--- 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKlTDDKKNINELRQKvgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 82 -----NTIPNsLKVEELIAFFQsISDNPLTNQEVQEH-LQFKE-----DQYQQFADKLSGGQRRLLAFVLCLIDKPKILF 150
Cdd:cd03262 81 vfqqfNLFPH-LTVLENITLAP-IKVKGMSKAEAEERaLELLEkvglaDKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 151 LDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
16-206 |
1.02e-27 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 105.47 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPgkaknkitVLLQENTIpnslkvEELIA 95
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP--------VSDLEKAL------SSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 96 FFqsisdnpltNQEVqeHLqFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKK 175
Cdd:cd03247 79 VL---------NQRP--YL-FDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK 146
|
170 180 190
....*....|....*....|....*....|.
gi 1081348506 176 sGVTILYSSHYIEEVEHtADRILVLHQGKLI 206
Cdd:cd03247 147 -DKTLIWITHHLTGIEH-MDKILFLENGKII 175
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-206 |
1.15e-27 |
|
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: 106.85 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 9 TSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGkpgkaknKITVLLQENT-IPNS 87
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------RVSSLLGLGGgFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 88 LKVEELIAFFQSISDnpLTNQEVQEHLQFKED--QYQQFADK----LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTS 161
Cdd:cd03220 99 LTGRENIYLNGRLLG--LSRKEIDEKIDEIIEfsELGDFIDLpvktYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081348506 162 TRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:cd03220 177 FQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-211 |
1.36e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 109.92 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-----PgKAKNKITVLL 79
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvP-PYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 80 QENTIPNSLKVEELIAFfqSISDNPLTNQE----VQEHLQFKedQYQQFADK----LSGGQRRLLAFVLCLIDKPKILFL 151
Cdd:PRK11607 98 QSYALFPHMTVEQNIAF--GLKQDKLPKAEiasrVNEMLGLV--HMQEFAKRkphqLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 152 DEPTAGMDTSTRQRF-WEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:PRK11607 174 DEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-208 |
1.67e-27 |
|
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: 106.13 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG------KPGKAKNKITVLLQENTIpnslkveeli 94
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqlDPADLRRNIGYVPQDVTL---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 95 aFFQSISDN------PLTNQEVQEHLQFK-------------EDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPT 155
Cdd:cd03245 90 -FYGTLRDNitlgapLADDERILRAAELAgvtdfvnkhpnglDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 156 AGMDTSTRQRFWEIVNDLkKSGVTILYSSHYIEEVEhTADRILVLHQGKLIRD 208
Cdd:cd03245 169 SAMDMNSEERLKERLRQL-LGDKTLIIITHRPSLLD-LVDRIIVMDSGRIVAD 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-211 |
1.76e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 109.04 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 13 KRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGkpgkaknkitvllqENTIPNSLKVEE 92
Cdd:PRK11432 14 KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG--------------EDVTHRSIQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 93 LIAFFQ--------SISDN------------PLTNQEVQEHLQFK-----EDQYqqfADKLSGGQRRLLAFVLCLIDKPK 147
Cdd:PRK11432 80 ICMVFQsyalfphmSLGENvgyglkmlgvpkEERKQRVKEALELVdlagfEDRY---VDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 148 ILFLDEPTAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
26-222 |
3.76e-27 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 105.32 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 26 FEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-PGKAKNKITVLLQ--ENTIPNSLKVEELIAFFQSISD 102
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAsPGKGWRHIGYVPQrhEFAWDFPISVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 103 NPLTNQEVQEHLQ----FKEDQYQQFADK----LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLK 174
Cdd:TIGR03771 81 GWLRRPCVADFAAvrdaLRRVGLTELADRpvgeLSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081348506 175 KSGVTILYSSHYIEEVEHTADRILVLHqGKLIRDTTPYAMRHEEKEKQ 222
Cdd:TIGR03771 161 GAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQDPAPWMT 207
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-221 |
5.37e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 105.94 E-value: 5.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP--GKAKNKITVLL----QE---NTIPNsL 88
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtKLPEYKRAKYIgrvfQDpmmGTAPS-M 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 89 KVEE--LIAFF--QSISDNPLTNQEVQEHlqFK----------EDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEP 154
Cdd:COG1101 98 TIEEnlALAYRrgKRRGLRRGLTKKRREL--FRellatlglglENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348506 155 TAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDttpyaMRHEEKEK 221
Cdd:COG1101 176 TAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD-----VSGEEKKK 238
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-206 |
6.02e-27 |
|
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: 104.26 E-value: 6.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN---KITVLLQE-NTIPNSLKVE 91
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKErrkSIGYVMQDvDYQLFTDSVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 92 ELIAFfqSISDNPLTNQEVQEHLQfKEDQYQqFADK----LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFW 167
Cdd:cd03226 91 EELLL--GLKELDAGNEQAETVLK-DLDLYA-LKERhplsLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVG 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081348506 168 EIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:cd03226 167 ELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-207 |
1.04e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.00 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 8 VTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDgkPGKaknKITVLLQENTIPNS 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP--KGL---RIGYLPQEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 88 LKV------------------EELIAFFQSISDNPLTNQEVQEH-------------------LQFKEDQYQQFADKLSG 130
Cdd:COG0488 76 LTVldtvldgdaelraleaelEELEAKLAEPDEDLERLAELQEEfealggweaearaeeilsgLGFPEEDLDRPVSELSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 131 GQRRLLAfvLC--LIDKPKILFLDEPTAGMDTSTRQrfW-EivNDLKKSGVTILYSSH---YIEEVehtADRILVLHQGK 204
Cdd:COG0488 156 GWRRRVA--LAraLLSEPDLLLLDEPTNHLDLESIE--WlE--EFLKNYPGTVLVVSHdryFLDRV---ATRILELDRGK 226
|
...
gi 1081348506 205 LIR 207
Cdd:COG0488 227 LTL 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-206 |
1.17e-26 |
|
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: 104.34 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-----PGKAKNKITVLLQENTIPNsLKVEELIA 95
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlPPEKRDISYVPQNYALFPH-MTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 96 FFQSISDNPLTN--QEVQE--------HLqfkedqYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQR 165
Cdd:cd03299 94 YGLKKRKVDKKEieRKVLEiaemlgidHL------LNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1081348506 166 FWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:cd03299 168 LREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-211 |
1.94e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.01 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 12 GKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGkpgkaknKITVLLQENTIPN-SLKV 90
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------RVSALLELGAGFHpELTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 91 EELIAFFQSISDnpLTNQEVQEHLQFKEDqyqqFAD----------KLSGGQR-RlLAFVLCLIDKPKILFLDEPTAGMD 159
Cdd:COG1134 106 RENIYLNGRLLG--LSRKEIDEKFDEIVE----FAElgdfidqpvkTYSSGMRaR-LAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 160 TSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:COG1134 179 AAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-208 |
4.27e-26 |
|
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: 102.19 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 23 DISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG------KPgkAKNKITVLLQENTIPNSLKVEELIAF 96
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaaPP--ADRPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 97 FQS--ISDNPLTNQEV-----QEHLQFKEdqyQQFADKLSGGQRRLLAFVLCLI-DKPkILFLDEPTAGMDTSTRQRFWE 168
Cdd:cd03298 94 GLSpgLKLTAEDRQAIevalaRVGLAGLE---KRLPGELSGGERQRVALARVLVrDKP-VLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1081348506 169 IVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRD 208
Cdd:cd03298 170 LVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
21-208 |
4.40e-26 |
|
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: 107.64 E-value: 4.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG------KPGKAKNKITVLLQENTIpnslkveeli 94
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGvdirqiDPADLRRNIGYVPQDPRL---------- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 95 aFFQSISDN-----PLTNQE--------------VQEHLQFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPT 155
Cdd:TIGR03375 551 -FYGTLRDNialgaPYADDEeilraaelagvtefVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPT 629
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348506 156 AGMDTSTRQRFWEIVNDLkKSGVTILYSSHyieeveHTA-----DRILVLHQGKLIRD 208
Cdd:TIGR03375 630 SAMDNRSEERFKDRLKRW-LAGKTLVLVTH------RTSlldlvDRIIVMDNGRIVAD 680
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-206 |
4.64e-26 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 102.66 E-value: 4.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGK----RIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-----PGK----A 71
Cdd:cd03258 1 MIELKNVSKvfgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllSGKelrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 72 KNKITVLLQENTIPNSLKVEELIAFFQSISDNPLTNQE--VQEHLQF-----KEDQYqqfADKLSGGQRRLLAFVLCLID 144
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEerVLELLELvgledKADAY---PAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 145 KPKILFLDEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-205 |
5.01e-26 |
|
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: 101.95 E-value: 5.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-----PGKAKNkITVLLQ 80
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlPPKDRD-IAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 81 ENTIPNSLKVEELIAFFQSISDNPLTN-----QEVQEHLQFkEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPT 155
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEidervREVAELLQI-EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 156 AGMDTSTR-QRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:cd03301 159 SNLDAKLRvQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-188 |
5.04e-26 |
|
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: 101.35 E-value: 5.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP--------GKAKNKITVLLQEntiPNsl 88
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPldysrkglLERRQRVGLVFQD---PD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 89 kvEELIA--FFQSISDNPLT--------NQEVQEHLQFKEdqYQQFADK----LSGGQRRLLAFVLCLIDKPKILFLDEP 154
Cdd:TIGR01166 79 --DQLFAadVDQDVAFGPLNlglseaevERRVREALTAVG--ASGLRERpthcLSGGEKKRVAIAGAVAMRPDVLLLDEP 154
|
170 180 190
....*....|....*....|....*....|....
gi 1081348506 155 TAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIE 188
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRRLRAEGMTVVISTHDVD 188
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-211 |
5.49e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.65 E-value: 5.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK------PGKA-KN 73
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsPRDAiAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 74 KI-------------TVLlqENTIpnsLKVEELIAFFQSISDnplTNQEVQE-----HLQFKEDQYqqfADKLSGGQRRL 135
Cdd:COG3845 81 GIgmvhqhfmlvpnlTVA--ENIV---LGLEPTKGGRLDRKA---ARARIRElseryGLDVDPDAK---VEDLSVGEQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 136 LAFVLCLIDKPKILFLDEPTAGMdtsTRQ---RFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI-----R 207
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVL---TPQeadELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVgtvdtA 226
|
....
gi 1081348506 208 DTTP 211
Cdd:COG3845 227 ETSE 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-206 |
6.44e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 106.79 E-value: 6.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKA------KNKITVLLQENTIpnslk 89
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDltleslRRQIGVVPQDTFL----- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 90 veeliaFFQSISDN------PLTNQEVQEHLQ------F---KEDQYQ----QFADKLSGGQRRLLAFVLCLIDKPKILF 150
Cdd:COG1132 426 ------FSGTIRENirygrpDATDEEVEEAAKaaqaheFieaLPDGYDtvvgERGVNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348506 151 LDEPTAGMDTSTRQRFWEIVNDLKKsGVTILYSSHYIEEVEHtADRILVLHQGKLI 206
Cdd:COG1132 500 LDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRN-ADRILVLDDGRIV 553
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-211 |
1.11e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.99 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP----------GKAKNKITVLLQ-------ENT 83
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitpetgnknlKKLRKKVSLVFQfpeaqlfENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 84 IpnsLKVEELIAFFQSISDNPLTNQEVQ--EHLQFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTS 161
Cdd:PRK13641 103 V---LKDVEFGPKNFGFSEDEAKEKALKwlKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1081348506 162 TRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASP 229
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-206 |
1.53e-25 |
|
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: 101.06 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 19 TILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-------GKAKNKITVLLQENTIPNSLKVE 91
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDitklpphERARAGIAYVPQGREIFPRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 92 EliaffqsisdNPLTNQEVQ--EHLQFKEDQYQQF----------ADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMD 159
Cdd:TIGR03410 94 E----------NLLTGLAALprRSRKIPDEIYELFpvlkemlgrrGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQ 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081348506 160 TSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:TIGR03410 164 PSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVV 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-204 |
2.13e-25 |
|
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: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVlidgkpgkaknkitvllqenTIP 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------------------TWG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 86 NSLKveelIAFFqsisdnpltnqevqehlqfkedqyqqfaDKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQr 165
Cdd:cd03221 61 STVK----IGYF----------------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIE- 107
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081348506 166 fWeIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGK 204
Cdd:cd03221 108 -A-LEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-207 |
2.45e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.72 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 3 ETVIQVTSLGkrikGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK------PGKA-KNKI 75
Cdd:COG1129 254 EVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsPRDAiRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 tVLLQENTipnslKVEELIAFfQSISDN-PLTNQEVQEHLQF----KEDQY---------------QQFADKLSGG--QR 133
Cdd:COG1129 330 -AYVPEDR-----KGEGLVLD-LSIRENiTLASLDRLSRGGLldrrRERALaeeyikrlriktpspEQPVGNLSGGnqQK 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081348506 134 RLLAfvLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIR 207
Cdd:COG1129 403 VVLA--KWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-206 |
3.69e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 104.63 E-value: 3.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMScILGDKKPS---SGQVLIDGKPGKAKN---- 73
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMK-VLSGVYPHgtyEGEIIFEGEELQASNirdt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 74 ---KITVLLQENTIPNSLKVEELIAFFQSISDNPLTN--------QEVQEHLQFKEDQYQQFADkLSGGQRRLLAFVLCL 142
Cdd:PRK13549 80 eraGIAIIHQELALVKELSVLENIFLGNEITPGGIMDydamylraQKLLAQLKLDINPATPVGN-LGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081348506 143 IDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-211 |
5.12e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 102.72 E-value: 5.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-----PGKAKNKI 75
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 TVLLQENTIPNsLKVEELIAFFQSISDNPltNQEVQEHLQ--FKEDQYQQFADK----LSGGQRRLLAFVLCLIDKPKIL 149
Cdd:PRK09452 90 TVFQSYALFPH-MTVFENVAFGLRMQKTP--AAEITPRVMeaLRMVQLEEFAQRkphqLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348506 150 FLDEPTAGMDTSTRQrfwEIVNDLK----KSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:PRK09452 167 LLDESLSALDYKLRK---QMQNELKalqrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
16-211 |
5.16e-25 |
|
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: 100.07 E-value: 5.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN------KITVLLQENTIPNSLK 89
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDpvelrrKIGYVIQQIGLFPHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 90 VEELIAFFQSIS--DNPLTNQEVQEHLQFKEDQYQQFADK----LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTR 163
Cdd:cd03295 92 VEENIALVPKLLkwPKEKIRERADELLALVGLDPAEFADRypheLSGGQQQRVGVARALAADPPLLLMDEPFGALDPITR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1081348506 164 QRFWEIVNDLKK-SGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:cd03295 172 DQLQEEFKRLQQeLGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-218 |
7.83e-25 |
|
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: 99.23 E-value: 7.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG------KPGKAKNKITVLLQEnTIPNSLK 89
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdyTLASLRRQIGLVSQD-VFLFNDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 90 VEELIAFfqsiSDNPLTNQEV---------QEHLQFKEDQYQQF----ADKLSGGQRRLLAFVLCLIDKPKILFLDEPTA 156
Cdd:cd03251 92 VAENIAY----GRPGATREEVeeaaraanaHEFIMELPEGYDTVigerGVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 157 GMDTSTRQRFWEIVNDLKKsGVTILYSSHYIEEVEHtADRILVLHQGKLIRDTTpyamrHEE 218
Cdd:cd03251 168 ALDTESERLVQAALERLMK-NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGT-----HEE 222
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-205 |
8.26e-25 |
|
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: 99.08 E-value: 8.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKA------KNKITVLLQENTIpNSLKVEEL 93
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkylHSKVSLVGQEPVL-FARSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 94 IAF-FQSISDNPLTNQEVQEH----LQFKEDQYQQFADK----LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQ 164
Cdd:cd03248 108 IAYgLQSCSFECVKEAAQKAHahsfISELASGYDTEVGEkgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1081348506 165 RFWEIVNDLKKSgVTILYSSHYIEEVEHtADRILVLHQGKL 205
Cdd:cd03248 188 QVQQALYDWPER-RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-211 |
8.96e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.47 E-value: 8.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKG--KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN----- 73
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 74 -KITVLLQ--ENTIPNSlKVEELIAFfqSISDNPLTNQEVQEHLQFKEDQ--YQQFAD----KLSGGQRRLLAFVLCLID 144
Cdd:PRK13635 81 rQVGMVFQnpDNQFVGA-TVQDDVAF--GLENIGVPREEMVERVDQALRQvgMEDFLNrephRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348506 145 KPKILFLDEPTAGMDTSTRQRFWEIVNDLK-KSGVTILYSSHYIEEVEhTADRILVLHQGKLIRDTTP 211
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKeQKGITVLSITHDLDEAA-QADRVIVMNKGEILEEGTP 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-208 |
1.44e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.50 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 25 SFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGK----AKNKITVLLQENTIPNSLKVEELIAffqsI 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTttppSRRPVSMLFQENNLFSHLTVAQNIG----L 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 101 SDNP---LTNQEvQEHLQ------FKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVN 171
Cdd:PRK10771 95 GLNPglkLNAAQ-REKLHaiarqmGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1081348506 172 DL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRD 208
Cdd:PRK10771 174 QVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWD 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-200 |
2.68e-24 |
|
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: 97.89 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 3 ETVIQVTSLGKRIK-----GKTI--LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPG-----K 70
Cdd:COG4778 2 TTLLEVENLSKTFTlhlqgGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGwvdlaQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 71 AKNKITVLLQENTI---PNSLKV------EELIAffqsisdNPLTNQEVQE------------HLQFKEDQYQQFADKLS 129
Cdd:COG4778 82 ASPREILALRRRTIgyvSQFLRViprvsaLDVVA-------EPLLERGVDReearararellaRLNLPERLWDLPPATFS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 130 GG-QRRL-LAfvLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVL 200
Cdd:COG4778 155 GGeQQRVnIA--RGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-216 |
5.93e-24 |
|
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: 102.01 E-value: 5.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 23 DISFEINQgdCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKA-----KNKITVLLQENTIPNSLKVEELIAFF 97
Cdd:TIGR01257 950 NITFYENQ--ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETnldavRQSLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 98 QSISDNplTNQEVQEHLQ-FKED-----QYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVn 171
Cdd:TIGR01257 1028 AQLKGR--SWEEAQLEMEaMLEDtglhhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL- 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1081348506 172 dLK-KSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRH 216
Cdd:TIGR01257 1105 -LKyRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-205 |
1.10e-23 |
|
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: 95.70 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 25 SFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP----GKAKNKITVLLQENTIPNSLKVEELIAF--FQ 98
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQShtglAPYQRPVSMLFQENNLFAHLTVRQNIGLglHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 99 SISDNPLTNQEVQEHLQFK--EDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDL-KK 175
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVgiADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLcSE 177
|
170 180 190
....*....|....*....|....*....|
gi 1081348506 176 SGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-218 |
1.23e-23 |
|
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: 96.40 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG------KPGKAKNKITVLLQENTIPNSlKV 90
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlalaDPAWLRRQVGVVLQENVLFNR-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 91 EELIAffqsISDNPLTNQEVQE-------H---LQFKEDQYQQFADK---LSGGQRRLLAFVLCLIDKPKILFLDEPTAG 157
Cdd:cd03252 93 RDNIA----LADPGMSMERVIEaaklagaHdfiSELPEGYDTIVGEQgagLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 158 MDTSTRQrfwEIVNDLKK--SGVTILYSSHYIEEVEhTADRILVLHQGKLIRDTtpyamRHEE 218
Cdd:cd03252 169 LDYESEH---AIMRNMHDicAGRTVIIIAHRLSTVK-NADRIIVMEKGRIVEQG-----SHDE 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-207 |
1.34e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.85 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSL--GKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPgkaknkIT-- 76
Cdd:COG4525 1 MSMLTVRHVSVryPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP------VTgp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 77 -----VLLQENTIPNSLKVEELIAF---FQSISdnPLTNQEVQEHLQFK---EDQYQQFADKLSGGQRRLLAFVLCLIDK 145
Cdd:COG4525 75 gadrgVVFQKDALLPWLNVLDNVAFglrLRGVP--KAERRARAEELLALvglADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 146 PKILFLDEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVL--HQGKLIR 207
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-206 |
3.14e-23 |
|
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: 95.03 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTILEDISFEINQGDCVALIGPNGAGKTVLM---SCILGDKKPSSGQVLIDGKPGKA---KNKITVLLQENTIPNSLK 89
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLdaiSGRVEGGGTTSGQILFNGQPRKPdqfQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 90 VEELIAFfqsISDNPLTNQEVQEHLQFKEDQY--QQFADK---------LSGGQRRLLAFVLCLIDKPKILFLDEPTAGM 158
Cdd:cd03234 98 VRETLTY---TAILRLPRKSSDAIRKKRVEDVllRDLALTriggnlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1081348506 159 DTSTRQRFWEIVNDLKKSGVTILYSSHYI-EEVEHTADRILVLHQGKLI 206
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPrSDLFRLFDRILLLSSGEIV 223
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-206 |
3.29e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 95.57 E-value: 3.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP--GKAKNKITVL 78
Cdd:COG4674 6 MHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDltGLDEHEIARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 79 -----LQENTIPNSLKVEE--LIAF------FQSIS--DNPLTNQEVQEHLQ--FKEDQYQQFADKLSGGQRRLLAFVLC 141
Cdd:COG4674 86 gigrkFQKPTVFEELTVFEnlELALkgdrgvFASLFarLTAEERDRIEEVLEtiGLTDKADRLAGLLSHGQKQWLEIGML 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 142 LIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGvTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:COG4674 166 LAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKH-SVVVVEHDMEFVRQIARKVTVLHQGSVL 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-211 |
5.27e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.64 E-value: 5.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN-----KITVLLQENTIPN--SLKV 90
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENirevrKFVGLVFQNPDDQifSPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 91 EELIAF--FQSISDNPLTNQEVQE--HLQFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRF 166
Cdd:PRK13652 97 EQDIAFgpINLGLDEETVAHRVSSalHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKEL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1081348506 167 WEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:PRK13652 177 IDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTV 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
6.95e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.30 E-value: 6.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIK-GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNKITVLL 79
Cdd:PRK13636 1 MEDYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 80 QENtipnslkveeLIAFFQSiSDNPLTNQEVQE-------HLQFKEDQYQQFADK-----------------LSGGQRRL 135
Cdd:PRK13636 81 RES----------VGMVFQD-PDNQLFSASVYQdvsfgavNLKLPEDEVRKRVDNalkrtgiehlkdkpthcLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 136 LAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP--- 211
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPkev 229
|
250
....*....|....*
gi 1081348506 212 YAMRHEEKEKQVTLP 226
Cdd:PRK13636 230 FAEKEMLRKVNLRLP 244
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-211 |
1.36e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 93.62 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG---KPGKAKNKI------ 75
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvNDPKVDERLirqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 TVLLQENTIPNSLKVEELIafFQSISDNPLTNQEVQEhlQFKE--------DQYQQFADKLSGGQRRLLAFVLCLIDKPK 147
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVM--FGPLRVRGASKEEAEK--QAREllakvglaERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081348506 148 ILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDP 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-205 |
1.65e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.04 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 23 DISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG------KPGKAKNKITVLLQENTIPNSLKVEELIAF 96
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGkeinalSTAQRLARGLVYLPEDRQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 97 FQS---ISDNPLTNQEVQEH---------LQFKEDQYQQFADKLSGG--QRRLLAfvLCLIDKPKILFLDEPTAGMDTST 162
Cdd:PRK15439 361 NVCaltHNRRGFWIKPARENavleryrraLNIKFNHAEQAARTLSGGnqQKVLIA--KCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081348506 163 RQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-205 |
4.16e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 94.37 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSEtvIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPgkaknkitVllq 80
Cdd:COG3839 1 MAS--LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD--------V--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 81 entipNSLKVEEL-IAF-FQS--------ISDN---PLTN---------QEVQE-----HLqfkEDQYQQFADKLSGGQR 133
Cdd:COG3839 68 -----TDLPPKDRnIAMvFQSyalyphmtVYENiafPLKLrkvpkaeidRRVREaaellGL---EDLLDRKPKQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 134 ------RllafvlCLIDKPKILFLDEPTAGMD----TSTRQrfwEIVNDLKKSGVTILYSSHyiEEVE-HT-ADRILVLH 201
Cdd:COG3839 140 qrvalgR------ALVREPKVFLLDEPLSNLDaklrVEMRA---EIKRLHRRLGTTTIYVTH--DQVEaMTlADRIAVMN 208
|
....
gi 1081348506 202 QGKL 205
Cdd:COG3839 209 DGRI 212
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-206 |
5.46e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 92.21 E-value: 5.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGdKKPSSGQVLIDGKPGKAKNKIT------VLLQENTIPNSLKVEELI 94
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDWSAAElarhraYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 95 AFFQSISDNPLTNQEVQEHL--QFK-EDQYQQFADKLSGG--QRRLLAFVLCLID-----KPKILFLDEPTAGMDTSTRQ 164
Cdd:COG4138 91 ALHQPAGASSEAVEQLLAQLaeALGlEDKLSRPLTQLSGGewQRVRLAAVLLQVWptinpEGQLLLLDEPMNSLDVAQQA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081348506 165 RFWEIVNDLKKSGVTILYSSHyieEVEHT---ADRILVLHQGKLI 206
Cdd:COG4138 171 ALDRLLRELCQQGITVVMSSH---DLNHTlrhADRVWLLKQGKLV 212
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-200 |
6.40e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.37 E-value: 6.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAknkitVLLQENTIPNSL--KVEELI 94
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVA-----YVPQRSEVPDSLplTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 95 A--FFQ--------SISDNPLTNQEVqEHLQFKEDQYQQFaDKLSGGQRR--LLAFVLclIDKPKILFLDEPTAGMDTST 162
Cdd:NF040873 79 AmgRWArrglwrrlTRDDRAAVDDAL-ERVGLADLAGRQL-GELSGGQRQraLLAQGL--AQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1081348506 163 RQRFWEIVNDLKKSGVTILYSSHYIEEVEhTADRILVL 200
Cdd:NF040873 155 RERIIALLAEEHARGATVVVVTHDLELVR-RADPCVLL 191
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-226 |
6.86e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.50 E-value: 6.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKA--KNK--------ITVLLQentIPNSLKV 90
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsKNKdikqirkkVGLVFQ---FPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 91 EELIA---------FFQSISDNPLTNQEVQEHLQFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTS 161
Cdd:PRK13649 100 EETVLkdvafgpqnFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348506 162 TRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHE---EKEKQVTLP 226
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDvdfLEEKQLGVP 247
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-211 |
9.18e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 91.21 E-value: 9.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK----PGKAKNKI----- 75
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEdltdSKKDINKLrrkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 ------------TVLlqENTIPNSLKV-----EELIAffqsisdnpltnqEVQEHLQfK---EDQYQQFADKLSGGQRRL 135
Cdd:COG1126 81 mvfqqfnlfphlTVL--ENVTLAPIKVkkmskAEAEE-------------RAMELLE-RvglADKADAYPAQLSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 136 LAFV--LCLidKPKILFLDEPTAGMDTstrqrfwEIVN-------DLKKSGVTILYSSH---YIEEVehtADRILVLHQG 203
Cdd:COG1126 145 VAIAraLAM--EPKVMLFDEPTSALDP-------ELVGevldvmrDLAKEGMTMVVVTHemgFAREV---ADRVVFMDGG 212
|
....*...
gi 1081348506 204 KLIRDTTP 211
Cdd:COG1126 213 RIVEEGPP 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
21-218 |
1.21e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.09 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-------PGKAKNKITVLLQENTIPNSLKVEEL 93
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqtAKIMREAVAIVPEGRRVFSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 94 IAFFQSISDNPLTNQEVQEHLQFKEDQYQ---QFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIV 170
Cdd:PRK11614 101 LAMGGFFAERDQFQERIKWVYELFPRLHErriQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081348506 171 NDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHEE 218
Cdd:PRK11614 181 EQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANE 228
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-205 |
1.47e-21 |
|
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: 92.87 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 23 DISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK----PGKA------KNKITVLLQENTIPNSLKVEE 92
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdSRKGiflppeKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 93 LIAFFQSISDNPLTN---QEVQEHLQFkEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDtstRQRFWEI 169
Cdd:TIGR02142 95 NLRYGMKRARPSERRisfERVIELLGI-GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD---DPRKYEI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1081348506 170 VNDLKK----SGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:TIGR02142 171 LPYLERlhaeFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-211 |
1.50e-21 |
|
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: 92.56 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 36 LIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-----PGKaKNKITVLLQENTIPNSLKVEELIAFFQSISDNPltNQEV 110
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEdvtnvPPH-LRHINMVFQSYALFPHMTVEENVAFGLKMRKVP--RAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 111 QEHLQ--FKEDQYQQFADK----LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFW-EIVNDLKKSGVTILYS 183
Cdd:TIGR01187 78 KPRVLeaLRLVQLEEFADRkphqLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQlELKTIQEQLGITFVFV 157
|
170 180
....*....|....*....|....*...
gi 1081348506 184 SHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTP 185
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-218 |
1.52e-21 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 94.12 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMScILGDKKPS---SGQVLIDGKPGKAKN-------K 74
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMK-ILSGVYPHgtwDGEIYWSGSPLKASNirdteraG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 75 ITVLLQENTIPNSLKVEELIAFFQSISDN-PLTN--------QEVQEHLQFKEDQYQQFADKLSGGQRRLLAFVLCLIDK 145
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEITLPgGRMAynamylraKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 146 PKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHEE 218
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDD 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-218 |
1.65e-21 |
|
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: 90.37 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKA------KNKITVLLQE-----NTIP 85
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtldslRRAIGVVPQDtvlfnDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 86 NSLKVEELIAffqsisdnplTNQEVQE-----HLqfkEDQYQQFAD-----------KLSGGQRRLLAFVLCLIDKPKIL 149
Cdd:cd03253 93 YNIRYGRPDA----------TDEEVIEaakaaQI---HDKIMRFPDgydtivgerglKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348506 150 FLDEPTAGMDTSTRQRFWEIVNDLKKsGVTILYSSHYIEEVEHtADRILVLHQGKLIRDTTpyamrHEE 218
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT-----HEE 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-211 |
1.85e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 91.30 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGK-------AKNKITVLLQ--ENTIPN 86
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeenlwdIRNKAGMVFQnpDNQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 87 SLkVEELIAFF-QSISDNPLTNQE-VQEHLQ-FKEDQYQQFADK-LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTST 162
Cdd:PRK13633 101 TI-VEEDVAFGpENLGIPPEEIRErVDESLKkVGMYEYRRHAPHlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1081348506 163 RQRFWEIVNDL-KKSGVTILYSSHYIEEVEHtADRILVLHQGKLIRDTTP 211
Cdd:PRK13633 180 RREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTP 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-258 |
2.39e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 91.69 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQV---LIDGKPGKAKNKITVLLQENTI--PNSLKVEELIA 95
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEKVLEKLVIqkTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 96 F-------FQsISDNPLTNQEVQEHLQF--------KEDQYQQFAD-----------------KLSGGQRRLLAFVLCLI 143
Cdd:PRK13651 103 IrrrvgvvFQ-FAEYQLFEQTIEKDIIFgpvsmgvsKEEAKKRAAKyielvgldesylqrspfELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 144 DKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHEEK--EK 221
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNKflIE 261
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1081348506 222 QVTLPSSFVSIVHGLE----DIYEVTEKRDVISFMTKDIEK 258
Cdd:PRK13651 262 NNMEPPKLLNFVNKLEkkgiDVPKVTSIEELASEINMYLEK 302
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-228 |
2.59e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 91.23 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK---PGKAKNKITVLLQENTI----PNSLKVEEL 93
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitAGKKNKKLKPLRKKVGIvfqfPEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 94 IA---------FFQSISDNPLTNQEVQEHLQFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQ 164
Cdd:PRK13634 103 VEkdicfgpmnFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348506 165 RFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP---YAMRHEEKEKQVTLPSS 228
Cdd:PRK13634 183 EMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPreiFADPDELEAIGLDLPET 250
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-207 |
3.52e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.05 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 12 GKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNK-------ITVLLQE-NT 83
Cdd:PRK11288 11 GKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtaalaagVAIIYQElHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 84 IPNsLKVEELIAFFQ-----SISDNPLTNQEVQ---EHLQFKEDQYQQFAdKLSGGQRRLLAFVLCLIDKPKILFLDEPT 155
Cdd:PRK11288 91 VPE-MTVAENLYLGQlphkgGIVNRRLLNYEAReqlEHLGVDIDPDTPLK-YLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 156 AGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIR 207
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-214 |
4.40e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 90.03 E-value: 4.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG--------KPGKAK 72
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdKDGQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 73 -----------NKITVLLQENTIPNSLKVEELI--AFFQSISdnpLTNQEVQEHLQF-------KEDQYQQFADKLSGGQ 132
Cdd:PRK10619 81 vadknqlrllrTRLTMVFQHFNLWSHMTVLENVmeAPIQVLG---LSKQEARERAVKylakvgiDERAQGKYPVHLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 133 RRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPY 212
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPE 237
|
..
gi 1081348506 213 AM 214
Cdd:PRK10619 238 QL 239
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-203 |
8.43e-21 |
|
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: 88.68 E-value: 8.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK----PGKAKnkiTVLLQENTIPNSLKVEELIAF 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKqitePGPDR---MVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 97 F--QSISDNPLTNQE--VQEHLQFKedQYQQFADK----LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWE 168
Cdd:TIGR01184 78 AvdRVLPDLSKSERRaiVEEHIALV--GLTEAADKrpgqLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1081348506 169 -IVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQG 203
Cdd:TIGR01184 156 eLMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-205 |
1.11e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 91.65 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK------PGKA-KNKITV 77
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltPAKAhQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 78 LLQENTIPNSLKVEELIAFfqSISDNPLTNQEVQEHL-----QFKEDQYqqfADKLSGGQRRLLAFVLCLIDKPKILFLD 152
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILF--GLPKRQASMQKMKQLLaalgcQLDLDSS---AGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 153 EPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:PRK15439 166 EPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-207 |
1.22e-20 |
|
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: 91.64 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNK------ITVLLQE-NTIPNSLKv 90
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRetfgkhIGYLPQDvELFPGTVA- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 91 eELIAFFqsisDNPLTNQEVQE-------H---LQFkEDQYQQF----ADKLSGGQRRLLAFVLCLIDKPKILFLDEPTA 156
Cdd:TIGR01842 410 -ENIARF----GENADPEKIIEaaklagvHeliLRL-PDGYDTVigpgGATLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 157 GMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEhTADRILVLHQGKLIR 207
Cdd:TIGR01842 484 NLDEEGEQALANAIKALKARGITVVVITHRPSLLG-CVDKILVLQDGRIAR 533
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-211 |
1.27e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 90.14 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSetvIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGK---AKN-KIT 76
Cdd:PRK10851 1 MS---IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSrlhARDrKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 77 VLLQENTIPNSLKVEELIAFFQSI------SDNPLTNQEVQEHLQFKedQYQQFADK----LSGGQRRLLAFVLCLIDKP 146
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFGLTVlprrerPNAAAIKAKVTQLLEMV--QLAHLADRypaqLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348506 147 KILFLDEPTAGMDTSTRQ--RFW--EIVNDLKKSGVtilYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKelRRWlrQLHEELKFTSV---FVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-206 |
1.28e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.14 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGK----TILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-----PGK----AK 72
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltalSERelraAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 73 NKITV------LLQENTipnslkVEELIAFfqsisdnPL---------TNQEVQEHLQF-----KEDQYqqfADKLSGGQ 132
Cdd:COG1135 82 RKIGMifqhfnLLSSRT------VAENVAL-------PLeiagvpkaeIRKRVAELLELvglsdKADAY---PSQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 133 R------RLLAfvlcliDKPKILFLDEPTAGMDTSTRQrfwEIVNDLKKS----GVTILYSSHYIEEVEHTADRILVLHQ 202
Cdd:COG1135 146 KqrvgiaRALA------NNPKVLLCDEATSALDPETTR---SILDLLKDInrelGLTIVLITHEMDVVRRICDRVAVLEN 216
|
....
gi 1081348506 203 GKLI 206
Cdd:COG1135 217 GRIV 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-206 |
2.06e-20 |
|
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: 88.96 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGK----TILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKP---SSGQVLIDGK-----PGKA- 71
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEdllklSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 72 ----KNKITVLLQEntiP-NSL----KVEELIA----FFQSISDNPLTnQEVQEHLQ-----FKEDQYQQFADKLSGGQR 133
Cdd:COG0444 81 rkirGREIQMIFQD---PmTSLnpvmTVGDQIAeplrIHGGLSKAEAR-ERAIELLErvglpDPERRLDRYPHELSGGMR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348506 134 R--LLAFVLCLidKPKILFLDEPTAGMDTSTRQrfwEIVNDLK----KSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:COG0444 157 QrvMIARALAL--EPKLLIADEPTTALDVTIQA---QILNLLKdlqrELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-210 |
2.34e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 90.94 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN-----KITVLLQENTIPNSLKVEELI 94
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhhylhRQVALVGQEPVLFSGSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 95 AF-FQSISDNPLTNQEVQEH-----LQFKEDQYQQFADK---LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQR 165
Cdd:TIGR00958 576 AYgLTDTPDEEIMAAAKAANahdfiMEFPNGYDTEVGEKgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL 655
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081348506 166 FWEivnDLKKSGVTILYSSHYIEEVEHtADRILVLHQGKLIRDTT 210
Cdd:TIGR00958 656 LQE---SRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGT 696
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-206 |
3.71e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 90.02 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG----KPGKA--KNKITVLLQENTIpnslkveeli 94
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirTVTRAslRRNIAVVFQDAGL---------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 95 aFFQSISDNPL------TNQEVQEHLQ------F---KEDQYQQFA----DKLSGGQRRLLAFVLCLIDKPKILFLDEPT 155
Cdd:PRK13657 421 -FNRSIEDNIRvgrpdaTDEEMRAAAEraqahdFierKPDGYDTVVgergRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 156 AGMDTSTRQRFWEIVNDLKKsGVTILYSSHYIEEVEHtADRILVLHQGKLI 206
Cdd:PRK13657 500 SALDVETEAKVKAALDELMK-GRTTFIIAHRLSTVRN-ADRILVFDNGRVV 548
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-211 |
4.16e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 90.18 E-value: 4.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLI-DGKPGKAKNKITVL----- 78
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlGGDMADARHRRAVCpriay 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 79 ----LQENTIPnSLKVEELIAFF-----QSISDNpltNQEVQEHLQ------FKEDQyqqfADKLSGGQRRLLAfvLC-- 141
Cdd:NF033858 81 mpqgLGKNLYP-TLSVFENLDFFgrlfgQDAAER---RRRIDELLRatglapFADRP----AGKLSGGMKQKLG--LCca 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 142 LIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKS--GVTILYSSHYIEEVEHTaDRILVLHQGKLIRDTTP 211
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTP 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-211 |
4.35e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 4.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN------KITVLL 79
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSaraasrRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 80 QENTIPNSLKVEELIAF--------FQSISDnplTNQEVQEHLQFKEDqYQQFADK----LSGG--QRRLLAFVLCliDK 145
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMgrtphrsrFDTWTE---TDRAAVERAMERTG-VAQFADRpvtsLSGGerQRVLLARALA--QA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348506 146 PKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKlIRDTTP 211
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGR-VRAAGP 222
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-218 |
5.08e-20 |
|
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: 89.78 E-value: 5.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPgkaknkitvlLQENTIPN-----SLKVE 91
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHD----------LADYTLASlrrqvALVSQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 92 ELIAFFQSISDN-------PLTNQEVQEHLQfkeDQY-QQFADK---------------LSGGQRRLLAFVLCLIDKPKI 148
Cdd:TIGR02203 414 DVVLFNDTIANNiaygrteQADRAEIERALA---AAYaQDFVDKlplgldtpigengvlLSGGQRQRLAIARALLKDAPI 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 149 LFLDEPTAGMDTSTRQRFWEIVNDLKKsGVTILYSSHYIEEVEHtADRILVLHQGKLIRDTTpyamrHEE 218
Cdd:TIGR02203 491 LILDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGT-----HNE 553
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-211 |
5.36e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 86.53 E-value: 5.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGdKKPSSGQVLIDGKP-------GKAKNKiTVLLQENTIPNSLKVEEL 93
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPleawsaaELARHR-AYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 94 IAFFQS----ISDNPLTNQEVQEHLQFkEDQYQQFADKLSGG--QRRLLAFVlCLIDKPKI------LFLDEPTAGMDTS 161
Cdd:PRK03695 90 LTLHQPdktrTEAVASALNEVAEALGL-DDKLGRSVNQLSGGewQRVRLAAV-VLQVWPDInpagqlLLLDEPMNSLDVA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1081348506 162 TRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-206 |
5.92e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.61 E-value: 5.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSetvIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG-------KPG-KA- 71
Cdd:PRK11124 1 MS---IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfskTPSdKAi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 72 ----KNKITVLLQENTIPNSLKVEELIAFFQSIS--DNPLTNQEVQEHLqfKEDQYQQFADK----LSGGQRRLLAFVLC 141
Cdd:PRK11124 78 relrRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLglSKDQALARAEKLL--ERLRLKPYADRfplhLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 142 LIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-211 |
6.14e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 86.97 E-value: 6.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP------GKAKNKITVLLQEntiPNS---- 87
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITiskenlKEIRKKIGIIFQN---PDNqfig 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 88 LKVEELIAF-----------FQSISDNPLTNQEVQEHLQfKEDQYqqfadkLSGGQRRLLAFVLCLIDKPKILFLDEPTA 156
Cdd:PRK13632 99 ATVEDDIAFglenkkvppkkMKDIIDDLAKKVGMEDYLD-KEPQN------LSGGQKQRVAIASVLALNPEIIIFDESTS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348506 157 GMDTSTRQRFWEIVNDLKKSGV-TILYSSHYIEEVEhTADRILVLHQGKLIRDTTP 211
Cdd:PRK13632 172 MLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIAQGKP 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-185 |
8.00e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.31 E-value: 8.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNKITV---LLQENTIPNSLKVEEL 93
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchyLGHRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 94 IAFFQSISDNPLTN----------QEVqEHLQFKEdqyqqfadkLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTR 163
Cdd:PRK13539 94 LEFWAAFLGGEELDiaaaleavglAPL-AHLPFGY---------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|..
gi 1081348506 164 QRFWEIVNDLKKSGVTILYSSH 185
Cdd:PRK13539 164 ALFAELIRAHLAQGGIVIAATH 185
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-211 |
8.55e-20 |
|
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: 85.95 E-value: 8.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKGK----TILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-------G 69
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDlfaldedA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 70 KAKnkitvLLQENtipnslkveelIAF-FQS---IS-----DN---PLtnqEVQEH---------------LQFKEDQY- 121
Cdd:COG4181 84 RAR-----LRARH-----------VGFvFQSfqlLPtltalENvmlPL---ELAGRrdarararallervgLGHRLDHYp 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 122 QQfadkLSGG--QRRLLA--FVLclidKPKILFLDEPTAGMDTSTRQRfweiVNDL-----KKSGVTILYSSHYiEEVEH 192
Cdd:COG4181 145 AQ----LSGGeqQRVALAraFAT----EPAILFADEPTGNLDAATGEQ----IIDLlfelnRERGTTLVLVTHD-PALAA 211
|
250
....*....|....*....
gi 1081348506 193 TADRILVLHQGKLIRDTTP 211
Cdd:COG4181 212 RCDRVLRLRAGRLVEDTAA 230
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-211 |
8.84e-20 |
|
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: 85.62 E-value: 8.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 14 RIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP------GKAKNKITVLLQENTIpns 87
Cdd:cd03244 13 RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskiglHDLRSRISIIPQDPVL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 88 lkveeliaFFQSISDN--PL---TNQEVQEHL---QFKEdQYQQFADKL-----------SGGQRRLLAFVLCLIDKPKI 148
Cdd:cd03244 90 --------FSGTIRSNldPFgeySDEELWQALervGLKE-FVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 149 LFLDEPTAGMDTSTRQRFWEIVNDlKKSGVTILYSSHYIEEVeHTADRILVLHQGKLIRDTTP 211
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTI-IDSDRILVLDKGRVVEFDSP 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-203 |
1.36e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.30 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-------PGKAKN 73
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 74 KITVLLQENTIPNSLKVEELI---------AFFQSISDNPLTNQEVQEHLQ---FKEDQYQQFADkLSGGQRRLLAFVLC 141
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLyigrhltkkVCGVNIIDWREMRVRAAMMLLrvgLKVDLDEKVAN-LSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 142 LIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQG 203
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-243 |
1.44e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.19 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG----KPGKAKN--KITVLLQENtiPNSL-- 88
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgDFSKLQGirKLVGIVFQN--PETQfv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 89 --KVEELIAF------FQSISDNPLTNQEVQEhlqFKEDQYQQFADK-LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMD 159
Cdd:PRK13644 92 grTVEEDLAFgpenlcLPPIEIRKRVDRALAE---IGLEKYRHRSPKtLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 160 TSTRQRFWEIVNDLKKSGVTILYSSHYIEEVeHTADRILVLHQGKLIRDTTPYAMRHEEKEKQVTL-PSSFVSIV----- 233
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLtPPSLIELAenlkm 247
|
250
....*....|
gi 1081348506 234 HGLEDIYEVT 243
Cdd:PRK13644 248 HGVVIPWENT 257
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-203 |
1.51e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.52 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP--GKAKNKITVLLQENT 83
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPveGPGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 84 IPnSLKVEELIAFFQSISDNPLTNQEVQEHLQFK----EDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMD 159
Cdd:PRK11248 82 LP-WRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKkvglEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081348506 160 TSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQG 203
Cdd:PRK11248 161 AFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-205 |
1.52e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.06 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 3 ETVIQV---TSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGD-KKPSSGQVLIDGKPGKAKNK---- 74
Cdd:PRK13549 257 EVILEVrnlTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPqqai 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 75 ----------------ITVL-LQENTipnSLKVEELIAFFQSISDNP---LTNQEVQeHLQFKEDQYQQFADKLSGG--Q 132
Cdd:PRK13549 337 aqgiamvpedrkrdgiVPVMgVGKNI---TLAALDRFTGGSRIDDAAelkTILESIQ-RLKVKTASPELAIARLSGGnqQ 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 133 RRLLAfvLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:PRK13549 413 KAVLA--KCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-211 |
1.66e-19 |
|
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: 88.32 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 24 ISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN------KITV----------LLQENTIPNS 87
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNreayrqLFSAvfsdfhlfdrLLGLDGEADP 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 88 LKVEELIAFFqsisdnpltnqEVQEHLQFKEDQyqqFAD-KLSGGQRRLLAFVLCLI-DKPkILFLDEPTAGMDTSTRQR 165
Cdd:COG4615 431 ARARELLERL-----------ELDHKVSVEDGR---FSTtDLSQGQRKRLALLVALLeDRP-ILVFDEWAADQDPEFRRV 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1081348506 166 FW-EIVNDLKKSGVTILYSSH---YIeeveHTADRILVLHQGKLIRDTTP 211
Cdd:COG4615 496 FYtELLPELKARGKTVIAISHddrYF----DLADRVLKMDYGKLVELTGP 541
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-203 |
1.72e-19 |
|
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: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPS--SGQVLIDGKPGKAK-NKITVLLQENTI-PNSLKVEEL 93
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNfQRSTGYVEQQDVhSPNLTVREA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 94 IAFFQSISDnpltnqevqehlqfkedqyqqfadkLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRqrfWEIVNDL 173
Cdd:cd03232 100 LRFSALLRG-------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA---YNIVRFL 151
|
170 180 190
....*....|....*....|....*....|....
gi 1081348506 174 KK---SGVTILYSSHY-IEEVEHTADRILVLHQG 203
Cdd:cd03232 152 KKladSGQAILCTIHQpSASIFEKFDRLLLLKRG 185
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-206 |
2.06e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 85.06 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK----PGKAKNKITVLL-- 79
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfSQKPSEKAIRLLrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 80 -------QENTIPNsLKVEE-LIAFFQSISDnpLTNQEVQEHLQ--FKEDQYQQFADK----LSGGQRRLLAFVLCLIDK 145
Cdd:COG4161 83 kvgmvfqQYNLWPH-LTVMEnLIEAPCKVLG--LSKEQAREKAMklLARLRLTDKADRfplhLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 146 PKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-207 |
3.13e-19 |
|
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: 83.35 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILG--DKKPSSGQVLIDGK-------PGKAKNKIT 76
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEditdlppEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 77 VLLQEN-TIPnSLKVEELIaffqsisdnpltnQEVQEhlqfkedqyqqfadKLSGGQRRLLAFVLCLIDKPKILFLDEPT 155
Cdd:cd03217 81 LAFQYPpEIP-GVKNADFL-------------RYVNE--------------GFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 156 AGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEH-TADRILVLHQGKLIR 207
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYiKPDRVHVLYDGRIVK 185
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-200 |
6.05e-19 |
|
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: 86.57 E-value: 6.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN------KITVLLQENTIpnslkveeli 94
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADadswrdQIAWVPQHPFL---------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 95 aFFQSISDNPL------TNQEVQEHLQ------FKEDQYQQFADK-------LSGGQRRLLAFVLCLIDKPKILFLDEPT 155
Cdd:TIGR02857 408 -FAGTIAENIRlarpdaSDAEIREALEragldeFVAALPQGLDTPigeggagLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081348506 156 AGMDTSTRQRFWEIVNDLkKSGVTILYSSHYIEEVEhTADRILVL 200
Cdd:TIGR02857 487 AHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAA-LADRIVVL 529
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-205 |
7.14e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 86.18 E-value: 7.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 24 ISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNKIT-----------------VLLQENTIPN 86
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrklfsavftdfhlfdqLLGPEGKPAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 87 SLKVEELIAFFQ-----SISDNPLTNQevqehlqfkedqyqqfadKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTS 161
Cdd:PRK10522 422 PALVEKWLERLKmahklELEDGRISNL------------------KLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081348506 162 TRQRFW-EIVNDLKKSGVTILYSSHYIEEVEHtADRILVLHQGKL 205
Cdd:PRK10522 484 FRREFYqVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQL 527
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-216 |
7.43e-19 |
|
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: 84.09 E-value: 7.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVL--------IDGKPGKA-KNKITVLLQENtiPNSL 88
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdlyqLDRKQRRAfRRDVQLVFQDS--PSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 89 K----VEELIAffqsisdNPLTN-------------QEVQEHLQFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFL 151
Cdd:TIGR02769 102 NprmtVRQIIG-------EPLRHltsldeseqkariAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348506 152 DEPTAGMDTSTRQRFWEIVNDLK-KSGVTILYSSHYIEEVEHTADRILVLHQGKLI--RDTTP-YAMRH 216
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLQqAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVeeCDVAQlLSFKH 243
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-211 |
7.55e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.88 E-value: 7.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK------PGKAKNKITVLLQENTIPNSLKVE 91
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyaSKEVARRIGLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 92 ELIAFFQsISDNPLTNQEVQEHLQFKEDQYQ---------QFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTST 162
Cdd:PRK10253 100 ELVARGR-YPHQPLFTRWRKEDEEAVTKAMQatgithladQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1081348506 163 RQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:PRK10253 179 QIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-206 |
1.05e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 83.63 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 3 ETVIQVTSLGKRIK-GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN------KI 75
Cdd:PRK13647 2 DNIIEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENekwvrsKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 TVLLQEntiPN----SLKVEELIAFfqsisdNP----LTNQEVQEHLQ--FKEDQYQQFADK----LSGGQRRLLAFVLC 141
Cdd:PRK13647 82 GLVFQD---PDdqvfSSTVWDDVAF------GPvnmgLDKDEVERRVEeaLKAVRMWDFRDKppyhLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 142 LIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-212 |
1.11e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.52 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 19 TILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG---KPGKAKNKITVLLQENTIPNSLKVEELIA 95
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyiGDKKNNHELITNPYSKKIKNFKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 96 FFQSISDNPLTNQEVQEHLQF--------KEDQYQQ-------------FADK----LSGGQRRLLAFVLCLIDKPKILF 150
Cdd:PRK13631 120 MVFQFPEYQLFKDTIEKDIMFgpvalgvkKSEAKKLakfylnkmglddsYLERspfgLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 151 LDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPY 212
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPY 261
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-205 |
1.15e-18 |
|
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: 85.57 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG------KPGKAKNKI-----TVLLQENTIp 85
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwDREELGRHIgylpqDVELFDGTI- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 86 nslkvEELIAFFQSISDnpltnQEVQE-------HlqfkeDQYQQFAD-----------KLSGGQRRLLAFVLCLIDKPK 147
Cdd:COG4618 423 -----AENIARFGDADP-----EKVVAaaklagvH-----EMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348506 148 ILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHtADRILVLHQGKL 205
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAA-VDKLLVLRDGRV 544
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-217 |
1.32e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.14 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 3 ETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLM----SCILGDKKPSSGQVLI------DGKPG--- 69
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIELLgrtvqrEGRLArdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 70 -KAKNKITVLLQENTIPNSLKVEELIaFFQSISDNPL--------TNQEVQEHLQ-FKEDQYQQFADK----LSGGQRRL 135
Cdd:PRK09984 82 rKSRANTGYIFQQFNLVNRLSVLENV-LIGALGSTPFwrtcfswfTREQKQRALQaLTRVGMVHFAHQrvstLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 136 LAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAM 214
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
...
gi 1081348506 215 RHE 217
Cdd:PRK09984 241 DNE 243
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-206 |
1.58e-18 |
|
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: 82.59 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN------KITVLLQENTIpnslkveel 93
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNlrwlrsQIGLVSQEPVL--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 94 iaFFQSISDN------PLTNQEVQEHLQFKE---------DQYQ----QFADKLSGGQRRLLAFVLCLIDKPKILFLDEP 154
Cdd:cd03249 89 --FDGTIAENirygkpDATDEEVEEAAKKANihdfimslpDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 155 TAGMDTSTRQRFWEIVNDLKKsGVTILYSSHYIEEVEHtADRILVLHQGKLI 206
Cdd:cd03249 167 TSALDAESEKLVQEALDRAMK-GRTTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
13-205 |
1.64e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.35 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 13 KRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNKIT-----VLL------QE 81
Cdd:PRK11288 261 DGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairagIMLcpedrkAE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 82 NTIPNSlKVEELIA--------FFQSISDNPLTNQEVQEH---LQFKEDQYQQFADKLSGG--QRRLLAFVLCliDKPKI 148
Cdd:PRK11288 341 GIIPVH-SVADNINisarrhhlRAGCLINNRWEAENADRFirsLNIKTPSREQLIMNLSGGnqQKAILGRWLS--EDMKV 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348506 149 LFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-203 |
1.77e-18 |
|
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: 85.84 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 28 INQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-----GKAKNKITVLLQENTIPNSLKVEELIAFFQSISD 102
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltniSDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 103 NPLTNQEVQEHLQFKEDQYQQFADKL----SGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGV 178
Cdd:TIGR01257 2042 VPAEEIEKVANWSIQSLGLSLYADRLagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR 2121
|
170 180
....*....|....*....|....*
gi 1081348506 179 TILYSSHYIEEVEHTADRILVLHQG 203
Cdd:TIGR01257 2122 AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-210 |
1.88e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.80 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 4 TVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-GKAKNKITVLLQE- 81
Cdd:PRK11247 11 TPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPlAEAREDTRLMFQDa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 82 NTIPnslkveeliafFQSISDN---PLTNQEVQEHLQFKE-----DQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDE 153
Cdd:PRK11247 91 RLLP-----------WKKVIDNvglGLKGQWRDAALQALAavglaDRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348506 154 PTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTT 210
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLT 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-211 |
2.45e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.91 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNK----------ITVLLQentIPNSL-- 88
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirpvrkrIGMVFQ---FPESQlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 89 --KVEELIAFFQSISDNPLTNQEVQEH-----LQFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTS 161
Cdd:PRK13646 100 edTVEREIIFGPKNFKMNLDEVKNYAHrllmdLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 162 TRQRFWEIVNDLK-KSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:PRK13646 180 SKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP 230
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
14-207 |
2.48e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.04 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 14 RIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKK--PSSGQVLIDGK------------------------ 67
Cdd:COG0396 9 SVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEdilelspderaragiflafqypve 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 68 -PGkaknkITV--LLQenTIPNSLKVEELiaffqsisDNPLTNQEVQEH---LQFKEDqyqqFADK-----LSGGQRRLL 136
Cdd:COG0396 89 iPG-----VSVsnFLR--TALNARRGEEL--------SAREFLKLLKEKmkeLGLDED----FLDRyvnegFSGGEKKRN 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081348506 137 AFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHY---IEEVEhtADRILVLHQGKLIR 207
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDGRIVK 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-212 |
3.16e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 84.71 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMScILGDKKPS----SGQVLIDGKPGKAK--NKITVLLQENTIpnslkve 91
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMN-ALAFRSPKgvkgSGSVLLNGMPIDAKemRAISAYVQQDDL------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 92 eliaFFQSisdnpLTnqeVQEHLQFK----------EDQYQQFADK-----------------------LSGGQRRLLAF 138
Cdd:TIGR00955 110 ----FIPT-----LT---VREHLMFQahlrmprrvtKKEKRERVDEvlqalglrkcantrigvpgrvkgLSGGERKRLAF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 139 VLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHY-IEEVEHTADRILVLHQGKLIRDTTPY 212
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPD 252
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-206 |
3.32e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 81.72 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 4 TVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQV-----LIDG-KP-GKAKNKIT 76
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSlSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 77 VLLQE--------NTIPNSLKVEELIaffqsisDNPL-TNQEVQEH-------------LQFKEDQYQQfadKLSGGQRR 134
Cdd:PRK11264 82 QLRQHvgfvfqnfNLFPHRTVLENII-------EGPViVKGEPKEEatararellakvgLAGKETSYPR---RLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 135 LLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-211 |
3.32e-18 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 80.92 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP------GKAKNKITVLLQE-----NTIPNSL 88
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDistiplEDLRSSLTIIPQDptlfsGTIRSNL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 89 KVEeliaffqsisdNPLTNQEVQEHLQFKEDqyqqfADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWE 168
Cdd:cd03369 103 DPF-----------DEYSDEEIYGALRVSEG-----GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081348506 169 IVNDLkKSGVTILYSSHYIEEVEhTADRILVLHQGKLIRDTTP 211
Cdd:cd03369 167 TIREE-FTNSTILTIAHRLRTII-DYDKILVMDAGEVKEYDHP 207
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-206 |
3.55e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.14 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 3 ETVIQVTSLGKRIKGKTIL---------EDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP----- 68
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlhfgd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 69 -GKAKNKITVLLQENTipNSLKVEELIAffqSISDNPL---TNQEVQEHLQ----------FKEDQYQQFADKLSGGQRR 134
Cdd:PRK15112 82 ySYRSQRIRMIFQDPS--TSLNPRQRIS---QILDFPLrlnTDLEPEQREKqiietlrqvgLLPDHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 135 LLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLK-KSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-205 |
3.63e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.28 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAK-------NKItVLLQENTIPNSL----K 89
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdglaNGI-VYISEDRKRDGLvlgmS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 90 VEE---LIA--FFQSISDNPLTNQEVQEHLQF------KEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGM 158
Cdd:PRK10762 347 VKEnmsLTAlrYFSRAGGSLKHADEQQAVSDFirlfniKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081348506 159 DTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:PRK10762 427 DVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-211 |
3.73e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.47 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLI------------DGKPgkAKNKITVLLQentIPNSL 88
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskqkEIKP--VRKKVGVVFQ---FPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 89 KVEELIafFQSISDNP----LTNQEVQ-------EHLQFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAG 157
Cdd:PRK13643 97 LFEETV--LKDVAFGPqnfgIPKEKAEkiaaeklEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1081348506 158 MDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-181 |
4.64e-18 |
|
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: 80.48 E-value: 4.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPgkaKNKITVLLQENT--------IPNSL 88
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP---LAEQRDEPHENIlylghlpgLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 89 KVEELIAFFQSIS---DNPLTNQEVQEHLQFKEDqyqQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQR 165
Cdd:TIGR01189 89 SALENLHFWAAIHggaQRTIEDALAAVGLTGFED---LPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170
....*....|....*..
gi 1081348506 166 FWEIVND-LKKSGVTIL 181
Cdd:TIGR01189 166 LAGLLRAhLARGGIVLL 182
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-224 |
7.77e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 80.73 E-value: 7.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCI-----LGDKKPSSGQVLIDGKP------GKAKNKITVLLQ-ENTIPNs 87
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDifkmdvIELRRRVQMVFQiPNPIPN- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 88 LKVEELIAFFQSISDNPLTNQEVQEHLQFKEDQYQQF----------ADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAG 157
Cdd:PRK14247 97 LSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWdevkdrldapAGKLSGGQQQRLCIARALAFQPEVLLADEPTAN 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081348506 158 MDTSTRQRFWEIVNDLKKSgVTILYSSHYIEEVEHTADRILVLHQGKLIRD-------TTPyamRHEEKEKQVT 224
Cdd:PRK14247 177 LDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWgptrevfTNP---RHELTEKYVT 246
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-206 |
7.83e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.34 E-value: 7.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKA------KNKITVLLQENTIPN-SLKVEE 92
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADyseaalRQAISVVSQRVHLFSaTLRDNL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 93 LIAFFQsISDNPLTN--QEV--QEHLQFKE--DQY-----QQfadkLSGG-QRRL-LAFVLcLIDKPkILFLDEPTAGMD 159
Cdd:PRK11160 435 LLAAPN-ASDEALIEvlQQVglEKLLEDDKglNAWlgeggRQ----LSGGeQRRLgIARAL-LHDAP-LLLLDEPTEGLD 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081348506 160 TSTRQRFWEIVNDLKKsGVTILYSSHYIEEVEHTaDRILVLHQGKLI 206
Cdd:PRK11160 508 AETERQILELLAEHAQ-NKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-218 |
8.75e-18 |
|
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: 82.95 E-value: 8.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPS-SGQVLIDGKPGKAKNKITVLLQE-NTIPNSLKVEELI---- 94
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGiAMVPEDRKRHGIVpilg 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 95 -------AFFQSISDNPLTNQEVQE--------HLQFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMD 159
Cdd:TIGR02633 356 vgknitlSVLKSFCFKMRIDAAAELqiigsaiqRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348506 160 TSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHEE 218
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQ 494
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-226 |
1.15e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.91 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 3 ETVIQVTSLGKRIKGKtiLEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK------PGKAKNK-- 74
Cdd:PRK09700 263 ETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprsPLDAVKKgm 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 75 --ITVLLQENTIPNSLKVEELIAFFQSISDNPL--------------TNQEVQEHLQFKEDQYQQFADKLSGG--QRRLL 136
Cdd:PRK09700 341 ayITESRRDNGFFPNFSIAQNMAISRSLKDGGYkgamglfhevdeqrTAENQRELLALKCHSVNQNITELSGGnqQKVLI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 137 AFVLCLidKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRH 216
Cdd:PRK09700 421 SKWLCC--CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMS 498
|
250
....*....|
gi 1081348506 217 EEKEKQVTLP 226
Cdd:PRK09700 499 EEEIMAWALP 508
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-206 |
1.48e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.59 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGdKKPSSGQVLIDGK------PGKAKNKITVLLQENTIPNslkv 90
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIelreldPESWRKHLSWVGQNPQLPH---- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 91 eeliaffQSISDNPL------TNQEVQEHLQ------FKEDQYQ----QFADK---LSGGQRRLLAFVLCLIDKPKILFL 151
Cdd:PRK11174 437 -------GTLRDNVLlgnpdaSDEQLQQALEnawvseFLPLLPQgldtPIGDQaagLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 152 DEPTAGMDTSTRQRFWEIVNDLKKSGVTILYsSHYIEEVEHtADRILVLHQGKLI 206
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAASRRQTTLMV-THQLEDLAQ-WDQIWVMQDGQIV 562
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-211 |
2.01e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.05 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-GKAKNKITVLLQEnt 83
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPlDYSKRGLLALRQQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 84 IPNSLKVEELIAFFQSISDN---PLTN---------QEVQEHLQFKEDQY--QQFADKLSGGQRRLLAFVLCLIDKPKIL 149
Cdd:PRK13638 79 VATVFQDPEQQIFYTDIDSDiafSLRNlgvpeaeitRRVDEALTLVDAQHfrHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 150 FLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-206 |
2.35e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 80.55 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKR--IKG----KTI-----LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPg 69
Cdd:COG4608 3 MAEPLLEVRDLKKHfpVRGglfgRTVgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 70 kaknkITVLLQENTIP-------------NSL----KVEELIAFfqsisdnPLTNQE----------VQEHLQ---FKED 119
Cdd:COG4608 82 -----ITGLSGRELRPlrrrmqmvfqdpyASLnprmTVGDIIAE-------PLRIHGlaskaerrerVAELLElvgLRPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 120 QYQQFADKLSGGQR------RLLAFvlclidKPKILFLDEPTAGMDTSTR-QrfweIVN---DLKKS-GVTILYSSHYIE 188
Cdd:COG4608 150 HADRYPHEFSGGQRqrigiaRALAL------NPKLIVCDEPVSALDVSIQaQ----VLNlleDLQDElGLTYLFISHDLS 219
|
250
....*....|....*...
gi 1081348506 189 EVEHTADRILVLHQGKLI 206
Cdd:COG4608 220 VVRHISDRVAVMYLGKIV 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-211 |
2.38e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 80.16 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN------KITVLLQ--ENTIPNSlK 89
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwdirhKIGMVFQnpDNQFVGA-T 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 90 VEELIAFfqSISDNPLTNQE----VQEHLQFKEdqYQQFADK----LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTS 161
Cdd:PRK13650 99 VEDDVAF--GLENKGIPHEEmkerVNEALELVG--MQDFKEReparLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 162 TRQRFWEIVNDLKKS-GVTILYSSHYIEEVEhTADRILVLHQGKLIRDTTP 211
Cdd:PRK13650 175 GRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTP 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-206 |
4.98e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 79.84 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGK----TILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGkpgkaknkitvllQ 80
Cdd:PRK11153 1 MIELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDG-------------Q 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 81 ENTipnSLKVEELIAFFQSIS---------------DN---PLT---------NQEVQEHLQFK--EDQYQQFADKLSGG 131
Cdd:PRK11153 68 DLT---ALSEKELRKARRQIGmifqhfnllssrtvfDNvalPLElagtpkaeiKARVTELLELVglSDKADRYPAQLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348506 132 QRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-264 |
5.62e-17 |
|
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: 80.62 E-value: 5.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILG--DKKPSSGQVLI----------------DGK 67
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYhvalcekcgyverpskVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 68 PGKA-----------------------KNKITVLLQ--------ENTIPNSLKVEELIAFfqSISDNPLTNQEVQEHLQF 116
Cdd:TIGR03269 81 PCPVcggtlepeevdfwnlsdklrrriRKRIAIMLQrtfalygdDTVLDNVLEALEEIGY--EGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 117 kEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRqrfwEIVND-----LKKSGVTILYSSHYIEEVE 191
Cdd:TIGR03269 159 -SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTA----KLVHNaleeaVKASGISMVLTSHWPEVIE 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 192 HTADRILVLHQGKLIRDTTPyamrheekekqVTLPSSFVSIVHGLEDIYEVTEKRDVISfmTKDIEKVWQSLE 264
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTP-----------DEVVAVFMEGVSEVEKECEVEVGEPIIK--VRNVSKRYISVD 293
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-226 |
6.87e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.29 E-value: 6.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 2 SETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-----GKA-KNKI 75
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsSKAfARKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 TVLLQENTIPNSLKVEELIAFFQSISDNPLTNQEVQEHLQFKE--------DQYQQFADKLSGGQRRLLAFVLCLIDKPK 147
Cdd:PRK10575 88 AYLPQQLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEaislvglkPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 148 ILFLDEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYA-MRHEEKEKQVTL 225
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAElMRGETLEQIYGI 247
|
.
gi 1081348506 226 P 226
Cdd:PRK10575 248 P 248
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-209 |
7.51e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.55 E-value: 7.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 23 DISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN------------------KITVL------ 78
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDiatrrrvgymsqafslygELTVRqnlelh 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 79 -----LQENTIPNslKVEELIAFFQsisdnpLtnQEVQEHLqfkedqyqqfADKLSGGQR-RL-LAfVLClIDKPKILFL 151
Cdd:NF033858 364 arlfhLPAAEIAA--RVAEMLERFD------L--ADVADAL----------PDSLPLGIRqRLsLA-VAV-IHKPELLIL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 152 DEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHtADRILVLHQGK-LIRDT 209
Cdd:NF033858 422 DEPTSGVDPVARDMFWRLLIELsREDGVTIFISTHFMNEAER-CDRISLMHAGRvLASDT 480
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-206 |
7.54e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.17 E-value: 7.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 2 SETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSC------ILGDKKPSSGQVLIDGK------PG 69
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKdifqidAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 70 KAKNKITVLLQE-NTIPNsLKVEELIAF---FQSISDNPLTNQEVQEHLQ----FKE--DQYQQFADKLSGGQRRLLAFV 139
Cdd:PRK14246 87 KLRKEVGMVFQQpNPFPH-LSIYDNIAYplkSHGIKEKREIKKIVEECLRkvglWKEvyDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348506 140 LCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSgVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-197 |
7.92e-17 |
|
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: 77.15 E-value: 7.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-----GKAKNKITVLLQENTIPNSLKVE 91
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPldfqrDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 92 ELIAFFQSISDNPLTNQEVQE-HLQFKEDQYqqfADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIV 170
Cdd:cd03231 92 ENLRFWHADHSDEQVEEALARvGLNGFEDRP---VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
170 180
....*....|....*....|....*...
gi 1081348506 171 -NDLKKSGVTILYSSHYIEEVEHTADRI 197
Cdd:cd03231 169 aGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
17-210 |
8.99e-17 |
|
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: 80.17 E-value: 8.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNKITVLLQENTIPnslkvEELIAF 96
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLP-----QEPYIF 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 97 FQSISDNPL-------TNQEVQEHLQFKE--DQYQQF-----------ADKLSGGQRRLLAFVLCLIDKPKILFLDEPTA 156
Cdd:TIGR01193 561 SGSILENLLlgakenvSQDEIWAACEIAEikDDIENMplgyqtelseeGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1081348506 157 GMDTSTRQRFweIVNDLKKSGVTILYSSHYIEEVEHTaDRILVLHQGKLIRDTT 210
Cdd:TIGR01193 641 NLDTITEKKI--VNNLLNLQDKTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGS 691
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
18-202 |
1.40e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.46 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK--PGKAKNKITVllqENTIPnsLKVEELIA 95
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYL---DTTLP--LTVNRFLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 96 FFQSISDN---PLTNQEVQEHLqfkedqYQQFADKLSGG--QRRLLAfvLCLIDKPKILFLDEPTAGMDTSTRQRFWEIV 170
Cdd:PRK09544 92 LRPGTKKEdilPALKRVQAGHL------IDAPMQKLSGGetQRVLLA--RALLNRPQLLVLDEPTQGVDVNGQVALYDLI 163
|
170 180 190
....*....|....*....|....*....|...
gi 1081348506 171 NDLKKS-GVTILYSSHYIEEVEHTADRILVLHQ 202
Cdd:PRK09544 164 DQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
125-208 |
1.40e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 78.62 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 125 ADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGK 204
Cdd:NF000106 142 AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGR 221
|
....
gi 1081348506 205 LIRD 208
Cdd:NF000106 222 VIAD 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-216 |
2.65e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.15 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK------PgkAKNKITVLLQENTIPNSLKVEEL 93
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvpP--AERGVGMVFQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 94 IAFFQSIS--DNPLTNQEVQ---EHLQFkEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTR-QRFW 167
Cdd:PRK11000 96 MSFGLKLAgaKKEEINQRVNqvaEVLQL-AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRvQMRI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1081348506 168 EIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRH 216
Cdd:PRK11000 175 EISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYH 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-211 |
2.67e-16 |
|
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: 76.91 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 23 DISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKA----------KNKITVLLQENTIPNSLKVEE 92
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrkelrelrRKKISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 93 LIAFFQSISDNPLTNQE--VQEHLQFK--EDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWE 168
Cdd:cd03294 122 NVAFGLEVQGVPRAEREerAAEALELVglEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQD 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1081348506 169 IVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:cd03294 202 ELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-200 |
3.32e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 74.50 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMScILGDKKPS-SGQVlidGKPgkAKNKITVLLQENTIPN-SLKveELI 94
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFR-ALAGLWPWgSGRI---GMP--EGEDLLFLPQRPYLPLgTLR--EQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 95 AFfqsisdnPLtnqevqehlqfkedqyqqfADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIvndLK 174
Cdd:cd03223 85 IY-------PW-------------------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL---LK 135
|
170 180
....*....|....*....|....*.
gi 1081348506 175 KSGVTILYSSHYiEEVEHTADRILVL 200
Cdd:cd03223 136 ELGITVISVGHR-PSLWKFHDRVLDL 160
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-211 |
4.65e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.38 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCIlgdkkpsSGQVLIDGKPgkaKNKITVLLQENTIPNSLKVEELIAF- 96
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLI-------NGLLLPDDNP---NSKITVDGITLTAKTVWDIREKVGIv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 97 FQSiSDNPLTNQEVQEHLQFKEDQYQ--------------------QFADK----LSGGQRRLLAFVLCLIDKPKILFLD 152
Cdd:PRK13640 90 FQN-PDNQFVGATVGDDVAFGLENRAvprpemikivrdvladvgmlDYIDSepanLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 153 EPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHtADRILVLHQGKLIRDTTP 211
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSP 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-185 |
6.38e-16 |
|
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: 77.40 E-value: 6.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPgkaknkitvllqentiPNSLKVEELIA---- 95
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVP----------------VSSLDQDEVRRrvsv 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 96 -------FFQSISDNPL------TNQEV---------QEHLQFKEDQYQ----QFADKLSGGQRRLLAFVLCLIDKPKIL 149
Cdd:TIGR02868 414 caqdahlFDTTVRENLRlarpdaTDEELwaalervglADWLRALPDGLDtvlgEGGARLSGGERQRLALARALLADAPIL 493
|
170 180 190
....*....|....*....|....*....|....*...
gi 1081348506 150 FLDEPTAGMDTSTRQrfwEIVNDLKK--SGVTILYSSH 185
Cdd:TIGR02868 494 LLDEPTEHLDAETAD---ELLEDLLAalSGRTVVLITH 528
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-203 |
6.89e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.54 E-value: 6.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIdgkPgkAKNKITVLLQENTIPN-SLKveELIA 95
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---P--AGARVLFLPQRPYLPLgTLR--EALL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 96 FFQSISDnpLTNQEVQE--------HLQFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFW 167
Cdd:COG4178 448 YPATAEA--FSDAELREaleavglgHLAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
170 180 190
....*....|....*....|....*....|....*.
gi 1081348506 168 EIVNDlKKSGVTILYSSHyIEEVEHTADRILVLHQG 203
Cdd:COG4178 526 QLLRE-ELPGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-216 |
6.96e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.57 E-value: 6.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 2 SETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK--PG-------KAK 72
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEniPAmsrsrlyTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 73 NKITVLLQENTIPNSLKVEELIAFfqsisdnPLtnqevQEHLQFKED-----------------QYQQFADKLSGGQRRL 135
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAY-------PL-----REHTQLPAPllhstvmmkleavglrgAAKLMPSELSGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 136 LAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAM 214
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
..
gi 1081348506 215 RH 216
Cdd:PRK11831 232 QA 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-206 |
8.59e-16 |
|
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: 77.03 E-value: 8.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 11 LGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGdKKPSSGQVLIDGKP-----GKA----KNKITVLLQE 81
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDldglsRRAlrplRRRMQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 82 ntiPNS-----LKVEELIAFFQSISDNPLTNQE----VQEHLQ---FKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKIL 149
Cdd:COG4172 371 ---PFGslsprMTVGQIIAEGLRVHGPGLSAAErrarVAEALEevgLDPAARHRYPHEFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348506 150 FLDEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:COG4172 448 VLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-205 |
1.13e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.14 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-GKAKNK--------ITVLLQENTIPNS 87
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDiTRLKNRevpflrrqIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 88 LKVEELIAFFQSISDnpLTNQEVQEHLQFKEDQY------QQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTS 161
Cdd:PRK10908 94 RTVYDNVAIPLIIAG--ASGDDIRRRVSAALDKVglldkaKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1081348506 162 TRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:PRK10908 172 LSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
16-206 |
1.83e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.30 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP------GKAKNKITVLLQ--------- 80
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPlsslshSVLRQGVAMVQQdpvvladtf 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 81 -----------ENTIPNSLKVEELIAFFQSISD---NPLTNQevqehlqfkedqyqqfADKLSGGQRRLLAFVLCLIDKP 146
Cdd:PRK10790 432 lanvtlgrdisEEQVWQALETVQLAELARSLPDglyTPLGEQ----------------GNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 147 KILFLDEPTAGMDTSTRQRFWEIVNDLKKSgVTILYSSHYIEE-VEhtADRILVLHQGKLI 206
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLSTiVE--ADTILVLHRGQAV 553
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-220 |
1.87e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.43 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCI--LGDKKPS---SGQVLIDGKPGKAKNKI 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 TVLL---------QENTIPNSlkVEELIAF---FQSISDNPLTNQEVQEHLQFK------EDQYQQFADKLSGGQRRLLA 137
Cdd:PRK14239 81 TVDLrkeigmvfqQPNPFPMS--IYENVVYglrLKGIKDKQVLDEAVEKSLKGAsiwdevKDRLHDSALGLSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 138 FVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSgVTILYSSHYIEEVEHTADRILVLHQGKLIR--DTTPYAMR 215
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEynDTKQMFMN 237
|
....*
gi 1081348506 216 HEEKE 220
Cdd:PRK14239 238 PKHKE 242
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-211 |
1.96e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.99 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 3 ETVIQVTSLGKR--------IKGktiLEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLI---------- 64
Cdd:TIGR03269 277 EPIIKVRNVSKRyisvdrgvVKA---VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmt 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 65 ----DGKpGKAKNKITVLLQENTI-PNSLKVEELIaffQSIS-DNP--LTNQEVQEHLQ---FKEDQYQQFADK----LS 129
Cdd:TIGR03269 354 kpgpDGR-GRAKRYIGILHQEYDLyPHRTVLDNLT---EAIGlELPdeLARMKAVITLKmvgFDEEKAEEILDKypdeLS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 130 GGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWE-IVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRD 208
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
...
gi 1081348506 209 TTP 211
Cdd:TIGR03269 510 GDP 512
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
13-204 |
3.72e-15 |
|
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: 72.50 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 13 KRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGkpgkaknKITVLLQENTIPN-SLKve 91
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------SIAYVSQEPWIQNgTIR-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 92 ELIAFFQsisdnPLTNQEVQEHL---QFKEDqYQQFADK-----------LSGGQRRLLAFVLCLIDKPKILFLDEPTAG 157
Cdd:cd03250 84 ENILFGK-----PFDEERYEKVIkacALEPD-LEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1081348506 158 MDTSTRQRFWE--IVNDLKKSGVTILySSHYIEEVEHtADRILVLHQGK 204
Cdd:cd03250 158 VDAHVGRHIFEncILGLLLNNKTRIL-VTHQLQLLPH-ADQIVVLDNGR 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
14-200 |
4.18e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 72.51 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 14 RIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKP---SSGQVLIDGKPGKAKN----KITVLLQENTI-P 85
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPaeqrRIGILFQDDLLfP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 86 NsLKVEELIAFfqSISDNPLTNQ---EVQEHLQfkEDQYQQFADK----LSGGQRRLLAFVLCLIDKPKILFLDEPTAGM 158
Cdd:COG4136 90 H-LSVGENLAF--ALPPTIGRAQrraRVEQALE--EAGLAGFADRdpatLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1081348506 159 DTSTRQRFWEIV-NDLKKSGVTILYSSHYIEEVEhTADRILVL 200
Cdd:COG4136 165 DAALRAQFREFVfEQIRQRGIPALLVTHDEEDAP-AAGRVLDL 206
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-211 |
6.86e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.86 E-value: 6.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNK------ITVLLQ--ENTIPNSLkVEE 92
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFeklrkhIGIVFQnpDNQFVGSI-VKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 93 LIAFfqSISDNPLTNQEVQEHLQ--FKEDQYQQFAD----KLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRF 166
Cdd:PRK13648 104 DVAF--GLENHAVPYDEMHRRVSeaLKQVDMLERADyepnALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1081348506 167 WEIVNDLKKS-GVTILYSSHYIEEVEHtADRILVLHQGKLIRDTTP 211
Cdd:PRK13648 182 LDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTP 226
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-206 |
7.30e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 74.54 E-value: 7.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVlidgkpgK-AKN-KITVLLQENT 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-------KwSENaNIGYYAQDHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 84 --IPNSLKVEELIAFFQSISDNPLTNQEVQEHLQFKEDQYQQFADKLSGG-QRRLLaFVLCLIDKPKILFLDEPTAGMDT 160
Cdd:PRK15064 393 ydFENDLTLFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGeKGRML-FGKLMMQKPNVLVMDEPTNHMDM 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081348506 161 STrqrfWEIVND-LKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:PRK15064 472 ES----IESLNMaLEKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-211 |
1.16e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.43 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKN------KITVLLQ--ENTIPNSlKVEE 92
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrrKIGMVFQnpDNQFVGA-TVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 93 LIAFfqSISDNPLTNQEVQEH----------LQFKEDQyqqfADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTST 162
Cdd:PRK13642 102 DVAF--GMENQGIPREEMIKRvdeallavnmLDFKTRE----PARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1081348506 163 RQRFWEIVNDLK-KSGVTILYSSHYIEEVEhTADRILVLHQGKLIRDTTP 211
Cdd:PRK13642 176 RQEIMRVIHEIKeKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKEAAP 224
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-189 |
1.73e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 73.13 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGD-------------KKPSSGQVLIDgkpgkAKNKI----TVLLQ 80
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqgysndltlfgRRRGSGETIWD-----IKKHIgyvsSSLHL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 81 ENTIPNSLKVEELIAFFQSISdnplTNQEVQEHLQFKEDQY-------QQFADK----LSGGQRRLLAFVLCLIDKPKIL 149
Cdd:PRK10938 348 DYRVSTSVRNVILSGFFDSIG----IYQAVSDRQQKLAQQWldilgidKRTADApfhsLSWGQQRLALIVRALVKHPTLL 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1081348506 150 FLDEPTAGMDTSTRQ---RFWEIvndLKKSGVT-ILYSSHYIEE 189
Cdd:PRK10938 424 ILDEPLQGLDPLNRQlvrRFVDV---LISEGETqLLFVSHHAED 464
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-204 |
2.07e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 72.30 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG----KPGKA-----KNKITVLLQEntiP-NSL-- 88
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdllKADPEaqkllRQKIQIVFQN---PyGSLnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 89 --KVEeliaffqSISDNPL---TN----------QEVQEHLQFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDE 153
Cdd:PRK11308 108 rkKVG-------QILEEPLlinTSlsaaerrekaLAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 154 PTAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGK 204
Cdd:PRK11308 181 PVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGR 232
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-206 |
2.18e-14 |
|
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: 70.37 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSlGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCI---LGDKKPSSGQVLIDGKPGK-AKNK-- 74
Cdd:cd03233 4 LSWRNISFTT-GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKeFAEKyp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 75 ---ITVLLQENTIPNsLKVEELIAFFQSISDNpltnqevqehlqfkedqyqQFADKLSGGQRRLLAFVLCLIDKPKILFL 151
Cdd:cd03233 83 geiIYVSEEDVHFPT-LTVRETLDFALRCKGN-------------------EFVRGISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 152 DEPTAGMDTSTRqrfWEIVNDLK----KSGVTILYS-SHYIEEVEHTADRILVLHQGKLI 206
Cdd:cd03233 143 DNSTRGLDSSTA---LEILKCIRtmadVLKTTTFVSlYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-211 |
2.34e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.84 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 9 TSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNKITVLlqENTIpnSL 88
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEAL--ENGI--SM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 89 KVEELIAFFQ-SISDN------PLTNQEVqEHLQFKEDQYQQFAD------------KLSGGQRRLLAFVLCLIDKPKIL 149
Cdd:PRK10982 78 VHQELNLVLQrSVMDNmwlgryPTKGMFV-DQDKMYRDTKAIFDEldididprakvaTLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 150 FLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIrDTTP 211
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI-ATQP 217
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
5-206 |
2.62e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.37 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILG--DKKPSSGQVLI-DGKPGKAKNKITVLLQE 81
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVpDNQFGREASLIDAIGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 82 NTIPnsLKVEELIAFfqSISDNPLtnqevqehlqfkedqYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTS 161
Cdd:COG2401 110 GDFK--DAVELLNAV--GLSDAVL---------------WLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081348506 162 TRQRFWEIVNDL-KKSGVTILYSSHyIEEVEHT--ADRILVLHQGKLI 206
Cdd:COG2401 171 TAKRVARNLQKLaRRAGITLVVATH-HYDVIDDlqPDLLIFVGYGGVP 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-208 |
3.07e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.28 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCI--LGDKKPS---SGQVLIDGKP-------GKAKNKITVLLQE-NT 83
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrMNDKVSGyrySGDVLLGGRSifnyrdvLEFRRRVGMLFQRpNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 84 IPNSL--------KVEELIAF--FQSISDNPLTNQEVQEHLQfkeDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDE 153
Cdd:PRK14271 113 FPMSImdnvlagvRAHKLVPRkeFRGVAQARLTEVGLWDAVK---DRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 154 PTAGMDTSTRQRFWEIVNDLKKSgVTILYSSHYIEEVEHTADRILVLHQGKLIRD 208
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-206 |
3.34e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.43 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 13 KRIKG-KTILEDISFEINQGDCVALIGPNGAGKTV----LMSCIlgdkkPSSGQVLIDGKPGKAKN---------KITVL 78
Cdd:PRK15134 293 KRTVDhNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNrrqllpvrhRIQVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 79 LQEntiPNS-----LKVEELIAFFQSISDNPLTNQE-------VQEHLQFKEDQYQQFADKLSGGQRRLLAFVLCLIDKP 146
Cdd:PRK15134 368 FQD---PNSslnprLNVLQIIEEGLRVHQPTLSAAQreqqviaVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 147 KILFLDEPTAGMDTSTRQRFWEIVNDLK-KSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQqKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-200 |
3.80e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.13 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 2 SETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK------PGKAKNKI 75
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 TVLLQENTIPNSLKVEELIAFFQSISDNPLTNQEVQEHLQFK--EDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDE 153
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLERFAlpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081348506 154 PTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHtADRILVL 200
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-210 |
4.57e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.49 E-value: 4.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 4 TVIQVTSLGKRIKG---------KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAknk 74
Cdd:PRK10419 2 TLLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 75 itvllqentipnsLKVEELIAF-------FQ-SISD-NP--------------LTN----------QEVQEHLQFKEDQY 121
Cdd:PRK10419 79 -------------LNRAQRKAFrrdiqmvFQdSISAvNPrktvreiireplrhLLSldkaerlaraSEMLRAVDLDDSVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 122 QQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLK-KSGVTILYSSHYIEEVEHTADRILVL 200
Cdd:PRK10419 146 DKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQqQFGTACLFITHDLRLVERFCQRVMVM 225
|
250
....*....|
gi 1081348506 201 HQGKLIRDTT 210
Cdd:PRK10419 226 DNGQIVETQP 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-224 |
4.81e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.26 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCI-----LGDKKPSSGQVLIDGK--------PGKAKNKITVLLQ-ENTIP 85
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRniyspdvdPIEVRREVGMVFQyPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 86 NsLKVEELIAFFQSISDNPLTNQEVQEHLQFK----------EDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPT 155
Cdd:PRK14267 99 H-LTIYDNVAIGVKLNGLVKSKKELDERVEWAlkkaalwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 156 AGMDTSTRQRFWEIVNDLKKSgVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAM----RHEEKEKQVT 224
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVfenpEHELTEKYVT 249
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-206 |
9.32e-14 |
|
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: 71.25 E-value: 9.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKG----KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILG----DKKPSSGQVLIDGK----- 67
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRllpdPAAHPSGSILFDGQdllgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 68 PGKAK-----NKITVLLQEntiP----NSLK-----VEELIAFFQSISDNPLtNQEVQEHLQF-----KEDQYQQFADKL 128
Cdd:COG4172 82 SERELrrirgNRIAMIFQE---PmtslNPLHtigkqIAEVLRLHRGLSGAAA-RARALELLERvgipdPERRLDAYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 129 SGGQR-R-LLAFVLCLidKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:COG4172 158 SGGQRqRvMIAMALAN--EPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
.
gi 1081348506 206 I 206
Cdd:COG4172 236 V 236
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-204 |
1.04e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.06 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 13 KRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSS--GQVLI-DGKPGKAKNKIT-VLLQENTIPNSL 88
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILAnNRKPTKQILKRTgFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 89 KVEELIAFFQSIS-DNPLTNQE-------VQEHLQFKEDQY----QQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTA 156
Cdd:PLN03211 156 TVRETLVFCSLLRlPKSLTKQEkilvaesVISELGLTKCENtiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1081348506 157 GMDTSTRQRFWEIVNDLKKSGVTILYSSHY-IEEVEHTADRILVLHQGK 204
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-195 |
1.17e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.53 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 4 TVIQVTSLGKriKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKA---KNKITVLLQ 80
Cdd:PRK15056 8 VVNDVTVTWR--NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQalqKNLVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 81 ENTIPNSLKV--EELI---------------AFFQSISDNPLTNQEVQEHlqfkedQYQQFADkLSGGQRRLLAFVLCLI 143
Cdd:PRK15056 86 SEEVDWSFPVlvEDVVmmgryghmgwlrrakKRDRQIVTAALARVDMVEF------RHRQIGE-LSGGQKKRVFLARAIA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 144 DKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTAD 195
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-162 |
1.18e-13 |
|
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: 70.73 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIdGKpgkaknkiTVLL----- 79
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GE--------TVKLayvdq 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 80 -QENTIPNSlkveeliAFFQSISDN----PLTNQEVQEH-----LQFK-EDQyQQFADKLSGGQRRLLAFVLCLIDKPKI 148
Cdd:TIGR03719 393 sRDALDPNK-------TVWEEISGGldiiKLGKREIPSRayvgrFNFKgSDQ-QKKVGQLSGGERNRVHLAKTLKSGGNV 464
|
170
....*....|....
gi 1081348506 149 LFLDEPTAGMDTST 162
Cdd:TIGR03719 465 LLLDEPTNDLDVET 478
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-205 |
1.23e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 68.65 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 2 SETVIQVTSLGKRI-KGK---TILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPG-------- 69
Cdd:PRK10584 3 AENIVEVHHLKKSVgQGEhelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdeear 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 70 ---KAKNKITVLLQENTIP--NSLKVEELIAFFQSISDNPLTNQEVQ--EHLQFKEDQYQQFAdKLSGGQRRLLAFVLCL 142
Cdd:PRK10584 83 aklRAKHVGFVFQSFMLIPtlNALENVELPALLRGESSRQSRNGAKAllEQLGLGKRLDHLPA-QLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 143 IDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-211 |
4.59e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 68.91 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG----KPGKA------KNKITVLLQENTIPNSLKV 90
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiaKISDAelrevrRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 91 EELIAFFQSISDNPLTNQEVQEHLQFKEDQYQQFA----DKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRF 166
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAhsypDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1081348506 167 W-EIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTP 211
Cdd:PRK10070 204 QdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-206 |
4.85e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 67.37 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 2 SETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCI--LGDKKPS---SGQVLIDGKPGKAKNKIT 76
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGarvEGEILLDGEDIYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 77 VLL---------QENTIPNSlkVEELIAF---FQSISDNPLTNQEVQEHLQ----FKE--DQYQQFADKLSGGQ-RRL-L 136
Cdd:COG1117 88 VELrrrvgmvfqKPNPFPKS--IYDNVAYglrLHGIKSKSELDEIVEESLRkaalWDEvkDRLKKSALGLSGGQqQRLcI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348506 137 AFVLCLidKPKILFLDEPTAGMD-TSTrQRFWEIVNDLKKSgVTILysshyIeeVEHT-------ADRILVLHQGKLI 206
Cdd:COG1117 166 ARALAV--EPEVLLMDEPTSALDpIST-AKIEELILELKKD-YTIV-----I--VTHNmqqaarvSDYTAFFYLGELV 232
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-203 |
5.37e-13 |
|
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: 67.57 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVlidgkpgKAKNKITVLLQENTI-PNSLKveELIA 95
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------KHSGRISFSSQFSWImPGTIK--ENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 96 FfqSISDNPLTNQEVQEHLQFKEDqYQQFADK-----------LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQ 164
Cdd:cd03291 120 F--GVSYDEYRYKSVVKACQLEED-ITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1081348506 165 RFWE-IVNDLKKSGVTILYSShyieEVEH--TADRILVLHQG 203
Cdd:cd03291 197 EIFEsCVCKLMANKTRILVTS----KMEHlkKADKILILHEG 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-203 |
5.67e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 69.17 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK-----------PGKAKNKITVLLQEN--- 82
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRisfspqtswimPGTIKDNIIFGLSYDeyr 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 83 --TIPNSLKVEELIAFFQSISDNPLTNQEVqehlqfkedqyqqfadKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDT 160
Cdd:TIGR01271 518 ytSVIKACQLEEDIALFPEKDKTVLGEGGI----------------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1081348506 161 STRQRFWE-IVNDLKKSGVTILYSShyieEVEH--TADRILVLHQG 203
Cdd:TIGR01271 582 VTEKEIFEsCLCKLMSNKTRILVTS----KLEHlkKADKILLLHEG 623
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-195 |
5.79e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 67.37 E-value: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETV--IQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCiLGDKKPSSGQVLIDGKP---------- 68
Cdd:PRK14258 1 MSKLIpaIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVeffnqniyer 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 69 ----GKAKNKITVLL-QENTIPNSlkVEELIAF------------FQSISDNPLTNQEVQEHLQFKedqYQQFADKLSGG 131
Cdd:PRK14258 80 rvnlNRLRRQVSMVHpKPNLFPMS--VYDNVAYgvkivgwrpkleIDDIVESALKDADLWDEIKHK---IHKSALDLSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 132 QRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLK-KSGVTILYSSHYIEEVEHTAD 195
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSD 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-210 |
1.02e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.38 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIK-GKT---ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP-GKAKNKI 75
Cdd:PRK11629 1 MNKILLQCDNLCKRYQeGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 TVLLQENTIPNSLKVEELIAFFQSISD--NPL---------TNQEVQEHLQFK--EDQYQQFADKLSGGQRRLLAFVLCL 142
Cdd:PRK11629 81 KAELRNQKLGFIYQFHHLLPDFTALENvaMPLligkkkpaeINSRALEMLAAVglEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348506 143 IDKPKILFLDEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIeEVEHTADRILVLHQGKLIRDTT 210
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLTAELS 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-215 |
1.12e-12 |
|
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: 66.28 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 27 EINQGDCVALIGPNGAGKTVLMSCILGDKKPSsgqvliDGKPGKAKNKITVLLQENTIPNSLKVEELIAffqSISDNPLT 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPD------EGDIEIELDTVSYKPQYIKADYEGTVRDLLS---SITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 107 ----NQEVQEHLQFkEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDL-KKSGVTIL 181
Cdd:cd03237 92 hpyfKTEIAKPLQI-EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaENNEKTAF 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1081348506 182 YSSHYIEEVEHTADRILVL--HQGKLIRDTTPYAMR 215
Cdd:cd03237 171 VVEHDIIMIDYLADRLIVFegEPSVNGVANPPQSLR 206
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-206 |
1.73e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.36 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 3 ETVIQVTSLG-KRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKP--GKAKNKITVL- 78
Cdd:COG3845 255 EVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDitGLSPRERRRLg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 79 --------LQENTIPN-SLkVEELIafFQSISDNPLTN------QEVQEHLQFKEDQY-------QQFADKLSGG--QRR 134
Cdd:COG3845 335 vayipedrLGRGLVPDmSV-AENLI--LGRYRRPPFSRggfldrKAIRAFAEELIEEFdvrtpgpDTPARSLSGGnqQKV 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 135 LLAfvLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:COG3845 412 ILA--RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-188 |
3.33e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 66.86 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILgDKKPSSGQVLIDGKpgkAKNKITvlLQE-----NTIPNslKVE 91
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGV---SWNSVT--LQTwrkafGVIPQ--KVF 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 92 ELIAFFQSISD--NPLTNQE---VQEHLQFKEdQYQQFADKL-----------SGGQRRLLAFVLCLIDKPKILFLDEPT 155
Cdd:TIGR01271 1303 IFSGTFRKNLDpyEQWSDEEiwkVAEEVGLKS-VIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
170 180 190
....*....|....*....|....*....|....*
gi 1081348506 156 AGMDTSTRQRfweIVNDLKK--SGVTILYSSHYIE 188
Cdd:TIGR01271 1382 AHLDPVTLQI---IRKTLKQsfSNCTVILSEHRVE 1413
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-206 |
5.67e-12 |
|
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: 66.00 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 19 TILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPgkaknkITVLLQEntipnSLKveELIA--- 95
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD------IRDVTQA-----SLR--AAIGivp 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 96 -----FFQSISDNPL------TNQEVQE-----HL-QFKEDQYQQFAD-------KLSGGQRRLLAFVLCLIDKPKILFL 151
Cdd:COG5265 439 qdtvlFNDTIAYNIAygrpdaSEEEVEAaaraaQIhDFIESLPDGYDTrvgerglKLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348506 152 DEPTAGMDTSTRQrfwEIVNDLKK--SGVTILYSSHYIEEVEHtADRILVLHQGKLI 206
Cdd:COG5265 519 DEATSALDSRTER---AIQAALREvaRGRTTLVIAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-162 |
8.83e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.14 E-value: 8.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 4 TVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIdGKpgkaknkiTVLL---- 79
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE--------TVKLayvd 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 80 Q-------ENTIpnslkveeliafFQSISDN----PLTNQEVQEH-----LQFK-EDQyQQFADKLSGGQR-RL-LAfvL 140
Cdd:PRK11819 394 QsrdaldpNKTV------------WEEISGGldiiKVGNREIPSRayvgrFNFKgGDQ-QKKVGVLSGGERnRLhLA--K 458
|
170 180
....*....|....*....|..
gi 1081348506 141 CLIDKPKILFLDEPTAGMDTST 162
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDVET 480
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-185 |
1.12e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.66 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKA-----KNKITVLL 79
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlctyQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 80 QENTIPNSLKVEELIAFFQSISDnplTNQEVQEHLQ-FKEDQYQQF-ADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAG 157
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIHFSP---GAVGITELCRlFSLEHLIDYpCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180
....*....|....*....|....*...
gi 1081348506 158 MDTSTRQRFWEIVNDLKKSGVTILYSSH 185
Cdd:PRK13540 158 LDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-199 |
1.64e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 27 EINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDgkpgkakNKITVLLQENTIPNSLKVEELIAFFQSISDNPLT 106
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------LKISYKPQYIKPDYDGTVEDLLRSITDDLGSSYY 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 107 NQEVQEHLQFkEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTR-------QRFWEivndlkKSGVT 179
Cdd:PRK13409 434 KSEIIKPLQL-ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavakaiRRIAE------EREAT 506
|
170 180
....*....|....*....|
gi 1081348506 180 ILYSSHYIEEVEHTADRILV 199
Cdd:PRK13409 507 ALVVDHDIYMIDYISDRLMV 526
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-159 |
1.67e-11 |
|
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: 64.19 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDgkPGKaknKITVLLQENTIPNSLKVEE---- 92
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ--PGI---KVGYLPQEPQLDPTKTVREnvee 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 93 -------LIAFFQSIS----------DNPLTNQ-EVQEHLQFK-----EDQYQQFAD------------KLSGGQRRLLA 137
Cdd:TIGR03719 92 gvaeikdALDRFNEISakyaepdadfDKLAAEQaELQEIIDAAdawdlDSQLEIAMDalrcppwdadvtKLSGGERRRVA 171
|
170 180
....*....|....*....|....
gi 1081348506 138 fvLC--LIDKPKILFLDEPTAGMD 159
Cdd:TIGR03719 172 --LCrlLLSKPDMLLLDEPTNHLD 193
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-185 |
2.11e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVlidgKPGKaknkitvllqenti 84
Cdd:PRK11147 319 VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGT-------------- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 85 pnslKVEelIAFF----------QSISDNpLTN--QEV-----QEH----LQ---FKEDQYQQFADKLSGGQR-RLLAFV 139
Cdd:PRK11147 381 ----KLE--VAYFdqhraeldpeKTVMDN-LAEgkQEVmvngrPRHvlgyLQdflFHPKRAMTPVKALSGGERnRLLLAR 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081348506 140 LCLidKP-KILFLDEPTAGMDTSTRQRFWEIVNDLKKsgvTILYSSH 185
Cdd:PRK11147 454 LFL--KPsNLLILDEPTNDLDVETLELLEELLDSYQG---TVLLVSH 495
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-206 |
2.27e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.88 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGkpgkaknkitVLLQENTIPNslkVEELIAFfqsI 100
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG----------HDLRDYTLAS---LRNQVAL---V 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 101 SDN-PLTNQEVQEHLQF-KEDQYQQ--------------FADK---------------LSGGQRRLLAFVLCLIDKPKIL 149
Cdd:PRK11176 423 SQNvHLFNDTIANNIAYaRTEQYSReqieeaarmayamdFINKmdngldtvigengvlLSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348506 150 FLDEPTAGMDTSTRQRFWEIVNDLKKSGvTILYSSHYIEEVEHtADRILVLHQGKLI 206
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-212 |
2.69e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 62.72 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 23 DISFEINQGDCValIGPNGAGKTVLMSCILGDKKPSSGQVLI-DGK-PGKAKNKITVLLQENTIPNSLKVEELIAFFQSI 100
Cdd:PRK13645 31 SLTFKKNKVTCV--IGTTGSGKSTMIQLTNGLIISETGQTIVgDYAiPANLKKIKEVKRLRKEIGLVFQFPEYQLFQETI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 101 SDN----PL----TNQEVQEHL-------QFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQR 165
Cdd:PRK13645 109 EKDiafgPVnlgeNKQEAYKKVpellklvQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEED 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081348506 166 FWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPY 212
Cdd:PRK13645 189 FINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-228 |
3.05e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.59 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMScILG--DKkPSSGQVLIDGKpgkaknkiTVLLQENTIPNSLKVEELIAFF 97
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGclDK-PTSGTYRVAGQ--------DVATLDADALAQLRREHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 98 QSISDNP-LT---NQEV----------------QEHLQFK--EDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPT 155
Cdd:PRK10535 93 QRYHLLShLTaaqNVEVpavyaglerkqrllraQELLQRLglEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 156 AGMDTSTRQRFWEIVNDLKKSGVTILYSSHYiEEVEHTADRILVLHQGKLIRDtTPYAMRHEEKEKQVTLPSS 228
Cdd:PRK10535 173 GALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRN-PPAQEKVNVAGGTEPVVNT 243
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-206 |
3.14e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.48 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 3 ETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNK-------I 75
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssqeagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 TVLLQE-NTIPNsLKVEELIAF-------FQSIsDNPLTNQEVQEHLQFKEDQY--QQFADKLSGGQRRLLAFVLCLIDK 145
Cdd:PRK10762 82 GIIHQElNLIPQ-LTIAENIFLgrefvnrFGRI-DWKKMYAEADKLLARLNLRFssDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 146 PKILFLDEPT-AGMDTSTRQRFwEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:PRK10762 160 SKVIIMDEPTdALTDTETESLF-RVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-215 |
4.66e-11 |
|
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: 62.88 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 27 EINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVlidgkpgKAKNKITVLLQENTIPNSLKVEELI--AFFQSISDNP 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------DEDLKISYKPQYISPDYDGTVEEFLrsANTDDFGSSY 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 105 LtNQEVQEHLQFkEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTR-------QRFWEivndlkKSG 177
Cdd:COG1245 435 Y-KTEIIKPLGL-EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavakaiRRFAE------NRG 506
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1081348506 178 VTILYSSHYIEEVEHTADRILVLH--QGKLIRDTTPYAMR 215
Cdd:COG1245 507 KTAMVVDHDIYLIDYISDRLMVFEgePGVHGHASGPMDMR 546
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-205 |
5.02e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.88 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVlidgkpGKAKN-KITVLLQENTipNSLKVEEliAF 96
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI------GLAKGiKLGYFAQHQL--EFLRADE--SP 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 97 FQSISDnpLTNQEVQEHLQ-------FKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEI 169
Cdd:PRK10636 395 LQHLAR--LAPQELEQKLRdylggfgFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
|
170 180 190
....*....|....*....|....*....|....*.
gi 1081348506 170 VNDLKKSGVTILYSSHYIEEvehTADRILVLHQGKL 205
Cdd:PRK10636 473 LIDFEGALVVVSHDRHLLRS---TTDDLYLVHDGKV 505
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-204 |
5.84e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.80 E-value: 5.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKG--KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGdKKPS------SGQVLIDGKP--------- 68
Cdd:PRK15134 8 IENLSVAFRQQQtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILR-LLPSppvvypSGDIRFHGESllhaseqtl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 69 -GKAKNKITVLLQENTIpnslkveeliaffqsiSDNPLTNQEVQ------------------EHLQFKE--------DQY 121
Cdd:PRK15134 87 rGVRGNKIAMIFQEPMV----------------SLNPLHTLEKQlyevlslhrgmrreaargEILNCLDrvgirqaaKRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 122 QQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVL 200
Cdd:PRK15134 151 TDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVM 230
|
....
gi 1081348506 201 HQGK 204
Cdd:PRK15134 231 QNGR 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-195 |
1.34e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.57 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCI--LGDKKPS---SGQVLIDGK--------PGKAKNKITVLLQE-NTIPN 86
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKnlyapdvdPVEVRRRIGMVFQKpNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 87 SLKveELIAFFQSISD-----NPLTNQEVQEHLQFKE--DQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMD 159
Cdd:PRK14243 106 SIY--DNIAYGARINGykgdmDELVERSLRQAALWDEvkDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1081348506 160 TSTRQRFWEIVNDLKKSgVTILYSSHYIEEVEHTAD 195
Cdd:PRK14243 184 PISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-203 |
1.34e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.88 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTI--LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPgkaknkitvLLQENTIPNSLKVEEL 93
Cdd:PRK15079 30 PPKTLkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKD---------LLGMKDDEWRAVRSDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 94 IAFFQS--ISDNP------------------LTNQEVQEHLQ-------FKEDQYQQFADKLSGGQRRLLAFVLCLIDKP 146
Cdd:PRK15079 101 QMIFQDplASLNPrmtigeiiaeplrtyhpkLSRQEVKDRVKammlkvgLLPNLINRYPHEFSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 147 KILFLDEPTAGMDTSTRQrfwEIVNDLKK----SGVTILYSSHYIEEVEHTADRILVLHQG 203
Cdd:PRK15079 181 KLIICDEPVSALDVSIQA---QVVNLLQQlqreMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-214 |
1.44e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.61 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPS--------SGQVLIDGKPGKAKNKI------TVLLQE 81
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPrlarlrAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 82 NTIPNSLKVEELI----------AFFQSISDNPLTNQEVQehLQFKEDQYQQFADKLSGGQ--RRLLAFVLCLI------ 143
Cdd:PRK13547 92 AQPAFAFSAREIVllgrypharrAGALTHRDGEIAWQALA--LAGATALVGRDVTTLSGGElaRVQFARVLAQLwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1081348506 144 -DKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAM 214
Cdd:PRK13547 170 aQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-205 |
1.51e-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: 61.89 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG----KPG--KAKNKITVLLQENTI-PNSLKVEe 92
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniaKIGlhDLRFKITIIPQDPVLfSGSLRMN- 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 93 lIAFFQSISDNPLTNQEVQEHLQ-FKEDQYQQF-------ADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTrq 164
Cdd:TIGR00957 1380 -LDPFSQYSDEEVWWALELAHLKtFVSALPDKLdhecaegGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET-- 1456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1081348506 165 rfweivNDLKKSGV-------TILYSSHYIEEV-EHTadRILVLHQGKL 205
Cdd:TIGR00957 1457 ------DNLIQSTIrtqfedcTVLTIAHRLNTImDYT--RVIVLDKGEV 1497
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-206 |
1.82e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.10 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKP----SSGQVLIDGKP---GKAKNKITVLLQENtiPNSL---- 88
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPvapCALRGRKIATIMQN--PRSAfnpl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 89 ------KVEELIAFFQSISDNPLTnqEVQEHLQFKEDQ--YQQFADKLSGG--QRRLLAFVLcLIDKPkILFLDEPTAGM 158
Cdd:PRK10418 96 htmhthARETCLALGKPADDATLT--AALEAVGLENAArvLKLYPFEMSGGmlQRMMIALAL-LCEAP-FIIADEPTTDL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1081348506 159 DTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:PRK10418 172 DVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
17-159 |
2.48e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.03 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLidgkpGKAKNKITVLLQENTIPNSLKVEELIAF 96
Cdd:PLN03073 521 GPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----RSAKVRMAVFSQHHVDGLDLSSNPLLYM 595
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1081348506 97 FQSISDNPltNQEVQEHL---QFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMD 159
Cdd:PLN03073 596 MRCFPGVP--EQKLRAHLgsfGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-205 |
2.66e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK------PGKAKNKITVLLQENT----IPNSLKV 90
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKkinnhnANEAINHGFALVTEERrstgIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 91 E--ELIAFFQS-------ISDNPLTN--QEVQEHLQFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMD 159
Cdd:PRK10982 344 GfnSLISNIRNyknkvglLDNSRMKSdtQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1081348506 160 TSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:PRK10982 424 VGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-206 |
2.90e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 60.27 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 35 ALIGPNGAGKTVLMSCILGDKKPSSG------QVLIDGKPG----KAKNKITVLLQENTIPNSLKVEELIAFFQSISDNP 104
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGrivlngRVLFDAEKGiclpPEKRRIGYVFQDARLFPHYKVRGNLRYGMAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 105 LTNQEVQ----EHLqfkedqYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTStRQRfwEIVNDL----KKS 176
Cdd:PRK11144 108 QFDKIVAllgiEPL------LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP-RKR--ELLPYLerlaREI 178
|
170 180 190
....*....|....*....|....*....|
gi 1081348506 177 GVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:PRK11144 179 NIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-206 |
3.59e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.25 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNKITVLLQENTIPNSLKVE--ELIAFFQ 98
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRHVRgaDMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 99 S--ISDNPL--TNQEVQEHLQFKE---------------DQYQ---------QFADKLSGGQRRLLAFVLCLIDKPKILF 150
Cdd:PRK10261 112 EpmTSLNPVftVGEQIAESIRLHQgasreeamveakrmlDQVRipeaqtilsRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1081348506 151 LDEPTAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
15-156 |
4.07e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.28 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 15 IKGKTIL-EDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNkiTVLLQE-------NTIPN 86
Cdd:PRK13538 10 ERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR--DEYHQDllylghqPGIKT 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348506 87 SLKVEELIAFFQSISdNPLTNQEVQEHLQfkedqyQQ----FAD----KLSGGQRRLLAFVLCLIDKPKILFLDEP-TA 156
Cdd:PRK13538 88 ELTALENLRFYQRLH-GPGDDEALWEALA------QVglagFEDvpvrQLSAGQQRRVALARLWLTRAPLWILDEPfTA 159
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-234 |
4.68e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG----KPGKAK-NKITVLLQENTIPNSLKVEELI 94
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvaKFGLTDlRRVLSIIPQSPVLFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 95 AFFQSISDNPLTNQEVQEHLQ-------FKED-QYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRF 166
Cdd:PLN03232 1331 DPFSEHNDADLWEALERAHIKdvidrnpFGLDaEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI 1410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1081348506 167 WEIVNDLKKSgVTILYSSHYIEEVEhTADRILVLHQGKLIRDTTPYAMRHEEKekqvtlpSSFVSIVH 234
Cdd:PLN03232 1411 QRTIREEFKS-CTMLVIAHRLNTII-DCDKILVLSSGQVLEYDSPQELLSRDT-------SAFFRMVH 1469
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-206 |
5.13e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.78 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNKITV--- 77
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALsea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 78 ----LL-------QENtiP-NSLKV---------EELIAF----FQSISDNPLT-NQEVQEHLQFKEDQYQQFadklSGG 131
Cdd:PRK11701 82 errrLLrtewgfvHQH--PrDGLRMqvsaggnigERLMAVgarhYGDIRATAGDwLERVEIDAARIDDLPTTF----SGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348506 132 QRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWE----IVNDLkksGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDllrgLVREL---GLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-205 |
5.92e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 58.67 E-value: 5.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 16 KGKTI--LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGkpgkaknKITVLLQENTIPNSLKVEEL 93
Cdd:PRK13546 33 KNKTFfaLDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-------EVSVIAISAGLSGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 94 IAF------FQSISDNPLTnQEVQEHLQFKEDQYQQfADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFW 167
Cdd:PRK13546 106 IEFkmlcmgFKRKEIKAMT-PKIIEFSELGEFIYQP-VKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1081348506 168 EIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:PRK13546 184 DKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-220 |
6.49e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 6.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDkkpssgQVLIDGKPGKAKNKITVLLQENT-----------IPNSL 88
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGE------VLLDDGRIIYEQDLIVARLQQDPprnvegtvydfVAEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 89 K-VEELIAFFQSISDNPLTN------------QEVQEHL---QFkEDQYQQF-------ADK----LSGGQRRLLAFVLC 141
Cdd:PRK11147 92 EeQAEYLKRYHDISHLVETDpseknlnelaklQEQLDHHnlwQL-ENRINEVlaqlgldPDAalssLSGGWLRKAALGRA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348506 142 LIDKPKILFLDEPTAGMDTSTRQrfWeIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLIRDTTPYAMRHEEKE 220
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIETIE--W-LEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKE 246
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-203 |
1.51e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 15 IKGKT--ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKP---SSGQVLIDGKPGKAK-NKITVLLQENTI--PN 86
Cdd:TIGR00956 771 IKKEKrvILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSfQRSIGYVQQQDLhlPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 87 SLKVEELI--AFF---QSISDNPlTNQEVQEHLQFKEdqYQQFADKLSG--------GQRRLLAFVLCLIDKPK-ILFLD 152
Cdd:TIGR00956 851 STVRESLRfsAYLrqpKSVSKSE-KMEYVEEVIKLLE--MESYADAVVGvpgeglnvEQRKRLTIGVELVAKPKlLLFLD 927
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1081348506 153 EPTAGMDTstrQRFWEIVNDLKK---SGVTILYSSH-----YIEEVehtaDRILVLHQG 203
Cdd:TIGR00956 928 EPTSGLDS---QTAWSICKLMRKladHGQAILCTIHqpsaiLFEEF----DRLLLLQKG 979
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-205 |
1.55e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.36 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGkpgkAKNKITVLLQENTIPNSLKVEELIAFFQSi 100
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG----SAALIAISSGLNGQLTGIENIELKGLMMG- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 101 sdnpLTNQEVQEHLQfkedQYQQFAD----------KLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIV 170
Cdd:PRK13545 115 ----LTKEKIKEIIP----EIIEFADigkfiyqpvkTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190
....*....|....*....|....*....|....*
gi 1081348506 171 NDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKL 205
Cdd:PRK13545 187 NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
17-205 |
5.66e-09 |
|
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: 56.02 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILgDKKPSSGQVLIDGKpgkakNKITVLLQENTIPNSLKVEELIAF 96
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGV-----SWNSVPLQKWRKAFGVIPQKVFIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 97 FQSISDN--PLTNQEVQEHLQFKEDQ-----YQQFADKL-----------SGGQRRLLAFVLCLIDKPKILFLDEPTAGM 158
Cdd:cd03289 90 SGTFRKNldPYGKWSDEEIWKVAEEVglksvIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1081348506 159 DTSTRQrfwEIVNDLKK--SGVTILYSSHYIEEVEHtADRILVLHQGKL 205
Cdd:cd03289 170 DPITYQ---VIRKTLKQafADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-204 |
6.51e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.89 E-value: 6.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 19 TILEDISFEINQGDCVALIGPNGAGKT----VLMScILGDKKPSSGQVLIDGKpgkaknkiTVL-LQENTIpNSLKVEEL 93
Cdd:PRK09473 30 TAVNDLNFSLRAGETLGIVGESGSGKSqtafALMG-LLAANGRIGGSATFNGR--------EILnLPEKEL-NKLRAEQI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 94 IAFFQS--ISDNPL--TNQEVQEHLQF-----KEDQYQQ-------------------FADKLSGGQRRLLAFVLCLIDK 145
Cdd:PRK09473 100 SMIFQDpmTSLNPYmrVGEQLMEVLMLhkgmsKAEAFEEsvrmldavkmpearkrmkmYPHEFSGGMRQRVMIAMALLCR 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 146 PKILFLDEPTAGMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGK 204
Cdd:PRK09473 180 PKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-185 |
6.67e-09 |
|
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: 56.68 E-value: 6.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMScILGDKKPSSGQVLIdgKPgkAKNKITVLLQENTIPNSLKVEELI-- 94
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLT--KP--AKGKLFYVPQRPYMTLGTLRDQIIyp 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 95 -----AFFQSISDNPLTN--QEVQ-EHLQFKE---DQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTR 163
Cdd:TIGR00954 539 dssedMKRRGLSDKDLEQilDNVQlTHILEREggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE 618
|
170 180
....*....|....*....|..
gi 1081348506 164 QRfweIVNDLKKSGVTILYSSH 185
Cdd:TIGR00954 619 GY---MYRLCREFGITLFSVSH 637
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-211 |
7.11e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.67 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG----KPGKAK-NKITVLLQENTIPNSLKVEELI 94
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdisKFGLMDlRKVLGIIPQAPVLFSGTVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 95 AFFQSISDNPLTNQEVQEHL--------QFKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRF 166
Cdd:PLN03130 1334 DPFNEHNDADLWESLERAHLkdvirrnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALI 1413
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1081348506 167 WEIVNDLKKSgVTILYSSHYIEEVEhTADRILVLHQGKLIRDTTP 211
Cdd:PLN03130 1414 QKTIREEFKS-CTMLIIAHRLNTII-DCDRILVLDAGRVVEFDTP 1456
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-155 |
7.86e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRI-KGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDgkPGkaknkITV-- 77
Cdd:PRK11819 2 MAQYIYTMNRVSKVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA--PG-----IKVgy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 78 LLQENTIPNSLKVEE-----------LIAFFQSIS----------DNPLTNQ-EVQEHLQFK-----EDQYQQFAD---- 126
Cdd:PRK11819 75 LPQEPQLDPEKTVREnveegvaevkaALDRFNEIYaayaepdadfDALAAEQgELQEIIDAAdawdlDSQLEIAMDalrc 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081348506 127 --------KLSGGQRRLLAfvLC--LIDKPKILFLDEPT 155
Cdd:PRK11819 155 ppwdakvtKLSGGERRRVA--LCrlLLEKPDMLLLDEPT 191
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-206 |
9.05e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 55.68 E-value: 9.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPS----------SGQVLIDGKPGKAKN----KITVLLQEntiP 85
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwNGIDLLKLSPRERRKiigrEIAMIFQE---P 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 86 N-----SLKVEELIAffQSISDNPLTNQEVQEHLQFK---------------EDQYQQFADKLSGG--QRRLLAfvLCLI 143
Cdd:COG4170 99 SscldpSAKIGDQLI--EAIPSWTFKGKWWQRFKWRKkraiellhrvgikdhKDIMNSYPHELTEGecQKVMIA--MAIA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081348506 144 DKPKILFLDEPTAGMDTSTRQRFWEIVNDLKK-SGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-159 |
1.18e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKAKNK---ITVLLQENTIPNSLKVEELIAF 96
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRsrfMAYLGHLPGLKADLSTLENLHF 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 97 F--------QSISDNPLTNQEVQEHlqfkedqYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMD 159
Cdd:PRK13543 106 LcglhgrraKQMPGSALAIVGLAGY-------EDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
88-185 |
2.45e-08 |
|
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: 54.32 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 88 LKVEELIAFFQSISDNPLTNQEVQEHLQFKEDQYQQFADKLSGGQRRLLAFV---LCLIDKPKILFLDEPTAGMDTSTRQ 164
Cdd:pfam13304 197 LNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLaalLSALPKGGLLLIDEPESGLHPKLLR 276
|
90 100
....*....|....*....|.
gi 1081348506 165 RFWEIVNDLKKSGVTILYSSH 185
Cdd:pfam13304 277 RLLELLKELSRNGAQLILTTH 297
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-206 |
2.60e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.41 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 13 KRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMScILGDKKPS---SGQVLIDGKPGKAKN-------KITVLLQE- 81
Cdd:NF040905 9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMK-VLSGVYPHgsyEGEILFDGEVCRFKDirdsealGIVIIHQEl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 82 NTIPNsLKVEELIaFF------QSISDNPLTNQEVQEHLQ---FKEDQYQQFADkLSGGQRRLLAFVLCLIDKPKILFLD 152
Cdd:NF040905 88 ALIPY-LSIAENI-FLgnerakRGVIDWNETNRRARELLAkvgLDESPDTLVTD-IGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1081348506 153 EPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:NF040905 165 EPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-200 |
2.78e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGKA-------KNKITVLLQE-----NTIPNS 87
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKdinlkwwRSKIGVVSQDpllfsNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 88 LKV-------------------------------------------------EELIAF---FQSISDNPLTNQE----VQ 111
Cdd:PTZ00265 480 IKYslyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsNELIEMrknYQTIKDSEVVDVSkkvlIH 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 112 EHLQFKEDQYQQF----ADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLK--KSGVTILYsSH 185
Cdd:PTZ00265 560 DFVSALPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIII-AH 638
|
250
....*....|....*
gi 1081348506 186 YIEEVEHtADRILVL 200
Cdd:PTZ00265 639 RLSTIRY-ANTIFVL 652
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-201 |
3.24e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCIL----------------------------GDKKPSSG-------QVLI 64
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtneqdyqGDEEQNVGmknvnefSLTK 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 65 DGKPGKA----KNKITVLLQENTIPNsLKVEELIAFFQSISDNP-LTNQEVQEHLQF-KED------------------- 119
Cdd:PTZ00265 1263 EGGSGEDstvfKNSGKILLDGVDICD-YNLKDLRNLFSIVSQEPmLFNMSIYENIKFgKEDatredvkrackfaaidefi 1341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 120 -----QYQQ----FADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLK-KSGVTILYSSHYIEE 189
Cdd:PTZ00265 1342 eslpnKYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIAS 1421
|
250
....*....|..
gi 1081348506 190 VEHTaDRILVLH 201
Cdd:PTZ00265 1422 IKRS-DKIVVFN 1432
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-206 |
5.27e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDK--KPSSGQVLIDGKP------GKA-KNKIT-----------VLL 79
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEvdvstvSDAiDAGLAyvtedrkgyglNLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 80 ---QENTIPNSLKveeliaffqSISDNPLTNQ--EVQEHLQFKED------QYQQFADKLSGG-QRRLlafVLC--LIDK 145
Cdd:NF040905 355 ddiKRNITLANLG---------KVSRRGVIDEneEIKVAEEYRKKmniktpSVFQKVGNLSGGnQQKV---VLSkwLFTD 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 146 PKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:NF040905 423 PDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-238 |
6.29e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 25 SFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSG-----------------QVLIDgKPGKAKNkiTVLLQENTIPNS 87
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshitrlsfeqlQKLVS-DEWQRNN--TDMLSPGEDDTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 88 LKVEELIAffQSISDNPLTNQEVQ----EHL---QFKedqyqqfadKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDT 160
Cdd:PRK10938 100 RTTAEIIQ--DEVKDPARCEQLAQqfgiTALldrRFK---------YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 161 STRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTADRILVL------HQGK---LIRDTTPYAMRHEEKEKQVTLPSSF-V 230
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLadctlaETGEreeILQQALVAQLAHSEQLEGVQLPEPDeP 248
|
....*...
gi 1081348506 231 SIVHGLED 238
Cdd:PRK10938 249 SARHALPA 256
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-206 |
2.31e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.78 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK------PGK---AKNKITVLLQE---------- 81
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlsPGKlqaLRRDIQFIFQDpyasldprqt 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 82 --NTIPNSLKVEELIaffqsisDNPLTNQEVQEHLQ---FKEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTA 156
Cdd:PRK10261 420 vgDSIMEPLRVHGLL-------PGKAAAARVAWLLErvgLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 157 GMDTSTRQRFWEIVNDLKKS-GVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-203 |
2.48e-07 |
|
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: 50.41 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 17 GKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGK--------PGKAKNKITVLL--QENTIPN 86
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnesepsfeATRSRNRYSVAYaaQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 87 SlKVEELIAFfqsisDNPLTNQE---VQEHLQFKED-QYQQFADK---------LSGGQRRLLAFVLCLIDKPKILFLDE 153
Cdd:cd03290 93 A-TVEENITF-----GSPFNKQRykaVTDACSLQPDiDLLPFGDQteigerginLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 154 PTAGMDTSTRQRFWE--IVNDLKKSGVTILYSSHYIEEVEHtADRILVLHQG 203
Cdd:cd03290 167 PFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
22-198 |
2.81e-07 |
|
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: 49.91 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 22 EDISFEinqGDCVALIGPNGAGKTVLMSCIL----GDKKPSSGQVLIDGKP-GKAKNKITVLLQ-ENTIPNSLKVEELIA 95
Cdd:cd03240 16 SEIEFF---SPLTLIVGQNGAGKTTIIEALKyaltGELPPNSKGGAHDPKLiREGEVRAQVKLAfENANGKKYTITRSLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 96 FFQSI-------SDNPLTnqevqehlqfkedqyqQFADKLSGGQRRLLAFVL------CLIDKPKILFLDEPTAGMDT-S 161
Cdd:cd03240 93 ILENVifchqgeSNWPLL----------------DMRGRCSGGEKVLASLIIrlalaeTFGSNCGILALDEPTTNLDEeN 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1081348506 162 TRQRFWEIVNDLKKSGV--TILYSSHyiEEVEHTADRIL 198
Cdd:cd03240 157 IEESLAEIIEERKSQKNfqLIVITHD--EELVDAADHIY 193
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-212 |
3.75e-07 |
|
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: 51.48 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKpgkaknkITVLLQENTIPNSlKVEELIAFFQSI 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------VAYVPQQAWIQND-SLRENILFGKAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 101 sdNPLTNQEVQEHLQFKED-------QYQQFADK---LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIV 170
Cdd:TIGR00957 726 --NEKYYQQVLEACALLPDleilpsgDRTEIGEKgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHV 803
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1081348506 171 NDLK-----KSGVTILYSSHYIEEVehtaDRILVLHQGKlIRDTTPY 212
Cdd:TIGR00957 804 IGPEgvlknKTRILVTHGISYLPQV----DVIIVMSGGK-ISEMGSY 845
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-207 |
4.26e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.87 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKPgkaknkitvllqentIPNsLKVEELIAFF 97
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIP---------------LTK-LQLDSWRSRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 98 QSISDNPL-----------------TNQEVQE-------H---LQFKEDQYQQFADK---LSGGQRRLLAFVLCLIDKPK 147
Cdd:PRK10789 392 AVVSQTPFlfsdtvannialgrpdaTQQEIEHvarlasvHddiLRLPQGYDTEVGERgvmLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081348506 148 ILFLDEPTAGMDTSTRQrfwEIVNDLKK--SGVTILYSSHYIEEVEHtADRILVLHQGKLIR 207
Cdd:PRK10789 472 ILILDDALSAVDGRTEH---QILHNLRQwgEGRTVIISAHRLSALTE-ASEILVMQHGHIAQ 529
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-159 |
4.41e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 20 ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPS--SGQVLIDGKPGKAKN--KITVLLQENTI--PNSLKVEEL 93
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETfaRISGYCEQNDIhsPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 94 I--AFFQsisdnplTNQEV--QEHLQFKeDQYQQFAD---------------KLSGGQRRLLAFVLCLIDKPKILFLDEP 154
Cdd:PLN03140 975 IysAFLR-------LPKEVskEEKMMFV-DEVMELVEldnlkdaivglpgvtGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
....*
gi 1081348506 155 TAGMD 159
Cdd:PLN03140 1047 TSGLD 1051
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-206 |
5.31e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGD----KKPSSGQVLIDGKPG----KAKNKITVLLQENTI--PNs 87
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNtdgfHIGVEGVITYDGITPeeikKHYRGDVVYNAETDVhfPH- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 88 LKVEELIAF---FQSISDNP--LTNQEVQEHLQfkeDQY---------------QQFADKLSGGQRRLLAFVLCLIDKPK 147
Cdd:TIGR00956 153 LTVGETLDFaarCKTPQNRPdgVSREEYAKHIA---DVYmatyglshtrntkvgNDFVRGVSGGERKRVSIAEASLGGAK 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 148 ILFLDEPTAGMDTSTRqrfWEIVNDLKKSgVTILYSSHYI------EEVEHTADRILVLHQGKLI 206
Cdd:TIGR00956 230 IQCWDNATRGLDSATA---LEFIRALKTS-ANILDTTPLVaiyqcsQDAYELFDKVIVLYEGYQI 290
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
22-198 |
5.95e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.51 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 22 EDISFeiNQGDCVALIGPNGAGKTVLMSCILgdkkpssgqvlidgkpgkaknkitvllqentipnslkveeLIAFFQSIS 101
Cdd:cd03227 14 NDVTF--GEGSLTIITGPNGSGKSTILDAIG----------------------------------------LALGGAQSA 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 102 DNPLTNQEVQEHLQFKEDQYQQFADKLSGGQRRL----LAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSG 177
Cdd:cd03227 52 TRRRSGVKAGCIVAAVSAELIFTRLQLSGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKG 131
|
170 180
....*....|....*....|.
gi 1081348506 178 VTILYSSHYiEEVEHTADRIL 198
Cdd:cd03227 132 AQVIVITHL-PELAELADKLI 151
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-207 |
1.06e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.87 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 1 MSETVIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILG--DKKPSSGQVLIDGK----------- 67
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGEsildlepeera 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 68 --------------PGkAKNKITVLLQENTIPNSLKVEEL--IAFFQSISDNpLTNQEVQEHlqFKEdqyQQFADKLSGG 131
Cdd:CHL00131 83 hlgiflafqypieiPG-VSNADFLRLAYNSKRKFQGLPELdpLEFLEIINEK-LKLVGMDPS--FLS---RNVNEGFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 132 QRR---LLAFVLClidKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEH-TADRILVLHQGKLIR 207
Cdd:CHL00131 156 EKKrneILQMALL---DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYiKPDYVHVMQNGKIIK 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-203 |
1.57e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 48.69 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 6 IQVTSLGKRIKGKT-ILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGKpgkaknkitvllqenti 84
Cdd:PRK11650 4 LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR----------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 85 pnslKVEEL------IAF-FQ--------SISDN------------PLTNQEVQEHLQFKEdqYQQFAD----KLSGGQR 133
Cdd:PRK11650 67 ----VVNELepadrdIAMvFQnyalyphmSVRENmayglkirgmpkAEIEERVAEAARILE--LEPLLDrkprELSGGQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1081348506 134 RLLAFVLCLIDKPKILFLDEPTAGMDTSTR-QRFWEIvNDLKKS-GVTILYSSHyiEEVEHT--ADRILVLHQG 203
Cdd:PRK11650 141 QRVAMGRAIVREPAVFLFDEPLSNLDAKLRvQMRLEI-QRLHRRlKTTSLYVTH--DQVEAMtlADRVVVMNGG 211
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-207 |
3.31e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 5 VIQVTSLGKRIKGKTILEDISFEINQGDCVALIGPNGAGKTVLMSCILG--DKKPSSGQVLIDGK-------PGKAKNKI 75
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKdllelspEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 76 TVLLQENT-IPNSLKveeliAFFQSISDNPLTNQEVQEHL------QFKEDQYQQF---ADKL--------SGGQRRLLA 137
Cdd:PRK09580 81 FMAFQYPVeIPGVSN-----QFFLQTALNAVRSYRGQEPLdrfdfqDLMEEKIALLkmpEDLLtrsvnvgfSGGEKKRND 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 138 FVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIEEVEHTA-DRILVLHQGKLIR 207
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVK 226
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
118-211 |
4.00e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.49 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 118 EDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADR 196
Cdd:PRK15093 149 KDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADK 228
|
90
....*....|....*
gi 1081348506 197 ILVLHQGKLIRDTTP 211
Cdd:PRK15093 229 INVLYCGQTVETAPS 243
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-198 |
4.51e-06 |
|
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: 46.16 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALIGPNGAGKTVLMSCILgdkKPSSGQVLIDGKPGKAKNKITVLLQentipnslkveeliafFQSI 100
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL---YASGKARLISFLPKFSRNKLIFIDQ----------------LQFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 101 SDNPLT----NQEVQehlqfkedqyqqfadKLSGG--QRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLK 174
Cdd:cd03238 72 IDVGLGyltlGQKLS---------------TLSGGelQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLI 136
|
170 180
....*....|....*....|....
gi 1081348506 175 KSGVTILYSSHYiEEVEHTADRIL 198
Cdd:cd03238 137 DLGNTVILIEHN-LDVLSSADWII 159
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-203 |
7.42e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 30 QGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIdgkpgkaknkitvllqentipnslkveeliaffqsISDNPLTNQE 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------------------IDGEDILEEV 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 110 VQEHLQFKEDQYQqfaDKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIV------NDLKKSGVTILYS 183
Cdd:smart00382 46 LDQLLLIIVGGKK---ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrlllLLKSEKNLTVILT 122
|
170 180
....*....|....*....|....*
gi 1081348506 184 SHYIE-----EVEHTADRILVLHQG 203
Cdd:smart00382 123 TNDEKdlgpaLLRRRFDRRIVLLLI 147
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-201 |
1.30e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.87 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 27 EINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDGkpgkaknkITVLLQENTIpnslkveeliaffqsisdnplt 106
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG--------ITPVYKPQYI---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 107 nqevqehlqfkedqyqqfadKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGV-TILYSSH 185
Cdd:cd03222 71 --------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEH 130
|
170
....*....|....*.
gi 1081348506 186 YIEEVEHTADRILVLH 201
Cdd:cd03222 131 DLAVLDYLSDRIHVFE 146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-261 |
1.90e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPS-SGQVLIDGKPGKAKNK---ITVLLQENTIPNSLKVEEl 93
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVPQVswiFNATVRENILFGSDFESE- 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 94 iAFFQSISDNPLtnqevQEHLQ-FKEDQYQQFADK---LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTS-TRQRFWE 168
Cdd:PLN03232 709 -RYWRAIDVTAL-----QHDLDlLPGRDLTEIGERgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDS 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 169 IVNDLKKSGVTILYSS--HYIEEVehtaDRILVLHQGKLIRDTTpyamrHEEKEKQVTLPSSFVSIVHGLEDIYEVTEKR 246
Cdd:PLN03232 783 CMKDELKGKTRVLVTNqlHFLPLM----DRIILVSEGMIKEEGT-----FAELSKSGSLFKKLMENAGKMDATQEVNTND 853
|
250
....*....|....*
gi 1081348506 247 DVISFMTKDIEKVWQ 261
Cdd:PLN03232 854 ENILKLGPTVTIDVS 868
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-206 |
1.94e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.50 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 24 ISFEINQGDCVALIGPNGAGKTVLMSCILGdkkpssgqvLIDgKPGKAKNKITVLLQEN--TIPNSLKVEELIAFFQSIS 101
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMG---------LID-YPGRVMAEKLEFNGQDlqRISEKERRNLVGAEVAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 102 DNPLTNQ--------EVQEHLQF-----KEDQYQQFAD-------------------KLSGG--QRRLLAFVL-ClidKP 146
Cdd:PRK11022 96 QDPMTSLnpcytvgfQIMEAIKVhqggnKKTRRQRAIDllnqvgipdpasrldvyphQLSGGmsQRVMIAMAIaC---RP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 147 KILFLDEPTAGMDTSTRQRFWEIVNDL-KKSGVTILYSSHYIEEVEHTADRILVLHQGKLI 206
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-185 |
2.47e-05 |
|
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: 44.99 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQgDCVALIGPNGAGKTVLM---SCILG--------------DKKPSSGQVLIDGKPGKAKNKITVLLQENT 83
Cdd:COG3593 14 IKDLSIELSD-DLTVLVGENNSGKSSILealRLLLGpsssrkfdeedfylGDDPDLPEIEIELTFGSLLSRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 84 IPNSLKV------EELIAFFQSISD-------------------NPLTNQEVQEHLQFK-EDQYQQFADKLSGGQRRLLA 137
Cdd:COG3593 93 DKEELEEaleelnEELKEALKALNEllseylkelldgldlelelSLDELEDLLKSLSLRiEDGKELPLDRLGSGFQRLIL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 138 FVLCLI-------DKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSH 185
Cdd:COG3593 173 LALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-210 |
2.74e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKP-SSGQVLIDGkpgkaknKITVLLQENTIPNSlkveeliaf 96
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRG-------TVAYVPQVSWIFNA--------- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 97 fqSISDNPLTNQEvqehlqFKEDQYQQFAD------------------------KLSGGQRRLLAFVLCLIDKPKILFLD 152
Cdd:PLN03130 694 --TVRDNILFGSP------FDPERYERAIDvtalqhdldllpggdlteigergvNISGGQKQRVSMARAVYSNSDVYIFD 765
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1081348506 153 EPTAGMDTST-RQRFWEIVND--LKKSGVTILYSSHYIEEVehtaDRILVLHQGKLIRDTT 210
Cdd:PLN03130 766 DPLSALDAHVgRQVFDKCIKDelRGKTRVLVTNQLHFLSQV----DRIILVHEGMIKEEGT 822
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-205 |
2.85e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLidgkpgkAKNKITVLLQENTIPNSlKVEELIAFF 97
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------AERSIAYVPQQAWIMNA-TVRGNILFF 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 98 QsiSDNPLTNQEVQEHLQFKEDQYQ-------QFADK---LSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRfw 167
Cdd:PTZ00243 745 D--EEDAARLADAVRVSQLEADLAQlgggletEIGEKgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER-- 820
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1081348506 168 eIVNDL---KKSGVTILYSSHYIEEVEHtADRILVLHQGKL 205
Cdd:PTZ00243 821 -VVEECflgALAGKTRVLATHQVHVVPR-ADYVVALGDGRV 859
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-65 |
5.04e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 5.04e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLID 65
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD 61
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-201 |
1.66e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 42.35 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 31 GDCVALIGPNGAGKTVLMSCILGDKKPSSGQvlIDGKP----------GKA-KNKITVLLQE-----------NTIPNSL 88
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeildefrGSElQNYFTKLLEGdvkvivkpqyvDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 89 K--VEELIaffqSISDNPLTNQEVQEHLQFkEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRF 166
Cdd:cd03236 104 KgkVGELL----KKKDERGKLDELVDQLEL-RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1081348506 167 WEIVNDLKKSGVTILYSSHYIEEVEHTADRILVLH 201
Cdd:cd03236 179 ARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-218 |
2.82e-04 |
|
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: 41.43 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 18 KTILEDISFEINQGDCVALIGPNGAGKTVLMSCILGDKKPSSGQVLIDG------KPGKAKNKITVLLQE-----NTIPN 86
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklPLHTLRSRLSIILQDpilfsGSIRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 87 SLKVEeliaffQSISDNPLtnQEVQEHLQFK----------EDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTA 156
Cdd:cd03288 114 NLDPE------CKCTDDRL--WEALEIAQLKnmvkslpgglDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081348506 157 GMDTSTRQRFWEIVND--LKKSGVTILYSSHYIEEvehtADRILVLHQGKLIR-DTTPYAMRHEE 218
Cdd:cd03288 186 SIDMATENILQKVVMTafADRTVVTIAHRVSTILD----ADLVLVLSRGILVEcDTPENLLAQED 246
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
35-177 |
6.86e-04 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 39.60 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 35 ALIGPNGAGKTVLMSCI---LGDKKpssgqvlidGKPGKAKNKITVLLQENTIPNSLKVEeliAFFQSIsdNPLTNQEvq 111
Cdd:cd03239 26 AIVGPNGSGKSNIVDAIcfvLGGKA---------AKLRRGSLLFLAGGGVKAGINSASVE---ITFDKS--YFLVLQG-- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 112 ehlqfkedQYQQFadkLSGGQRRLLA----FVLCLIDKPKILFLDEPTAGMDTSTRQRFWEIVNDLKKSG 177
Cdd:cd03239 90 --------KVEQI---LSGGEKSLSAlaliFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHT 148
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
21-185 |
2.22e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.31 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 21 LEDISFEINQGDCVALI------------GPNGAGKTVLMSCILGDKKPSSGQVLIDGKPGK--AKNKITVLLQENTIPN 86
Cdd:PRK13541 4 LHQLQFNIEQKNLFDLSitflpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINniAKPYCTYIGHNLGLKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 87 SLKVEELIAFFQSISDNPLTNQEVQEHLQFkEDQYQQFADKLSGGQRRLLAFVLCLIDKPKILFLDEPTAGMDTSTRQRF 166
Cdd:PRK13541 84 EMTVFENLKFWSEIYNSAETLYAAIHYFKL-HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170
....*....|....*....
gi 1081348506 167 WEIVNDLKKSGVTILYSSH 185
Cdd:PRK13541 163 NNLIVMKANSGGIVLLSSH 181
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
123-211 |
3.42e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081348506 123 QFADKLSGG--QRRLLAFVLCLIDKPKILF-LDEPTAGMDTSTRQRFWEIVNDLKKSGVTILYSSHYIeEVEHTADRILV 199
Cdd:TIGR00630 825 QPATTLSGGeaQRIKLAKELSKRSTGRTLYiLDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL-DVIKTADYIID 903
|
90
....*....|....*...
gi 1081348506 200 L------HQGKLIRDTTP 211
Cdd:TIGR00630 904 LgpeggdGGGTVVASGTP 921
|
|
| |
