|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
9-257 |
5.82e-84 |
|
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: 251.50 E-value: 5.82e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSRRAEQVVYL 87
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSL-SLPPGEVTALLGPNGSGKSTLLRALAGlLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 88 PQTLPAGVHLHVLESIIV---AQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLL 164
Cdd:COG1120 81 PQEPPAPFGLTVRELVALgryPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 165 LDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAAVYGVRGR 244
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
250
....*....|...
gi 488981874 245 IEPCSQGVRQVII 257
Cdd:COG1120 241 VIEDPVTGRPLVL 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-224 |
1.82e-60 |
|
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: 189.18 E-value: 1.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 10 SLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQVVYLP 88
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSL-SIEAGEIVGILGPNGAGKSTLLKTLAGLlKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 89 QtlpagvhlhvlesiivaqraaggrhspqrqeevmaLLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEP 168
Cdd:cd03214 80 Q-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488981874 169 LSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDG 224
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-240 |
1.53e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 176.05 E-value: 1.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-----GPCRGELllegenlltQPFSRRAEQ 83
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSL-TIPPGEFVAIVGPNGAGKSTLLKAILGLlpptsGTVRLFG---------KPPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 84 VVYLPQ--TLPAGVHLHVLEsiIVA-----QRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSL 156
Cdd:COG1121 77 IGYVPQraEVDWDFPITVRD--VVLmgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 157 IRQPRLLLLDEPLSALDLNYQFHVMDLVRREtRRRNIVTLVVVHDINIALRHADHVLMLkAGQLLGDGTPAAVITPETLA 236
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLS 232
|
....
gi 488981874 237 AVYG 240
Cdd:COG1121 233 RAYG 236
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-247 |
9.06e-54 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 174.53 E-value: 9.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSRRAEQVVYL 87
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSL-TLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 88 PQTLPAGVHLHVLEsiIVAQ-RAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLI-------RQ 159
Cdd:COG4559 81 PQHSSLAFPFTVEE--VVALgRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 160 PRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVtLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAAVY 239
Cdd:COG4559 159 PRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGV-VAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
|
....*...
gi 488981874 240 GVRGRIEP 247
Cdd:COG4559 238 GADLRVLA 245
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-247 |
8.08e-50 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 164.56 E-value: 8.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 20 RRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAG-----LGPCRGELLLEGENLLTQPFSRRAeqvvYLPQTLPAG 94
Cdd:PRK13548 14 GRTLLDDVSL-TLRPGEVVAILGPNGAGKSTLLRALSGelspdSGEVRLNGRPLADWSPAELARRRA----VLPQHSSLS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 95 VHLHVLEsiIVAQ-RAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIR------QPRLLLLDE 167
Cdd:PRK13548 89 FPFTVEE--VVAMgRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 168 PLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAAVYGVRGRIEP 247
Cdd:PRK13548 167 PTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYGADVLVQP 246
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
9-250 |
3.00e-47 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 157.87 E-value: 3.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVPhLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRR-AEQVVYL 87
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLS-LPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 88 PQtlpagvHLHVLESIIVAQRAAGGRH---------SPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIR 158
Cdd:PRK11231 82 PQ------HHLTPEGITVRELVAYGRSpwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 159 QPRLLLLDEPLSALDLNYQFHVMDLVRR-ETRRRNIVTlvVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAA 237
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRElNTQGKTVVT--VLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRT 233
|
250
....*....|....*
gi 488981874 238 VYGVRGRI--EPCSQ 250
Cdd:PRK11231 234 VFDVEAEIhpEPVSG 248
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-216 |
8.50e-46 |
|
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: 152.69 E-value: 8.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 10 SLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPcrgeLLLEGENLLTQPFSRRAEQVVYLPQ 89
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSF-EVKPGEFLAIVGPNGAGKSTLLKAILGLLK----PTSGSIRVFGKPLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 90 ------TLPAGVhLHVLESIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLL 163
Cdd:cd03235 76 rrsidrDFPISV-RDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488981874 164 LLDEPLSALDLNYQFHVMDLVrRETRRRNIVTLVVVHDINIALRHADHVLMLK 216
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELL-RELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
18-241 |
2.70e-43 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 147.54 E-value: 2.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 18 YPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAGVH 96
Cdd:COG4604 11 YGGKVVLDDVSL-TIPKGGITALIGPNGAGKSTLLSMISRLlPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHINSR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 97 LHVLE---------SiivaqraaGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDE 167
Cdd:COG4604 90 LTVRElvafgrfpyS--------KGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488981874 168 PLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAAVYGV 241
Cdd:COG4604 162 PLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDT 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-224 |
1.38e-40 |
|
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: 139.19 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAeqVVYL 87
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSL-TVEPGEFLALLGPSGCGKTTLLRLIAGLeRPDSGEILIDGRDVTGVPPERRN--IGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 88 PQTLPAGVHLHVLESIIVAQRAAGGRHsPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDE 167
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPK-AEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488981874 168 PLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDG 224
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
9-240 |
2.83e-40 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 139.42 E-value: 2.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYP-RRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-----GPCRGELLLEGENLLTQPFSRRAe 82
Cdd:COG3638 3 LELRNLSKRYPgGTPALDDVSL-EIERGEFVALIGPSGAGKSTLLRCLNGLveptsGEILVDGQDVTALRGRALRRLRR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 83 QVVYLPQTLPAGVHLHVLESIIVAQ-------RAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQS 155
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGRlgrtstwRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 156 LIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAViTPETL 235
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL-TDAVL 239
|
....*
gi 488981874 236 AAVYG 240
Cdd:COG3638 240 REIYG 244
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-230 |
8.74e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 137.89 E-value: 8.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSRRAE------ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSL-TVEPGEIFGLLGPNGAGKTTTIRMLLGL---------------LRPTSGEVRvlgedv 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 83 ---------QVVYLPQTLPAGVHLHVLESIIVAQRAAGGRHSpQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLA 153
Cdd:COG1131 65 ardpaevrrRIGYVPQEPALYPDLTVRENLRFFARLYGLPRK-EARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488981874 154 QSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRREtRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVI 230
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-251 |
1.19e-39 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 138.38 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 1 MSDQTLS---GLSLSHFSAGYPRRKVIENLTVPhLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPF 77
Cdd:PRK10575 1 MQEYTNHsdtTFALRNVSFRVPGRTLLHPLSLT-FPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 78 SRR-AEQVVYLPQTLPAGVHLHVLESIIVAQ---RAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLA 153
Cdd:PRK10575 80 SKAfARKVAYLPQQLPAAEGMTVRELVAIGRypwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 154 QSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPE 233
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
250
....*....|....*...
gi 488981874 234 TLAAVYGVRGRIEPCSQG 251
Cdd:PRK10575 240 TLEQIYGIPMGILPHPAG 257
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-239 |
3.08e-39 |
|
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: 136.54 E-value: 3.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPR-RKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFS-----RRa 81
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSL-SINPGEFVALIGPSGAGKSTLLRCLNGLvEPTSGSVLIDGTDINKLKGKalrqlRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 82 eQVVYLPQTLPAGVHLHVLESIIVAQ-------RAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQ 154
Cdd:cd03256 79 -QIGMIFQQFNLIERLSVLENVLSGRlgrrstwRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 155 SLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAvITPET 234
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEV 236
|
....*
gi 488981874 235 LAAVY 239
Cdd:cd03256 237 LDEIY 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-238 |
8.30e-38 |
|
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: 138.88 E-value: 8.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYP--RRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGEL----LLEGENLLTQPFSRRAE 82
Cdd:COG1123 5 LEVRDLSVRYPggDVPAVDGVSL-TIAPGETVALVGESGSGKSTLALALMGLLPHGGRIsgevLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 83 QVVYLPQ-TLPAGVHLHVLESIIVAQRAaGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPR 161
Cdd:COG1123 84 RIGMVFQdPMTQLNPVTVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488981874 162 LLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT-PETLAAV 238
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAaPQALAAV 240
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
5-218 |
1.79e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 132.52 E-value: 1.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 5 TLSGLSLShFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAeqv 84
Cdd:COG1116 9 ELRGVSKR-FPTGGGGVTALDDVSL-TVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRG--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 85 vYLPQT---LPagvHLHVLESIIVAQRAAGGRHSpQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPR 161
Cdd:COG1116 84 -VVFQEpalLP---WLTVLDNVALGLELRGVPKA-ERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488981874 162 LLLLDEPLSALDlnYQ--FHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAG 218
Cdd:COG1116 159 VLLMDEPFGALD--ALtrERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-219 |
5.73e-37 |
|
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: 129.89 E-value: 5.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 10 SLSHFSAGYPR--RKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQVVY 86
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISL-TIKKGEFVLIVGPNGSGKSTLLRLLNGLlGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQTlPAG--VHLHVLESIIVAQRAAGGRHSpQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLL 164
Cdd:cd03225 80 VFQN-PDDqfFGPTVEEEVAFGLENLGLPEE-EIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488981874 165 LDEPLSALDLNYQFHVMDLVRRetRRRNIVTLVVV-HDINIALRHADHVLMLKAGQ 219
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKK--LKAEGKTIIIVtHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
34-240 |
7.64e-37 |
|
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: 130.50 E-value: 7.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQpfSRRAE------QVVYLPQTLPAGVHLHVLESIIVAQ 107
Cdd:TIGR02315 27 PGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITK--LRGKKlrklrrRIGMIFQHYNLIERLTVLENVLHGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 108 RAAG-------GRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHV 180
Cdd:TIGR02315 105 LGYKptwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 181 MDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAvITPETLAAVYG 240
Cdd:TIGR02315 185 MDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSE-LDDEVLRHIYG 243
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
34-245 |
6.21e-36 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 128.03 E-value: 6.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAGL----GPCRGELLLEGENLLTQPFSRRAeqvvYLPQTLPAGVHLHVLESIIVAQRA 109
Cdd:COG4138 21 AGELIHLIGPNGAGKSTLLARMAGLlpgqGEILLNGRPLSDWSAAELARHRA----YLSQQQSPPFAMPVFQYLALHQPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 110 AGgrHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIR-------QPRLLLLDEPLSALDLNYQFhVMD 182
Cdd:COG4138 97 GA--SSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQA-ALD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488981874 183 LVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAAVYGVRGRI 245
Cdd:COG4138 174 RLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRR 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-217 |
8.87e-36 |
|
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: 126.82 E-value: 8.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 5 TLSGLSLsHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-----GPCRGElllegenllTQPFSR 79
Cdd:cd03293 2 EVRNVSK-TYGGGGGAVTALEDISL-SVEEGEFVALVGPSGCGKSTLLRIIAGLerptsGEVLVD---------GEPVTG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 80 RAEQVVYLPQT---LPagvHLHVLESIIVAQRAAGGRHSpQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSL 156
Cdd:cd03293 71 PGPDRGYVFQQdalLP---WLTVLDNVALGLELQGVPKA-EARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488981874 157 IRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKA 217
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-229 |
9.86e-36 |
|
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: 127.61 E-value: 9.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 6 LSGLSLShFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSR-RAEQV 84
Cdd:COG1124 4 VRNLSVS-YGQGGRRVPVLKDVSL-EVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKaFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 85 VYLPQTLPAGVH-LHVLESIIVAQRAAGGRhsPQRQEEVMALLRQLGI-AHLAMSYLDQLSGGQKQLVGLAQSLIRQPRL 162
Cdd:COG1124 82 QMVFQDPYASLHpRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488981874 163 LLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
9-237 |
1.67e-35 |
|
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: 126.68 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPR-RKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQVVY 86
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSL-SIEKGEFVAIIGPNGSGKSTLLRLLNGLlKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQ---------TlpagvhlhVLESIIVAQRAAGgrHSP-QRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSL 156
Cdd:COG1122 80 VFQnpddqlfapT--------VEEDVAFGPENLG--LPReEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 157 IRQPRLLLLDEPLSALDLNYQFHVMDLVRReTRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT-PETL 235
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKR-LNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSdYELL 228
|
..
gi 488981874 236 AA 237
Cdd:COG1122 229 EE 230
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-245 |
2.43e-35 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 127.41 E-value: 2.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 4 QTLSGLSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRR-AE 82
Cdd:PRK10253 3 ESVARLRGEQLTLGYGKYTVAENLTV-EIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 83 QVVYLPQ--TLPAgvhlhvleSIIVAQRAAGGR--HSP-------QRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVG 151
Cdd:PRK10253 82 RIGLLAQnaTTPG--------DITVQELVARGRypHQPlftrwrkEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 152 LAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT 231
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
250
....*....|....
gi 488981874 232 PETLAAVYGVRGRI 245
Cdd:PRK10253 234 AELIERIYGLRCMI 247
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-237 |
2.95e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 129.11 E-value: 2.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 8 GLSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSRR---AEQV 84
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSL-EIASGELVALLGPSGSGKTTLLRIIAGL---------------ETPDSGRivlNGRD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 85 VYL---PQTLPAGV---------HLHVLESIivaqrAAGGRHSP----QRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQ 148
Cdd:COG1118 66 LFTnlpPRERRVGFvfqhyalfpHMTVAENI-----AFGLRVRPpskaEIRARVEELLELVQLEGLADRYPSQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 149 LVGLAQSLIRQPRLLLLDEPLSALDlnyqFHVMDLVRRETRR----RNIVTLVVVHDINIALRHADHVLMLKAGQLLGDG 224
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALD----AKVRKELRRWLRRlhdeLGGTTVFVTHDQEEALELADRVVVMNQGRIEQVG 216
|
250
....*....|....
gi 488981874 225 TPAAVIT-PETLAA 237
Cdd:COG1118 217 TPDEVYDrPATPFV 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-231 |
1.27e-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: 127.33 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 5 TLSGLSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGP-------CRGELLLEGENLLTQPF 77
Cdd:COG1123 262 EVRNLSKRYPVRGKGGVRAVDDVSL-TLRRGETLGLVGESGSGKSTLARLLLGLLRptsgsilFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 78 SRRAeQVVY------LPQTLPagvhlhVLESIIVAQRAAGGRHSPQRQEEVMALLRQLGI-AHLAMSYLDQLSGGQKQLV 150
Cdd:COG1123 341 RRRV-QMVFqdpyssLNPRMT------VGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 151 GLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVI 230
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
.
gi 488981874 231 T 231
Cdd:COG1123 494 A 494
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-224 |
3.58e-33 |
|
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: 120.30 E-value: 3.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRR----KVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGP----CRGELLLEGENLLTQPFSRR 80
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSF-SIKKGETLGLVGESGSGKSTLARAILGLLKptsgSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 81 AEQVVYLPQTlPAGV---HLHVLESIIVAQRAAGGRHSPQRQEE-VMALLRQLGIAHLAM-SYLDQLSGGQKQLVGLAQS 155
Cdd:cd03257 81 RKEIQMVFQD-PMSSlnpRMTIGEQIAEPLRIHGKLSKKEARKEaVLLLLVGVGLPEEVLnRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488981874 156 LIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDG 224
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-220 |
4.34e-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: 4.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 6 LSGLSLShFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-----GPCRGELLLEGENLLTQPFSRR 80
Cdd:cd03255 3 LKNLSKT-YGGGGEKVQALKGVSL-SIEKGEFVAIVGPSGSGKSTLLNILGGLdrptsGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 81 AEQVVYLPQT---LPagvHLHVLESIIVAQRAAGgRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLI 157
Cdd:cd03255 81 RRHIGFVFQSfnlLP---DLTALENVELPLLLAG-VPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488981874 158 RQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIAlRHADHVLMLKAGQL 220
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-229 |
5.64e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 122.90 E-value: 5.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 7 SGLSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFS-------- 78
Cdd:COG3842 4 PALELENVSKRYGDVTALDDVSL-SIEPGEFVALLGPSGCGKTTLLRMIAGF---------------ETPDSgrilldgr 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 79 --------RRaeQVVYLPQTL---PagvHLHVLESIivaqrAAG----GRHSPQRQEEVMALLRQLGIAHLAMSYLDQLS 143
Cdd:COG3842 68 dvtglppeKR--NVGMVFQDYalfP---HLTVAENV-----AFGlrmrGVPKAEIRARVAELLELVGLEGLADRYPHQLS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 144 GGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGD 223
Cdd:COG3842 138 GGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQV 217
|
....*.
gi 488981874 224 GTPAAV 229
Cdd:COG3842 218 GTPEEI 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-219 |
6.77e-33 |
|
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: 117.73 E-value: 6.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 10 SLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenlltqpfsrraeqvvylpq 89
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSL-TLKAGEIVALVGPNGSGKSTLLRAIAGL------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 90 TLPAGVHLHVLESIIvaqraaggrhspqRQEEVMALLRQLGiahlamsYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPL 169
Cdd:cd00267 49 LKPTSGEILIDGKDI-------------AKLPLEELRRRIG-------YVPQLSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488981874 170 SALDLNYQFHVMDLVRRETRRRNIVtLVVVHDINIALRHADHVLMLKAGQ 219
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTV-IIVTHDPELAELAADRVIVLKDGK 157
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-223 |
9.28e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 119.38 E-value: 9.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 6 LSGLSLShFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-----------Gpcrgelllegenllt 74
Cdd:COG1136 7 LRNLTKS-YGTGEGEVTALRGVSL-SIEAGEFVAIVGPSGSGKSTLLNILGGLdrptsgevlidG--------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 75 QPFSR---------RAEQVVYLPQT---LPagvHLHVLESIIVAQRAAGgRHSPQRQEEVMALLRQLGIAHLAMSYLDQL 142
Cdd:COG1136 70 QDISSlserelarlRRRHIGFVFQFfnlLP---ELTALENVALPLLLAG-VSRKERRERARELLERVGLGDRLDHRPSQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 143 SGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIvTLVVV-HDINIAlRHADHVLMLKAGQLL 221
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGT-TIVMVtHDPELA-ARADRVIRLRDGRIV 223
|
..
gi 488981874 222 GD 223
Cdd:COG1136 224 SD 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-220 |
9.68e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.07 E-value: 9.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-----GPCRGELLLEGENLLTQpfSRRaeQ 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSL-TLEAGECVAITGPSGSGKSTLLRALADLdpptsGEIYLDGKPLSAMPPPE--WRR--Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 84 VVYLPQTlPAGVHLHVLESIivaQRAAGGRHSPQRQEEVMALLRQLGIAHlamSYLDQ----LSGGQKQLVGLAQSLIRQ 159
Cdd:COG4619 76 VAYVPQE-PALWGGTVRDNL---PFPFQLRERKFDRERALELLERLGLPP---DILDKpverLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488981874 160 PRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQL 220
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-220 |
1.06e-31 |
|
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: 114.80 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSRRA------- 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISL-TVEKGEIYGLLGPNGAGKTTLIKIILGL---------------LKPDSGEIkvlgkdi 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 82 --------EQVVYLPQTLPAGVHLHVLEsiivaqraaggrhspqrqeevmallrqlgiahlamsYLDqLSGGQKQLVGLA 153
Cdd:cd03230 65 kkepeevkRRIGYLPEEPSLYENLTVRE------------------------------------NLK-LSGGMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488981874 154 QSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVtLVVVHDINIALRHADHVLMLKAGQL 220
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTI-LLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
32-231 |
1.30e-31 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 119.44 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSRR----------AEQVVYLP----------QT- 90
Cdd:COG4148 22 LPGRGVTALFGPSGSGKTTLLRAIAGL---------------ERPDSGRirlggevlqdSARGIFLPphrrrigyvfQEa 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 91 --LPagvHLHVLESIIVAQRAAGGRHSPQRQEEVMALLrqlGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEP 168
Cdd:COG4148 87 rlFP---HLSVRGNLLYGRKRAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488981874 169 LSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT 231
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
31-231 |
1.42e-31 |
|
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: 116.38 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQ-PFSRRAE-------QVvylPQTLPagvHLHVLES 102
Cdd:cd03219 22 SVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlPPHEIARlgigrtfQI---PRLFP---ELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 103 IIVAQRAAGGRHS---------PQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALD 173
Cdd:cd03219 96 VMVAAQARTGSGLllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488981874 174 LNYQFHVMDLVRReTRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT 231
Cdd:cd03219 176 PEETEELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
9-257 |
8.35e-31 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 115.69 E-value: 8.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVPHLPrGKITALLGPNGSGKSTLMRAMAG----LGPCRGELLLEGENLLTQPFS-----R 79
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEP-GRVTALLGRNGAGKSTLLKALAGdltgGGAPRGARVTGDVTLNGEPLAaidapR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 80 RAEQVVYLPQTLPAGVHLHVLESIIVA---QRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSL 156
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 157 ---------IRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPA 227
Cdd:PRK13547 161 aqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250 260 270
....*....|....*....|....*....|
gi 488981874 228 AVITPETLAAVYGVRGRIEPCSQGVRQVII 257
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRLVDAGDGVPPVIV 270
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
31-240 |
8.35e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.47 E-value: 8.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAgvHLHVLESIIVAQRA 109
Cdd:COG3840 21 TIAAGERVAILGPSGAGKSTLLNLIAGfLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFP--HLTVAQNIGLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 110 aGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETR 189
Cdd:COG3840 99 -GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488981874 190 RRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVI---TPETLAAVYG 240
Cdd:COG3840 178 ERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLdgePPPALAAYLG 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
9-241 |
1.16e-30 |
|
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: 114.41 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGlgpcrgelllegenlltqpfsrraeqvvYLP 88
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISW-TVKPGEHWAILGPNGAGKSTLLSLITG----------------------------DLP 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 89 QTlpAGVHLHVL------ESI--------IVAQRAAG--------------------GRH---SPQRQEEVMALLRQLGI 131
Cdd:COG1119 55 PT--YGNDVRLFgerrggEDVwelrkrigLVSPALQLrfprdetvldvvlsgffdsiGLYrepTDEQRERARELLELLGL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 132 AHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADH 211
Cdd:COG1119 133 AHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITH 212
|
250 260 270
....*....|....*....|....*....|
gi 488981874 212 VLMLKAGQLLGDGTPAAVITPETLAAVYGV 241
Cdd:COG1119 213 VLLLKDGRVVAAGPKEEVLTSENLSEAFGL 242
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-243 |
2.69e-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: 113.20 E-value: 2.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 8 GLSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRaeQVVY 86
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSL-DIPSGELVALLGPSGSGKTTLLRLIAGLeRPDSGTILFGGEDATDVPVQER--NVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQTLPAGVHLHVLESIIVAQRAAGGRHSP---QRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLL 163
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVKPRSERPpeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 164 LLDEPLSALDLNyqfhvmdlVRRETRR--------RNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETL 235
Cdd:cd03296 159 LLDEPFGALDAK--------VRKELRRwlrrlhdeLHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPAS 230
|
....*...
gi 488981874 236 AAVYGVRG 243
Cdd:cd03296 231 PFVYSFLG 238
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
9-201 |
3.46e-30 |
|
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: 112.19 E-value: 3.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAEQVVYLP 88
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSF-TLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 89 QTLPAGVHLHVLESIIVAQRAAGGRHSpqrQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEP 168
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRAD---REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|...
gi 488981874 169 LSALDLNYQFHVMDLVRRETRRRNIVtLVVVHD 201
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAV-LLTTHQ 190
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
18-229 |
4.82e-30 |
|
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: 112.64 E-value: 4.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 18 YPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSRRaEQVVYLPQTLPAGVH 96
Cdd:COG4555 11 YGKVPALKDVSF-TAKDGEITGLLGPNGAGKTTLLRMLAGlLKPDSGSILIDGEDVRKEPREAR-RQIGVLPDERGLYDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 97 LHVLEsIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNY 176
Cdd:COG4555 89 LTVRE-NIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488981874 177 QFHVMDLVRReTRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:COG4555 168 RRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
35-224 |
6.52e-30 |
|
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: 111.62 E-value: 6.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 35 GKITALLGPNGSGKSTLMRAMAGL-----GPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAGVHLHVLESIIVAQRA 109
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLekpdgGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 110 AGGRHSPQRQEEVMALLrqlGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETR 189
Cdd:cd03297 103 KRNREDRISVDELLDLL---GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 488981874 190 RRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDG 224
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-215 |
8.39e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 110.79 E-value: 8.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 17 GYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-----GPCRGelllegenlltqpfsRRAEQVVYLPQ-- 89
Cdd:NF040873 1 GYGGRPVLHGVDL-TIPAGSLTAVVGPNGSGKSTLLKVLAGVlrptsGTVRR---------------AGGARVAYVPQrs 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 90 TLPAGVHLHVLESIIV---AQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLD 166
Cdd:NF040873 65 EVPDSLPLTVRDLVAMgrwARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488981874 167 EPLSALDLNYQFHVMDLVRREtRRRNIVTLVVVHDINIALRHaDHVLML 215
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELVRRA-DPCVLL 191
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
26-231 |
1.07e-29 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 111.62 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPhlpRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSRR---AEQVVYLPQTLPAGV------- 95
Cdd:COG1126 21 SLDVE---KGEVVVIIGPSGSGKSTLLRCINLL---------------EEPDSGTitvDGEDLTDSKKDINKLrrkvgmv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 96 --------HLHVLESIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDE 167
Cdd:COG1126 83 fqqfnlfpHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488981874 168 PLSALD-------LNyqfhVMdlvrRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT 231
Cdd:COG1126 163 PTSALDpelvgevLD----VM----RDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
32-229 |
1.21e-29 |
|
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: 114.05 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGL-----------GPCRGELLLEGENlltqPFSRRAEQVVYLPQTL-PagvHLHV 99
Cdd:TIGR02142 20 LPGQGVTAIFGRSGSGKTTLIRLIAGLtrpdegeivlnGRTLFDSRKGIFL----PPEKRRIGYVFQEARLfP---HLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 100 LESIIVAQRAAGGRHSPQRQEEVMALLrqlGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFH 179
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488981874 180 VMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-203 |
2.47e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 109.88 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 8 GLSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAG-LGP---CRGELLLEGENLLTQPFSRRaeQ 83
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSL-TVAPGEILTLMGPSGSGKSTLLAAIAGtLSPafsASGEVLLNGRRLTALPAEQR--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 84 VVYLPQTLPAGVHLHVLESIIVAQRAAGGRhsPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLL 163
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALPPTIGR--AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488981874 164 LLDEPLSALD--LNYQFHvmDLVRRETRRRNIVTLVVVHDIN 203
Cdd:COG4136 156 LLDEPFSKLDaaLRAQFR--EFVFEQIRQRGIPALLVTHDEE 195
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
31-230 |
2.53e-29 |
|
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: 110.50 E-value: 2.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSRRaeQVVYLPQTLPAGVHLHVLESIivaqrA 109
Cdd:cd03299 21 EVERGDYFVILGPTGSGKSVLLETIAGfIKPDSGKILLNGKDITNLPPEKR--DISYVPQNYALFPHMTVYKNI-----A 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 110 AGGRH----SPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVR 185
Cdd:cd03299 94 YGLKKrkvdKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488981874 186 RETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVI 230
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-234 |
6.45e-29 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 112.10 E-value: 6.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 11 LSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrGELLLEGENLLTQPFSR---RAEQVVYL 87
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISL-DIPSGQMVALLGPSGSGKTTLLRIIAGL----EHQTSGHIRFHGTDVSRlhaRDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 88 PQTLPAGVHLHVLESIIVAQRAAGGRHSPQRQE---EVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLL 164
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAikaKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488981874 165 LDEPLSALDLNyqfhvmdlVRRETRR--RNI------VTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVI-TPET 234
Cdd:PRK10851 160 LDEPFGALDAQ--------VRKELRRwlRQLheelkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWrEPAT 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-230 |
7.73e-29 |
|
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: 114.93 E-value: 7.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRK--VIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFS-------- 78
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISL-TIKPGERVAIVGRSGSGKSTLLKLLLGL---------------YEPTSgrilidgi 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 79 ----------RRaeQVVYLPQTlpagVHLH---VLESIIVAQRAAGgrhspqrQEEVMALLRQLG----IAHLAMSYL-- 139
Cdd:COG2274 538 dlrqidpaslRR--QIGVVLQD----VFLFsgtIRENITLGDPDAT-------DEEIIEAARLAGlhdfIEALPMGYDtv 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 140 -----DQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRnivTLVVV-HDINIaLRHADHVL 213
Cdd:COG2274 605 vgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR---TVIIIaHRLST-IRLADRII 680
|
250
....*....|....*..
gi 488981874 214 MLKAGQLLGDGTPAAVI 230
Cdd:COG2274 681 VLDKGRIVEDGTHEELL 697
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
9-229 |
9.73e-29 |
|
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: 108.68 E-value: 9.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLT--QPFSRRAEQVVY 86
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSL-TVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglPPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQTLPAGVHLHVLESIIVAQRAAGGRHSPQRQEEVMAL-------LRQLGiahlamsylDQLSGGQKQLVGLAQSLIRQ 159
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELfprlkerRKQLA---------GTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 160 PRLLLLDEPLSALDLNYQFHVMDLVRREtRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
32-239 |
1.10e-28 |
|
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: 109.36 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFS------------RRAEQVVYL--------PQTL 91
Cdd:COG0411 27 VERGEIVGLIGPNGAGKTTLFNLITGF---------------YRPTSgrilfdgrditgLPPHRIARLgiartfqnPRLF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 92 PagvHLHVLESIIVAQRAAGG--------------RHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLI 157
Cdd:COG0411 92 P---ELTVLENVLVAAHARLGrgllaallrlprarREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 158 RQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAA 237
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPRVIE 248
|
..
gi 488981874 238 VY 239
Cdd:COG0411 249 AY 250
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
34-259 |
3.49e-28 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 108.10 E-value: 3.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAGVHLHVLESIIVAQRAagGR 113
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLHQPD--KT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 114 HSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIR-------QPRLLLLDEPLSALDLNyQFHVMDLVRR 186
Cdd:PRK03695 99 RTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVA-QQAALDRLLS 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488981874 187 ETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAAVYGVRgriepcsqgVRQVIIDG 259
Cdd:PRK03695 178 ELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVN---------FRRLDVEG 241
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-219 |
4.35e-28 |
|
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: 105.73 E-value: 4.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-----GPCRGELLLEGENLLTQPFSRRAEQ 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSL-NIEAGEIVALLGPSGSGKSTLLRCIAGLeepdsGSILIDGEDLTDLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 84 VVYL-PQTLPagvHLHVLESIIVAqraaggrhspqrqeevmallrqlgiahlamsyldqLSGGQKQLVGLAQSLIRQPRL 162
Cdd:cd03229 80 MVFQdFALFP---HLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488981874 163 LLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQ 219
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
26-220 |
1.61e-27 |
|
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: 105.30 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPhlpRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPfSRRAEQV------VYLPQTLPAgvHLHV 99
Cdd:cd03262 20 DLTVK---KGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDD-KKNINELrqkvgmVFQQFNLFP--HLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 100 LESIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFH 179
Cdd:cd03262 94 LENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488981874 180 VMDlVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQL 220
Cdd:cd03262 174 VLD-VMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
34-242 |
2.48e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 108.78 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAGVHLHVLESIIVAQ---RA 109
Cdd:PRK09536 28 EGSLVGLVGPNGAGKTTLLRAINGtLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDVRQVVEMGRtphRS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 110 AGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRR--E 187
Cdd:PRK09536 108 RFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRlvD 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488981874 188 TRRrniVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAAVYGVR 242
Cdd:PRK09536 188 DGK---TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDAR 239
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-228 |
6.36e-27 |
|
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: 109.08 E-value: 6.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 7 SGLSLSHFSAGYP-RRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSRRAEQV 84
Cdd:COG4988 335 PSIELEDVSFSYPgGRPALDGLSL-TIPPGERVALVGPSGAGKSTLLNLLLGfLPPYSGSILINGVDLSDLDPASWRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 85 VYLPQ--TLPAGVhlhVLESIIVAQRAAGgrhspqrQEEVMALLRQLGIAHLAMSY---LD--------QLSGGQKQLVG 151
Cdd:COG4988 414 AWVPQnpYLFAGT---IRENLRLGRPDAS-------DEELEAALEAAGLDEFVAALpdgLDtplgeggrGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488981874 152 LAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRniVTLVVVHDINiALRHADHVLMLKAGQLLGDGTPAA 228
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLA-LLAQADRILVLDDGRIVEQGTHEE 557
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-229 |
7.06e-27 |
|
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: 104.29 E-value: 7.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPfsrRAEQVVYLP 88
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSL-DVPRGEILAIIGGSGSGKSVLLKLIIGL---------------LRP---DSGEILVDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 89 QTLPA-------------GV---------HLHVLESIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQ 146
Cdd:COG1127 67 QDITGlsekelyelrrriGMlfqggalfdSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 147 KQLVGLAQSLIRQPRLLLLDEPLSALD------LNyqfhvmDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQL 220
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDpitsavID------ELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
....*....
gi 488981874 221 LGDGTPAAV 229
Cdd:COG1127 221 IAEGTPEEL 229
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
32-170 |
1.16e-26 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 101.19 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGLGPC---RGELLLEGENLLTQPFSRRaeQVVYLPQTLPAGVHLHVLESIIVAQR 108
Cdd:pfam00005 8 LNPGEILALVGPNGAGKSTLLKLIAGLLSPtegTILLDGQDLTDDERKSLRK--EIGYVFQDPQLFPRLTVRENLRLGLL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488981874 109 AAG--GRHSPQRQEEVMALLRQLGIAH-LAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLS 170
Cdd:pfam00005 86 LKGlsKREKDARAEEALEKLGLGDLADrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
32-224 |
1.52e-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: 102.57 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAgvHLHVLESIIVAqRAA 110
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFA--HLTVEQNVGLG-LSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 111 GGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRR 190
Cdd:cd03298 98 GLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAE 177
|
170 180 190
....*....|....*....|....*....|....
gi 488981874 191 RNIVTLVVVHDINIALRHADHVLMLKAGQLLGDG 224
Cdd:cd03298 178 TKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-226 |
3.15e-26 |
|
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: 102.32 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQVVYl 87
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSL-DIKEGEFFTLLGPSGCGKTTLLRLIAGFeTPTSGEILLDGKDITNLPPHKRPVNTVF- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 88 pQTLPAGVHLHVLESIIVAQRAAGGRHSPQRqEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDE 167
Cdd:cd03300 79 -QNYALFPHLTVFENIAFGLRLKKLPKAEIK-ERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488981874 168 PLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTP 226
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTP 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-239 |
3.86e-26 |
|
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: 102.24 E-value: 3.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQ-VVY 86
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSL-SVKQGEIVGLLGPNGAGKTTTFYMIVGLvKPDSGKILLDGQDITKLPMHKRARLgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQTLPAGVHLHVLESIIVAQRAAGgRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLD 166
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRG-LSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488981874 167 EPLSALDlnyQFHVMDLVR--RETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAAVY 239
Cdd:cd03218 159 EPFAGVD---PIAVQDIQKiiKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-219 |
4.51e-26 |
|
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: 101.20 E-value: 4.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrGELLLEGENLLTQPFSRRAEQVV-YL 87
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISF-SVEKGEIFGLLGPNGAGKTTTIRMILGI----ILPDSGEVLFDGKPLDIAARNRIgYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 88 PQTLPAGVHLHVLESIIVAQRAAGGRHSpQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDE 167
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKE-EARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488981874 168 PLSALDLNYQFHVMDLVrRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQ 219
Cdd:cd03269 155 PFSGLDPVNVELLKDVI-RELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-231 |
4.52e-26 |
|
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: 101.81 E-value: 4.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-----------GPCRGELLLEGEnlltQPF 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDL-DVRRGEILAIIGPSGSGKSTLLRLIVGLlrpdsgevlidGEDISGLSEAEL----YRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 78 SRRAeqvvylpqtlpaGV---------HLHVLESIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQ 148
Cdd:cd03261 76 RRRM------------GMlfqsgalfdSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 149 LVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAA 228
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
...
gi 488981874 229 VIT 231
Cdd:cd03261 224 LRA 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-220 |
4.57e-26 |
|
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: 101.18 E-value: 4.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 10 SLSHFSAGYPR-RKVIENLTVPhLPRGKITALLGPNGSGKSTLMRAMAGLGpcRGELLLEGENLLTQPFSRRAEQVVYLP 88
Cdd:cd03226 1 RIENISFSYKKgTEILDDLSLD-LYAGEIIALTGKNGAGKTTLAKILAGLI--KESSGSILLNGKPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 89 QTLpaGVHLH---VLESIIVAQRAAGGrhSPQRQEEVmalLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLL 165
Cdd:cd03226 78 QDV--DYQLFtdsVREELLLGLKELDA--GNEQAETV---LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488981874 166 DEPLSALDLNYQFHVMDLVRRETRRRNIVtLVVVHDINIALRHADHVLMLKAGQL 220
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAV-IVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
14-225 |
1.24e-25 |
|
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: 100.73 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 14 FSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-----GpcrGELLLEGENLLTQPFSRRAE--QVVY 86
Cdd:cd03258 11 FGDTGGKVTALKDVSL-SVPKGEIFGIIGRSGAGKSTLIRCINGLerptsG---SVLVDGTDLTLLSGKELRKArrRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQtlpagvHLHVLESIIVAQRAA-----GGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPR 161
Cdd:cd03258 87 IFQ------HFNLLSSRTVFENVAlpleiAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488981874 162 LLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGT 225
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
23-226 |
1.71e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 102.88 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 23 VIENLTVPhLPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQVVYlpQTLPAGVHLHVLE 101
Cdd:PRK11432 21 VIDNLNLT-IKQGTMVTLLGPSGCGKTTVLRLVAGLeKPTEGQIFIDGEDVTHRSIQQRDICMVF--QSYALFPHMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 102 SIIVAQRAAGgRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVM 181
Cdd:PRK11432 98 NVGYGLKMLG-VPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488981874 182 DLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTP 226
Cdd:PRK11432 177 EKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
9-219 |
6.88e-25 |
|
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: 97.07 E-value: 6.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYP--RRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenlltqpfsrraeqvvY 86
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSL-TIKPGEKVAIVGPSGSGKSTLLKLLLRL---------------------------Y 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQtlpAGvhlhvleSIIVaqraaGGRHspqrqeevmalLRQLGIAHL--AMSYLDQ-------------LSGGQKQLVG 151
Cdd:cd03228 53 DPT---SG-------EILI-----DGVD-----------LRDLDLESLrkNIAYVPQdpflfsgtireniLSGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488981874 152 LAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRniVTLVVVHDINiALRHADHVLMLKAGQ 219
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-226 |
7.18e-25 |
|
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: 100.65 E-value: 7.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 40 LLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQ-PFSRRAEQVVYlpQTLPAGVHLHVLESIIVAQRAAGGRHSpQR 118
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNvPPHLRHINMVF--QSYALFPHMTVEENVAFGLKMRKVPRA-EI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 119 QEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVV 198
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFV 157
|
170 180
....*....|....*....|....*...
gi 488981874 199 VHDINIALRHADHVLMLKAGQLLGDGTP 226
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTP 185
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
26-225 |
9.23e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 99.32 E-value: 9.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPHlprGKITALLGPNGSGKSTLMRAMAGL--GPCRGELLLEGENLLTQPFSRRAE-------QVVYLPQTLPAGVH 96
Cdd:PRK09984 24 DLNIHH---GEMVALLGPSGSGKSTLLRHLSGLitGDKSAGSHIELLGRTVQREGRLARdirksraNTGYIFQQFNLVNR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 97 LHVLESIIVAQ-------RAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPL 169
Cdd:PRK09984 101 LSVLENVLIGAlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488981874 170 SALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGT 225
Cdd:PRK09984 181 ASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-231 |
1.06e-24 |
|
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: 98.53 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYP-RRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQVVY 86
Cdd:cd03295 1 IEFENVTKRYGgGKKAVNNLNL-EIAKGEFLVLIGPSGSGKTTTMKMINRLiEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQTLPAGVHLHVLESI-IVAQRAAGGRHS-PQRQEEVMALLRqLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLL 164
Cdd:cd03295 80 VIQQIGLFPHMTVEENIaLVPKLLKWPKEKiRERADELLALVG-LDPAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488981874 165 LDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT 231
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
9-239 |
2.47e-24 |
|
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: 97.36 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLT-QPFSRRAEQ-VVY 86
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSL-EVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITgLPPHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQTlpAGV--HLHVLESIIVAQRAAGGRHSP-QRQEEVMAL-------LRQLGiahlamsylDQLSGGQKQLVGLAQSL 156
Cdd:COG0410 83 VPEG--RRIfpSLTVEENLLLGAYARRDRAEVrADLERVYELfprlkerRRQRA---------GTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 157 IRQPRLLLLDEPLSALDLNYQFHVMDLVRReTRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLA 236
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRR-LNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVR 230
|
...
gi 488981874 237 AVY 239
Cdd:COG0410 231 EAY 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
18-228 |
3.86e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 96.66 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 18 YPR-RKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-----------GpcrgelllegenlltQPFSR-RAEQV 84
Cdd:COG2884 11 YPGgREALSDVSL-EIEKGEFVFLTGPSGAGKSTLLKLLYGEerptsgqvlvnG---------------QDLSRlKRREI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 85 VYLPQTLpaGV---------HLHVLESIIVAQRAAGgRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQS 155
Cdd:COG2884 75 PYLRRRI--GVvfqdfrllpDRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488981874 156 LIRQPRLLLLDEPLSALDLNYQFHVMDLVrRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAA 228
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELL-EEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-229 |
6.87e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 98.61 E-value: 6.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 7 SGLSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFS---RRAEQ 83
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDL-DIEDGEFLVLLGPSGCGKSTLLRMIAGL---------------EDPTSgeiLIGGR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 84 VVylpQTLPAG------V--------HLHVLESIIVAQRAAgGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQL 149
Cdd:COG3839 66 DV---TDLPPKdrniamVfqsyalypHMTVYENIAFPLKLR-KVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 150 VGLAQSLIRQPRLLLLDEPLSALDlnyqFHVMDLVRRE----TRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGT 225
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLD----AKLRVEMRAEikrlHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
....
gi 488981874 226 PAAV 229
Cdd:COG3839 218 PEEL 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-229 |
7.03e-24 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 96.10 E-value: 7.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVPhLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGEL---------LLEGENLLTQPFSR 79
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLD-IPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdegevlldGKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 80 RAeQVVYLPQTlPAGVHLHVLESIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLD--QLSGGQKQLVGLAQSLI 157
Cdd:cd03260 80 RR-RVGMVFQK-PNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488981874 158 RQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVtlVVVHDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIV--IVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-220 |
8.64e-24 |
|
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: 95.40 E-value: 8.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSRR----AEQV 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNL-DIADGEFVVLLGPSGCGKTTTLRMIAGL---------------EEPTSGRiyigGRDV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 85 VYLP----------QTLPAGVHLHVLESIIVAQRAaggRHSPQRQ--EEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGL 152
Cdd:cd03301 65 TDLPpkdrdiamvfQNYALYPHMTVYDNIAFGLKL---RKVPKDEidERVREVAELLQIEHLLDRKPKQLSGGQRQRVAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488981874 153 AQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQL 220
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-206 |
1.10e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.47 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 1 MSDQTLSGLSLsHFSAGYPRRKVIE--NLTvphLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFS 78
Cdd:COG4525 1 MSMLTVRHVSV-RYPGGGQPQPALQdvSLT---IESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 79 RRAeqVVYLPQTL-PagvHLHVLESIIVAQRAAG-GRHspQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSL 156
Cdd:COG4525 77 DRG--VVFQKDALlP---WLNVLDNVAFGLRLRGvPKA--ERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488981874 157 IRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIAL 206
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEAL 199
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
9-243 |
1.26e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 95.95 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSRRAEQ----- 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSL-ELKPGKILTLLGPNGAGKSTLVRVVLGL---------------VAPDEGVIKRngklr 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 84 VVYLPQTLpagvHLHVLESIIVAQ--RAAGGrhspQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPR 161
Cdd:PRK09544 69 IGYVPQKL----YLDTTLPLTVNRflRLRPG----TKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 162 LLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKaGQLLGDGTPAAVITPETLAAVYGV 241
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVVSLHPEFISMFGP 219
|
..
gi 488981874 242 RG 243
Cdd:PRK09544 220 RG 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-221 |
2.23e-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: 94.65 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 21 RKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPcRGELLLEGENLLTQPFSRRAEQ--VVYLPQ---TLPagv 95
Cdd:cd03234 20 ARILNDVSL-HVESGQVMAILGSSGSGKTTLLDAISGRVE-GGGTTSGQILFNGQPRKPDQFQkcVAYVRQddiLLP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 96 HLHVLESIIVAQRAAGGRHSPQRQEEVMA---LLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSAL 172
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSSDAIRKKRVedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488981874 173 DLNYQFHVMDLVRRETRRRNIVtLVVVH----DIniaLRHADHVLMLKAGQLL 221
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIV-ILTIHqprsDL---FRLFDRILLLSSGEIV 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-224 |
4.98e-23 |
|
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: 93.41 E-value: 4.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGkITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAEQVVYLP 88
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSL-TLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 89 QTLPAGVHLHVLEsiIVAQRAA-GGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDE 167
Cdd:cd03264 79 QEFGVYPNFTVRE--FLDYIAWlKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488981874 168 PLSALDLNYQFHVMDLVRR--ETRrrniVTLVVVHDINIALRHADHVLMLKAGQLLGDG 224
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSElgEDR----IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-220 |
8.86e-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: 92.62 E-value: 8.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPhlpRGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAgvHLHVLESII 104
Cdd:TIGR01277 18 DLNVA---DGEIVAIMGPSGAGKSTLLNLIAGfIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFA--HLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 105 VAQRAaGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLV 184
Cdd:TIGR01277 93 LGLHP-GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 488981874 185 RRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQL 220
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-237 |
1.16e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 92.72 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAgvHLHVLESIIVAQrA 109
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGfLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFS--HLTVAQNIGLGL-N 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 110 AGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETR 189
Cdd:PRK10771 98 PGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488981874 190 RRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAA 237
Cdd:PRK10771 178 ERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASAS 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-229 |
3.10e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 93.25 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-----------GpcrgelllegenlltQPF 77
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSF-TVPKGEIFGLLGPNGAGKTTTIRIILGIlapdsgevlwdG---------------EPL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 78 SRRA--------------------EQVVYLPQtlpagvhLHvlesiivaqraagGRHSPQRQEEVMALLRQLGIAHLAMS 137
Cdd:COG4152 66 DPEDrrrigylpeerglypkmkvgEQLVYLAR-------LK-------------GLSKAEAKRRADEWLERLGLGDRANK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 138 YLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALD-LNYQfHVMDLVRRetRRRNIVTLVVV-HDINIALRHADHVLML 215
Cdd:COG4152 126 KVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDpVNVE-LLKDVIRE--LAAKGTTVIFSsHQMELVEELCDRIVII 202
|
250
....*....|....
gi 488981874 216 KAGQLLGDGTPAAV 229
Cdd:COG4152 203 NKGRKVLSGSVDEI 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
33-234 |
5.38e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 91.23 E-value: 5.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 33 PRGKITALLGPNGSGKSTLMRA-----MAGLGPCRGELLLEGENLLTQPFSRRA--EQVVYLPQTLPAGVHLHVLESIIV 105
Cdd:PRK11124 26 PQGETLVLLGPSGAGKSSLLRVlnlleMPRSGTLNIAGNHFDFSKTPSDKAIRElrRNVGMVFQQYNLWPHLTVQQNLIE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 106 AQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVr 185
Cdd:PRK11124 106 APCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSII- 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488981874 186 RETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPET 234
Cdd:PRK11124 185 RELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQPQT 233
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-230 |
7.00e-22 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 94.45 E-value: 7.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 8 GLSLSHFSAGYP--RRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQ-PFSRRAEQV 84
Cdd:COG4987 333 SLELEDVSFRYPgaGRPVLDGLSL-TLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 85 VYLPQTlpagVHLH---VLESIIVAQRAAGgrhspqrQEEVMALLRQLGIAHLAMSY---LD--------QLSGGQKQLV 150
Cdd:COG4987 412 AVVPQR----PHLFdttLRENLRLARPDAT-------DEELWAALERVGLGDWLAALpdgLDtwlgeggrRLSGGERRRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 151 GLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRnivTLVVV-HDInIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR---TVLLItHRL-AGLERMDRILVLEDGRIVEQGTHEEL 556
|
.
gi 488981874 230 I 230
Cdd:COG4987 557 L 557
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
9-235 |
8.00e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.79 E-value: 8.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYP--RRKVIENLTVPhLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSRRAEQVVY 86
Cdd:PRK13640 6 VEFKHVSFTYPdsKKPALNDISFS-IPRGSWTALIGHNGSGKSTISKLINGL---------------LLPDDNPNSKITV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQTLPAGVHLHVLESI-IVAQR--------------AAG----GRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQK 147
Cdd:PRK13640 70 DGITLTAKTVWDIREKVgIVFQNpdnqfvgatvgddvAFGlenrAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 148 QLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIAlRHADHVLMLKAGQLLGDGTPA 227
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPV 228
|
....*...
gi 488981874 228 AVITPETL 235
Cdd:PRK13640 229 EIFSKVEM 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
33-234 |
1.28e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.46 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 33 PRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTqpFSRR--AEQVVYLPQTLpaGV---------HLHVLE 101
Cdd:COG4161 26 PSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFD--FSQKpsEKAIRLLRQKV--GMvfqqynlwpHLTVME 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 102 SIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVM 181
Cdd:COG4161 102 NLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVV 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488981874 182 DLVrRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPET 234
Cdd:COG4161 182 EII-RELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQPQT 233
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
31-228 |
1.47e-21 |
|
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: 89.80 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAGL-----------GpcrgelllegenlltQPFSR---------RAEQVVYLPQT 90
Cdd:COG4181 34 EVEAGESVAIVGASGSGKSTLLGLLAGLdrptsgtvrlaG---------------QDLFAldedararlRARHVGFVFQS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 91 ---LPagvHLHVLESIIVAQRAAGGRHSPQRQEevmALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDE 167
Cdd:COG4181 99 fqlLP---TLTALENVMLPLELAGRRDARARAR---ALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488981874 168 PLSALDLNYQFHVMDLVRRETRRRNiVTLVVV-HDINIALRhADHVLMLKAGQLLGDGTPAA 228
Cdd:COG4181 173 PTGNLDAATGEQIIDLLFELNRERG-TTLVLVtHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
9-218 |
3.95e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.37 E-value: 3.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAeqVVYLP 88
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINL-TLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERG--VVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 89 QTLPAgvHLHVLESIIVAQRAAG-GRhsPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDE 167
Cdd:PRK11248 79 EGLLP--WRNVQDNVAFGLQLAGvEK--MQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488981874 168 PLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAG 218
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-229 |
5.40e-21 |
|
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: 89.43 E-value: 5.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 11 LSH-FSAGYP-RRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSrraEQVVYLP 88
Cdd:TIGR04521 6 VSYiYQPGTPfEKKALDDVSL-TIEDGEFVAIIGHTGSGKSTLIQHLNGL---------------LKPTS---GTVTIDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 89 QTLPA--GVHLH---------------------VLESIIVAQRAAGgrHSPQRQEE-VMALLRQLGIAHlamSYLDQ--- 141
Cdd:TIGR04521 67 RDITAkkKKKLKdlrkkvglvfqfpehqlfeetVYKDIAFGPKNLG--LSEEEAEErVKEALELVGLDE---EYLERspf 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 142 -LSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQL 220
Cdd:TIGR04521 142 eLSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKI 221
|
....*....
gi 488981874 221 LGDGTPAAV 229
Cdd:TIGR04521 222 VLDGTPREV 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-239 |
7.03e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.41 E-value: 7.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 6 LSGLSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLT-QPFSRRAEQV 84
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSL-TVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISlLPLHARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 85 V-YLPQTLPAGVHLHVLESIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLL 163
Cdd:PRK10895 80 IgYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488981874 164 LLDEPLSALDlnyQFHVMDLVR--RETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAAVY 239
Cdd:PRK10895 160 LLDEPFAGVD---PISVIDIKRiiEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
35-231 |
1.07e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.84 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 35 GKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFS-----RRAEQVVYlpQTLPAGVHLHVLESIIVAQRA 109
Cdd:PRK09493 27 GEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVderliRQEAGMVF--QQFYLFPHLTALENVMFGPLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 110 AGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDlVRRETR 189
Cdd:PRK09493 105 VRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLK-VMQDLA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488981874 190 RRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT 231
Cdd:PRK09493 184 EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
17-227 |
1.18e-20 |
|
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: 87.18 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 17 GYPRRKVIENLTVPhLPRGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSRRAEqVVYLPQ--TLPa 93
Cdd:cd03263 11 KKGTKPAVDDLSLN-VYKGEIFGLLGHNGAGKTTTLKMLTGeLRPTSGTAYINGYSIRTDRKAARQS-LGYCPQfdALF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 94 gVHLHVLESIIVAQRAAGGRHSpQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALD 173
Cdd:cd03263 88 -DELTVREHLRFYARLKGLPKS-EIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488981874 174 LNYQFHVMDLVRRETRRRNIvtLVVVHDINIALRHADHVLMLKAGQLLGDGTPA 227
Cdd:cd03263 166 PASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
9-226 |
1.23e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.62 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIE--NLTVPHlprGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQ-PFSRRAEQVV 85
Cdd:PRK09452 15 VELRGISKSFDGKEVISnlDLTINN---GEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 86 YLPQTL-PagvHLHVLESIIVAQRAAGgRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLL 164
Cdd:PRK09452 92 FQSYALfP---HMTVFENVAFGLRMQK-TPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488981874 165 LDEPLSALDlnYQFHV-MDL-VRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTP 226
Cdd:PRK09452 168 LDESLSALD--YKLRKqMQNeLKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
39-231 |
1.42e-20 |
|
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: 90.70 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 39 ALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQ--PFSRRAeQVVYLPQ--TLPAGVhlhVLESIIVAQRAAggrh 114
Cdd:TIGR03375 495 AIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQidPADLRR-NIGYVPQdpRLFYGT---LRDNIALGAPYA---- 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 115 spqRQEEVMALLRQLGIAHLAMSY---LD--------QLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDL 183
Cdd:TIGR03375 567 ---DDEEILRAAELAGVTEFVRRHpdgLDmqigergrSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDR 643
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488981874 184 VRRETRRRnivTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT 231
Cdd:TIGR03375 644 LKRWLAGK---TLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVLE 688
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-220 |
1.57e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.81 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrGELLLEGENLLTQPFSRRAEQVVYLP 88
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDL-HIPAGQFVAVVGRSGCGKSTLLRLLAGL----ETPSAGELLAGTAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 89 QT---LPAGvhlHVLESIIVAQRaagGRHSPQRQEEvmalLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLL 165
Cdd:PRK11247 88 QDarlLPWK---KVIDNVGLGLK---GQWRDAALQA----LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488981874 166 DEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQL 220
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
34-231 |
1.68e-20 |
|
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: 87.70 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAGL-----GPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAGVHLHVLESIivaqr 108
Cdd:cd03294 49 EGEIFVIMGLSGSGKSTLLRCINRLieptsGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENV----- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 109 AAG----GRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALD----LNYQFHV 180
Cdd:cd03294 124 AFGlevqGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDEL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488981874 181 MDLVRRetRRRNIVtlVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT 231
Cdd:cd03294 204 LRLQAE--LQKTIV--FITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
32-220 |
1.72e-20 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 86.69 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGL-----GPCRGELLLEGENLLTQ-PFSRRAEQVVYlpQTLPAGVHLHVLESIIV 105
Cdd:cd03292 24 ISAGEFVFLVGPSGAGKSTLLKLIYKEelptsGTIRVNGQDVSDLRGRAiPYLRRKIGVVF--QDFRLLPDRNVYENVAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 106 AQRAAGgrHSPQR-QEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLV 184
Cdd:cd03292 102 ALEVTG--VPPREiRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLL 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 488981874 185 RRETRRRNIVtLVVVHDINIALRHADHVLMLKAGQL 220
Cdd:cd03292 180 KKINKAGTTV-VVATHAKELVDTTRHRVIALERGKL 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-230 |
2.11e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.01 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 7 SGLSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQ-PFSRRAEQ-V 84
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSL-EVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlPMHKRARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 85 VYLPQTlpAGV--HLHVLESI-IVAQRAagGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPR 161
Cdd:COG1137 81 GYLPQE--ASIfrKLTVEDNIlAVLELR--KLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488981874 162 LLLLDEPLSALD-LNyqfhVMDLVR--RETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVI 230
Cdd:COG1137 157 FILLDEPFAGVDpIA----VADIQKiiRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEIL 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-224 |
8.28e-20 |
|
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: 84.95 E-value: 8.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 18 YP--RRKVIENLTVPHLPRGKItALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQVVYLPQTlpag 94
Cdd:cd03245 12 YPnqEIPALDNVSLTIRAGEKV-AIIGRVGSGKSTLLKLLAGLyKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQD---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 95 VHL---HVLESIIVAQRAAggrhspqRQEEVMALLRQLGIAHLA------MSYL-----DQLSGGQKQLVGLAQSLIRQP 160
Cdd:cd03245 87 VTLfygTLRDNITLGAPLA-------DDERILRAAELAGVTDFVnkhpngLDLQigergRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488981874 161 RLLLLDEPLSALDLNYQFHVMDLVRRETRRRnivTLVVVHDINIALRHADHVLMLKAGQLLGDG 224
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDK---TLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-219 |
9.05e-20 |
|
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: 84.44 E-value: 9.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 8 GLSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGlgpcrgelllegENLLTQPFSRRAEQVVYL 87
Cdd:cd03250 5 DASFTWDSGEQETSFTLKDINL-EVPKGELVAIVGPVGSGKSSLLSALLG------------ELEKLSGSVSVPGSIAYV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 88 PQT---LPAGVHlhvlESIIvaqraAGGRHSPQRQEEVM---ALLRQLGIahlaMSYLDQ---------LSGGQKQLVGL 152
Cdd:cd03250 72 SQEpwiQNGTIR----ENIL-----FGKPFDEERYEKVIkacALEPDLEI----LPDGDLteigekginLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488981874 153 AQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIaLRHADHVLMLKAGQ 219
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQL-LPHADQIVVLDNGR 204
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
31-223 |
1.11e-19 |
|
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: 83.25 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSrraeqvvylpqtlpaGvhlhvleSIIVAQRAA 110
Cdd:cd03216 22 SVRRGEVHALLGENGAGKSTLMKILSGL---------------YKPDS---------------G-------EILVDGKEV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 111 GgRHSPQRQeevmallRQLGIAhlaMSYldQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRReTRR 190
Cdd:cd03216 65 S-FASPRDA-------RRAGIA---MVY--QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRR-LRA 130
|
170 180 190
....*....|....*....|....*....|...
gi 488981874 191 RNIVTLVVVHDINIALRHADHVLMLKAGQLLGD 223
Cdd:cd03216 131 QGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-231 |
1.22e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.51 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 14 FSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGP-------CRGELLLEGENLLTQPFsRRAEQVVY 86
Cdd:PRK10419 18 LSGKHQHQTVLNNVSL-SLKSGETVALLGRSGCGKSTLARLLVGLESpsqgnvsWRGEPLAKLNRAQRKAF-RRDIQMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 lpQTLPAGVHLH--VLESIIVAQRAAGGRHSPQRQEEVMALLRQLGiahLAMSYLD----QLSGGQKQLVGLAQSLIRQP 160
Cdd:PRK10419 96 --QDSISAVNPRktVREIIREPLRHLLSLDKAERLARASEMLRAVD---LDDSVLDkrppQLSGGQLQRVCLARALAVEP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488981874 161 RLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT 231
Cdd:PRK10419 171 KLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
9-229 |
3.11e-19 |
|
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: 83.73 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQ--PFSRRAEQVVY 86
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSL-EVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKlpPHERARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQTLPAGVHLHVLESIIV--AQRAAGGRHSPQRQEEVMALLRQLgiahlamsyLDQ----LSGGQKQLVGLAQSLIRQP 160
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTglAALPRRSRKIPDEIYELFPVLKEM---------LGRrggdLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488981874 161 RLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:TIGR03410 151 KLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
32-230 |
3.85e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 85.86 E-value: 3.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGL-----GPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAGVHLHVLESIIVA 106
Cdd:PRK10070 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLieptrGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 107 QRAAGgRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMD-LVR 185
Cdd:PRK10070 131 MELAG-INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDeLVK 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488981874 186 RETRRRNIVTLvVVHDINIALRHADHVLMLKAGQLLGDGTPAAVI 230
Cdd:PRK10070 210 LQAKHQRTIVF-ISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
10-221 |
7.22e-19 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 82.37 E-value: 7.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 10 SLSH-FSAGYPRRKVIENLTVPHLPrGKITALLGPNGSGKSTLMRAMAGL-----GPCRGELLLEGENLLTQPFSRRaEQ 83
Cdd:TIGR02982 6 NLNHyYGHGSLRKQVLFDINLEINP-GEIVILTGPSGSGKTTLLTLIGGLrsvqeGSLKVLGQELHGASKKQLVQLR-RR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 84 VVYLPQTLPAGVHLHVLESIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLL 163
Cdd:TIGR02982 84 IGYIFQAHNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488981874 164 LLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIaLRHADHVLMLKAGQLL 221
Cdd:TIGR02982 164 LADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRI-LDVADRILQMEDGKLL 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-220 |
9.70e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.12 E-value: 9.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 6 LSGLSLShfsagYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFS-----RR 80
Cdd:COG0488 1 LENLSKS-----FGGRPLLDDVSL-SINPGDRIGLVGRNGAGKSTLLKILAGE---------------LEPDSgevsiPK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 81 AEQVVYLPQTLPAGVHLHVLESII---------------VAQRAAGGRHSPQRQEEVMALLRQLG----------IAH-- 133
Cdd:COG0488 60 GLRIGYLPQEPPLDDDLTVLDTVLdgdaelraleaeleeLEAKLAEPDEDLERLAELQEEFEALGgweaearaeeILSgl 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 134 -LAMSYLDQ----LSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDL-------NYqfhvmdLVRRETrrrnivTLVVV-H 200
Cdd:COG0488 140 gFPEEDLDRpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLesiewleEF------LKNYPG------TVLVVsH 207
|
250 260
....*....|....*....|....*
gi 488981874 201 DinialRH-----ADHVLMLKAGQL 220
Cdd:COG0488 208 D-----RYfldrvATRILELDRGKL 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-224 |
9.88e-19 |
|
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: 81.88 E-value: 9.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-----GPCRgelLLEGENLLTQPFSRRAEQ 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISL-HVKKGEIYGFLGPNGAGKTTTMKIILGLikpdsGEIT---FDGKSYQKNIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 84 VVYLPQTLPagvHLHVLESIIVAQRAAGGRHspqrqEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLL 163
Cdd:cd03268 77 LIEAPGFYP---NLTARENLRLLARLLGIRK-----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488981874 164 LLDEPLSALDLNYQFHVMDLVRREtRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDG 224
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-233 |
1.14e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.24 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 5 TLSGLSLSHfsagyPR-RKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenlltQPFSR---- 79
Cdd:COG4178 364 ALEDLTLRT-----PDgRPLLEDLSL-SLKPGERLLITGPSGSGKSTLLRAIAGL----------------WPYGSgria 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 80 --RAEQVVYLPQT--LPAGVHLHVLesiivAQRAAGGRHSPqrqEEVMALLRQLGIAHLAmSYLDQ-------LSGGQKQ 148
Cdd:COG4178 422 rpAGARVLFLPQRpyLPLGTLREAL-----LYPATAEAFSD---AELREALEAVGLGHLA-ERLDEeadwdqvLSLGEQQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 149 LVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRrniVTLVVV-HDINIALRHaDHVLMLKAGqllGDGTPA 227
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG---TTVISVgHRSTLAAFH-DRVLELTGD---GSWQLL 565
|
....*.
gi 488981874 228 AVITPE 233
Cdd:COG4178 566 PAEAPA 571
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-229 |
1.53e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 82.76 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYP--RRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQP----FSRRAE 82
Cdd:PRK13635 6 IRVEHISFRYPdaATYALKDVSF-SVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtvwdVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 83 QVVYLP--QTLPAGVHLHV---LESIivaqraagGRHSPQRQEEVMALLRQLGIahlaMSYLDQ----LSGGQKQLVGLA 153
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVafgLENI--------GVPREEMVERVDQALRQVGM----EDFLNRephrLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488981874 154 QSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRhADHVLMLKAGQLLGDGTPAAV 229
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
32-258 |
2.77e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGLgpcrGELLLEGENLLTQPFSRRAEQ--VVYLPQTLPAGVHLHVLESIIVAQRA 109
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGF----VRLASGKISILGQPTRQALQKnlVAYVPQSEEVDWSFPVLVEDVVMMGR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 110 AGG-----RHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLV 184
Cdd:PRK15056 106 YGHmgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488981874 185 rRETRRRNIVTLVVVHDINIALRHADHVLMLKaGQLLGDGTPAAVITPETLAAVYGVRGRIEPCSQGVRQVIID 258
Cdd:PRK15056 186 -RELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELAFSGVLRHVALNGSEESIITD 257
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-217 |
3.23e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.91 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 13 HFSAGypRRKVIENLTVPhLPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQVVYLPQTl 91
Cdd:PRK10247 14 GYLAG--DAKILNNISFS-LRAGEFKLITGPSGCGKSTLLKIVASLiSPTSGTLLFEGEDISTLKPEIYRQQVSYCAQT- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 92 PAGVHLHVLESIIVAQRAAGGRHSPQrqeevmALLRQLGIAHLAMSYLDQ----LSGGQKQLVGLAQSLIRQPRLLLLDE 167
Cdd:PRK10247 90 PTLFGDTVYDNLIFPWQIRNQQPDPA------IFLDDLERFALPDTILTKniaeLSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488981874 168 PLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINiALRHADHVLMLKA 217
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD-EINHADKVITLQP 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-215 |
3.47e-18 |
|
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: 83.49 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 7 SGLSLSHFSAGYP-RRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCrGELLLEGENLLTQPFSRRA--EQ 83
Cdd:TIGR02857 320 SSLEFSGVSVAYPgRRPALRPVSF-TVPPGERVALVGPSGAGKSTLLNLLLGFVDP-TEGSIAVNGVPLADADADSwrDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 84 VVYLPQT--LPAGVhlhVLESIIVAQRAAGGRHSPQ--RQEEVMALLRQL--GIAHLAMSYLDQLSGGQKQLVGLAQSLI 157
Cdd:TIGR02857 398 IAWVPQHpfLFAGT---IAENIRLARPDASDAEIREalERAGLDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488981874 158 RQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRniVTLVVVHDINIALRhADHVLML 215
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAAL-ADRIVVL 529
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-229 |
3.75e-18 |
|
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: 83.58 E-value: 3.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVPH----------LPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELL------LEGENL 72
Cdd:COG4172 276 LEARDLKVWFPIKRGLFRRTVGHvkavdgvsltLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRfdgqdlDGLSRR 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 73 LTQPFsRRAEQVVY------------LPQTLPAGVHLHvlesiivaqraAGGRHSPQRQEEVMALLRQLGIAHLAMS-YL 139
Cdd:COG4172 356 ALRPL-RRRMQVVFqdpfgslsprmtVGQIIAEGLRVH-----------GPGLSAAERRARVAEALEEVGLDPAARHrYP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 140 DQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINI--ALrhADHVLMLKA 217
Cdd:COG4172 424 HEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVvrAL--AHRVMVMKD 501
|
250
....*....|..
gi 488981874 218 GQLLGDGTPAAV 229
Cdd:COG4172 502 GKVVEQGPTEQV 513
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
26-226 |
5.94e-18 |
|
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: 80.11 E-value: 5.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPhlpRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAGVHLHVLESIIV 105
Cdd:cd03265 20 SFRVR---RGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSVDDELTGWENLYI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 106 AQRAAG--GRHSPQRQEEvmaLLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDL 183
Cdd:cd03265 97 HARLYGvpGAERRERIDE---LLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488981874 184 VRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTP 226
Cdd:cd03265 174 IEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
31-220 |
6.90e-18 |
|
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: 81.25 E-value: 6.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSRRAEQVVYLPQTLpagVHLH------------ 98
Cdd:COG0444 27 DVRRGETLGLVGESGSGKSTLARAILGL---------------LPPPGITSGEILFDGEDL---LKLSekelrkirgrei 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 99 ----------------VLESIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHlAMSYLD----QLSGGQKQLVGLAQSLIR 158
Cdd:COG0444 89 qmifqdpmtslnpvmtVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPD-PERRLDryphELSGGMRQRVMIARALAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488981874 159 QPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQL 220
Cdd:COG0444 168 EPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-220 |
9.28e-18 |
|
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: 79.44 E-value: 9.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 18 YPRR---KVIENLTVPHLPrGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPag 94
Cdd:cd03248 21 YPTRpdtLVLQDVSFTLHP-GEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEP-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 95 vhlhVLESIIVAQRAAGGRHSPQrQEEVMALLRQLG----IAHLAMSYLD-------QLSGGQKQLVGLAQSLIRQPRLL 163
Cdd:cd03248 98 ----VLFARSLQDNIAYGLQSCS-FECVKEAAQKAHahsfISELASGYDTevgekgsQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488981874 164 LLDEPLSALDLNYQFHVMDLVRRETRRRNIvtLVVVHDINIaLRHADHVLMLKAGQL 220
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALYDWPERRTV--LVIAHRLST-VERADQILVLDGGRI 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-223 |
1.25e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.74 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSH----FSAGYPR-RKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSRRAE 82
Cdd:COG1101 2 LELKNlsktFNPGTVNeKRALDGLNL-TIEEGDFVTVIGSNGAGKSTLLNAIAGsLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 83 QV--VYlpQ-----TLPagvHLHVLESIIVAQRAAGGRH-----SPQRQEEVMALLRQLGiahLAM-SYLDQ----LSGG 145
Cdd:COG1101 81 YIgrVF--QdpmmgTAP---SMTIEENLALAYRRGKRRGlrrglTKKRRELFRELLATLG---LGLeNRLDTkvglLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488981874 146 QKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGD 223
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
9-230 |
2.79e-17 |
|
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: 80.95 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYP--RRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQ-PFSRRAEQVV 85
Cdd:COG4618 331 LSVENLTVVPPgsKRPILRGVSF-SLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 86 YLPQtlpaGVHLhvL----------------ESIIVAQRAAGgrhspqrqeeVMALlrqlgIAHLAMSYlD--------Q 141
Cdd:COG4618 410 YLPQ----DVEL--FdgtiaeniarfgdadpEKVVAAAKLAG----------VHEM-----ILRLPDGY-DtrigeggaR 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 142 LSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRReTRRRNIVTLVVVHDINIaLRHADHVLMLKAGQLL 221
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRA-LKARGATVVVITHRPSL-LAAVDKLLVLRDGRVQ 545
|
....*....
gi 488981874 222 GDGTPAAVI 230
Cdd:COG4618 546 AFGPRDEVL 554
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-224 |
3.94e-17 |
|
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: 78.14 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 7 SGLSLSHFSAGYPRRKVIE-----NLTVPhlpRGKITALLGPNGSGKSTLMRAMAGL-----GPCRGELLLegenlltqP 76
Cdd:cd03267 17 PGLIGSLKSLFKRKYREVEalkgiSFTIE---KGEIVGFIGPNGAGKTTTLKILSGLlqptsGEVRVAGLV--------P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 77 FSRRAE----------QVVYLPQTLPAGVHLHVLESI--IVAQRAAggrhspQRQEEVMALLRqlgIAHLAMSYLDQLSG 144
Cdd:cd03267 86 WKRRKKflrrigvvfgQKTQLWWDLPVIDSFYLLAAIydLPPARFK------KRLDELSELLD---LEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 145 GQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDG 224
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-227 |
4.53e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 80.21 E-value: 4.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 8 GLSLSHFSAGYPR-RKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-----------GpcrgelllegenlltQ 75
Cdd:COG1132 339 EIEFENVSFSYPGdRPVLKDISL-TIPPGETVALVGPSGSGKSTLVNLLLRFydptsgrilidG---------------V 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 76 P---FSRRA--EQVVYLPQTlpagVHL-H--VLESIIVAQRAAGgrhspqrQEEVMALLRQLGIAHLAMSyLDQ------ 141
Cdd:COG1132 403 DirdLTLESlrRQIGVVPQD----TFLfSgtIRENIRYGRPDAT-------DEEVEEAAKAAQAHEFIEA-LPDgydtvv 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 142 ------LSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRniVTLVVVHDINiALRHADHVLML 215
Cdd:COG1132 471 gergvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLS-TIRNADRILVL 547
|
250
....*....|..
gi 488981874 216 KAGQLLGDGTPA 227
Cdd:COG1132 548 DDGRIVEQGTHE 559
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
31-219 |
5.21e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.15 E-value: 5.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSRR----------AEQVVYLPqtlpagvhlhvl 100
Cdd:PRK11144 20 TLPAQGITAIFGRSGAGKTSLINAISGL---------------TRPQKGRivlngrvlfdAEKGICLP------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 101 esiiVAQRAAG-----GR---H-----------SPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPR 161
Cdd:PRK11144 73 ----PEKRRIGyvfqdARlfpHykvrgnlrygmAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488981874 162 LLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQ 219
Cdd:PRK11144 149 LLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
32-229 |
5.23e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.74 E-value: 5.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAG-LGPcrgelLLEGENLLTQPFSRRAEQVVYLPQTLpaGVHL----HVLESIIVA 106
Cdd:PRK13636 29 IKKGEVTAILGGNGAGKSTLFQNLNGiLKP-----SSGRILFDGKPIDYSRKGLMKLRESV--GMVFqdpdNQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 107 QRAAGGRHS---PQR--QEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVM 181
Cdd:PRK13636 102 QDVSFGAVNlklPEDevRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488981874 182 DLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:PRK13636 182 KLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-230 |
5.61e-17 |
|
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: 77.51 E-value: 5.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPhlpRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRaeQVVYlpQTLPAGVHLHVLESIIV 105
Cdd:TIGR01184 5 NLTIQ---QGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR--MVVF--QNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 106 A-QRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDL----NYQFHV 180
Cdd:TIGR01184 78 AvDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488981874 181 MDLVrRETRrrnIVTLVVVHDINIALRHADHVLMLKAGqllgdgtPAAVI 230
Cdd:TIGR01184 158 MQIW-EEHR---VTVLMVTHDVDEALLLSDRVVMLTNG-------PAANI 196
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
20-221 |
5.85e-17 |
|
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: 78.31 E-value: 5.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 20 RRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQ--PFSRRA----EQVVYlpQTLPA 93
Cdd:TIGR02769 23 RAPVLTNVSL-SIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldRKQRRAfrrdVQLVF--QDSPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 94 GVH--LHVLESIIVAQRAAGGRHSPQRQEEVMALLRQLGI-AHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLS 170
Cdd:TIGR02769 100 AVNprMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488981874 171 ALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLL 221
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
34-226 |
8.66e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.11 E-value: 8.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQVVYlpQTLPAGVHLHVLESIivaqrAAGG 112
Cdd:PRK11607 44 KGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMLDGVDLSHVPPYQRPINMMF--QSYALFPHMTVEQNI-----AFGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 113 RHSPQRQEEVMALLRQ-LGIAHL---AMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLN----YQFHVMDLV 184
Cdd:PRK11607 117 KQDKLPKAEIASRVNEmLGLVHMqefAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDIL 196
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488981874 185 RREtrrrNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTP 226
Cdd:PRK11607 197 ERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-251 |
1.15e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.44 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 3 DQTLSGLSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL----------GPCRGELLLEGENL 72
Cdd:PRK14271 16 DAAAPAMAAVNLTLGFAGKTVLDQVSM-GFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgyrysGDVLLGGRSIFNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 73 LTQPFSRRAEQVVYLPQTLPagvhLHVLESIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLD----QLSGGQKQ 148
Cdd:PRK14271 95 DVLEFRRRVGMLFQRPNPFP----MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 149 LVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRrnIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAA 228
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQ 248
|
250 260
....*....|....*....|....*..
gi 488981874 229 VIT----PETLAAVYGVRGRIEPCSQG 251
Cdd:PRK14271 249 LFSspkhAETARYVAGLSGDVKDAKRG 275
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
32-226 |
1.50e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.10 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFS--RRAEQVVYL-PQTLPAGVhlhvlesiIVAQ 107
Cdd:PRK13648 32 IPKGQWTSIVGHNGSGKSTIAKLMIGIeKVKSGEIFYNNQAITDDNFEklRKHIGIVFQnPDNQFVGS--------IVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 108 RAAGG--RHS---PQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMD 182
Cdd:PRK13648 104 DVAFGleNHAvpyDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488981874 183 LVRRETRRRNIVTLVVVHDINIALrHADHVLMLKAGQLLGDGTP 226
Cdd:PRK13648 184 LVRKVKSEHNITIISITHDLSEAM-EADHVIVMNKGTVYKEGTP 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
13-233 |
2.25e-16 |
|
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: 76.04 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 13 HFSagYPRR---KVIENLTVpHLPRGKITALLGPNGSGKSTLMramaGL-----GPCRGELLLEGENLLTQPFSRRAEQV 84
Cdd:cd03249 7 SFR--YPSRpdvPILKGLSL-TIPPGKTVALVGSSGCGKSTVV----SLlerfyDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 85 VYLPQTlPagvhlhVLESIIVAQRAAGGRHSPQrQEEVMALLRQLGIAHLAMSYLD-----------QLSGGQKQLVGLA 153
Cdd:cd03249 80 GLVSQE-P------VLFDGTIAENIRYGKPDAT-DEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 154 QSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRetRRRNIVTLVVVHDINiALRHADHVLMLKAGQLLGDGTPAAVITPE 233
Cdd:cd03249 152 RALLRNPKILLLDEATSALDAESEKLVQEALDR--AMKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
34-229 |
2.81e-16 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 75.99 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAGL-GPCR--------GELLLEGENLLTQPFSRRaeQVVYLPQTLpAGV--------H 96
Cdd:COG4598 33 KGDVISIIGSSGSGKSTFLRCINLLeTPDSgeirvggeEIRLKPDRDGELVPADRR--QLQRIRTRL-GMVfqsfnlwsH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 97 LHVLESIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALD--- 173
Cdd:COG4598 110 MTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDpel 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488981874 174 LNYQFHVMDLVRRETRrrnivTLVVV-HDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:COG4598 190 VGEVLKVMRDLAEEGR-----TMLVVtHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-220 |
3.60e-16 |
|
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: 74.17 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYP--RRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQVV 85
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSF-SIEPGESLAIIGPSGSGKSTLARLILGLlRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 86 YLPQ--TLPAGVhlhVLESIivaqraaggrhspqrqeevmallrqlgiahlamsyldqLSGGQKQLVGLAQSLIRQPRLL 163
Cdd:cd03246 80 YLPQddELFSGS---IAENI--------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488981874 164 LLDEPLSALDLNYQFHVMDLVRReTRRRNIVTLVVVHDINiALRHADHVLMLKAGQL 220
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAA-LKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-225 |
4.10e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.84 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 13 HFSagYPRR---KVIENLTVPHLPrGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPfsrRAEQV----V 85
Cdd:TIGR00958 485 SFS--YPNRpdvPVLKGLTFTLHP-GEVVALVGPSGSGKSTVAALLQNL---------------YQP---TGGQVlldgV 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 86 YLPQTLPAGVHLHVlesIIVAQR------------AAGGRHSPqrQEEVMALLRQLGiAHLAMSYLD------------Q 141
Cdd:TIGR00958 544 PLVQYDHHYLHRQV---ALVGQEpvlfsgsvreniAYGLTDTP--DEEIMAAAKAAN-AHDFIMEFPngydtevgekgsQ 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 142 LSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRrrniVTLVVVHDINIAlRHADHVLMLKAGQLL 221
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASR----TVLLIAHRLSTV-ERADQILVLKKGSVV 692
|
....
gi 488981874 222 GDGT 225
Cdd:TIGR00958 693 EMGT 696
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
9-229 |
4.61e-16 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 75.54 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPR--RKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenlltqpfsrraeqvvY 86
Cdd:TIGR04520 1 IEVENVSFSYPEseKPALKNVSL-SIEKGEFVAIIGHNGSGKSTLAKLLNGL---------------------------L 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQ----------TLPAGVHLHVLESI-IVAQraaggrhSPQRQ------EEVMAL-LRQLGIAHLAM------------ 136
Cdd:TIGR04520 53 LPTsgkvtvdgldTLDEENLWEIRKKVgMVFQ-------NPDNQfvgatvEDDVAFgLENLGVPREEMrkrvdealklvg 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 137 --SYLDQ----LSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALrHAD 210
Cdd:TIGR04520 126 meDFRDRephlLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LAD 204
|
250
....*....|....*....
gi 488981874 211 HVLMLKAGQLLGDGTPAAV 229
Cdd:TIGR04520 205 RVIVMNKGKIVAEGTPREI 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-220 |
5.52e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.03 E-value: 5.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGlgpcrgelllegenlLTQPFS---RRAE--Q 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSL-RIDRGDRIGLIGPNGAGKSTLLKLLAG---------------ELEPDSgtvKLGEtvK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 84 VVYLPQtlpagvHLHVL---ESII--VAQRAAGGrhspqRQEEVMALLRQLGIA-HLAMSYLDQLSGGQKQLVGLAQSLI 157
Cdd:COG0488 380 IGYFDQ------HQEELdpdKTVLdeLRDGAPGG-----TEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488981874 158 RQPRLLLLDEPLSALDLnyqfhvmdlvrrETrrRNIV---------TLVVV-HDinialRH-----ADHVLMLKAGQL 220
Cdd:COG0488 449 SPPNVLLLDEPTNHLDI------------ET--LEALeealddfpgTVLLVsHD-----RYfldrvATRILEFEDGGV 507
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-226 |
6.14e-16 |
|
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: 74.57 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 13 HFSAGyPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQVVYLPQ-- 89
Cdd:cd03254 9 NFSYD-EKKPVLKDINF-SIKPGETVAIVGPTGAGKTTLINLLMRFyDPQKGQILIDGIDIRDISRKSLRSMIGVVLQdt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 90 TLPAGVhlhVLESIIVAQRAAggrhspqRQEEVMALLRQLGIAHLAMS----YLDQ-------LSGGQKQLVGLAQSLIR 158
Cdd:cd03254 87 FLFSGT---IMENIRLGRPNA-------TDEEVIEAAKEAGAHDFIMKlpngYDTVlgenggnLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488981874 159 QPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRniVTLVVVHDINIaLRHADHVLMLKAGQLLGDGTP 226
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLST-IKNADKILVLDDGKIIEEGTH 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-237 |
6.36e-16 |
|
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: 74.75 E-value: 6.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGenlltqpfsrraEQVVYLPQTLPAGVHLHV---LESIIvaqra 109
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGvLKPDEGDIEIEL------------DTVSYKPQYIKADYEGTVrdlLSSIT----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 110 AGGRHSPQRQEEVMallRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETR 189
Cdd:cd03237 87 KDFYTHPYFKTEIA---KPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488981874 190 RRNIVTLVVVHDINIALRHADHVLMLkagqllgDGTPAA---VITPETLAA 237
Cdd:cd03237 164 NNEKTAFVVEHDIIMIDYLADRLIVF-------EGEPSVngvANPPQSLRS 207
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
32-231 |
7.26e-16 |
|
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: 76.62 E-value: 7.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQpFSRR--AEQVVYLPQtlpaGVHLHvleSIIVAQRA 109
Cdd:TIGR01842 341 LQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQ-WDREtfGKHIGYLPQ----DVELF---PGTVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 110 AGGRHSPQrQEEVMALLRQLG----IAHLAMSYlDQ--------LSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQ 177
Cdd:TIGR01842 413 ARFGENAD-PEKIIEAAKLAGvhelILRLPDGY-DTvigpggatLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGE 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488981874 178 FHVMDLVRReTRRRNIVTLVVVHDINiALRHADHVLMLKAGQLLGDGTPAAVIT 231
Cdd:TIGR01842 491 QALANAIKA-LKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-202 |
9.83e-16 |
|
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: 76.36 E-value: 9.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAG-LGPcrgelllegenllTQPFSRRAEQVVYLPQTLPAGVHLHVLEsiIVAQRAAGG 112
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGvLKP-------------DEGEVDEDLKISYKPQYISPDYDGTVEE--FLRSANTDD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 113 RHSPQRQEEVmalLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRN 192
Cdd:COG1245 430 FGSSYYKTEI---IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRG 506
|
170
....*....|
gi 488981874 193 IVTLVVVHDI 202
Cdd:COG1245 507 KTAMVVDHDI 516
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
26-225 |
1.06e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 75.50 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPhlpRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFS------------------RRAEQVVyl 87
Cdd:COG1135 25 SLTIE---KGEIFGIIGYSGAGKSTLIRCINLL---------------ERPTSgsvlvdgvdltalserelRAARRKI-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 88 pqtlpaGV---HLHVLESIIVAQ------RAAGgRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIR 158
Cdd:COG1135 85 ------GMifqHFNLLSSRTVAEnvalplEIAG-VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488981874 159 QPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGT 225
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGP 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
35-240 |
1.17e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 76.02 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 35 GKITALLGPNGSGKSTLMRAMAGLGPCrgELLLEGENLLTQPFSRR------AEQVVYLPQTLPAGVHLHVLESIIVAQR 108
Cdd:TIGR02633 27 GECVGLCGENGAGKSTLMKILSGVYPH--GTWDGEIYWSGSPLKASnirdteRAGIVIIHQELTLVPELSVAENIFLGNE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 109 AA--GGR-HSPQRQEEVMALLRQLGIAHLAMS-YLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLV 184
Cdd:TIGR02633 105 ITlpGGRmAYNAMYLRAKNLLRELQLDADNVTrPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDII 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488981874 185 rRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAAVYG 240
Cdd:TIGR02633 185 -RDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
9-173 |
1.51e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.04 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVPHLPRGkITALLGPNGSGKSTLMRA---MAGLGPcRGELLLEGENLLTQPFSRRAEQV- 84
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNE-ITALIGPSGSGKSTLLRSinrMNDLNP-EVTITGSIVYNGHNIYSPRTDTVd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 85 -------VYL-PQTLPAGVHlhvlESIIVAQRAAGGRHSPQRQEEVMALLRQLGI-----AHLAMSYLDqLSGGQKQLVG 151
Cdd:PRK14239 84 lrkeigmVFQqPNPFPMSIY----ENVVYGLRLKGIKDKQVLDEAVEKSLKGASIwdevkDRLHDSALG-LSGGQQQRVC 158
|
170 180
....*....|....*....|..
gi 488981874 152 LAQSLIRQPRLLLLDEPLSALD 173
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALD 180
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-230 |
2.52e-15 |
|
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: 73.03 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGY-PRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAM-------AGlgpcRGELLLEGENLLTQPFSRR 80
Cdd:cd03253 1 IEFENVTFAYdPGRPVLKDVSF-TIPAGKKVAIVGPSGSGKSTILRLLfrfydvsSG----SILIDGQDIREVTLDSLRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 81 AEQVVylPQTLpagvhlhVLESIIVAQRAAGGRHSPQrQEEVMALLRQLGIAHLAMSYLDQ-----------LSGGQKQL 149
Cdd:cd03253 76 AIGVV--PQDT-------VLFNDTIGYNIRYGRPDAT-DEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 150 VGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNivTLVVVHDINIALrHADHVLMLKAGQLLGDGTPAAV 229
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRT--TIVIAHRLSTIV-NADKIIVLKDGRIVERGTHEEL 222
|
.
gi 488981874 230 I 230
Cdd:cd03253 223 L 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-231 |
2.78e-15 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 75.11 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 1 MSDQTL---SGLSLShFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPcrgelllegenlltQPF 77
Cdd:COG4172 1 MMSMPLlsvEDLSVA-FGQGGGTVEAVKGVSF-DIAAGETLALVGESGSGKSVTALSILRLLP--------------DPA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 78 SRRAEQVVYLPQTLPA-------GVH-----------------LH-----VLESIIVAQRAAGgrhsPQRQEEVMALLRQ 128
Cdd:COG4172 65 AHPSGSILFDGQDLLGlserelrRIRgnriamifqepmtslnpLHtigkqIAEVLRLHRGLSG----AAARARALELLER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 129 LGIAHLAM---SYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIA 205
Cdd:COG4172 141 VGIPDPERrldAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVV 220
|
250 260
....*....|....*....|....*.
gi 488981874 206 LRHADHVLMLKAGQLLGDGTPAAVIT 231
Cdd:COG4172 221 RRFADRVAVMRQGEIVEQGPTAELFA 246
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-187 |
2.92e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.42 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 21 RKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGenlltqpfsrRAEQVVYLPQT--LPAGVhlh 98
Cdd:cd03223 14 RVLLKDLSF-EIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP----------EGEDLLFLPQRpyLPLGT--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 99 vlesiivaqraaggrhspqrqeevmalLRQLgiahLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQF 178
Cdd:cd03223 80 ---------------------------LREQ----LIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
....*....
gi 488981874 179 HVMDLVRRE 187
Cdd:cd03223 129 RLYQLLKEL 137
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-174 |
3.72e-15 |
|
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: 70.56 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGlgpcrgelllegenlLTQPFSrraeqvvylp 88
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISL-TINPGDRIGLVGRNGAGKSTLLKLIAG---------------ELEPDE---------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 89 qtlpagvhlhvlesiivaqraaGGRHSPQRQEevmallrqlgiahlaMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEP 168
Cdd:cd03221 55 ----------------------GIVTWGSTVK---------------IGYFEQLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
....*.
gi 488981874 169 LSALDL 174
Cdd:cd03221 98 TNHLDL 103
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
31-225 |
4.17e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.50 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAEQVVYLPQ--TLPAGVhlhVLESIIVAQR 108
Cdd:PRK11174 372 TLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESWRKHLSWVGQnpQLPHGT---LRDNVLLGNP 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 109 AAGgrhspqrQEEVMALLRQLGIAH--------LAMSYLDQ---LSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQ 177
Cdd:PRK11174 449 DAS-------DEQLQQALENAWVSEflpllpqgLDTPIGDQaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488981874 178 FHVMDLVRRETRRRniVTLVVVHDINiALRHADHVLMLKAGQLLGDGT 225
Cdd:PRK11174 522 QLVMQALNAASRRQ--TTLMVTHQLE-DLAQWDQIWVMQDGQIVQQGD 566
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
31-226 |
4.60e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 73.28 E-value: 4.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLT--------QPFSRRAEQVVYLPQTlpagvhlHVLES 102
Cdd:PRK13646 29 EFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkyiRPVRKRIGMVFQFPES-------QLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 103 IIVAQRAAGGRHSPQRQEEVMA----LLRQLGIAHLAMSYLD-QLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQ 177
Cdd:PRK13646 102 TVEREIIFGPKNFKMNLDEVKNyahrLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488981874 178 FHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTP 226
Cdd:PRK13646 182 RQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP 230
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-202 |
9.57e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.69 E-value: 9.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAGlgpcrgelllegenlLTQPFSRRAEQVV---YLPQTLPAGVHLHV---LESIivaq 107
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAG---------------VLKPDEGEVDPELkisYKPQYIKPDYDGTVedlLRSI---- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 108 raAGGRHSPQRQEEVMallRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRE 187
Cdd:PRK13409 425 --TDDLGSSYYKSEII---KPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRI 499
|
170
....*....|....*
gi 488981874 188 TRRRNIVTLVVVHDI 202
Cdd:PRK13409 500 AEEREATALVVDHDI 514
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
9-235 |
1.28e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.19 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRR-----KVIENLTVPhLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAEQ 83
Cdd:PRK13631 22 LRVKNLYCVFDEKqenelVALNNISYT-FEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 84 VVYLPQTLPAGVHLHVLESI-----------------IVAQRAAGGRHSPQRQEEVMALLRQLGiahLAMSYLD----QL 142
Cdd:PRK13631 101 TNPYSKKIKNFKELRRRVSMvfqfpeyqlfkdtiekdIMFGPVALGVKKSEAKKLAKFYLNKMG---LDDSYLErspfGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 143 SGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVrRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLG 222
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
250
....*....|...
gi 488981874 223 DGTPAAVITPETL 235
Cdd:PRK13631 257 TGTPYEIFTDQHI 269
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
34-229 |
1.28e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.07 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAGL-----GPCRG---ELLLEGENLLTQPFSRRAEQVVYLPQTlpagvhlHVLESIIV 105
Cdd:PRK13643 31 KGSYTALIGHTGSGKSTLLQHLNGLlqpteGKVTVgdiVVSSTSKQKEIKPVRKKVGVVFQFPES-------QLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 106 AQRAAGGRH---SPQRQEEVMAllRQLGIAHLAMSYLD----QLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQF 178
Cdd:PRK13643 104 KDVAFGPQNfgiPKEKAEKIAA--EKLEMVGLADEFWEkspfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488981874 179 HVMDLVRRETRRRNIVTLvVVHDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:PRK13643 182 EMMQLFESIHQSGQTVVL-VTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-173 |
1.29e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.05 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 19 PRRKVIENLTVPHLPRGKItALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSRRAE-----QVVYLPQTLPA 93
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKI-GVLGLNGAGKSTLLRIMAGV---------------DKDFNGEARpqpgiKVGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 94 GVHLHVLEsiIVAQRAAGGRHSPQRQEEVMALL------------------------------RQLGIAHLAM------S 137
Cdd:TIGR03719 80 DPTKTVRE--NVEEGVAEIKDALDRFNEISAKYaepdadfdklaaeqaelqeiidaadawdldSQLEIAMDALrcppwdA 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 488981874 138 YLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALD 173
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
32-231 |
1.32e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.04 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFS--RRAEQ--VVYLPQTLPAGVHLHVLESIIV-A 106
Cdd:PRK13549 28 VRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEELQASniRDTERagIAIIHQELALVKELSVLENIFLgN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 107 QRAAGGR-HSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVr 185
Cdd:PRK13549 108 EITPGGImDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDII- 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488981874 186 RETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDgTPAAVIT 231
Cdd:PRK13549 187 RDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGT-RPAAGMT 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
35-224 |
1.33e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 71.32 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 35 GKITALLGPNGSGKSTLMRAMAGL-----GPCRGELLLEGEnllTQPFSRRA-------EQVVYLPQTLPAGVHLHVLES 102
Cdd:PRK11264 29 GEVVAIIGPSGSGKTTLLRCINLLeqpeaGTIRVGDITIDT---ARSLSQQKglirqlrQHVGFVFQNFNLFPHRTVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 103 IIVAQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMD 182
Cdd:PRK11264 106 IIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLN 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488981874 183 LVRR--ETRRrnivTLVVV-HDINIALRHADHVLMLKAGQLLGDG 224
Cdd:PRK11264 186 TIRQlaQEKR----TMVIVtHEMSFARDVADRAIFMDQGRIVEQG 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-245 |
1.42e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 71.23 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 21 RKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENL--------LTQPFSRRAE--QVVYLPQT 90
Cdd:PRK14246 23 KAILKDITI-KIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkdifQIDAIKLRKEvgMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 91 LPagvHLHVLESIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLD----QLSGGQKQLVGLAQSLIRQPRLLLLD 166
Cdd:PRK14246 102 FP---HLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNspasQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 167 EPLSALDLNYQFHVMDLVrreTRRRNIVTLVVV-HDINIALRHADHVLMLKAGQLLGDGTPAAVIT-PETLAAVYGVRGR 244
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLI---TELKNEIAIVIVsHNPQQVARVADYVAFLYNGELVEWGSSNEIFTsPKNELTEKYVIGR 255
|
.
gi 488981874 245 I 245
Cdd:PRK14246 256 I 256
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
34-220 |
1.56e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.58 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAGL-----GPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAGVHLHVLESIivaQR 108
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLddgssGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNALENV---EL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 109 AA--GGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRR 186
Cdd:PRK10584 112 PAllRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFS 191
|
170 180 190
....*....|....*....|....*....|....
gi 488981874 187 ETRRRNIVTLVVVHDINIALRhADHVLMLKAGQL 220
Cdd:PRK10584 192 LNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-201 |
2.01e-14 |
|
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: 72.39 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 8 GLSLSHFSAGYPRRKVIENLTVPHLPRGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSRRAEQVVY 86
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlLDPLQGEVTLDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQTlpagVHLH---VLESIIVAQRAAGGrhspqrqEEVMALLRQLGIAHLAMSYLD-----------QLSGGQKQLVGL 152
Cdd:TIGR02868 414 CAQD----AHLFdttVRENLRLARPDATD-------EELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488981874 153 AQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRniVTLVVVHD 201
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHH 529
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
32-237 |
2.89e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.53 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAGvhlHVLESIIVAQRAAG 111
Cdd:PRK13647 28 IPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPDD---QVFSSTVWDDVAFG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 112 GRHSPQRQEEVM----ALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRE 187
Cdd:PRK13647 105 PVNMGLDKDEVErrveEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488981874 188 TRRRNIVtLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAA 237
Cdd:PRK13647 185 HNQGKTV-IVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
95-229 |
3.15e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 71.31 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 95 VHLHVLESIIVAQraaGGRHSPQRQEEVmALLRQLGIAHLAmSYLD----QLSGGQKQLVGLAQSLIRQPRLLLLDEPLS 170
Cdd:PRK11022 108 VGFQIMEAIKVHQ---GGNKKTRRQRAI-DLLNQVGIPDPA-SRLDvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488981874 171 ALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-229 |
3.75e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.42 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 18 YPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpCRGELLLEGENLLTQPFSRRA-----EQVVYLPQTLP 92
Cdd:PRK13638 11 YQDEPVLKGLNL-DFSLSPVTGLVGANGCGKSTLFMNLSGL--LRPQKGAVLWQGKPLDYSKRGllalrQQVATVFQDPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 93 AGVHLHVLES-IIVAQRAAGGRHS--PQRQEEVMALLRQLGIAHLAMSYLdqlSGGQKQLVGLAQSLIRQPRLLLLDEPL 169
Cdd:PRK13638 88 QQIFYTDIDSdIAFSLRNLGVPEAeiTRRVDEALTLVDAQHFRHQPIQCL---SHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 170 SALDLNYQFHVMDLVRRETRRRNIVtLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
34-220 |
5.31e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.46 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAE----QVVYLPQtlpagVHlHVLESIIVAQR 108
Cdd:PRK11629 34 EGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSKLSSAAKAElrnqKLGFIYQ-----FH-HLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 109 AA-----GGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDL 183
Cdd:PRK11629 108 VAmplliGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 488981874 184 VRRETRRRNIVTLVVVHDINIALRHADHVLMlKAGQL 220
Cdd:PRK11629 188 LGELNRLQGTAFLVVTHDLQLAKRMSRQLEM-RDGRL 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
35-226 |
5.34e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.83 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 35 GKITALLGPNGSGKSTLMRAMAGL----------GPCRGELLlegenlltqPFSRRAEQVVYlpQTLPAGVHLHVLESII 104
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGLeditsgdlfiGEKRMNDV---------PPAERGVGMVF--QSYALYPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 105 VAQRAAGGRHSpQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALD--LNYQFHVMd 182
Cdd:PRK11000 98 FGLKLAGAKKE-EINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaaLRVQMRIE- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488981874 183 lVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTP 226
Cdd:PRK11000 176 -ISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
31-237 |
5.38e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.20 E-value: 5.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAGL-----------GpcrgelllegenlltQPFS----RRAEQ----VVYlpQTL 91
Cdd:COG1129 26 ELRPGEVHALLGENGAGKSTLMKILSGVyqpdsgeilldG---------------EPVRfrspRDAQAagiaIIH--QEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 92 ---PagvHLHVLESIIVAQ--RAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLD 166
Cdd:COG1129 89 nlvP---NLSVAENIFLGRepRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488981874 167 EPLSALDLNYQFHVMDLVRReTRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGtPAAVITPETLAA 237
Cdd:COG1129 166 EPTASLTEREVERLFRIIRR-LKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTG-PVAELTEDELVR 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
9-239 |
5.59e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.52 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRA--EQVVY 86
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSL-HINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKImrEAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQTLPAGVHLHVLESIIVAQRAAGGRHSPQRQEEVMALLRQLgiAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLD 166
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRL--HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488981874 167 EPLSALDLNYQFHVMDLVRReTRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAAVY 239
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQ-LREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
32-237 |
5.77e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.05 E-value: 5.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSrraEQVVYLPQTLPAGVHLHVLESI-----IVA 106
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGL---------------LQPTS---GTVTIGERVITAGKKNKKLKPLrkkvgIVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 107 QR--------------AAGGRHSPQRQEEVMALLRQ-LGIAHLAMSYLDQ----LSGGQKQLVGLAQSLIRQPRLLLLDE 167
Cdd:PRK13634 92 QFpehqlfeetvekdiCFGPMNFGVSEEDAKQKAREmIELVGLPEELLARspfeLSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488981874 168 PLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT-PETLAA 237
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAdPDELEA 242
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-205 |
6.50e-14 |
|
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: 68.54 E-value: 6.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 21 RKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAGVHLHVL 100
Cdd:TIGR01189 13 RMLFEGLSF-TLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 101 ESIIVAQRAAGGRhspqrQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHV 180
Cdd:TIGR01189 92 ENLHFWAAIHGGA-----QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170 180
....*....|....*....|....*
gi 488981874 181 MDLVRRETRRRNIVTLVVVHDINIA 205
Cdd:TIGR01189 167 AGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
111-219 |
1.02e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 111 GGRHSPQRQEeVMALLRQLGIAHLAMSYLD---QLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRE 187
Cdd:PRK15134 124 GMRREAARGE-ILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLREL 202
|
90 100 110
....*....|....*....|....*....|..
gi 488981874 188 TRRRNIVTLVVVHDINIALRHADHVLMLKAGQ 219
Cdd:PRK15134 203 QQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-224 |
1.17e-13 |
|
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: 67.58 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 20 RRKVIENLTVPHLPrGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSRRAeQVVYLPQtlpagvHLH 98
Cdd:cd03213 21 GKQLLKNVSGKAKP-GELTAIMGPSGAGKSTLLNALAGrRTGLGVSGEVLINGRPLDKRSFRK-IIGYVPQ------DDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 99 VLESIIVaqraaggrhspqrQEEVM--ALLRqlgiahlamsyldQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNY 176
Cdd:cd03213 93 LHPTLTV-------------RETLMfaAKLR-------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488981874 177 QFHVMDLVRREtRRRNIVTLVVVHDI-NIALRHADHVLMLKAGQLLGDG 224
Cdd:cd03213 147 ALQVMSLLRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-236 |
1.71e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.73 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 17 GYPRRKVIENLTVPH----LPRGKITALLGPNGSGKST----LMRAMAGLGPCRGELLLEGENLLTQ--PFSRRAeQVVY 86
Cdd:PRK15134 290 GILKRTVDHNVVVKNisftLRPGETLGLVGESGSGKSTtglaLLRLINSQGEIWFDGQPLHNLNRRQllPVRHRI-QVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQTLPAGVHLHVLESIivaqrAAGGR-HSP-----QRQEEVMALLRQLGI-AHLAMSYLDQLSGGQKQLVGLAQSLIRQ 159
Cdd:PRK15134 369 QDPNSSLNPRLNVLQII-----EEGLRvHQPtlsaaQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 160 PRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDG-------TPAAVITP 232
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGdcervfaAPQQEYTR 523
|
....
gi 488981874 233 ETLA 236
Cdd:PRK15134 524 QLLA 527
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3-224 |
1.93e-13 |
|
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: 67.56 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 3 DQTLSGLSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFS---R 79
Cdd:cd03220 17 SSSLKKLGILGRKGEVGEFWALKDVSF-EVPRGERIGLIGRNGAGKSTLLRLLAGI---------------YPPDSgtvT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 80 RAEQVVYLPqTLPAGVH--LHVLESIIVAQRAAG--GRHSPQRQEEVMAlLRQLGiahlamSYLDQ----LSGGQKQLVG 151
Cdd:cd03220 81 VRGRVSSLL-GLGGGFNpeLTGRENIYLNGRLLGlsRKEIDEKIDEIIE-FSELG------DFIDLpvktYSSGMKARLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488981874 152 LAQSLIRQPRLLLLDEPLSALDLNYQFHVMDlvRRETRRRNIVTLVVV-HDINIALRHADHVLMLKAGQLLGDG 224
Cdd:cd03220 153 FAIATALEPDILLIDEVLAVGDAAFQEKCQR--RLRELLKQGKTVILVsHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
31-235 |
2.03e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 68.18 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAG-LGP---------------------CRGELLLEGENLLTQPFSRRAEQ-VVYL 87
Cdd:PRK13639 24 KAEKGEMVALLGPNGAGKSTLFLHFNGiLKPtsgevlikgepikydkkslleVRKTVGIVFQNPDDQLFAPTVEEdVAFG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 88 PQTLpagvhlhvlesiivaqraagGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDE 167
Cdd:PRK13639 104 PLNL--------------------GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488981874 168 PLSALDLNYQFHVMDLVrRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT-PETL 235
Cdd:PRK13639 164 PTSGLDPMGASQIMKLL-YDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSdIETI 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-173 |
2.14e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.38 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 19 PRRKVIENLTVPHLPRGKItALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFS---RRAE--QVVYLPQTLPA 93
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKI-GVLGLNGAGKSTLLRIMAGV---------------DKEFEgeaRPAPgiKVGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 94 GVHLHVLEsiIVAQRAAGGRHSPQRQEEVMALL------------------------------RQLGIAHLAM------S 137
Cdd:PRK11819 82 DPEKTVRE--NVEEGVAEVKAALDRFNEIYAAYaepdadfdalaaeqgelqeiidaadawdldSQLEIAMDALrcppwdA 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 488981874 138 YLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALD 173
Cdd:PRK11819 160 KVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-233 |
2.35e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 68.68 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrGELLLEGENLLTQPFSRRAEQ----V 84
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSF-HVQRGECFGLLGPNGAGKTTTLRMLLGL----THPDAGSISLCGEPVPSRARHarqrV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 85 VYLPQTLPAGVHLHVLESIIVAQRAAGgRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLL 164
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFG-LSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488981874 165 LDEPLSALDLNYQfHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPE 233
Cdd:PRK13537 162 LDEPTTGLDPQAR-HLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-256 |
2.41e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 69.37 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 6 LSGLSLShFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-----GPCRGELLLEGENLLTQPFSRR 80
Cdd:PRK10535 7 LKDIRRS-YPSGEEQVEVLKGISL-DIYAGEMVAIVGASGSGKSTLMNILGCLdkptsGTYRVAGQDVATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 81 AEQVVYLPQTLPAGVHLHVLESIIVAQRAAG-GRHspQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQ 159
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGlERK--QRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 160 PRLLLLDEPLSALDLNYQFHVMDLVrRETRRRNIVTLVVVHDINIAlRHADHVLMLKAGQLLGDgtPAAVITPEtlaaVY 239
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAIL-HQLRDRGHTVIIVTHDPQVA-AQAERVIEIRDGEIVRN--PPAQEKVN----VA 234
|
250
....*....|....*..
gi 488981874 240 GVRGRIEPCSQGVRQVI 256
Cdd:PRK10535 235 GGTEPVVNTASGWRQFV 251
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
32-205 |
2.91e-13 |
|
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: 66.75 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAGVHLHVLESIivaqRAAG 111
Cdd:cd03231 23 LAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL----RFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 112 GRHSPQRQEEVMALLRQLGIAHLAMSyldQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRR 191
Cdd:cd03231 99 ADHSDEQVEEALARVGLNGFEDRPVA---QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARG 175
|
170
....*....|....
gi 488981874 192 NIVTLVVVHDINIA 205
Cdd:cd03231 176 GMVVLTTHQDLGLS 189
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
33-239 |
3.61e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.52 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 33 PRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAgvhlHVLESIIVAQRAAGG 112
Cdd:PRK13652 28 PRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPD----DQIFSPTVEQDIAFG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 113 RHSPQRQEEVMA-----LLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRE 187
Cdd:PRK13652 104 PINLGLDEETVAhrvssALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488981874 188 TRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT-PETLAAVY 239
Cdd:PRK13652 184 PETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLqPDLLARVH 236
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
9-225 |
4.16e-13 |
|
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: 66.87 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYP--RRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAM-------AGlgpcRGELLLEGENLLTQPFSR 79
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISL-DIPAGETVALVGPSGSGKSTLVNLIprfydvdSG----RILIDGHDVRDYTLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 80 RaeQVVYLPQTlpagVHLHvleSIIVAQRAAGGRHSPQRqEEVMALLRQlgiAHlAMSYLD---------------QLSG 144
Cdd:cd03251 76 R--QIGLVSQD----VFLF---NDTVAENIAYGRPGATR-EEVEEAARA---AN-AHEFIMelpegydtvigergvKLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 145 GQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNivTLVVVHDINiALRHADHVLMLKAGQLLGDG 224
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRT--TFVIAHRLS-TIENADRIVVLEDGKIVERG 218
|
.
gi 488981874 225 T 225
Cdd:cd03251 219 T 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-230 |
6.63e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.55 E-value: 6.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAeQVVYL 87
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSF-TVASGECFGLLGPNGAGKSTIARMILGMtSPDAGKITVLGVPVPARARLARA-RIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 88 PQTLPAGVHLHVLESIIVAQRAAGgrHSPQRQEEVMALLrqLGIAHL---AMSYLDQLSGGQKQLVGLAQSLIRQPRLLL 164
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFG--MSTREIEAVIPSL--LEFARLeskADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488981874 165 LDEPLSALDLnyqfHVMDLVRRETRR---RNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVI 230
Cdd:PRK13536 196 LDEPTTGLDP----HARHLIWERLRSllaRGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-194 |
6.89e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 6.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 21 RKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPcrGELLLEGENLLTQPFSRRAEQVVYLPQTLPAGVHLHVL 100
Cdd:PRK13539 15 RVLFSGLSF-TLAAGEALVLTGPNGSGKTTLLRLIAGLLP--PAAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 101 ESIIVAQRAAGGRhsPQRQEEVMALLRQLGIAHLAMSYldqLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHV 180
Cdd:PRK13539 92 ENLEFWAAFLGGE--ELDIAAALEAVGLAPLAHLPFGY---LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170
....*....|....
gi 488981874 181 MDLVRRETRRRNIV 194
Cdd:PRK13539 167 AELIRAHLAQGGIV 180
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
31-219 |
7.23e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 65.92 E-value: 7.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAGlgpcrgelllegenlLTQPFS-----RRAEQVVYLPQTLPAGV---------- 95
Cdd:COG4778 33 SVAAGECVALTGPSGAGKSTLLKCIYG---------------NYLPDSgsilvRHDGGWVDLAQASPREIlalrrrtigy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 96 ---HLHVLESI----IVAQ--RAAGGRHSpQRQEEVMALLRQLGIA-HLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLL 165
Cdd:COG4778 98 vsqFLRVIPRVsaldVVAEplLERGVDRE-EARARARELLARLNLPeRLWDLPPATFSGGEQQRVNIARGFIADPPLLLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488981874 166 DEPLSALDLNYQFHVMDLVrRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQ 219
Cdd:COG4778 177 DEPTASLDAANRAVVVELI-EEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-226 |
7.34e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.76 E-value: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 19 PRRKVIENLTvPHLPRGKITALLGPNGSGKSTLMRAMAglgpCRGELLLEGENLLT---QPFSRRAEQVV--YLPQT--- 90
Cdd:TIGR00955 36 PRKHLLKNVS-GVAKPGELLAVMGSSGAGKTTLMNALA----FRSPKGVKGSGSVLlngMPIDAKEMRAIsaYVQQDdlf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 91 LPagvHLHVLESIIVAQRAAGGRHSP--QRQEEVMALLRQLGI---AHLAMSYLDQ---LSGGQKQLVGLAQSLIRQPRL 162
Cdd:TIGR00955 111 IP---TLTVREHLMFQAHLRMPRRVTkkEKRERVDEVLQALGLrkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488981874 163 LLLDEPLSALDLNYQFHVMDLVRRETRRRNIVtLVVVHDINIAL-RHADHVLMLKAGQLLGDGTP 226
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTI-ICTIHQPSSELfELFDKIILMAEGRVAYLGSP 251
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
35-229 |
9.21e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.15 E-value: 9.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 35 GKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLT--------QPFSRRAEQVV-----YLPQTLPAGVHLHVL 100
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLeKPSEGSIVVNGQTINLvrdkdgqlKVADKNQLRLLrtrltMVFQHFNLWSHMTVL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 101 ESIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHLAM-SYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFH 179
Cdd:PRK10619 111 ENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGE 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488981874 180 VMDLVRRETRRRNIVtLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:PRK10619 191 VLRIMQQLAEEGKTM-VVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-219 |
1.87e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.33 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 1 MSDQTLsgLSLSHFSAGYPRRKVIENLTVPHLPrGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSR 79
Cdd:PRK11701 1 MMDQPL--LSVRGLTKLYGPRKGCRDVSFDLYP-GEVLGIVGESGSGKTTLLNALSArLAPDAGEVHYRMRDGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 80 RAE-QVVYLPQTLPAGVHLHVLESII--------VAQR--AAGGRHSPQRQEEVMALLRQLGIAhlaMSYLDQL----SG 144
Cdd:PRK11701 78 LSEaERRRLLRTEWGFVHQHPRDGLRmqvsaggnIGERlmAVGARHYGDIRATAGDWLERVEID---AARIDDLpttfSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488981874 145 GQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQ 219
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
33-224 |
2.00e-12 |
|
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: 64.70 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 33 PRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQVVylpqtLPAGVHLHVLESIIVAQRAAG 111
Cdd:cd03266 29 KPGEVTGLLGPNGAGKTTTLRMLAGLlEPDAGFATVDGFDVVKEPAEARRRLGF-----VSDSTGLYDRLTARENLEYFA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 112 GRHSPQRQE---EVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVrRET 188
Cdd:cd03266 104 GLYGLKGDEltaRLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI-RQL 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 488981874 189 RRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDG 224
Cdd:cd03266 183 RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-232 |
2.53e-12 |
|
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: 65.08 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 27 LTVPHLprGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAGVhlhvlESIIV 105
Cdd:cd03236 20 LPVPRE--GQVLGLVGPNGIGKSTALKILAGkLKPNLGKFDDPPDWDEILDEFRGSELQNYFTKLLEGDV-----KVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 106 AQ------RAAGGR--------HSPQRQEEVMallRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSA 171
Cdd:cd03236 93 PQyvdlipKAVKGKvgellkkkDERGKLDELV---DQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488981874 172 LDLNYQFHVMDLVRRETRRRNIVtLVVVHDINIALRHADHVLMLKagqllgdGTPAA--VITP 232
Cdd:cd03236 170 LDIKQRLNAARLIRELAEDDNYV-LVVEHDLAVLDYLSDYIHCLY-------GEPGAygVVTL 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
32-230 |
2.74e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.20 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAGVH--LHVLESIIVAQR 108
Cdd:PRK15112 36 LREGQTLAIIGENGSGKSTLAKMLAGMiEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTSLNprQRISQILDFPLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 109 AAGGRHSPQRQEEVMALLRQLGI-AHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRE 187
Cdd:PRK15112 116 LNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488981874 188 TRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVI 230
Cdd:PRK15112 196 QEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
36-226 |
3.00e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.58 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 36 KITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAGVHLHVLESIIVAQRAAGgRHS 115
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKG-RSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 116 PQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVt 195
Cdd:TIGR01257 1036 EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTII- 1114
|
170 180 190
....*....|....*....|....*....|.
gi 488981874 196 lVVVHDINIALRHADHVLMLKAGQLLGDGTP 226
Cdd:TIGR01257 1115 -MSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
117-212 |
4.20e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 65.14 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 117 QRQEEVMALLRQLGiahLAMSYLD----QLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRN 192
Cdd:COG4608 132 ERRERVAELLELVG---LRPEHADryphEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELG 208
|
90 100
....*....|....*....|.
gi 488981874 193 IVTLVVVHDINIaLRH-ADHV 212
Cdd:COG4608 209 LTYLFISHDLSV-VRHiSDRV 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
31-222 |
5.29e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.74 E-value: 5.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQ------PFSRRAEQVVYLPQTL--PAGVHLHVLES 102
Cdd:PRK10908 24 HMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrevPFLRRQIGMIFQDHHLlmDRTVYDNVAIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 103 IIVAqraagGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMD 182
Cdd:PRK10908 104 LIIA-----GASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488981874 183 LVrRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLG 222
Cdd:PRK10908 179 LF-EEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-231 |
7.70e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.08 E-value: 7.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 14 FSAGYP-RRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQV---VYLP 88
Cdd:PRK13641 12 YSPGTPmEKKGLDNISF-ELEEGSFVALVGHTGSGKSTLMQHFNALlKPSSGTITIAGYHITPETGNKNLKKLrkkVSLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 89 QTLPAgVHLH---VLESIIVAQRAAGGRHSPQRqEEVMALLRQLGIAHLAMSYLD-QLSGGQKQLVGLAQSLIRQPRLLL 164
Cdd:PRK13641 91 FQFPE-AQLFentVLKDVEFGPKNFGFSEDEAK-EKALKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488981874 165 LDEPLSALDLNYQFHVMDLVRRETRRRNIVTLvVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT 231
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYQKAGHTVIL-VTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
31-225 |
7.91e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 64.44 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFS------------------RRAEQVVylpqtlp 92
Cdd:PRK11153 27 HIPAGEIFGVIGASGAGKSTLIRCINLL---------------ERPTSgrvlvdgqdltalsekelRKARRQI------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 93 aGV---HLHVLESIIVAQRAA-----GGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLL 164
Cdd:PRK11153 85 -GMifqHFNLLSSRTVFDNVAlplelAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488981874 165 LDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGT 225
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-231 |
1.27e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.13 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 6 LSGLSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLE-----------GENLLT 74
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSM-EIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEgrveffnqniyERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 75 QPFSRRAEQVVYLPQTLPAGVHlhvlESIIVAQRAAGGRHSPQRQEEVMALLRQLG----IAH-LAMSYLDqLSGGQKQL 149
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVY----DNVAYGVKIVGWRPKLEIDDIVESALKDADlwdeIKHkIHKSALD-LSGGQQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 150 VGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKA-----GQLLGDG 224
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFG 238
|
....*..
gi 488981874 225 TPAAVIT 231
Cdd:PRK14258 239 LTKKIFN 245
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
35-229 |
1.59e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.84 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 35 GKITALLGPNGSGKSTLMRAMAGLG-PCRGELLLEGENLLTQPFSRRAEQV---VYLPQTLPAGvhlHVLESIIVAQRAA 110
Cdd:PRK13649 33 GSYTAFIGHTGSGKSTIMQLLNGLHvPTQGSVRVDDTLITSTSKNKDIKQIrkkVGLVFQFPES---QLFEETVLKDVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 111 GGRHSPQRQEEVMALLRQ-LGIAHLAMSYLDQ----LSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVr 185
Cdd:PRK13649 110 GPQNFGVSQEEAEALAREkLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLF- 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488981874 186 RETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:PRK13649 189 KKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
9-224 |
1.84e-11 |
|
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: 61.18 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYP--RRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGlgpcrgelllegenlLTQPFSRRaeqvVY 86
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSL-ELKQGEKIALLGRSGSGKSTLLQLLTG---------------DLKPQQGE----IT 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LpqtlpAGVHLHVLESIIVAQRAAggrhSPQRQEEVMALLRQ-LGIahlamsyldQLSGGQKQLVGLAQSLIRQPRLLLL 165
Cdd:cd03247 61 L-----DGVPVSDLEKALSSLISV----LNQRPYLFDTTLRNnLGR---------RFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488981874 166 DEPLSALDLNYQFHVMDLVRRETRRRNIvtLVVVHDInIALRHADHVLMLKAGQLLGDG 224
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKDKTL--IWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
32-210 |
1.87e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 62.49 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRA---MAGLGP-CRGELLLE-----GENLLTQPFS--RRAEQVVYLPQTLPAGVHlhvl 100
Cdd:PRK14243 33 IPKNQITAFIGPSGCGKSTILRCfnrLNDLIPgFRVEGKVTfhgknLYAPDVDPVEvrRRIGMVFQKPNPFPKSIY---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 101 ESIIVAQRAAGGR-------HSPQRQ----EEVMALLRQLGIAhlamsyldqLSGGQKQLVGLAQSLIRQPRLLLLDEPL 169
Cdd:PRK14243 109 DNIAYGARINGYKgdmdelvERSLRQaalwDEVKDKLKQSGLS---------LSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488981874 170 SALDLNYQFHVMDLVRRETRRRNIVtlVVVHDINIALRHAD 210
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQYTII--IVTHNMQQAARVSD 218
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-220 |
2.34e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.02 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 19 PRRKVIENLTV-PHLP----------RGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFS------RRA 81
Cdd:PRK10418 2 PQQIELRNIALqAAQPlvhgvsltlqRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPVApcalrgRKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 82 EQVVYLPQTLPAGVHL---HVLESIivaqrAAGGRHSPQRQeeVMALLRQLGI---AHLAMSYLDQLSGGQKQLVGLAQS 155
Cdd:PRK10418 82 ATIMQNPRSAFNPLHTmhtHARETC-----LALGKPADDAT--LTAALEAVGLenaARVLKLYPFEMSGGMLQRMMIALA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488981874 156 LIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQL 220
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-225 |
2.57e-11 |
|
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: 63.20 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYP--RRKVIENLTVpHLPRGKITALLGPNGSGKSTLmramAGLGPCRGELLLEGENLLTQPFS-------R 79
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISL-VIEPGETVALVGRSGSGKSTL----VNLIPRFYEPDSGQILLDGHDLAdytlaslR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 80 RaeQVVYLPQtlpagvHLHVLESIIVAQRAAGgrhspQRQEEVMALLRQLGIAHLAMSYLDQ---------------LSG 144
Cdd:TIGR02203 406 R--QVALVSQ------DVVLFNDTIANNIAYG-----RTEQADRAEIERALAAAYAQDFVDKlplgldtpigengvlLSG 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 145 GQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNivTLVVVHDINiALRHADHVLMLKAGQLLGDG 224
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRT--TLVIAHRLS-TIEKADRIVVMDDGRIVERG 549
|
.
gi 488981874 225 T 225
Cdd:TIGR02203 550 T 550
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-231 |
3.11e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.85 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 22 KVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL------GPCRGELLLEGENLLTQPFS---RRAEQVVYLPQTLP 92
Cdd:PRK14247 17 EVLDGVNL-EIPDNTITALMGPSGSGKSTLLRVFNRLielypeARVSGEVYLDGQDIFKMDVIelrRRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 93 agvHLHVLESIIVA---QRAAGGRHspQRQEEVMALLRQLGIAHLAMSYLD----QLSGGQKQLVGLAQSLIRQPRLLLL 165
Cdd:PRK14247 96 ---NLSIFENVALGlklNRLVKSKK--ELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488981874 166 DEPLSALDLNYQFHVMDLVRRETRRRNIVtlVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT 231
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIV--LVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
119-229 |
3.16e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.42 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 119 QEEVMALLRQLGI-AHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLV 197
Cdd:PRK15079 138 KDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIF 217
|
90 100 110
....*....|....*....|....*....|..
gi 488981874 198 VVHDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:PRK15079 218 IAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
35-195 |
3.20e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.97 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 35 GKITALLGPNGSGKSTLMRAMAGL--GPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPagvHLHVLESIIVAQRAAGG 112
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTKQILKRTGFVTQDDILYP---HLTVRETLVFCSLLRLP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 113 RhSPQRQEEVMA---LLRQLGIAH-----LAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFH-VMDL 183
Cdd:PLN03211 171 K-SLTKQEKILVaesVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRlVLTL 249
|
170
....*....|..
gi 488981874 184 VRRETRRRNIVT 195
Cdd:PLN03211 250 GSLAQKGKTIVT 261
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
138-230 |
3.59e-11 |
|
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: 62.90 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 138 YLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKA 217
Cdd:TIGR03269 424 YPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRD 503
|
90
....*....|...
gi 488981874 218 GQLLGDGTPAAVI 230
Cdd:TIGR03269 504 GKIVKIGDPEEIV 516
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
35-224 |
3.70e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.88 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 35 GKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAEQ----VVYlpQTLPAGVHLHVLESIIVaqraa 110
Cdd:PRK09700 31 GEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlgigIIY--QELSVIDELTVLENLYI----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 111 gGRH-------------SPQRQEEVMALLRqLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSAL---DL 174
Cdd:PRK09700 104 -GRHltkkvcgvniidwREMRVRAAMMLLR-VGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnkEV 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488981874 175 NYQFHVMDLVRRETrrRNIVtlVVVHDINIALRHADHVLMLKAGQLLGDG 224
Cdd:PRK09700 182 DYLFLIMNQLRKEG--TAIV--YISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-173 |
4.59e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.59 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 21 RKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGEnlltQPFSRRAEQvvYLPQTL----PAGVH 96
Cdd:PRK13538 14 RILFSGLSF-TLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG----EPIRRQRDE--YHQDLLylghQPGIK 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488981874 97 --LHVLESIIVAQRAAGgrhsPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALD 173
Cdd:PRK13538 87 teLTALENLRFYQRLHG----PGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
36-235 |
5.28e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.56 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 36 KITALLGPNGSGKSTLMRAMAGL-----GPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPagvHLHVLESIIVAQRAA 110
Cdd:PRK13645 38 KVTCVIGTTGSGKSTMIQLTNGLiisetGQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQFP---EYQLFQETIEKDIAF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 111 GGRHSPQRQEEVMALLRQL-GIAHLAMSYLD----QLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVR 185
Cdd:PRK13645 115 GPVNLGENKQEAYKKVPELlKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFE 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488981874 186 RETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETL 235
Cdd:PRK13645 195 RLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-218 |
5.72e-11 |
|
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: 60.81 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 24 IENLTVpHLPRGKITALLGPNGSGKSTLMRAMAG-----LGPCRGELLLEGENLLTQPFSRRAEQVVYLPQTlPAGVHLH 98
Cdd:cd03290 17 LSNINI-RIPTGQLTMIVGQVGCGKSSLLLAILGemqtlEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQK-PWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 99 VLESIIVaqraaGGRHSPQRQEEVM-ALLRQLGIAHLAMSylDQ---------LSGGQKQLVGLAQSLIRQPRLLLLDEP 168
Cdd:cd03290 95 VEENITF-----GSPFNKQRYKAVTdACSLQPDIDLLPFG--DQteigerginLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488981874 169 LSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAG 218
Cdd:cd03290 168 FSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
32-227 |
6.08e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 61.26 E-value: 6.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQP----FSRRAEQVVYLPQTLPAGvhlhvleSIIVAQ 107
Cdd:PRK13642 30 ITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnvwnLRRKIGMVFQNPDNQFVG-------ATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 108 RAAGGRHSPQRQEEvmaLLRQLGIAHLAMSYLD-------QLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHV 180
Cdd:PRK13642 103 VAFGMENQGIPREE---MIKRVDEALLAVNMLDfktrepaRLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488981874 181 MDLVRRETRRRNIVTLVVVHDINIALRhADHVLMLKAGQLLGDGTPA 227
Cdd:PRK13642 180 MRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPS 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-237 |
6.88e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.97 E-value: 6.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPhlpRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSRRaeqvVYL---PQTLP-------AG- 94
Cdd:COG3845 25 SLTVR---PGEIHALLGENGAGKSTLMKILYGL---------------YQPDSGE----ILIdgkPVRIRsprdaiaLGi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 95 --VHLH--------VLESIIVAQRAAGGRHSPQRQ--EEVMALLRQLGIAhlamsyLD------QLSGGQKQLVGLAQSL 156
Cdd:COG3845 83 gmVHQHfmlvpnltVAENIVLGLEPTKGGRLDRKAarARIRELSERYGLD------VDpdakveDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 157 IRQPRLLLLDEPLSAL------DLnyqFHVMDLVRRETRrrnivTLVVV-HDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:COG3845 157 YRGARILILDEPTAVLtpqeadEL---FEILRRLAAEGK-----SIIFItHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
....*...
gi 488981874 230 iTPETLAA 237
Cdd:COG3845 229 -SEEELAE 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-173 |
7.59e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 60.82 E-value: 7.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVPhLPRGKITALLGPNGSGKSTLMRAMaglgpCRgelllegeNLLTQPFSRRAEQV---- 84
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLD-IPENKVTALIGPSGCGKSTLLRCL-----NR--------MNDLIPGARVEGEIlldg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 85 --VYLPQTLPAGVHLHVLesiIVAQR------------AAG----GRHSPQRQEE-VMALLRQLGI-----AHLAMSYLD 140
Cdd:COG1117 78 edIYDPDVDVVELRRRVG---MVFQKpnpfpksiydnvAYGlrlhGIKSKSELDEiVEESLRKAALwdevkDRLKKSALG 154
|
170 180 190
....*....|....*....|....*....|...
gi 488981874 141 qLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALD 173
Cdd:COG1117 155 -LSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-230 |
7.64e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.48 E-value: 7.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 4 QTLSGLSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFS---RR 80
Cdd:COG1134 22 RSLKELLLRRRRTRREEFWALKDVSF-EVERGESVGIIGRNGAGKSTLLKLIAGI---------------LEPTSgrvEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 81 AEQVVYLPQtLPAGVH--LHVLESIIVAQRAAGgrhspQRQEEVMALLRQ------LGiahlamSYLDQ----LSGGQKQ 148
Cdd:COG1134 86 NGRVSALLE-LGAGFHpeLTGRENIYLNGRLLG-----LSRKEIDEKFDEivefaeLG------DFIDQpvktYSSGMRA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 149 LVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRetRRRNIVTLVVV-HDINIALRHADHVLMLKAGQLLGDGTPA 227
Cdd:COG1134 154 RLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRE--LRESGRTVIFVsHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
...
gi 488981874 228 AVI 230
Cdd:COG1134 232 EVI 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
140-226 |
1.16e-10 |
|
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: 59.81 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 140 DQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRreTRRRNIVTLVVVHDINIALrHADHVLMLKAGQ 219
Cdd:cd03244 138 ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTII-DSDRILVLDKGR 214
|
....*..
gi 488981874 220 LLGDGTP 226
Cdd:cd03244 215 VVEFDSP 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-225 |
1.17e-10 |
|
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: 59.81 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 21 RKVIENLTVPHLPrGKITALLGPNGSGKSTLMRAMAGLGPC---RGELLLEGENLLTQPFSRRaeQVVYLPQTlpagvhl 97
Cdd:cd03252 15 PVILDNISLRIKP-GEVVGIVGRSGSGKSTLTKLIQRFYVPengRVLVDGHDLALADPAWLRR--QVGVVLQE------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 98 HVLESIIVAQRAAGGRHSPQRqEEVMALLRQLGiAHLAMSYLDQ------------LSGGQKQLVGLAQSLIRQPRLLLL 165
Cdd:cd03252 85 NVLFNRSIRDNIALADPGMSM-ERVIEAAKLAG-AHDFISELPEgydtivgeqgagLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 166 DEPLSALDLNYQFHVMDLVRRETRRRNIVtlVVVHDINiALRHADHVLMLKAGQLLGDGT 225
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDICAGRTVI--IIAHRLS-TVKNADRIIVMEKGRIVEQGS 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
138-225 |
1.21e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.89 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 138 YLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKA 217
Cdd:PRK09473 158 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA 237
|
....*...
gi 488981874 218 GQLLGDGT 225
Cdd:PRK09473 238 GRTMEYGN 245
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-229 |
1.47e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.29 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 6 LSGLSLShfsagYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAG-----------LGpcrgelllegeNLLT 74
Cdd:NF033858 4 LEGVSHR-----YGKTVALDDVSL-DIPAGCMVGLIGPDGVGKSSLLSLIAGarkiqqgrvevLG-----------GDMA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 75 QPFSRRA--EQVVYLPQTL-----PAgvhLHVLESI-----IVAQRAAggrhspQRQEEVMALLRQLGIAhlamSYLD-- 140
Cdd:NF033858 67 DARHRRAvcPRIAYMPQGLgknlyPT---LSVFENLdffgrLFGQDAA------ERRRRIDELLRATGLA----PFADrp 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 141 --QLSGGQKQLVGLAQSLIRQPRLLLLDEP------LSaldlNYQFhvMDLVRR-ETRRRNIVTLVVVHDINIALRHaDH 211
Cdd:NF033858 134 agKLSGGMKQKLGLCCALIHDPDLLILDEPttgvdpLS----RRQF--WELIDRiRAERPGMSVLVATAYMEEAERF-DW 206
|
250
....*....|....*...
gi 488981874 212 VLMLKAGQLLGDGTPAAV 229
Cdd:NF033858 207 LVAMDAGRVLATGTPAEL 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
34-229 |
1.98e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 59.62 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAGL-GPCRGELLLEGENLLTQPFSRRAEQ-VVYLPQTLPAGVHLHVLESIIVAQRA-- 109
Cdd:PRK11300 30 EQEIVSLIGPNGAGKTTVFNCLTGFyKPTGGTILLRGQHIEGLPGHQIARMgVVRTFQHVRLFREMTVIENLLVAQHQql 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 110 -----AGGRHSPQ-RQEEVMAL------LRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSAL----- 172
Cdd:PRK11300 110 ktglfSGLLKTPAfRRAESEALdraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLnpket 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488981874 173 -DLNyqfHVMDLVRREtrrRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:PRK11300 190 kELD---ELIAELRNE---HNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
99-230 |
2.59e-10 |
|
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: 60.20 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 99 VLESIIVAQRAAG--GRHSPQRQEEvmaLLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNY 176
Cdd:TIGR03269 127 VLDNVLEALEEIGyeGKEAVGRAVD---LIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQT 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 488981874 177 QFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVI 230
Cdd:TIGR03269 204 AKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVV 257
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
35-172 |
3.52e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 35 GKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAEQV-VYL-PQTLPAGVHLHVLESIIVaqraaGG 112
Cdd:PRK15439 37 GEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLvPQEPLLFPNLSVKENILF-----GL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488981874 113 RHSPQRQEEVMALLRQLGiAHLAmsyLDQLSG----GQKQLVGLAQSLIRQPRLLLLDEPLSAL 172
Cdd:PRK15439 112 PKRQASMQKMKQLLAALG-CQLD---LDSSAGslevADRQIVEILRGLMRDSRILILDEPTASL 171
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
26-229 |
3.59e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.01 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPhlpRGKITALLGPNGSGKSTLMRAMAG-LGPCRGELLLEGENLLTQPFSRRAE---QVVYLPQTLPAGVHLHVLE 101
Cdd:PRK11831 27 SLTVP---RGKITAIMGPSGIGKTTLLRLIGGqIAPDHGEILFDGENIPAMSRSRLYTvrkRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 102 SIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVM 181
Cdd:PRK11831 104 NVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488981874 182 DLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:PRK11831 184 KLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
26-226 |
4.29e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.54 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPhlpRGKITALLGPNGSGKSTLMRAMAG--------------------LGPcrgelllegenlltqpfSRRAEQVV 85
Cdd:COG0396 20 NLTIK---PGEVHAIMGPNGSGKSTLAKVLMGhpkyevtsgsilldgedileLSP-----------------DERARAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 86 YL----PQTLPaGVHLHVLESIIVAQRAAGGRHSPQRQEEVMALLRQLGiahLAMSYLDQ-----LSGGQKQLVGLAQSL 156
Cdd:COG0396 80 FLafqyPVEIP-GVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELG---LDEDFLDRyvnegFSGGEKKRNEILQML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488981874 157 IRQPRLLLLDEPLSALDLnyqfhvmDLVR------RETRRRNIVTLVVVHDINIaLRH--ADHVLMLKAGQLLGDGTP 226
Cdd:COG0396 156 LLEPKLAILDETDSGLDI-------DALRivaegvNKLRSPDRGILIITHYQRI-LDYikPDFVHVLVDGRIVKSGGK 225
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-219 |
8.28e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.65 E-value: 8.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPhlpRGKITALLGPNGSGKSTLMRAMAGLGP--------------CRgelllegenlltqpFS--RRAEQ--VVYL 87
Cdd:NF040905 21 NLSVR---EGEIHALCGENGAGKSTLMKVLSGVYPhgsyegeilfdgevCR--------------FKdiRDSEAlgIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 88 PQTLPAGVHLHVLESIIVA-QRAAGGRHS-PQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLL 165
Cdd:NF040905 84 HQELALIPYLSIAENIFLGnERAKRGVIDwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488981874 166 DEPLSALDLNYQFHVMDLVrRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQ 219
Cdd:NF040905 164 DEPTAALNEEDSAALLDLL-LELKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
138-229 |
8.56e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 58.32 E-value: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 138 YLD----QLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALD--LNYQfhvMDL-VRRETRRRNIVTLVVVHDINIALRHAD 210
Cdd:PRK11650 127 LLDrkprELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDakLRVQ---MRLeIQRLHRRLKTTSLYVTHDQVEAMTLAD 203
|
90
....*....|....*....
gi 488981874 211 HVLMLKAGQLLGDGTPAAV 229
Cdd:PRK11650 204 RVVVMNGGVAEQIGTPVEV 222
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
26-227 |
8.59e-10 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 57.66 E-value: 8.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPhlpRGKITALLGPNGSGKSTLMRAMAGLGPCRGEL---LLEGENLLTQPFSRRAEQVVYL----PQTLPAGVHLH 98
Cdd:TIGR01978 20 NLTVK---KGEIHAIMGPNGSGKSTLSKTIAGHPSYEVTSgtiLFKGQDLLELEPDERARAGLFLafqyPEEIPGVSNLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 99 VLESIIVAQRAAGGRHS---PQRQEEVMALLRQLGI-AHLAMSYLDQ-LSGGQKQLVGLAQSLIRQPRLLLLDEPLSALD 173
Cdd:TIGR01978 97 FLRSALNARRSARGEEPldlLDFEKLLKEKLALLDMdEEFLNRSVNEgFSGGEKKRNEILQMALLEPKLAILDEIDSGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488981874 174 LNYQFHVMDLVRReTRRRNIVTLVVVHDINIA-LRHADHVLMLKAGQLLGDGTPA 227
Cdd:TIGR01978 177 IDALKIVAEGINR-LREPDRSFLIITHYQRLLnYIKPDYVHVLLDGRIVKSGDVE 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-225 |
1.13e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.79 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 19 PRRKVIE-----NLTVPhlpRGKITALLGPNGSGKSTLMRAMAGL-----GPCRGELLLegenlltqPFSRRAEqvvYLP 88
Cdd:COG4586 30 REYREVEavddiSFTIE---PGEIVGFIGPNGAGKSTTIKMLTGIlvptsGEVRVLGYV--------PFKRRKE---FAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 89 QTlpaGV----------HLHVLES--IIvaqraaggRH----SPQRQEEVMALLRQ-LGIAHLamsyLD----QLSGGQK 147
Cdd:COG4586 96 RI---GVvfgqrsqlwwDLPAIDSfrLL--------KAiyriPDAEYKKRLDELVElLDLGEL----LDtpvrQLSLGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 148 QLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDIN--IALrhADHVLMLKAGQLLGDGT 225
Cdd:COG4586 161 MRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHGRIIYDGS 238
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-239 |
1.17e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 57.05 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPHlprGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPfsrrAEQVVYLPQT----LP------AGV 95
Cdd:COG4674 30 SLYVDP---GELRVIIGPNGAGKTTLMDVITGK---------------TRP----DSGSVLFGGTdltgLDeheiarLGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 96 -----------HLHVLESIIVAQRAAGG-------RHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLI 157
Cdd:COG4674 88 grkfqkptvfeELTVFENLELALKGDRGvfaslfaRLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 158 RQPRLLLLDEPlsaldlnyqfhVMDLVRRETRR-----RNIV---TLVVV-HDINIALRHADHVLMLKAGQLLGDGTPAA 228
Cdd:COG4674 168 QDPKLLLLDEP-----------VAGMTDAETERtaellKSLAgkhSVVVVeHDMEFVRQIARKVTVLHQGSVLAEGSLDE 236
|
250
....*....|.
gi 488981874 229 VITPETLAAVY 239
Cdd:COG4674 237 VQADPRVIEVY 247
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
140-236 |
1.24e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 140 DQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETrrRNIVTLVVVHDINIALrHADHVLMLKAGQ 219
Cdd:PLN03232 1370 ENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEF--KSCTMLVIAHRLNTII-DCDKILVLSSGQ 1446
|
90
....*....|....*..
gi 488981874 220 LLGDGTPAAVITPETLA 236
Cdd:PLN03232 1447 VLEYDSPQELLSRDTSA 1463
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
10-199 |
1.69e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 10 SLSHFSAGYPR--RKVIENLTVPhLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGelllegenlltqpfsrrAEQVVYL 87
Cdd:COG2401 30 VLEAFGVELRVveRYVLRDLNLE-IEPGEIVLIVGASGSGKSTLLRLLAGALKGTP-----------------VAGCVDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 88 PQtLPAGVHLHVLESIIVAQRAAggrhspqrqeEVMALLRQLGIAHlAMSYL---DQLSGGQKQLVGLAQSLIRQPRLLL 164
Cdd:COG2401 92 PD-NQFGREASLIDAIGRKGDFK----------DAVELLNAVGLSD-AVLWLrrfKELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190
....*....|....*....|....*....|....*
gi 488981874 165 LDEPLSALDLNYQFHVMDLVRRETRRRNIvTLVVV 199
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLARRAGI-TLVVA 193
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-225 |
2.04e-09 |
|
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: 57.83 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 2 SDQTLSGLSLSH--FSAGYpRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQpFSR 79
Cdd:TIGR01193 467 LNNLNGDIVINDvsYSYGY-GSNILSDISL-TIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD-IDR 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 80 RA--EQVVYLPQTlPAGVHLHVLESIIVaqraagGRHSPQRQEEVMALLR----QLGIAHLAMSYLDQL-------SGGQ 146
Cdd:TIGR01193 544 HTlrQFINYLPQE-PYIFSGSILENLLL------GAKENVSQDEIWAACEiaeiKDDIENMPLGYQTELseegssiSGGQ 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488981874 147 KQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIvtlVVVHDINIALRhADHVLMLKAGQLLGDGT 225
Cdd:TIGR01193 617 KQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTII---FVAHRLSVAKQ-SDKIIVLDHGKIIEQGS 691
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-215 |
2.42e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 134 LAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINiALRHADHVL 213
Cdd:PTZ00265 572 LVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIF 650
|
..
gi 488981874 214 ML 215
Cdd:PTZ00265 651 VL 652
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-237 |
2.44e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.48 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGlgpcrgelllegeNLLTQPFSRRAEQ-VVYLPQT---LPAGVHLHVLesIIVAQ 107
Cdd:PTZ00243 683 VPRGKLTVVLGATGSGKSTLLQSLLS-------------QFEISEGRVWAERsIAYVPQQawiMNATVRGNIL--FFDEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 108 RAAGgRHSPQRQEEVMALLRQLG------IAHLAMSyldqLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLnyqfHVM 181
Cdd:PTZ00243 748 DAAR-LADAVRVSQLEADLAQLGggleteIGEKGVN----LSGGQKARVSLARAVYANRDVYLLDDPLSALDA----HVG 818
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488981874 182 DLVRRET---RRRNIVTLVVVHDINIaLRHADHVLMLKAGQLLGDGTPAAVI-TP--ETLAA 237
Cdd:PTZ00243 819 ERVVEECflgALAGKTRVLATHQVHV-VPRADYVVALGDGRVEFSGSSADFMrTSlyATLAA 879
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
34-229 |
2.68e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 56.63 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAGL-----GPCRGELLLEGENLLTQPFSRRA-----------------EQVVYLPQTL 91
Cdd:PRK13633 35 KGEFLVILGRNGSGKSTIAKHMNALlipseGKVYVDGLDTSDEENLWDIRNKAgmvfqnpdnqivativeEDVAFGPENL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 92 ---PAGVHLHVLESIIVAQRAAGGRHSPqrqeevmallrqlgiaHLamsyldqLSGGQKQLVGLAQSLIRQPRLLLLDEP 168
Cdd:PRK13633 115 gipPEEIRERVDESLKKVGMYEYRRHAP----------------HL-------LSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488981874 169 LSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRhADHVLMLKAGQLLGDGTPAAV 229
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
26-226 |
3.16e-09 |
|
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: 55.23 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPHlprGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenlltqPFSRRAEQVVYLpqtlpAGVHLHVLEsiiV 105
Cdd:cd03217 20 NLTIKK---GEVHALMGPNGSGKSTLAKTIMGH-----------------PKYEVTEGEILF-----KGEDITDLP---P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 106 AQRAAGGRH-SPQRQEE-----VMALLRQLGiahlamsylDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDlnyqfh 179
Cdd:cd03217 72 EERARLGIFlAFQYPPEipgvkNADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD------ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488981874 180 vMDLVR------RETRRRNIVTLVVVHDINIA-LRHADHVLMLKAGQLLGDGTP 226
Cdd:cd03217 137 -IDALRlvaeviNKLREEGKSVLIITHYQRLLdYIKPDRVHVLYDGRIVKSGDK 189
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
118-231 |
3.59e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 56.35 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 118 RQEEVMALLRQLGI-AHLAM--SYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIV 194
Cdd:PRK15093 132 RKRRAIELLHRVGIkDHKDAmrSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTT 211
|
90 100 110
....*....|....*....|....*....|....*..
gi 488981874 195 TLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT 231
Cdd:PRK15093 212 ILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVT 248
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
14-233 |
3.63e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 56.15 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 14 FSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenlltqpfsrraeqvvYLPQtlpA 93
Cdd:PRK13632 15 FSYPNSENNALKNVSF-EINEGEYVAILGHNGSGKSTISKILTGL---------------------------LKPQ---S 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 94 G--------VHLHVLESI-----IVAQraaggrhSPQRQ------EEVMAL-----------LRQLgIAHLAM-----SY 138
Cdd:PRK13632 64 GeikidgitISKENLKEIrkkigIIFQ-------NPDNQfigatvEDDIAFglenkkvppkkMKDI-IDDLAKkvgmeDY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 139 LDQ----LSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVR--RETRRRNIVTlvVVHDINIALRhADHV 212
Cdd:PRK13632 136 LDKepqnLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLIS--ITHDMDEAIL-ADKV 212
|
250 260
....*....|....*....|.
gi 488981874 213 LMLKAGQLLGDGTPAAVITPE 233
Cdd:PRK13632 213 IVFSEGKLIAQGKPKEILNNK 233
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
9-225 |
3.80e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 56.76 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRR--KVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMaglgpCRG-ELLLEGENLLTQPFSRRAEQVv 85
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSL-QIKAGEKVALLGRTGCGKSTLLQLL-----TRAwDPQQGEILLNGQPIADYSEAA- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 86 yLPQT---LPAGVHL--HVL-ESIIVAQRAAGgrhspqrQEEVMALLRQLGIAHLAMSY--LD--------QLSGGQKQL 149
Cdd:PRK11160 412 -LRQAisvVSQRVHLfsATLrDNLLLAAPNAS-------DEALIEVLQQVGLEKLLEDDkgLNawlgeggrQLSGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488981874 150 VGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRnivTLVVVHDINIALRHADHVLMLKAGQLLGDGT 225
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK---TVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-221 |
4.15e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 55.62 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 18 YPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL----------GPCRGELLLEGENLLTQPFSRRAEQVVY- 86
Cdd:PRK14267 14 YGSNHVIKGVDL-KIPQNGVFALMGPSGCGKSTLLRTFNRLlelneearveGEVRLFGRNIYSPDVDPIEVRREVGMVFq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQTLPagvHLHVLESIIVAQRAAGGRHSPQRQEEVM-------ALLRQlgIAHLAMSYLDQLSGGQKQLVGLAQSLIRQ 159
Cdd:PRK14267 93 YPNPFP---HLTIYDNVAIGVKLNGLVKSKKELDERVewalkkaALWDE--VKDRLNDYPSNLSGGQRQRLVIARALAMK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488981874 160 PRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVtlVVVHDINIALRHADHVLMLKAGQLL 221
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFELKKEYTIV--LVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-225 |
4.59e-09 |
|
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: 56.37 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 13 HFsaGY-PRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAM-------AGlgpcRGELLLEGENLLTQPFSRRAEQV 84
Cdd:COG5265 364 SF--GYdPERPILKGVSF-EVPAGKTVAIVGPSGAGKSTLARLLfrfydvtSG----RILIDGQDIRDVTQASLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 85 VylPQ-TlpagvhlhVL--ESIivAQRAAGGRhsPQ-RQEEVMALLR--QLG--IAHLAMSYLDQ-------LSGGQKQL 149
Cdd:COG5265 437 V--PQdT--------VLfnDTI--AYNIAYGR--PDaSEEEVEAAARaaQIHdfIESLPDGYDTRvgerglkLSGGEKQR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 150 VGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNivTLVVVHdinialR-----HADHVLMLKAGQLLGDG 224
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRT--TLVIAH------RlstivDADEILVLEAGRIVERG 574
|
.
gi 488981874 225 T 225
Cdd:COG5265 575 T 575
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
117-236 |
5.84e-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: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 117 QRQEEVMALLRQLGIA-HLAM--SYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNI 193
Cdd:COG4170 131 WRKKRAIELLHRVGIKdHKDImnSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGT 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 488981874 194 VTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVIT----PETLA 236
Cdd:COG4170 211 SILLISHDLESISQWADTITVLYCGQTVESGPTEQILKsphhPYTKA 257
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-238 |
6.06e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 6.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 5 TLSGLSLsHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKS----TLMRAMAGLGpcrgelllEGENLLTQPFSRR 80
Cdd:PRK10261 14 AVENLNI-AFMQEQQKIAAVRNLSF-SLQRGETLAIVGESGSGKSvtalALMRLLEQAG--------GLVQCDKMLLRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 81 AEQVVYLPQTLPA-------------------------GVHLHVLESIIVAQRAagGRHSPQRQEEVMALLRQLGIAHLA 135
Cdd:PRK10261 84 SRQVIELSEQSAAqmrhvrgadmamifqepmtslnpvfTVGEQIAESIRLHQGA--SREEAMVEAKRMLDQVRIPEAQTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 136 MS-YLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLM 214
Cdd:PRK10261 162 LSrYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLV 241
|
250 260 270
....*....|....*....|....*....|.
gi 488981874 215 LKAGQLLGDGT-------PAAVITPETLAAV 238
Cdd:PRK10261 242 MYQGEAVETGSveqifhaPQHPYTRALLAAV 272
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
31-219 |
1.00e-08 |
|
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: 53.13 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAglgpcrgelllegenlltqpfsrraeqVVYLPQTLPAGVHLHVLESIIVAQRAA 110
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDAIG---------------------------LALGGAQSATRRRSGVKAGCIVAAVSA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 111 GgrhspqrqeevmallrqlgiahlAMSYLDQLSGGQKQLVGLA-----QSLIRQPrLLLLDEPLSALDLNYQFHVMDLVR 185
Cdd:cd03227 70 E-----------------------LIFTRLQLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAIL 125
|
170 180 190
....*....|....*....|....*....|....*.
gi 488981874 186 RETRRRNIVtLVVVHDINIALR--HADHVLMLKAGQ 219
Cdd:cd03227 126 EHLVKGAQV-IVITHLPELAELadKLIHIKKVITGV 160
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
116-229 |
1.09e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.97 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 116 PQRQEEVMALLRQLGI-AHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIV 194
Cdd:PRK11308 128 AERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLS 207
|
90 100 110
....*....|....*....|....*....|....*.
gi 488981874 195 TLVVVHDINIaLRH-ADHVLMLKAGQLLGDGTPAAV 229
Cdd:PRK11308 208 YVFISHDLSV-VEHiADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
134-226 |
1.14e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 54.71 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 134 LAMSYLDQ----LSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVrRETRRRNIVTLVVVHDINIALRHA 209
Cdd:PRK13651 154 LDESYLQRspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIF-DNLNKQGKTIILVTHDLDNVLEWT 232
|
90
....*....|....*..
gi 488981874 210 DHVLMLKAGQLLGDGTP 226
Cdd:PRK13651 233 KRTIFFKDGKIIKDGDT 249
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
31-211 |
1.21e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.80 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAEQVVYLPQTLPAGVHLHVLESIIVaqraa 110
Cdd:PRK13540 23 HLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLY----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 111 gGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVrRETRR 190
Cdd:PRK13540 98 -DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI-QEHRA 175
|
170 180
....*....|....*....|.
gi 488981874 191 RNIVTLVVVHDiNIALRHADH 211
Cdd:PRK13540 176 KGGAVLLTSHQ-DLPLNKADY 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-229 |
1.22e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.25 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 24 IENLTVPHLPrGKITALLGPNGSGKSTLMRAMAGLGPCRGELLL-------EGENLLTQPFsRRAEQVVYLPQTLPAGVH 96
Cdd:PRK10261 340 VEKVSFDLWP-GETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqridTLSPGKLQAL-RRDIQFIFQDPYASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 97 LHVLESIIVAQRAAGGRHSPQRQEEVMALLRQLGI-AHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLN 175
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488981874 176 YQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAV 229
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-175 |
1.56e-08 |
|
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: 54.94 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 13 HFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSRRAE-----QVVYL 87
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSF-KLPPGGIVGVIGPNGAGKSTLFRMITGQ---------------EQPDSGTIEigetvKLAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 88 PQTLPA-------------GVHLHVLESIIVAQRAAGGRHS---PQRQEEVmallrqlgiahlamsylDQLSGGQKQLVG 151
Cdd:TIGR03719 391 DQSRDAldpnktvweeisgGLDIIKLGKREIPSRAYVGRFNfkgSDQQKKV-----------------GQLSGGERNRVH 453
|
170 180
....*....|....*....|....
gi 488981874 152 LAQSLIRQPRLLLLDEPLSALDLN 175
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-235 |
1.71e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVPHLPrGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenlltqpFSRRAEQVVYLP 88
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYP-GRVMALVGENGAGKSTMMKVLTGI------------------YTRDAGSILYLG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 89 QTL---------PAGV-----------HLHVLESIIVAQ---RAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQLSGG 145
Cdd:PRK10762 66 KEVtfngpkssqEAGIgiihqelnlipQLTIAENIFLGRefvNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 146 QKQLVGLAQSLIRQPRLLLLDEPLSAL-DLNYQ--FHVMdlvrRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLG 222
Cdd:PRK10762 146 EQQMVEIAKVLSFESKVIIMDEPTDALtDTETEslFRVI----RELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIA 221
|
250
....*....|...
gi 488981874 223 DgTPAAVITPETL 235
Cdd:PRK10762 222 E-REVADLTEDSL 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
141-229 |
1.87e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.90 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 141 QLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQL 220
Cdd:PRK13637 144 ELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
....*....
gi 488981874 221 LGDGTPAAV 229
Cdd:PRK13637 224 ELQGTPREV 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-220 |
2.57e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.57 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGlgpcrgelllegENLLTQPFSRRAEQVVYLPQTlpAGVHLHVLESIIVaqraAG 111
Cdd:TIGR00957 661 IPEGALVAVVGQVGCGKSSLLSALLA------------EMDKVEGHVHMKGSVAYVPQQ--AWIQNDSLRENIL----FG 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 112 GRHSPQRQEEVM---ALLRQLGIahlaMSYLDQ---------LSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFH 179
Cdd:TIGR00957 723 KALNEKYYQQVLeacALLPDLEI----LPSGDRteigekgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488981874 180 VMD-LVRRETRRRNIVTLVVVHDINIaLRHADHVLMLKAGQL 220
Cdd:TIGR00957 799 IFEhVIGPEGVLKNKTRILVTHGISY-LPQVDVIIVMSGGKI 839
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-242 |
2.79e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 30 PHLPRGKITALLGPNGSGKSTLMRAMAG-----LGpcrgelllegeNLLTQP-------FSRRAEQVVYLpQTLPAGvhl 97
Cdd:PRK13409 94 PIPKEGKVTGILGPNGIGKTTAVKILSGelipnLG-----------DYEEEPswdevlkRFRGTELQNYF-KKLYNG--- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 98 hvleSIIVAqraaggrHSPQRQEE--------VMALLR-------------QLGIAHLAMSYLDQLSGGQKQLVGLAQSL 156
Cdd:PRK13409 159 ----EIKVV-------HKPQYVDLipkvfkgkVRELLKkvdergkldevveRLGLENILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 157 IRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIvtLVVVHDINIALRHAD--HVLMlkagqllgdGTPAA--VITP 232
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYV--LVVEHDLAVLDYLADnvHIAY---------GEPGAygVVSK 296
|
250
....*....|
gi 488981874 233 etlaaVYGVR 242
Cdd:PRK13409 297 -----PKGVR 301
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
26-225 |
3.34e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 53.95 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPhlPRGKItALLGPNGSGKSTLMRAMAGLGPcrgeLLLEGENLLTQPFSRRAEQV------------VYLPQTLPA 93
Cdd:PRK10790 361 NLSVP--SRGFV-ALVGHTGSGKSTLASLLMGYYP----LTEGEIRLDGRPLSSLSHSVlrqgvamvqqdpVVLADTFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 94 GVHLhvlesiivaqraagGRHSpqRQEEVMALLRQLGIAHLAMSYLD-----------QLSGGQKQLVGLAQSLIRQPRL 162
Cdd:PRK10790 434 NVTL--------------GRDI--SEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488981874 163 LLLDEPLSALDLNYQ---FHVMDLVRRETrrrnivTLVVvhdinIALR-----HADHVLMLKAGQLLGDGT 225
Cdd:PRK10790 498 LILDEATANIDSGTEqaiQQALAAVREHT------TLVV-----IAHRlstivEADTILVLHRGQAVEQGT 557
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
31-226 |
3.92e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.20 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQP----FSRRAEQVVYLP--QTLPAGVHLHV---LE 101
Cdd:PRK13650 29 HVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnvwdIRHKIGMVFQNPdnQFVGATVEDDVafgLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 102 SiivaqraAGGRHSpQRQEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVM 181
Cdd:PRK13650 109 N-------KGIPHE-EMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488981874 182 DLVRRETRRRNIVTLVVVHDIN-IALrhADHVLMLKAGQLLGDGTP 226
Cdd:PRK13650 181 KTIKGIRDDYQMTVISITHDLDeVAL--SDRVLVMKNGQVESTSTP 224
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-175 |
4.90e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.16 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAGLgpcrGELLLEGENLLTQPFSR--RAEQVVYL------PQTLPAGVHLHVLES 102
Cdd:PRK13543 33 HVDAGEALLVQGDNGAGKTTLLRVLAGL----LHVESGQIQIDGKTATRgdRSRFMAYLghlpglKADLSTLENLHFLCG 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488981874 103 IivaqraaGGRHSPQRQEEVMALLrqlGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLN 175
Cdd:PRK13543 109 L-------HGRRAKQMPGSALAIV---GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-200 |
1.16e-07 |
|
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: 52.44 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 22 KVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGLGPCRgelllegENLLTQPfsrRAEQVVYLPQTlPAGVHLHVLE 101
Cdd:TIGR00954 466 VLIESLSF-EVPSGNNLLICGPNGCGKSSLFRILGELWPVY-------GGRLTKP---AKGKLFYVPQR-PYMTLGTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 102 SIIVAQRAAGGRHSPQRQEEVMALLRQLGIAHL--------AM-SYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSAL 172
Cdd:TIGR00954 534 QIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHIlereggwsAVqDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180
....*....|....*....|....*...
gi 488981874 173 DLNyqfhVMDLVRRETRRRNIVTLVVVH 200
Cdd:TIGR00954 614 SVD----VEGYMYRLCREFGITLFSVSH 637
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
140-230 |
1.45e-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: 52.26 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 140 DQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRreTRRRNIVTLVVVHDINIALRHAdHVLMLKAGQ 219
Cdd:TIGR00957 1420 ENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGE 1496
|
90
....*....|.
gi 488981874 220 LLGDGTPAAVI 230
Cdd:TIGR00957 1497 VAEFGAPSNLL 1507
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
140-233 |
1.55e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 140 DQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETrrRNIVTLVVVHDINIALrHADHVLMLKAGQ 219
Cdd:PLN03130 1373 ENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEF--KSCTMLIIAHRLNTII-DCDRILVLDAGR 1449
|
90
....*....|....
gi 488981874 220 LLGDGTPAAVITPE 233
Cdd:PLN03130 1450 VVEFDTPENLLSNE 1463
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
9-199 |
1.81e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVPHLP--RGKITALLGPNGSGKSTLMRAMAGLGPcrgelllEGENLLTQPFSRraeqvvy 86
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTlnAGDSWAFVGANGSGKSALARALAGELP-------LLSGERQSQFSH------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 lpqtlPAGVHLHVLESII----------------------VAQRAAGGRHSPQRQEEvmaLLRQLGIAHLAMSYLDQLSG 144
Cdd:PRK10938 67 -----ITRLSFEQLQKLVsdewqrnntdmlspgeddtgrtTAEIIQDEVKDPARCEQ---LAQQFGITALLDRRFKYLST 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488981874 145 GQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVrrETRRRNIVTLVVV 199
Cdd:PRK10938 139 GETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELL--ASLHQSGITLVLV 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-242 |
1.82e-07 |
|
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: 51.71 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LP---RGKITALLGPNGSGKSTLMRAMAG-----LGpcrgelllegeNLLTQP-------FSRRAEQVVYLpQTLPAGvh 96
Cdd:COG1245 93 LPvpkKGKVTGILGPNGIGKSTALKILSGelkpnLG-----------DYDEEPswdevlkRFRGTELQDYF-KKLANG-- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 97 lhvleSIIVAqraaggrHSPQRQE--------EVMALLR-------------QLGIAHLAMSYLDQLSGGQKQLVGLAQS 155
Cdd:COG1245 159 -----EIKVA-------HKPQYVDlipkvfkgTVRELLEkvdergkldelaeKLGLENILDRDISELSGGELQRVAIAAA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 156 LIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVtLVVVHDINIALRHADHVLMLKagqllgdGTPAA--VITPe 233
Cdd:COG1245 227 LLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYV-LVVEHDLAILDYLADYVHILY-------GEPGVygVVSK- 297
|
....*....
gi 488981874 234 tlaaVYGVR 242
Cdd:COG1245 298 ----PKSVR 302
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-212 |
1.87e-07 |
|
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: 49.88 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPHLPRGKITALLGPNGSGKSTLMRAMAGlgpcrgelllegenlLTQPFSRRAE----QVVYLPQtlpagvhlhvle 101
Cdd:cd03222 16 LVELGVVKEGEVIGIVGPNGTGKTTAVKILAG---------------QLIPNGDNDEwdgiTPVYKPQ------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 102 siivaqraaggrhspqrqeevmallrqlgiahlamsYLDqLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVM 181
Cdd:cd03222 69 ------------------------------------YID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAA 111
|
170 180 190
....*....|....*....|....*....|.
gi 488981874 182 DLVRRETRRRNIVTLVVVHDINIALRHADHV 212
Cdd:cd03222 112 RAIRRLSEEGKKTALVVEHDLAVLDYLSDRI 142
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
138-175 |
2.10e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 2.10e-07
10 20 30
....*....|....*....|....*....|....*...
gi 488981874 138 YLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLN 175
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1392
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
34-244 |
2.11e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.45 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAGlgpcrgelllegenlLTQPFS---RRAEQVVYLPQT---LPAGV-----HLHVLES 102
Cdd:PRK11288 29 AGQVHALMGENGAGKSTLLKILSG---------------NYQPDAgsiLIDGQEMRFASTtaaLAAGVaiiyqELHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 103 IIVAQRAAGGrHSPQR---------QEEVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEP---LS 170
Cdd:PRK11288 94 MTVAENLYLG-QLPHKggivnrrllNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPtssLS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 171 ALDLNYQFHVMDLVRRETRrrniVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAA---------VYGV 241
Cdd:PRK11288 173 AREIEQLFRVIRELRAEGR----VILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDRDQLVQamvgreigdIYGY 248
|
...
gi 488981874 242 RGR 244
Cdd:PRK11288 249 RPR 251
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
140-226 |
2.88e-07 |
|
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: 49.72 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 140 DQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTlvVVHDINIALRHaDHVLMLKAGQ 219
Cdd:cd03369 124 LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILT--IAHRLRTIIDY-DKILVMDAGE 200
|
....*..
gi 488981874 220 LLGDGTP 226
Cdd:cd03369 201 VKEYDHP 207
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
9-235 |
3.73e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 49.99 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPR-RKVIENLTVPhLPRGKITALLGPNGSGKSTL-------MRAMAG--------------LGPCRGELL 66
Cdd:PRK13644 2 IRLENVSYSYPDgTPALENINLV-IKKGEYIGIIGKNGSGKSTLalhlnglLRPQKGkvlvsgidtgdfskLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 67 LEGENLLTQPFSRRAEQ-VVYLPQTLpagvhlhVLESIIVAQRaaggrhspqrqeeVMALLRQLGIAHLAMSYLDQLSGG 145
Cdd:PRK13644 81 IVFQNPETQFVGRTVEEdLAFGPENL-------CLPPIEIRKR-------------VDRALAEIGLEKYRHRSPKTLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 146 QKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVtLVVVHDINiALRHADHVLMLKAGQLLGDGT 225
Cdd:PRK13644 141 QGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTI-VYITHNLE-ELHDADRIIVMDRGKIVLEGE 218
|
250
....*....|
gi 488981874 226 PAAVITPETL 235
Cdd:PRK13644 219 PENVLSDVSL 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-220 |
4.05e-07 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 48.97 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 24 IENLTVPH--------LPRGKITALLGPNGSGKSTLMRAMAGLGPcrgelllegenlltqPFSRRaeqvVYLpqtlpAGV 95
Cdd:cd03215 7 VRGLSVKGavrdvsfeVRAGEIVGIAGLVGNGQTELAEALFGLRP---------------PASGE----ITL-----DGK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 96 HLHVLeSIIVAqRAAGGRHSPQ-RQEEvmALLRQLGIAH-LAMSYLdqLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALD 173
Cdd:cd03215 63 PVTRR-SPRDA-IRAGIAYVPEdRKRE--GLVLDLSVAEnIALSSL--LSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488981874 174 LNYQFHVMDLVrRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQL 220
Cdd:cd03215 137 VGAKAEIYRLI-RELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
141-225 |
5.80e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.96 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 141 QLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVrrETRRRNIVTLVVVHDINiALRHADHVLMLKAGQL 220
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL--DELMKGRTTFIIAHRLS-TVRNADRILVFDNGRV 547
|
....*
gi 488981874 221 LGDGT 225
Cdd:PRK13657 548 VESGS 552
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-213 |
7.15e-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: 48.37 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 37 ITALLGPNGSGKSTLMRA--MA--GLGPCRGELLLEGENLLTQPfSRRAEqvVYLPQTLPAGVHLHVLESIIVAQRAagg 112
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEAlkYAltGELPPNSKGGAHDPKLIREG-EVRAQ--VKLAFENANGKKYTITRSLAILENV--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 113 rhspqrqeevmALLRQLGIAHLAMSYLDQLSGGQKQLVG------LAQSLIRQPRLLLLDEPLSALD---LNYQFHvmDL 183
Cdd:cd03240 98 -----------IFCHQGESNWPLLDMRGRCSGGEKVLASliirlaLAETFGSNCGILALDEPTTNLDeenIEESLA--EI 164
|
170 180 190
....*....|....*....|....*....|
gi 488981874 184 VRRETRRRNIVTLVVVHDINIaLRHADHVL 213
Cdd:cd03240 165 IEERKSQKNFQLIVITHDEEL-VDAADHIY 193
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
35-218 |
7.43e-07 |
|
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: 48.39 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 35 GKITALLGPNGSGKSTLMRAMAGlgpcRGEL------LLEGENLLTQPFSRR---AEQV-VYLPQtlpagvhLHVLESIi 104
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAG----RKTAgvitgeILINGRPLDKNFQRStgyVEQQdVHSPN-------LTVREAL- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 105 vaqraaggrhspqrqeEVMALLRQLGIAhlamsyldqlsggQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLV 184
Cdd:cd03232 101 ----------------RFSALLRGLSVE-------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 488981874 185 RRETRR-RNIvtLVVVHDINIAL-RHADHVLMLKAG 218
Cdd:cd03232 152 KKLADSgQAI--LCTIHQPSASIfEKFDRLLLLKRG 185
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
9-175 |
2.02e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVI-ENLTVPHLPRGKItALLGPNGSGKSTLMRAMAGlgpcrgelllegenlLTQPFS----RRAE- 82
Cdd:PLN03073 509 ISFSDASFGYPGGPLLfKNLNFGIDLDSRI-AMVGPNGIGKSTILKLISG---------------ELQPSSgtvfRSAKv 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 83 QVVYLPQTLPAGVHLHVLESIIVAQRAAGgrhSPQrqEEVMALLRQLGIA-HLAMSYLDQLSGGQKQLVGLAQSLIRQPR 161
Cdd:PLN03073 573 RMAVFSQHHVDGLDLSSNPLLYMMRCFPG---VPE--QKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPH 647
|
170
....*....|....
gi 488981874 162 LLLLDEPLSALDLN 175
Cdd:PLN03073 648 ILLLDEPSNHLDLD 661
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-231 |
2.19e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.56 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 18 YP--RRKVIENLTVPHLPrGKITALLGPNGSGKSTLMRAM-----AGLGPCRGELLLEGENLLTQPFSRRAeqVVylPQT 90
Cdd:PRK10789 323 YPqtDHPALENVNFTLKP-GQMLGICGPTGSGKSTLLSLIqrhfdVSEGDIRFHDIPLTKLQLDSWRSRLA--VV--SQT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 91 lpagvhlHVLESIIVAQRAAGGR-HSPQRQEEVMALLRQL--GIAHLAMSYLDQ-------LSGGQKQLVGLAQSLIRQP 160
Cdd:PRK10789 398 -------PFLFSDTVANNIALGRpDATQQEIEHVARLASVhdDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488981874 161 RLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVtlVVVHDINiALRHADHVLMLKAGQLLGDGTPAAVIT 231
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQWGEGRTVI--ISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-225 |
2.65e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 32 LPRGKITALLGPNGSGKSTLMRAMAGLGPcrgelllegeNLLTQPFSRRAeQVVYLPQtLPAGVHLHVLESIIVAQRAAG 111
Cdd:PLN03232 640 IPVGSLVAIVGGTGEGKTSLISAMLGELS----------HAETSSVVIRG-SVAYVPQ-VSWIFNATVRENILFGSDFES 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 112 GRHSpqRQEEVMALLRQLGIahLAMSYLDQL-------SGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMD-L 183
Cdd:PLN03232 708 ERYW--RAIDVTALQHDLDL--LPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDsC 783
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488981874 184 VRRETRRRnivTLVVVHDINIALRHADHVLMLKAGQLLGDGT 225
Cdd:PLN03232 784 MKDELKGK---TRVLVTNQLHFLPLMDRIILVSEGMIKEEGT 822
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
115-186 |
3.57e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 3.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488981874 115 SPQRQEEVMALLRQLGI-AHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALD-LNYQfhvmdLVRR 186
Cdd:PRK10938 374 SDRQQKLAQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDpLNRQ-----LVRR 442
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-225 |
4.02e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.81 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTVPhlpRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLltqpfsrraeqVVYLPQT---LPAGVHLHVLes 102
Cdd:PLN03130 637 NLDVP---VGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGT-----------VAYVPQVswiFNATVRDNIL-- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 103 iivaqraAGGRHSPQRQE---EVMALLRQLGIahLAMSYLDQ-------LSGGQKQLVGLAQSLIRQPRLLLLDEPLSAL 172
Cdd:PLN03130 701 -------FGSPFDPERYEraiDVTALQHDLDL--LPGGDLTEigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488981874 173 DLNYQFHVMD-LVRRETRRRnivTLVVVHDINIALRHADHVLMLKAGQLLGDGT 225
Cdd:PLN03130 772 DAHVGRQVFDkCIKDELRGK---TRVLVTNQLHFLSQVDRIILVHEGMIKEEGT 822
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
35-218 |
4.07e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.92 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 35 GKITALLGPNGSGKSTLMRAMAGlgpcRGELLLEGENLLTQPFSRRAEQVV----YLPQTLPAGVHLHVLESIIVAQ--- 107
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG----RKTGGYIEGDIRISGFPKKQETFArisgYCEQNDIHSPQVTVRESLIYSAflr 981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 108 --RAAGGRHSPQRQEEVMAL--LRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDL 183
Cdd:PLN03140 982 lpKEVSKEEKMMFVDEVMELveLDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT 1061
|
170 180 190
....*....|....*....|....*....|....*...
gi 488981874 184 VRR--ETRRRNIVTlvvVHDINIALRHA-DHVLMLKAG 218
Cdd:PLN03140 1062 VRNtvDTGRTVVCT---IHQPSIDIFEAfDELLLMKRG 1096
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-237 |
5.08e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.13 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 19 PRRKVIENLTVPhLPRGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENlltQPFSRRAEQvvylpQTLPAGVHLh 98
Cdd:TIGR02633 271 PHRKRVDDVSFS-LRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFING---KPVDIRNPA-----QAIRAGIAM- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 99 VLESI----IVAQRAAG------------GRHSPQRQEEVMALLRQLGIAHLAMSYLD----QLSGGQKQLVGLAQSLIR 158
Cdd:TIGR02633 341 VPEDRkrhgIVPILGVGknitlsvlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFlpigRLSGGNQQKAVLAKMLLT 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488981874 159 QPRLLLLDEPLSALDLNYQFHVMDLVrRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQLLGDGTPAAVITPETLAA 237
Cdd:TIGR02633 421 NPRVLILDEPTRGVDVGAKYEIYKLI-NQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVLAA 498
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-58 |
6.48e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 6.48e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 488981874 13 HFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAGL 58
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSF-SLPPGGIVGIIGPNGAGKSTLFKMITGQ 373
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-209 |
7.39e-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: 44.67 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenlltqpFSRRAEQVVYLPQTLPAGVHLHVLESIIVAQRAAGGr 113
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE------------------LGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASG- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 114 HSPQRQEEVMALLRQlgiahlamsyldqlsggqkqlvglaqsliRQPRLLLLDEPLSALDLNYQFHVMDLVR-----RET 188
Cdd:smart00382 62 SGELRLRLALALARK-----------------------------LKPDVLILDEITSLLDAEQEALLLLLEElrlllLLK 112
|
170 180
....*....|....*....|.
gi 488981874 189 RRRNIVTLVVVHDINIALRHA 209
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPAL 133
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
8-225 |
8.08e-06 |
|
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: 46.00 E-value: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 8 GLSLSHFSA-GYPrrkVIENLTVpHLPRGKITALLGPNGSGKSTL-MRAMAGLGPCRGELllegenlltqpfsRRAEQVV 85
Cdd:cd03291 39 NLFFSNLCLvGAP---VLKNINL-KIEKGEMLAITGSTGSGKTSLlMLILGELEPSEGKI-------------KHSGRIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 86 YLPQT---LPAGVHLHVLESIIVAQ-RAAGGRHSPQRQEEVMALLRQ----LGIAHLAmsyldqLSGGQKQLVGLAQSLI 157
Cdd:cd03291 102 FSSQFswiMPGTIKENIIFGVSYDEyRYKSVVKACQLEEDITKFPEKdntvLGEGGIT------LSGGQRARISLARAVY 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488981874 158 RQPRLLLLDEPLSALDLNYQFHVMD-----LVRRETRRrnIVTLVVVHdiniaLRHADHVLMLKAGQLLGDGT 225
Cdd:cd03291 176 KDADLYLLDSPFGYLDVFTEKEIFEscvckLMANKTRI--LVTSKMEH-----LKKADKILILHEGSSYFYGT 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
35-186 |
1.24e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 35 GKITALLGPNGSGKSTLMRAMAG---LGPCRGELLLEGENLLTQPFSRRA----EQVVYLPQTLpagvhlhVLESIIVAQ 107
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAErvtTGVITGGDRLVNGRPLDSSFQRSIgyvqQQDLHLPTST-------VRESLRFSA 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 108 RAAGGRHSPQRQ-----EEVMALLRqlgiahlaM-SYLDQLSG--------GQKQLVGLAQSLIRQPRLLL-LDEPLSAL 172
Cdd:TIGR00956 862 YLRQPKSVSKSEkmeyvEEVIKLLE--------MeSYADAVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLDEPTSGL 933
|
170
....*....|....
gi 488981874 173 DLNYQFHVMDLVRR 186
Cdd:TIGR00956 934 DSQTAWSICKLMRK 947
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
9-175 |
1.33e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVPHLPRGKItALLGPNGSGKSTLMRAMAGlgpcrgelllegenlLTQPFSRRAEqvvylp 88
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRI-GLLGRNGAGKSTLIKLLAG---------------ELAPVSGEIG------ 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 89 qtLPAGVHL-----HVLESIIVAQRAAG--GRHSPQRQEEVMA-LLRQLGIAHLAMSYL-DQLSGGQKQLVGLAQSLIRQ 159
Cdd:PRK10636 371 --LAKGIKLgyfaqHQLEFLRADESPLQhlARLAPQELEQKLRdYLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQR 448
|
170
....*....|....*.
gi 488981874 160 PRLLLLDEPLSALDLN 175
Cdd:PRK10636 449 PNLLLLDEPTNHLDLD 464
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
31-230 |
1.52e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 45.78 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 31 HLPRGKITALLGPNGSGKSTlmraMAGLgpcrgelllegenlltqpFSRRAEqvVYLPQTLPAGVHL--HVLESI----- 103
Cdd:PRK11176 365 KIPAGKTVALVGRSGSGKST----IANL------------------LTRFYD--IDEGEILLDGHDLrdYTLASLrnqva 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 104 IVAQR--------------AAGGRHSpqrQEEVMALLRqlgIAHlAMSYLDQ---------------LSGGQKQLVGLAQ 154
Cdd:PRK11176 421 LVSQNvhlfndtianniayARTEQYS---REQIEEAAR---MAY-AMDFINKmdngldtvigengvlLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488981874 155 SLIRQPRLLLLDEPLSALDLNYQFHVMDLVrrETRRRNIVTLVVVHDINiALRHADHVLMLKAGQLLGDGTPAAVI 230
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAAL--DELQKNRTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELL 566
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-218 |
1.85e-05 |
|
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: 45.67 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 8 GLSLSHFSA-GYPrrkVIENLTVpHLPRGKITALLGPNGSGKSTL-MRAMAGLGPCRGELllegenlltqpfsRRAEQVV 85
Cdd:TIGR01271 428 GLFFSNFSLyVTP---VLKNISF-KLEKGQLLAVAGSTGSGKSSLlMMIMGELEPSEGKI-------------KHSGRIS 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 86 YLPQT---LPAGVHLHVLESIIVAQ-RAAGGRHSPQRQEEVMAL-------LRQLGIAhlamsyldqLSGGQKQLVGLAQ 154
Cdd:TIGR01271 491 FSPQTswiMPGTIKDNIIFGLSYDEyRYTSVIKACQLEEDIALFpekdktvLGEGGIT---------LSGGQRARISLAR 561
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488981874 155 SLIRQPRLLLLDEPLSALDLNYQFHVMD-----LVRRETRRrnIVTLVVVHdiniaLRHADHVLMLKAG 218
Cdd:TIGR01271 562 AVYKDADLYLLDSPFTHLDVVTEKEIFEsclckLMSNKTRI--LVTSKLEH-----LKKADKILLLHEG 623
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
127-240 |
2.73e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.04 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 127 RQLGIAhlaMSYLDQ----LSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRReTRRRNIVTLVVVHDI 202
Cdd:PRK15439 388 RALNIK---FNHAEQaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRS-IAAQNVAVLFISSDL 463
|
90 100 110
....*....|....*....|....*....|....*...
gi 488981874 203 NIALRHADHVLMLKAGQLLGDGTPAAVITPETLAAVYG 240
Cdd:PRK15439 464 EEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLAFG 501
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-177 |
2.92e-05 |
|
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: 45.29 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 5 TLSGLSLSHFSAGyprRKVIENLTVPHLPrGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGEN--LLTQPFSRRAE 82
Cdd:TIGR01271 1219 DVQGLTAKYTEAG---RAVLQDLSFSVEG-GQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSwnSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 83 QVVylPQTlpagvhLHVLESIIvaqRAAGGRHSPQRQEEVMALLRQLGIAHLAMSYLDQ-----------LSGGQKQLVG 151
Cdd:TIGR01271 1295 GVI--PQK------VFIFSGTF---RKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMC 1363
|
170 180
....*....|....*....|....*..
gi 488981874 152 LAQSLIRQPRLLLLDEPLSALD-LNYQ 177
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLDpVTLQ 1390
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
125-224 |
4.49e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 125 LLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTLVVVHdINI 204
Cdd:NF000106 128 LLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQY-MEE 206
|
90 100
....*....|....*....|
gi 488981874 205 ALRHADHVLMLKAGQLLGDG 224
Cdd:NF000106 207 AEQLAHELTVIDRGRVIADG 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
35-219 |
4.67e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 43.02 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 35 GKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGE--NLLTQPFSRRAE-QVVYLPQTlpaGVHLHVL---ESIIVAQR 108
Cdd:cd03233 33 GEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHynGIPYKEFAEKYPgEIIYVSEE---DVHFPTLtvrETLDFALR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 109 AAGGRhspqrqeevmallrqlgiahlamsYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVR--- 185
Cdd:cd03233 110 CKGNE------------------------FVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRtma 165
|
170 180 190
....*....|....*....|....*....|....
gi 488981874 186 RETRRRNIVTLVVVHDINIALrhADHVLMLKAGQ 219
Cdd:cd03233 166 DVLKTTTFVSLYQASDEIYDL--FDKVLVLYEGR 197
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
23-173 |
5.06e-05 |
|
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: 43.69 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 23 VIENLTVPHLPRGKItALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFS--RRAEQVVylPQTLpagvhlHVL 100
Cdd:cd03289 19 VLENISFSISPGQRV-GLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQkwRKAFGVI--PQKV------FIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 101 ESIIVAQRAAGGRHSpqrQEEVMALLRQLGIAHLAMSYLDQL-----------SGGQKQLVGLAQSLIRQPRLLLLDEPL 169
Cdd:cd03289 90 SGTFRKNLDPYGKWS---DEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
....
gi 488981874 170 SALD 173
Cdd:cd03289 167 AHLD 170
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-173 |
7.18e-05 |
|
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: 43.85 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 9 LSLSHFSAGYP--RRKVIENLTVPHLPrGKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEGENLLTQPFSRRAEQVVY 86
Cdd:TIGR01257 1938 LRLNELTKVYSgtSSPAVDRLCVGVRP-GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 87 LPQ------TLPAGVHLHVLESIivaqraaggRHSPQRQEEVMAllrQLGIAHLAMS-YLDQL----SGGQKQLVGLAQS 155
Cdd:TIGR01257 2017 CPQfdaiddLLTGREHLYLYARL---------RGVPAEEIEKVA---NWSIQSLGLSlYADRLagtySGGNKRKLSTAIA 2084
|
170
....*....|....*...
gi 488981874 156 LIRQPRLLLLDEPLSALD 173
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMD 2102
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
24-56 |
7.98e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 43.06 E-value: 7.98e-05
10 20 30
....*....|....*....|....*....|...
gi 488981874 24 IENLTVPHLPRGKITALLGPNGSGKSTLMRAMA 56
Cdd:COG3950 14 FEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIA 46
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-168 |
1.03e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.08 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 14 FSAGYPRRKV--------IENLTVPH--------LPRGKITALLGPNGSGKSTLMRAMAGLGPCRG--ELLLEGENLLTQ 75
Cdd:COG1129 241 LEDLFPKRAAapgevvleVEGLSVGGvvrdvsfsVRAGEILGIAGLVGAGRTELARALFGADPADSgeIRLDGKPVRIRS 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 76 PFSRRAEQVVYLP---QTLpaGVHLH--VLESIIVAQRAAGGRH---SPQRQEEVMA-LLRQLGIAhlaMSYLDQ----L 142
Cdd:COG1129 321 PRDAIRAGIAYVPedrKGE--GLVLDlsIRENITLASLDRLSRGgllDRRRERALAEeYIKRLRIK---TPSPEQpvgnL 395
|
170 180
....*....|....*....|....*.
gi 488981874 143 SGGQKQLVGLAQSLIRQPRLLLLDEP 168
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEP 421
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-230 |
1.52e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 33 PRGKITALLGPNGSGKSTLMRAMAGLGPC--------------RGELLLEGENLLTQPFSRRAEQVVYlpQTLPAGVHLH 98
Cdd:NF033858 290 RRGEIFGFLGSNGCGKSTTMKMLTGLLPAsegeawlfgqpvdaGDIATRRRVGYMSQAFSLYGELTVR--QNLELHARLF 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 99 VLESIIVAQRaaggrhspqrqeeVMALLRQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLS-----ALD 173
Cdd:NF033858 368 HLPAAEIAAR-------------VAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSgvdpvARD 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 174 lnyQF--HVMDLVRRETrrrniVTLVV-VHDINIALRhADHVLMLKAGQLLGDGTPAAVI 230
Cdd:NF033858 435 ---MFwrLLIELSREDG-----VTIFIsTHFMNEAER-CDRISLMHAGRVLASDTPAALV 485
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-57 |
2.28e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.55 E-value: 2.28e-04
10 20 30
....*....|....*....|....*....|....*..
gi 488981874 21 RKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAG 57
Cdd:CHL00131 20 NEILKGLNL-SINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
140-233 |
2.32e-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: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 140 DQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVRRETRRRNIVTlvVVHDINIALrHADHVLMLKAGQ 219
Cdd:cd03288 155 ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVT--IAHRVSTIL-DADLVLVLSRGI 231
|
90
....*....|....
gi 488981874 220 LLGDGTPAAVITPE 233
Cdd:cd03288 232 LVECDTPENLLAQE 245
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
126-173 |
3.04e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.86 E-value: 3.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488981874 126 LRQLGIAhlAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALD 173
Cdd:PRK11147 143 LAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
116-236 |
3.32e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 116 PQRQEEVMALLrQLGIAHLAMSY-LDQLSGGQKQLVGLAQSLI---RQPRLLLLDEPLSAL---DLNYQFHVMDLVrreT 188
Cdd:PRK00635 784 PSIHEKIHALC-SLGLDYLPLGRpLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLhthDIKALIYVLQSL---T 859
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488981874 189 RRRNIVtLVVVHDINIaLRHADHVLML------KAGQLLGDGTPAAVI---TPETLA 236
Cdd:PRK00635 860 HQGHTV-VIIEHNMHV-VKVADYVLELgpeggnLGGYLLASCSPEELIhlhTPTAKA 914
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
31-58 |
4.10e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.58 E-value: 4.10e-04
10 20
....*....|....*....|....*...
gi 488981874 31 HLPRGKITALLGPNGSGKSTLMRAMAGL 58
Cdd:pfam13555 18 PIDPRGNTLLTGPSGSGKSTLLDAIQTL 45
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
6-55 |
6.51e-04 |
|
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: 40.37 E-value: 6.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488981874 6 LSGLSLSHFsagypRRkvIENLTVPhlPRGKITALLGPNGSGKSTLMRAM 55
Cdd:COG3593 3 LEKIKIKNF-----RS--IKDLSIE--LSDDLTVLVGENNSGKSSILEAL 43
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
22-54 |
7.09e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.30 E-value: 7.09e-04
10 20 30
....*....|....*....|....*....|...
gi 488981874 22 KVIENLTVPhLPRgkITALLGPNGSGKSTLMRA 54
Cdd:COG4637 11 KSLRDLELP-LGP--LTVLIGANGSGKSNLLDA 40
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
37-58 |
9.00e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 9.00e-04
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
141-223 |
9.40e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.30 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 141 QLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLVrRETRRRNIVTLVVVHDINIALRHADHVLMLKAGQL 220
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLI-NQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
...
gi 488981874 221 LGD 223
Cdd:PRK13549 484 KGD 486
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
142-184 |
1.36e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 1.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 488981874 142 LSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLNYQFHVMDLV 184
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLI 434
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
34-173 |
1.56e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.55 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 34 RGKITALLGPNGSGKSTLMRAMAGlgpcrgelllegenlLTQPFSRRAE-----QVVYLPQtlpagvHLHVL--ESIIVA 106
Cdd:PRK11147 344 RGDKIALIGPNGCGKTTLLKLMLG---------------QLQADSGRIHcgtklEVAYFDQ------HRAELdpEKTVMD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 107 QRAAGgrhspqrQEEVMAllrqLGIAHLAMSYLDQ--------------LSGGQKQLVGLAQSLIRQPRLLLLDEPLSAL 172
Cdd:PRK11147 403 NLAEG-------KQEVMV----NGRPRHVLGYLQDflfhpkramtpvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
.
gi 488981874 173 D 173
Cdd:PRK11147 472 D 472
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
36-186 |
1.67e-03 |
|
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: 38.44 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 36 KITALLGPNGSGKSTLMRAMaglgpcrgelllegenlltqpfsrraeQVVYlpqtlpaGVHLHVLESIIVAQRAAGGRHS 115
Cdd:cd03239 23 SFNAIVGPNGSGKSNIVDAI---------------------------CFVL-------GGKAAKLRRGSLLFLAGGGVKA 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488981874 116 PQRQEEVMALLRQlGIAHLAMSYLDQ-LSGGQKQLVGLA-----QSLIRQPrLLLLDEPLSALDLNYQFHVMDLVRR 186
Cdd:cd03239 69 GINSASVEITFDK-SYFLVLQGKVEQiLSGGEKSLSALAlifalQEIKPSP-FYVLDEIDAALDPTNRRRVSDMIKE 143
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
35-175 |
1.82e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 38.62 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 35 GKITALLGPNGSGKSTLMRAMAGLGPCRGELLLEG----ENLLTQPfSRRAEQVVYL----PQTLPAGVHLHVLESIIVA 106
Cdd:PRK09580 27 GEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEfkgkDLLELSP-EDRAGEGIFMafqyPVEIPGVSNQFFLQTALNA 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488981874 107 QRAAGGRHSPQR------QEEVMALLrQLGIAHLAMSYLDQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLN 175
Cdd:PRK09580 106 VRSYRGQEPLDRfdfqdlMEEKIALL-KMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDID 179
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
139-187 |
2.02e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 38.82 E-value: 2.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 488981874 139 LDQLSGGQKQLVGLaqSLI------RQPRLLLLDEPLSALDLNYQFHVMDLVRRE 187
Cdd:cd03273 164 LTELSGGQRSLVAL--SLIlalllfKPAPMYILDEVDAALDLSHTQNIGRMIKTH 216
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
24-55 |
2.92e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 38.95 E-value: 2.92e-03
10 20 30
....*....|....*....|....*....|..
gi 488981874 24 IENLTVPHLPRGKITALLGPNGSGKSTLMRAM 55
Cdd:COG5192 58 MVDRTPKDLPPPFIVAVVGPPGTGKSTLIRSL 89
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
141-175 |
3.01e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 3.01e-03
10 20 30
....*....|....*....|....*....|....*
gi 488981874 141 QLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLN 175
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLH 378
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
9-56 |
3.36e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 37.68 E-value: 3.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488981874 9 LSLSHFSaGYPRRKVIEnltvphLPRGkITALLGPNGSGKSTLMRAMA 56
Cdd:COG0419 5 LRLENFR-SYRDTETID------FDDG-LNLIVGPNGAGKSTILEAIR 44
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
37-55 |
3.44e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.48 E-value: 3.44e-03
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-57 |
3.67e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.33 E-value: 3.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488981874 9 LSLSHFSAGYPRRKVIENLTVpHLPRGKITALLGPNGSGKSTLMRAMAG 57
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNL-LLEAGERLAIIGENGVGKTTLLRTLVG 367
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
125-175 |
4.55e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 37.95 E-value: 4.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 488981874 125 LLRQLGIA---HLA-MSyldQLSGGQKQLVGLAQSLIRQPRLLLLDEPLSALDLN 175
Cdd:PRK15064 138 LLLGVGIPeeqHYGlMS---EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIN 189
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
35-58 |
4.79e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 37.72 E-value: 4.79e-03
10 20
....*....|....*....|....
gi 488981874 35 GKITALLGPNGSGKSTLMRAMAGL 58
Cdd:COG1106 29 LRVNLIYGANASGKSNLLEALYFL 52
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
33-56 |
5.19e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 37.97 E-value: 5.19e-03
10 20
....*....|....*....|....
gi 488981874 33 PRGKITALLGPNGSGKSTLMRAMA 56
Cdd:COG4913 22 FDGRGTLLTGDNGSGKSTLLDAIQ 45
|
|
| PrkA |
COG2766 |
Predicted Ser/Thr protein kinase [Signal transduction mechanisms]; |
11-58 |
5.20e-03 |
|
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
Pssm-ID: 442049 [Multi-domain] Cd Length: 675 Bit Score: 37.89 E-value: 5.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488981874 11 LSHFSAGYPRRKvienltvphlprgKITALLGPNGSGKSTLMRA-MAGL 58
Cdd:COG2766 97 LRSAARGLGERK-------------RILLLHGPVGSGKSTLARClKRGL 132
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
120-186 |
6.11e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 37.24 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 120 EEVMALLRQLG--------------IAHLAMSYLD------QLSGGQKQLVGLAQSLIRQ-----PrLLLLDEPLSALDL 174
Cdd:cd03272 117 NDVMNLLESAGfsrsnpyyivpqgkINSLTNMKQDeqqemqQLSGGQKSLVALALIFAIQkcdpaP-FYLFDEIDAALDA 195
|
90
....*....|..
gi 488981874 175 NYQFHVMDLVRR 186
Cdd:cd03272 196 QYRTAVANMIKE 207
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-220 |
8.02e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 37.26 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 26 NLTvphLPRGKITALLGPNGSGKSTLMRAMAGLgpcrgelllegenllTQPFSRRaeqvVYL---PQTLPAGVHLHVLES 102
Cdd:PRK10522 343 NLT---IKRGELLFLIGGNGSGKSTLAMLLTGL---------------YQPQSGE----ILLdgkPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981874 103 IIVA-----QRAAGGRHSPQRQEEVMALLRQLGIAHlAMSYLD------QLSGGQKQLVGLAQSLIRQPRLLLLDEplSA 171
Cdd:PRK10522 401 AVFTdfhlfDQLLGPEGKPANPALVEKWLERLKMAH-KLELEDgrisnlKLSKGQKKRLALLLALAEERDILLLDE--WA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488981874 172 LDLNYQFhvmdlvRRE--------TRRRNIVTLVVVHDiNIALRHADHVLMLKAGQL 220
Cdd:PRK10522 478 ADQDPHF------RREfyqvllplLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
30-57 |
8.89e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 36.72 E-value: 8.89e-03
10 20
....*....|....*....|....*...
gi 488981874 30 PHLpRGKITALLGPNGSGKSTLMRAMAG 57
Cdd:PRK00098 160 PLL-AGKVTVLAGQSGVGKSTLLNALAP 186
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
37-60 |
9.51e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 36.67 E-value: 9.51e-03
10 20
....*....|....*....|....*..
gi 488981874 37 ITALLGPNGSGKSTLMRAMA---GLGP 60
Cdd:COG3910 39 VTFFVGENGSGKSTLLEAIAvaaGFNP 65
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
117-173 |
9.56e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 36.91 E-value: 9.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488981874 117 QRQEEVMALLRQLGIAHLAMSYLDQ----LSGGQKQLVGLAQSLIRQPRLLLLDEPLSALD 173
Cdd:PRK10762 367 KHADEQQAVSDFIRLFNIKTPSMEQaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| |
