|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-252 |
1.20e-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: 253.04 E-value: 1.20e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEKVVFL 82
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSL-SLPPGEVTALLGPNGSGKSTLLRALAGLLKpSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQSLPQSLPqgvhLQVLESVVVA----QRASGAGQNQAQAIAL--LEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRP 156
Cdd:COG1120 81 PQEPPAPFG----LTVRELVALGryphLGLFGRPSAEDREAVEeaLERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 157 ALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESLAQVYG 236
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYG 236
|
250
....*....|....*..
gi 545166817 237 VRGRVERCA-QGRSMVI 252
Cdd:COG1120 237 VEARVIEDPvTGRPLVL 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-220 |
1.31e-64 |
|
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: 199.20 E-value: 1.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 5 TINALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEKVVFLP 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLS-IEAGEIVGILGPNGAGKSTLLKTLAGLLKpSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 84 QSLpqslpqgvhlqvlesvvvaqrasgagqnqaqaiallEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDE 163
Cdd:cd03214 80 QAL------------------------------------ELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 164 PLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSG 220
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-243 |
1.91e-57 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 183.78 E-value: 1.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNEENLLSLPFARRAEKVVFL 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSL-TLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQSLPQSLPqgvhLQVLEsvVVA----QRASGAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLI----- 153
Cdd:COG4559 81 PQHSSLAFP----FTVEE--VVAlgraPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwep 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 154 --RRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVtLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESL 231
Cdd:COG4559 155 vdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGV-VAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELL 233
|
250
....*....|..
gi 545166817 232 AQVYGVRGRVER 243
Cdd:COG4559 234 ERVYGADLRVLA 245
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-241 |
3.08e-53 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 173.03 E-value: 3.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNEENLLSLPFARRAEKVVFL 82
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSL-TLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQSLPQSLPQGVhlqvlESVVVAQRASGAGQNQAQAIAL---LEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIR----- 154
Cdd:PRK13548 82 PQHSSLSFPFTV-----EEVVAMGRAPHGLSRAEDDALVaaaLAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 155 -RPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESLAQ 233
Cdd:PRK13548 157 gPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRR 236
|
....*...
gi 545166817 234 VYGVRGRV 241
Cdd:PRK13548 237 VYGADVLV 244
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-253 |
1.70e-51 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 168.65 E-value: 1.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEKVVFL 82
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLS-LPTGKITALIGPNGCGKSTLLKCFARLLTpQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQSLPqsLPQGVHLQVLesvvVAQRASG--------AGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIR 154
Cdd:PRK11231 82 PQHHL--TPEGITVREL----VAYGRSPwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 155 RPALLLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESLAQV 234
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLM-RELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTV 234
|
250 260
....*....|....*....|
gi 545166817 235 YGVRGRVER-CAQGRSMVIV 253
Cdd:PRK11231 235 FDVEAEIHPePVSGTPMCVV 254
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-241 |
3.16e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 162.18 E-value: 3.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSGLTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAwlneeNLLSLPFARRAEKV 79
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSL-TIPPGEFVAIVGPNGAGKSTLLKAILGLLPpTSGTV-----RLFGKPPRRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 80 VFLPQ--SLPQSLPqgvhLQVLEsVVVAQRASGAG-------QNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQ 150
Cdd:COG1121 78 GYVPQraEVDWDFP----ITVRD-VVLMGRYGRRGlfrrpsrADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 151 SLIRRPALLLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGkLIDSGDPQTVIHAES 230
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELL-RELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPEN 230
|
250
....*....|.
gi 545166817 231 LAQVYGVRGRV 241
Cdd:COG1121 231 LSRAYGGPVAL 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-220 |
9.35e-46 |
|
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: 152.29 E-value: 9.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEKVVFl 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSL-TVEPGEFLALLGPSGCGKTTLLRLIAGLERpDSGEILIDGRDVTGVPPERRNIGMVF- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 pqslpQSLPQGVHLQVLESVVVA--QRASGAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLL 160
Cdd:cd03259 79 -----QDYALFPHLTVAENIAFGlkLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 161 LDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSG 220
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-235 |
1.66e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 147.13 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAeKVVFL 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSL-TVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPtSGEVRVLGEDVARDPAEVRR-RIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQSLpqSLPQgvHLQVLESVVVAQRASGAGQNQAQAIA--LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLL 160
Cdd:COG1131 79 PQEP--ALYP--DLTVRENLRFFARLYGLPRKEARERIdeLLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545166817 161 LDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIhAESLAQVY 235
Cdd:COG1131 155 LDEPTSGLDPEARRELWELL-RELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK-ARLLEDVF 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-220 |
1.08e-41 |
|
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: 141.90 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 6 INALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAwlneeNLLSLPFARRAEKVVFLPQ 84
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSF-EVKPGEFLAIVGPNGAGKSTLLKAILGLLKpTSGSI-----RVFGKPLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 85 SLpqSLPQGVHLQVLESVV---VAQRASGAGQNQAQ---AIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPAL 158
Cdd:cd03235 76 RR--SIDRDFPISVRDVVLmglYGHKGLFRRLSKADkakVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545166817 159 LLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKeGKLIDSG 220
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELL-RELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-250 |
1.76e-41 |
|
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: 148.51 E-value: 1.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGY--GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLN----RASGEAWLNEENLLSLPFARRAE 77
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSL-TIAPGETVALVGESGSGKSTLALALMGLLphggRISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 78 KVVFLPQSLPQSL-PQGVHLQVLEsVVVAQRASGAgQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRP 156
Cdd:COG1123 84 RIGMVFQDPMTQLnPVTVGDQIAE-ALENLGLSRA-EARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 157 ALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHA-ESLAQVY 235
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAApQALAAVP 241
|
250
....*....|....*
gi 545166817 236 GVRGRVERCAQGRSM 250
Cdd:COG1123 242 RLGAARGRAAPAAAA 256
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-238 |
4.35e-41 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 142.05 E-value: 4.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 9 LCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENLLSLPFARRAEKVVFLPQSlp 87
Cdd:PRK10253 13 LTLGYGKYTVAENLTVE-IPDGHFTAIIGPNGCGKSTLLRTLSRLmTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 88 QSLPQGVHLQVL--------ESVVVAQRAsgagQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALL 159
Cdd:PRK10253 90 ATTPGDITVQELvargryphQPLFTRWRK----EDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 160 LLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESLAQVYGVR 238
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLR 244
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-236 |
1.26e-40 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 140.19 E-value: 1.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGY-GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAE---K 78
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSL-EIERGEFVALIGPSGAGKSTLLRCLNGLVEPtSGEILVDGQDVTALRGRALRRlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 79 VVFLPQSLPqsLPQgvHLQVLESVVVAQ--RASG--------AGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGL 148
Cdd:COG3638 82 IGMIFQQFN--LVP--RLSVLTNVLAGRlgRTSTwrsllglfPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 149 AQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTViHA 228
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL-TD 236
|
....*...
gi 545166817 229 ESLAQVYG 236
Cdd:COG3638 237 AVLREIYG 244
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-215 |
1.41e-40 |
|
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: 138.75 E-value: 1.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKVVFLPQSlPQSlpQ 92
Cdd:cd03225 12 GARPALDDISL-TIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPtSGEVLVDGKDLTKLSLKELRRKVGLVFQN-PDD--Q 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 93 GVHLQVLESVVVAQRASGAGQNQAQAIA--LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDL 170
Cdd:cd03225 88 FFGPTVEEEVAFGLENLGLPEEEIEERVeeALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 545166817 171 NYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGK 215
Cdd:cd03225 168 AGRRELLELL-KKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-225 |
1.46e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 142.93 E-value: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSGLTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKV 79
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSL-SIEPGEFVALLGPSGCGKTTLLRMIAGFETPdSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 80 VFlpqslpQSL---PqgvHLQVLESVVVAQRASGAGQNQAQAIA--LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIR 154
Cdd:COG3842 82 VF------QDYalfP---HLTVAENVAFGLRMRGVPKAEIRARVaeLLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 155 RPALLLLDEPLSALDLNyqfhvmdvvSRET---------RRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:COG3842 153 EPRVLLLDEPLSALDAK---------LREEmreelrrlqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-231 |
4.80e-40 |
|
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: 138.23 E-value: 4.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGY-GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKVVF 81
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSL-SIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPtSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 82 LPQSlPQSlpqgvhlQVLESVV---VAQ--RASGAGQNQAQAIA--LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIR 154
Cdd:COG1122 80 VFQN-PDD-------QLFAPTVeedVAFgpENLGLPREEIRERVeeALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 155 RPALLLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESL 231
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELL-KRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
12-216 |
1.38e-39 |
|
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: 136.47 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 12 GYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFAR----RAEKVVFLPQS- 85
Cdd:cd03255 13 GGEKVQALKGVSLS-IEKGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVRVDGTDISKLSEKElaafRRRHIGFVFQSf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 86 --LPqslpqgvHLQVLESVVVAQRASGAGQNQA--QAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLL 161
Cdd:cd03255 92 nlLP-------DLTALENVELPLLLAGVPKKERreRAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545166817 162 DEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIAlRHAAQVIMLKEGKL 216
Cdd:cd03255 165 DEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
12-218 |
2.38e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 133.63 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 12 GYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRA----EKVVFLPQS- 85
Cdd:COG1136 17 GEGEVTALRGVSLS-IEAGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVLIDGQDISSLSERELArlrrRHIGFVFQFf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 86 --LPqslpqgvHLQVLESVVVAQRASG--AGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLL 161
Cdd:COG1136 96 nlLP-------ELTALENVALPLLLAGvsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 162 DEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIAlRHAAQVIMLKEGKLID 218
Cdd:COG1136 169 DEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVS 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-211 |
1.35e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 131.06 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 3 GLTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLN----RASGEAWLNEENLLSLPFARRaeK 78
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSL-TVAPGEILTLMGPSGSGKSTLLAAIAGTLspafSASGEVLLNGRRLTALPAEQR--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 79 VVFLPQSlPQSLPqgvHLQVLESVVVAQRASGAGQN-QAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPA 157
Cdd:COG4136 78 IGILFQD-DLLFP---HLSVGENLAFALPPTIGRAQrRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 545166817 158 LLLLDEPLSALD--LNYQFHvmDVVSRETRRRNMVTLVVLHDINIALRhAAQVIML 211
Cdd:COG4136 154 ALLLDEPFSKLDaaLRAQFR--EFVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDL 206
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-248 |
1.62e-37 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 132.13 E-value: 1.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 5 TINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKVVFLP 83
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSL-TIPKGGITALIGPNGAGKSTLLSMISRLLPPdSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 84 QSL-----------------PQSlpQGvHLQVLESVVVAQrasgagqnqaqAIALLEELGIAHlamNYLDSLSGGQKQLV 146
Cdd:COG4604 82 QENhinsrltvrelvafgrfPYS--KG-RLTAEDREIIDE-----------AIAYLDLEDLAD---RYLDELSGGQRQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 147 GLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVI 226
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
|
250 260
....*....|....*....|..
gi 545166817 227 HAESLAQVYGVRGRVERCAQGR 248
Cdd:COG4604 225 TPEVLSDIYDTDIEVEEIDGKR 246
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-220 |
3.62e-37 |
|
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: 130.70 E-value: 3.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 12 GYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLP---FARRAEKVVFLPQ--- 84
Cdd:cd03257 14 GGGSVKALDDVSF-SIKKGETLGLVGESGSGKSTLARAILGLLKpTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQdpm 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 85 -SLPQSLPQGVhlQVLESVVVAQRASGAGQNQAQAIALLEELGIAHLAMN-YLDSLSGGQKQLVGLAQSLIRRPALLLLD 162
Cdd:cd03257 93 sSLNPRMTIGE--QIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNrYPHELSGGQRQRVAIARALALNPKLLIAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 545166817 163 EPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSG 220
Cdd:cd03257 171 EPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
14-214 |
3.77e-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: 131.37 E-value: 3.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRAS-GEAWLNEENLLSlPFARRAekVVFlpQSlPQSLPq 92
Cdd:COG1116 22 GGVTALDDVSL-TVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTsGEVLVDGKPVTG-PGPDRG--VVF--QE-PALLP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 93 gvHLQVLESVVVAQRASGAGQNQAQAIA--LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALD- 169
Cdd:COG1116 94 --WLTVLDNVALGLELRGVPKAERRERAreLLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDa 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545166817 170 ---LNYQFHVMDVVsretRRRNMVTLVVLHDINIALRHAAQVIMLKEG 214
Cdd:COG1116 172 ltrERLQDELLRLW----QETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-253 |
4.31e-37 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 131.87 E-value: 4.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAGL---------NRASGEAWLNEENLLSLPFAR 74
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEP-GRVTALLGRNGAGKSTLLKALAGDltgggaprgARVTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 75 RAEKVVFLPQSLPQSLPQGVHLQVLESVVVAQRASGAGQNQAQAIA--LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSL 152
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAwqALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 153 ---------IRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQ 223
Cdd:PRK13547 161 aqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250 260 270
....*....|....*....|....*....|
gi 545166817 224 TVIHAESLAQVYGVRGRVERCAQGRSMVIV 253
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRLVDAGDGVPPVIV 270
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-216 |
4.95e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.55 E-value: 4.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFA--RRaeKVV 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSL-TLEAGECVAITGPSGSGKSTLLRALADLDPpTSGEIYLDGKPLSAMPPPewRR--QVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 81 FLPQSlPQSLPQGV--HLQVlesvvvAQRASGAGQNQAQAIALLEELGIAHLAMNY-LDSLSGGQKQLVGLAQSLIRRPA 157
Cdd:COG4619 78 YVPQE-PALWGGTVrdNLPF------PFQLRERKFDRERALELLERLGLPPDILDKpVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 158 LLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKL 216
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
28-235 |
5.42e-37 |
|
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: 130.77 E-value: 5.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 28 PRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPF-----ARRAEKVVFlpqslpQSLPQGVHLQVLES 101
Cdd:cd03256 25 NPGEFVALIGPSGAGKSTLLRCLNGLVEpTSGSVLIDGTDINKLKGkalrqLRRQIGMIF------QQFNLIERLSVLEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 102 VVV---AQRASGAG-------QNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLN 171
Cdd:cd03256 99 VLSgrlGRRSTWRSlfglfpkEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545166817 172 YQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTvIHAESLAQVY 235
Cdd:cd03256 179 SSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVLDEIY 241
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-237 |
5.78e-37 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 131.45 E-value: 5.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 16 RRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRAS-GEAWLNEENLLSLPFARRAEKVVFLPQSLPQSlpQGv 94
Cdd:PRK10575 24 RTLLHPLSL-TFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSeGEILLDAQPLESWSSKAFARKVAYLPQQLPAA--EG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 95 hLQVLESVVVAQ--------RASGAGQNQA-QAIALLeelGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPL 165
Cdd:PRK10575 100 -MTVRELVAIGRypwhgalgRFGAADREKVeEAISLV---GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545166817 166 SALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESLAQVYGV 237
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGI 247
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-216 |
6.29e-37 |
|
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: 128.28 E-value: 6.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRaEKVVFL 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISL-TVEKGEIYGLLGPNGAGKTTLIKIILGLLKPdSGEIKVLGKDIKKEPEEVK-RRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQSLpqSLPQgvHLQVLEsvvvaqrasgagqnqaqaialleelgiahlamnYLDsLSGGQKQLVGLAQSLIRRPALLLLD 162
Cdd:cd03230 79 PEEP--SLYE--NLTVRE---------------------------------NLK-LSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545166817 163 EPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKL 216
Cdd:cd03230 121 EPTSGLDPESRREFWELL-RELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-239 |
2.39e-36 |
|
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: 131.76 E-value: 2.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRAS-------GEAWLNEENLLSLPFARRAEKVVFLPQSLpqsLPqgvHLQV 98
Cdd:COG4148 21 TLPGRGVTALFGPSGSGKTTLLRAIAGLERPDsgrirlgGEVLQDSARGIFLPPHRRRIGYVFQEARL---FP---HLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 99 LESVVVAQRASGAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMD 178
Cdd:COG4148 95 RGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545166817 179 VVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESLAQVYGVRG 239
Cdd:COG4148 175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEE 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-169 |
3.20e-36 |
|
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: 127.60 E-value: 3.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRAS-GEAWLNEENLLSLPFARRAEkVVFL 82
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSF-TLAAGEALALTGPNGSGKTTLLRILAGLLPPSaGEVLWNGEPIRDAREDYRRR-LAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQSLpqslpqGVH--LQVLESVVVAQRASGAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLL 160
Cdd:COG4133 81 GHAD------GLKpeLTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
....*....
gi 545166817 161 LDEPLSALD 169
Cdd:COG4133 155 LDEPFTALD 163
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
9-220 |
1.04e-35 |
|
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: 126.64 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 9 LCAGYGKRRIIEHLSISTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-------SGEAWLNEENLLSLPFARRAEKVVF 81
Cdd:cd03297 2 LCVDIEKRLPDFTLKIDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPdggtivlNGTVLFDSRKKINLPPQQRKIGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 82 LPQSLpqsLPqgvHLQVLESVVVAQRASGAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLL 161
Cdd:cd03297 82 QQYAL---FP---HLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 162 DEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSG 220
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-226 |
1.05e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 127.03 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRA--EKV- 79
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISL-DVEKGEVVVIIGPSGSGKSTLLRCINLLEEPdSGTITVDGEDLTDSKKDINKlrRKVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 80 -VFlpqslpQSL---PqgvHLQVLESVVVAQR-ASGAGQNQAQAIA--LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSL 152
Cdd:COG1126 81 mVF------QQFnlfP---HLTVLENVTLAPIkVKKMSKAEAEERAmeLLERVGLADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 153 IRRPALLLLDEPLSALD-------LNyqfhVMdvvsRETRRRNMVTLVVLHDINIAlRHAA-QVIMLKEGKLIDSGDPQT 224
Cdd:COG1126 152 AMEPKVMLFDEPTSALDpelvgevLD----VM----RDLAKEGMTMVVVTHEMGFA-REVAdRVVFMDGGRIVEEGPPEE 222
|
..
gi 545166817 225 VI 226
Cdd:COG1126 223 FF 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
29-254 |
1.52e-35 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 126.88 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAGLNRASGEAWLNEENLLSLPFARRAEKVVFLPQslpQSLPQGVhLQVLESVVVAQRA 108
Cdd:COG4138 21 AGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAELARHRAYLSQ---QQSPPFA-MPVFQYLALHQPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 109 SGAGQNQAQAIA-LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIR-------RPALLLLDEPLSALDLNYQFhVMDVV 180
Cdd:COG4138 97 GASSEAVEQLLAqLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQA-ALDRL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545166817 181 SRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESLAQVYGVRGRVERcAQGRSMVIVD 254
Cdd:COG4138 176 LRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLE-VEGHRWLIPT 248
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-227 |
1.92e-35 |
|
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: 126.05 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRR----IIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEEnllslPFARRAEK 78
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLS-VEEGEFVALVGPSGCGKSTLLRIIAGLERPtSGEVLVDGE-----PVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 79 VVFLPQSlPQSLPqgvHLQVLESVVVAQRASGAGQNQAQAIA--LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRP 156
Cdd:cd03293 75 RGYVFQQ-DALLP---WLTVLDNVALGLELQGVPKAEARERAeeLLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545166817 157 ALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLkegklidSGDPQTVIH 227
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL-------SARPGRIVA 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-225 |
4.62e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 128.34 E-value: 4.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSgLTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLS-LPFARRaeK 78
Cdd:COG1118 1 MS-IEVRNISKRFGSFTLLDDVSL-EIASGELVALLGPSGSGKTTLLRIIAGLETPdSGRIVLNGRDLFTnLPPRER--R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 79 VVFLPQS---LPqslpqgvHLQVLESVVVAQRASGAGQNQAQAIA--LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLI 153
Cdd:COG1118 77 VGFVFQHyalFP-------HMTVAENIAFGLRVRPPSKAEIRARVeeLLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 154 RRPALLLLDEPLSALDlnyqFHVmdvvsRETRRRNM---------VTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQT 224
Cdd:COG1118 150 VEPEVLLLDEPFGALD----AKV-----RKELRRWLrrlhdelggTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDE 220
|
.
gi 545166817 225 V 225
Cdd:COG1118 221 V 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-215 |
8.62e-35 |
|
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: 122.35 E-value: 8.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 5 TINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEKVVFLP 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSL-TLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 84 QslpqslpqgvhlqvlesvvvaqrasgagqnqaqaialleelgiahlamnyldsLSGGQKQLVGLAQSLIRRPALLLLDE 163
Cdd:cd00267 80 Q-----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 545166817 164 PLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGK 215
Cdd:cd00267 107 PTSGLDPASRERLLELL-RELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-223 |
1.08e-34 |
|
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: 124.92 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGK----RRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEK 78
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSL-EVAPGESFGLVGESGSGKSTLLRALAGLERpWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 79 VVFLPQSLPQSL-PqgvHLQVLESVVVAQRASGAGQNQAQAIALLEELGI-AHLAMNYLDSLSGGQKQLVGLAQSLIRRP 156
Cdd:COG1124 81 VQMVFQDPYASLhP---RHTVDRILAEPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 157 ALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQ 223
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-225 |
3.61e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 123.26 E-value: 3.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSGLTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRAS-GEAWLNEENLLSLPFARRAEKV 79
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDL-DIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTsGEILIGGRDVTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 80 VFlpQS---LPqslpqgvHLQVLESVVVAQRASGAGQNQAQAI--ALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIR 154
Cdd:COG3839 80 VF--QSyalYP-------HMTVYENIAFPLKLRKVPKAEIDRRvrEAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 155 RPALLLLDEPLSALdlnyqfhvmDVVSRET---------RRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:COG3839 151 EPKVFLLDEPLSNL---------DAKLRVEmraeikrlhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-228 |
6.44e-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: 125.40 E-value: 6.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKR-----RIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAE 77
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSL-TLRRGETLGLVGESGSGKSTLARLLLGLLRPtSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 78 ---KVVFLPQ----SLPQSLPqgVHLQVLESVVVAQRASGAgQNQAQAIALLEELGI-AHLAMNYLDSLSGGQKQLVGLA 149
Cdd:COG1123 340 lrrRVQMVFQdpysSLNPRMT--VGDIIAEPLRLHGLLSRA-ERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 150 QSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHA 228
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-229 |
1.15e-32 |
|
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: 119.31 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEK---- 78
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSL-DVPRGEILAIIGGSGSGKSVLLKLIIGLLRPdSGEILVDGQDITGLSEKELYELrrri 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 79 -VVFlpQS--LPQSLPqgvhlqVLESVVVAQRA-SGAGQNQAQAIAL--LEELGIAHLAMNYLDSLSGGQKQLVGLAQSL 152
Cdd:COG1127 85 gMLF--QGgaLFDSLT------VFENVAFPLREhTDLSEAEIRELVLekLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 153 IRRPALLLLDEPLSALD------LNyqfhvmDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVI 226
Cdd:COG1127 157 ALDPEILLYDEPTAGLDpitsavID------ELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
...
gi 545166817 227 HAE 229
Cdd:COG1127 231 ASD 233
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-225 |
2.41e-32 |
|
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: 118.42 E-value: 2.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRaEKVVFLPQSLPqsLP 91
Cdd:COG4555 11 YGKVPALKDVSF-TAKDGEITGLLGPNGAGKTTLLRMLAGLLKPdSGSILIDGEDVRKEPREAR-RQIGVLPDERG--LY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 92 QgvHLQVLESVVVAQRASG-AGQNQAQAIA-LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:COG4555 87 D--RLTVRENIRYFAELYGlFDEELKKRIEeLIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 545166817 170 LNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:COG4555 165 VMARRLLREIL-RALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-224 |
3.70e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 117.55 E-value: 3.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKrriiEHLSIS-TLPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNEENLLSLPFARRAEKVVF 81
Cdd:COG3840 2 LRLDDLTYRYGD----FPLRFDlTIAAGERVAILGPSGAGKSTLLNLIAGfLPPDSGRILWNGQDLTALPPAERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 82 LPQSL-PqslpqgvHLQVLESVVVAQRAS---GAGQnQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPA 157
Cdd:COG3840 78 QENNLfP-------HLTVAQNIGLGLRPGlklTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 158 LLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQT 224
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-216 |
4.67e-32 |
|
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: 116.86 E-value: 4.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLS----LPFARRAEKVVFlpqslp 87
Cdd:cd03262 10 FGDFHVLKGIDL-TVKKGEVVVIIGPSGSGKSTLLRCINLLEEPdSGTIIIDGLKLTDdkknINELRQKVGMVF------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 88 QSLPQGVHLQVLESVVVAQR-ASGAGQNQAQAIA--LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEP 164
Cdd:cd03262 83 QQFNLFPHLTVLENITLAPIkVKGMSKAEAEERAleLLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 545166817 165 LSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKL 216
Cdd:cd03262 163 TSALDPELVGEVLDVM-KDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
29-236 |
8.90e-32 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 117.01 E-value: 8.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLL-----SLPFARRAEKVVFlpqslpQSLPQGVHLQVLESV 102
Cdd:TIGR02315 27 PGEFVAIIGPSGAGKSTLLRCINRLVEpSSGSILLEGTDITklrgkKLRKLRRRIGMIF------QHYNLIERLTVLENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 103 VVAQRASG----------AGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNY 172
Cdd:TIGR02315 101 LHGRLGYKptwrsllgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKT 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545166817 173 QFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTvIHAESLAQVYG 236
Cdd:TIGR02315 181 SKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSE-LDDEVLRHIYG 243
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-217 |
9.35e-32 |
|
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: 115.82 E-value: 9.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 5 TINALCAGYGK-RRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENllsLPFARRAEKVVFL 82
Cdd:cd03226 1 RIENISFSYKKgTEILDDLSLD-LYAGEIIALTGKNGAGKTTLAKILAGLIKeSSGSILLNGKP---IKAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQSLpqslpqGVHL---QVLESVVVAQRASGAGQNQAQAIalLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALL 159
Cdd:cd03226 77 MQDV------DYQLftdSVREELLLGLKELDAGNEQAETV--LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545166817 160 LLDEPLSALDLnyqfHVMDVVS---RETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLI 217
Cdd:cd03226 149 IFDEPTSGLDY----KNMERVGeliRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
13-243 |
1.13e-31 |
|
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: 117.11 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR--ASGEAWL-----NEENLLSLpfaRRaeKVVFLPQS 85
Cdd:COG1119 13 RGGKTILDDISW-TVKPGEHWAILGPNGAGKSTLLSLITGDLPptYGNDVRLfgerrGGEDVWEL---RK--RIGLVSPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 86 LPQSLPqgVHLQVLESVVvaqraSGA-----------GQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIR 154
Cdd:COG1119 87 LQLRFP--RDETVLDVVL-----SGFfdsiglyreptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 155 RPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESLAQV 234
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEA 239
|
....*....
gi 545166817 235 YGVRGRVER 243
Cdd:COG1119 240 FGLPVEVER 248
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-239 |
2.02e-31 |
|
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: 115.90 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 3 GLTINALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKVVF 81
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLD-IPSGELVALLGPSGSGKTTLLRLIAGLERPdSGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 82 LPQSLPQslpqgvHLQVLESVV-------VAQRASGAgQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIR 154
Cdd:cd03296 81 QHYALFR------HMTVFDNVAfglrvkpRSERPPEA-EIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 155 RPALLLLDEPLSALDLNyqfhvmdvVSRETRR--------RNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVI 226
Cdd:cd03296 154 EPKVLLLDEPFGALDAK--------VRKELRRwlrrlhdeLHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
250
....*....|...
gi 545166817 227 HAESLAQVYGVRG 239
Cdd:cd03296 226 DHPASPFVYSFLG 238
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-166 |
3.21e-31 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 112.74 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEKVVFLPQsLPQSLPqgvHLQVLESVVV 104
Cdd:pfam00005 7 TLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLDGQDLTDDERKSLRKEIGYVFQ-DPQLFP---RLTVRENLRL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545166817 105 AQRASGAGQN--QAQAIALLEELGIAHLA----MNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLS 166
Cdd:pfam00005 83 GLLLKGLSKRekDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-225 |
3.40e-31 |
|
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: 118.29 E-value: 3.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-------SGEAWLNEENLLSLPFARRAEKVVFLPQSLpqsLPqgvHLQV 98
Cdd:TIGR02142 19 TLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPdegeivlNGRTLFDSRKGIFLPPEKRRIGYVFQEARL---FP---HLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 99 LESVVVAQRASGAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMD 178
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545166817 179 VVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-215 |
3.56e-31 |
|
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: 113.44 E-value: 3.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEK---- 78
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLN-IEAGEIVALLGPSGSGKSTLLRCIAGLEEpDSGSILIDGEDLTDLEDELPPLRrrig 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 79 VVFlpQSlPQSLPqgvHLQVLESVVVAqrasgagqnqaqaialleelgiahlamnyldsLSGGQKQLVGLAQSLIRRPAL 158
Cdd:cd03229 80 MVF--QD-FALFP---HLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 159 LLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGK 215
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-227 |
8.26e-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: 114.46 E-value: 8.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKVV-- 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFS-VRPGEIHGLIGPNGAGKTTLFNLISGFLRPtSGSVLFDGEDITGLPPHEIARLGIgr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 81 -F-LPQSLPqslpqgvHLQVLESVVVAQRASGAG------------QNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLV 146
Cdd:cd03219 80 tFqIPRLFP-------ELTVLENVMVAAQARTGSglllararreerEARERAEELLERVGLADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 147 GLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVI 226
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELI-RELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
.
gi 545166817 227 H 227
Cdd:cd03219 232 N 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-223 |
1.03e-30 |
|
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: 114.14 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 6 INALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAE---KVVF 81
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDL-DVRRGEILAIIGPSGSGKSTLLRLIVGLLRPdSGEVLIDGEDISGLSEAELYRlrrRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 82 LPQS--LPQSlpqgvhLQVLESVVVAQRASGA-GQNQAQAIAL--LEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRP 156
Cdd:cd03261 82 LFQSgaLFDS------LTVFENVAFPLREHTRlSEEEIREIVLekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 157 ALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQ 223
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPE 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-226 |
1.04e-30 |
|
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: 113.97 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYG--KRRIIEhLSIStlpRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNEENLLSLPFARRaeKVV 80
Cdd:cd03299 1 LKVENLSKDWKefKLKNVS-LEVE---RGDYFVILGPTGSGKSVLLETIAGfIKPDSGKILLNGKDITNLPPEKR--DIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 81 FLPQS---LPqslpqgvHLQVLESVVVA--QRASGAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRR 155
Cdd:cd03299 75 YVPQNyalFP-------HMTVYKNIAYGlkKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545166817 156 PALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVI 226
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-220 |
1.45e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 113.22 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSL-----PFARRAEKVVF-----L 82
Cdd:COG2884 13 GGREALSDVSL-EIEKGEFVFLTGPSGAGKSTLLKLLYGEERPtSGQVLVNGQDLSRLkrreiPYLRRRIGVVFqdfrlL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PqslpqslpqgvHLQVLESVVVAQRASGAGQNQAQ--AIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLL 160
Cdd:COG2884 92 P-----------DRTVYENVALPLRVTGKSRKEIRrrVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 161 LDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSG 220
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELL-EEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-235 |
1.52e-30 |
|
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: 113.54 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSGLTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEK- 78
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSL-EVEEGEIVALLGRNGAGKTTLLKAISGLLPPrSGSIRFDGEDITGLPPHRIARLg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 79 VVFLPQSlpqslpQGV--HLQVLESVVVAQRASGAGQNQAQAIAL-------LEELgIAHLAMnyldSLSGGQKQLVGLA 149
Cdd:COG0410 80 IGYVPEG------RRIfpSLTVEENLLLGAYARRDRAEVRADLERvyelfprLKER-RRQRAG----TLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 150 QSLIRRPALLLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAE 229
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEII-RRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
|
....*.
gi 545166817 230 SLAQVY 235
Cdd:COG0410 228 EVREAY 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-225 |
1.85e-30 |
|
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: 113.04 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLN------RASGEAWLNEENLLSLPFA----RRAEKVVF- 81
Cdd:cd03260 10 YGDKHALKDISLD-IPKGEITALIGPSGCGKSTLLRLLNRLNdlipgaPDEGEVLLDGKDIYDLDVDvlelRRRVGMVFq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 82 LPQSLPQSlpqgvhlqVLESVVVAQRASGAGQNQAQAIALLEELGIAHLAMNYLD-----SLSGGQKQLVGLAQSLIRRP 156
Cdd:cd03260 89 KPNPFPGS--------IYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDrlhalGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545166817 157 ALLLLDEPLSALDlnyqfhvmdvvSRETR---------RRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:cd03260 161 EVLLLDEPTSALD-----------PISTAkieeliaelKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-235 |
3.31e-30 |
|
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: 112.64 E-value: 3.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEK-VVF 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLS-VKQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGKILLDGQDITKLPMHKRARLgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 82 LPQSlpQSLPQGvhLQVLE--SVVVAQRASGAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALL 159
Cdd:cd03218 80 LPQE--ASIFRK--LTVEEniLAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545166817 160 LLDEPLSALDlnyQFHVMDV--VSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESLAQVY 235
Cdd:cd03218 156 LLDEPFAGVD---PIAVQDIqkIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-224 |
3.38e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 115.59 E-value: 3.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 9 LCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENLLSLPFARRAEKVVF-----L 82
Cdd:PRK11432 12 ITKRFGSNTVIDNLNL-TIKQGTMVTLLGPSGCGKTTVLRLVAGLeKPTEGQIFIDGEDVTHRSIQQRDICMVFqsyalF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQ-SLPQSLPQGVHLQVLESVVVAQRASGAgqnqaqaialLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLL 161
Cdd:PRK11432 91 PHmSLGENVGYGLKMLGVPKEERKQRVKEA----------LELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545166817 162 DEPLSALDLNYQFHVMDVVsRETRRR-NMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQT 224
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKI-RELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-216 |
5.36e-30 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 112.85 E-value: 5.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRASGEAWLNEENLLSLpfARRAEKVVFLP 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLH-IPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE--AREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 84 QSLpqsLPQGvhlQVLESVVVAQRasgaGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDE 163
Cdd:PRK11247 90 ARL---LPWK---KVIDNVGLGLK----GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545166817 164 PLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKL 216
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-223 |
7.53e-30 |
|
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: 111.56 E-value: 7.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKVVFl 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSL-DIKEGEFFTLLGPSGCGKTTLLRLIAGFETPtSGEILLDGKDITNLPPHKRPVNTVF- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 pqslpQSLPQGVHLQVLESVVVAQRASGAGQN--QAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLL 160
Cdd:cd03300 79 -----QNYALFPHLTVFENIAFGLRLKKLPKAeiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545166817 161 LDEPLSALDLNYQFHvMDVVSRETRRRNMVTLV-VLHDINIALRHAAQVIMLKEGKLIDSGDPQ 223
Cdd:cd03300 154 LDEPLGALDLKLRKD-MQLELKRLQKELGITFVfVTHDQEEALTMSDRIAVMNKGKIQQIGTPE 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-210 |
3.29e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 108.86 E-value: 3.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 12 GYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAwlneenllslpFARRAEKVVFLPQ--SLPQ 88
Cdd:NF040873 1 GYGGRPVLHGVDL-TIPAGSLTAVVGPNGSGKSTLLKVLAGVLRpTSGTV-----------RRAGGARVAYVPQrsEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 89 SLPqgvhLQVLESVVVA--QRASGAG----QNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLD 162
Cdd:NF040873 69 SLP----LTVRDLVAMGrwARRGLWRrltrDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545166817 163 EPLSALDLNYQFHVMDVVSRETRRRNMVtLVVLHDINIALRHAAQVIM 210
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATV-VVVTHDLELVRRADPCVLL 191
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-231 |
5.75e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 110.34 E-value: 5.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSGLTINALCAGYGKRR----IIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSlPFARR 75
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGqpqpALQDVSL-TIESGEFVVALGASGCGKTTLLNLIAGFLApSSGEITLDGVPVTG-PGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 76 AekVVFLPQSLpqsLPQgvhLQVLESVVVAQRASG--AGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLI 153
Cdd:COG4525 79 G--VVFQKDAL---LPW---LNVLDNVAFGLRLRGvpKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 154 RRPALLLLDEPLSALDL----NYQFHVMDvVSRETRRrnMVtLVVLHDINIALRHAAQVIMLkegklidSGDPQTVIHAE 229
Cdd:COG4525 151 ADPRFLLMDEPFGALDAltreQMQELLLD-VWQRTGK--GV-FLITHSVEEALFLATRLVVM-------SPGPGRIVERL 219
|
..
gi 545166817 230 SL 231
Cdd:COG4525 220 EL 221
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-225 |
8.73e-29 |
|
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: 111.05 E-value: 8.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 35 LLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEKVVFlpqslpQSLPQGVHLQVLESVVVAQRASGAGQ 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQpDSGSIMLDGEDVTNVPPHLRHINMVF------QSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 114 NQAQAiALLEELGIAHL---AMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMV 190
Cdd:TIGR01187 75 AEIKP-RVLEALRLVQLeefADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGIT 153
|
170 180 190
....*....|....*....|....*....|....*
gi 545166817 191 TLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:TIGR01187 154 FVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-225 |
1.19e-28 |
|
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: 108.29 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEK-VVF 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSL-TVPEGEIVALLGRNGAGKTTLLKTIMGLLPPrSGSIRFDGRDITGLPPHERARAgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 82 LPQSlpqslpQGV--HLQVLESVVVAQRASGAGQNQA---QAIALLEELG--IAHLAmnylDSLSGGQKQLVGLAQSLIR 154
Cdd:cd03224 80 VPEG------RRIfpELTVEENLLLGAYARRRAKRKArleRVYELFPRLKerRKQLA----GTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545166817 155 RPALLLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAI-RELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
3.34e-28 |
|
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: 106.96 E-value: 3.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKVVFl 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNL-DIADGEFVVLLGPSGCGKTTTLRMIAGLEEPtSGRIYIGGRDVTDLPPKDRDIAMVF- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 pqslpQSLPQGVHLQVLESVVVAQRASGAGQN----QAQAIAllEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPAL 158
Cdd:cd03301 79 -----QNYALYPHMTVYDNIAFGLKLRKVPKDeideRVREVA--ELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 545166817 159 LLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKL 216
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-241 |
5.20e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 110.32 E-value: 5.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNEENLLSLPFARRAEKVVFL 82
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLS-VREGSLVGLVGPNGAGKTTLLRAINGtLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQSLPQSLPQGVHlQVLESVVVAQRASGAGQNQAQAIAL---LEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALL 159
Cdd:PRK09536 83 PQDTSLSFEFDVR-QVVEMGRTPHRSRFDTWTETDRAAVeraMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 160 LLDEPLSALDLNYQFHVMDVVSR--ETRRrnmVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESLAQVYGV 237
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRlvDDGK---TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDA 238
|
....
gi 545166817 238 RGRV 241
Cdd:PRK09536 239 RTAV 242
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-254 |
1.38e-27 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 106.17 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAGLNRASGEAWLNEENLLSLPFARRAEKVVFLPQS------------LPQSLPQGVHL 96
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqtppfampvfqyLTLHQPDKTRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 97 QVLESVV--VAQRasgagqnqaqaialleeLGIAHLAMNYLDSLSGGQKQLVGLAQSLIR-----RPA--LLLLDEPLSA 167
Cdd:PRK03695 101 EAVASALneVAEA-----------------LGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 168 LDLNyQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESLAQVYGV---RGRVErc 244
Cdd:PRK03695 164 LDVA-QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVnfrRLDVE-- 240
|
250
....*....|
gi 545166817 245 aqGRSMVIVD 254
Cdd:PRK03695 241 --GHPMLIST 248
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-235 |
1.47e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 105.88 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSGLTINALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEK- 78
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLE-VNQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGRIFLDGEDITHLPMHKRARLg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 79 VVFLPQ--------SLPQSLpqgvhLQVLEsvvvaQRASGAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQ 150
Cdd:COG1137 80 IGYLPQeasifrklTVEDNI-----LAVLE-----LRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 151 SLIRRPALLLLDEPLSALD-LNyqfhVMDV--VSRETRRRNMVTLVVLHDINIALR---HAAqvIMlKEGKLIDSGDPQT 224
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDpIA----VADIqkIIRHLKERGIGVLITDHNVRETLGicdRAY--II-SEGKVLAEGTPEE 222
|
250
....*....|.
gi 545166817 225 VIHAESLAQVY 235
Cdd:COG1137 223 ILNNPLVRKVY 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
13-220 |
1.88e-27 |
|
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: 104.97 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLSIsTLPRGeVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAeKVVFLPQSLPQSlp 91
Cdd:cd03264 10 YGKKRALDGVSL-TLGPG-MYGLLGPNGAGKTTLMRILATLTPPsSGTIRIDGQDVLKQPQKLRR-RIGYLPQEFGVY-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 92 qgVHLQVLESVVVAQRASG--AGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALd 169
Cdd:cd03264 85 --PNFTVREFLDYIAWLKGipSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 170 lnyqfhvmDVVSREtRRRNMVT------LVVL--HDINIALRHAAQVIMLKEGKLIDSG 220
Cdd:cd03264 162 --------DPEERI-RFRNLLSelgedrIVILstHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
13-225 |
2.21e-27 |
|
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: 105.89 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEK-VV--F-LPQSLP 87
Cdd:COG0411 14 FGGLVAVDDVSL-EVERGEIVGLIGPNGAGKTTLFNLITGFYRPtSGRILFDGRDITGLPPHRIARLgIArtFqNPRLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 88 qslpqgvHLQVLESVVVAQRASGAG-----------------QNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQ 150
Cdd:COG0411 93 -------ELTVLENVLVAAHARLGRgllaallrlprarreerEARERAEELLERVGLADRADEPAGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545166817 151 SLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
26-218 |
2.28e-27 |
|
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: 105.21 E-value: 2.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSL---PFAR-RAEKVVFLPQSLpQSLPqgvHLQVLE 100
Cdd:COG4181 34 EVEAGESVAIVGASGSGKSTLLGLLAGLDRPtSGTVRLAGQDLFALdedARARlRARHVGFVFQSF-QLLP---TLTALE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 101 SVVVAQRASGAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVV 180
Cdd:COG4181 110 NVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLL 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 545166817 181 sRETRRRNMVTLV-VLHDINIALRhAAQVIMLKEGKLID 218
Cdd:COG4181 190 -FELNRERGTTLVlVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-215 |
4.14e-27 |
|
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: 102.85 E-value: 4.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYG--KRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKVV 80
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSL-TIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPtSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 81 FLPQSlpqslpqgVHLQ---VLESVvvaqrasgagqnqaqaialleelgiahlamnyldsLSGGQKQLVGLAQSLIRRPA 157
Cdd:cd03228 80 YVPQD--------PFLFsgtIRENI-----------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 545166817 158 LLLLDEPLSALDLNYQFHVMDVVSRetRRRNMVTLVVLHDINiALRHAAQVIMLKEGK 215
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRA--LAKGKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
26-232 |
5.51e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 104.33 E-value: 5.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGE-----------AWLNEENLLSLpfaRRAEKVVFLPQSL-Pqslpq 92
Cdd:PRK11124 24 DCPQGETLVLLGPSGAGKSSLLRVLNLLEMPrSGTlniagnhfdfsKTPSDKAIREL---RRNVGMVFQQYNLwP----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 93 gvHLQVLESVVVAQ-RASGAGQNQA--QAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:PRK11124 96 --HLTVQQNLIEAPcRVLGLSKDQAlaRAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 170 LNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGD------PQTVIHAESLA 232
Cdd:PRK11124 174 PEITAQIVSII-RELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDascftqPQTEAFKNYLS 241
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-226 |
5.67e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 104.40 E-value: 5.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRASGEAWLNEENLLSLPFA-----RRAEKVVFlpqslp 87
Cdd:PRK09493 11 FGPTQVLHNIDL-NIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVderliRQEAGMVF------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 88 QSLPQGVHLQVLESVVVA-QRASGAGQNQA--QAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEP 164
Cdd:PRK09493 84 QQFYLFPHLTALENVMFGpLRVRGASKEEAekQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545166817 165 LSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVI 226
Cdd:PRK09493 164 TSALDPELRHEVLKVM-QDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-229 |
1.14e-26 |
|
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: 107.92 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 2 SGLTINALCAGYGKRR-IIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKV 79
Cdd:COG4988 335 PSIELEDVSFSYPGGRpALDGLSL-TIPPGERVALVGPSGAGKSTLLNLLLGFLPPySGSILINGVDLSDLDPASWRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 80 VFLPQSlpqslPQGVHLQVLESVVVAQR-ASgagqnQAQAIALLEELGIAHLAMNY---LDS--------LSGGQKQLVG 147
Cdd:COG4988 414 AWVPQN-----PYLFAGTIRENLRLGRPdAS-----DEELEAALEAAGLDEFVAALpdgLDTplgeggrgLSGGQAQRLA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 148 LAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRnmVTLVVLHDINiALRHAAQVIMLKEGKLIDSGDPQTVIH 227
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLA-LLAQADRILVLDDGRIVEQGTHEELLA 560
|
..
gi 545166817 228 AE 229
Cdd:COG4988 561 KN 562
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-232 |
1.61e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 103.17 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 3 GLTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGE-----------AWLNEENLLSL 70
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINL-ECPSGETLVLLGPSGAGKSSLLRVLNLLETPdSGQlniaghqfdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 71 pfaRRAEKVVFLPQSL-PqslpqgvHLQVLESVVVAQ-RASGAGQNQAQ--AIALLEELGIAHLAMNYLDSLSGGQKQLV 146
Cdd:COG4161 81 ---RQKVGMVFQQYNLwP-------HLTVMENLIEAPcKVLGLSKEQARekAMKLLARLRLTDKADRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 147 GLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGD----- 221
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEII-RELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDashft 229
|
250
....*....|..
gi 545166817 222 -PQTVIHAESLA 232
Cdd:COG4161 230 qPQTEAFAHYLS 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-228 |
3.90e-26 |
|
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: 106.31 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 16 RRIIEHL----SIS-TLPRGEVTVLLGPNGCGKSTLLRALAGLNRASGEAWLNEENLLSLPFA-----RRAEKVVFlpqs 85
Cdd:COG4172 293 RRTVGHVkavdGVSlTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRRalrplRRRMQVVF---- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 86 lpQ----SL-PQgvhLQVLESV----VVAQRASGAGQNQAQAIALLEELGIAHLAMN-YLDSLSGGQKQLVGLAQSLIRR 155
Cdd:COG4172 369 --QdpfgSLsPR---MTVGQIIaeglRVHGPGLSAAERRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILE 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545166817 156 PALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINI--ALRHaaQVIMLKEGKLIDSGDPQTVIHA 228
Cdd:COG4172 444 PKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVvrALAH--RVMVMKDGKVVEQGPTEQVFDA 516
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-225 |
5.22e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.53 E-value: 5.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEKVVFl 82
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSL-TIYKGEIFALLGASGCGKSTLLRMLAGFEQpTAGQIMLDGVDLSHVPPYQRPINMMF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 pqslpQSLPQGVHLQVLESVvvaqrASGAGQNQ---AQAIALLEE-LGIAHL---AMNYLDSLSGGQKQLVGLAQSLIRR 155
Cdd:PRK11607 98 -----QSYALFPHMTVEQNI-----AFGLKQDKlpkAEIASRVNEmLGLVHMqefAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545166817 156 PALLLLDEPLSALDLN----YQFHVMDVVSRETRRRNMVTlvvlHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK11607 168 PKLLLLDEPMGALDKKlrdrMQLEVVDILERVGVTCVMVT----HDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-220 |
6.04e-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: 101.03 E-value: 6.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKVVFLPQSLpqslpqGVHLQVLESVVV 104
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPqSGRVLINGVDVTAAPPADRPVSMLFQENNL------FAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 105 AqRASGAGQN--QAQAI-ALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVS 181
Cdd:cd03298 94 G-LSPGLKLTaeDRQAIeVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 545166817 182 RETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSG 220
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-220 |
7.60e-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: 100.43 E-value: 7.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEEnllSLPFARRaEKVVFL 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFS-VEKGEIFGLLGPNGAGKTTTIRMILGIILPdSGEVLFDGK---PLDIAAR-NRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQSlpqslpQGVH--LQVLESVVVAQRASGAGQNQAQAIA--LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPAL 158
Cdd:cd03269 76 PEE------RGLYpkMKVIDQLVYLAQLKGLKKEEARRRIdeWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545166817 159 LLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSG 220
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVI-RELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-227 |
7.77e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 103.96 E-value: 7.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSGLTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEKV 79
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINL-DIHEGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGDLFIGEKRMNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 80 VFlpqslpQSLPQGVHLQVLESVVVAQRASGAGQNQAQ----AIAllEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRR 155
Cdd:PRK11000 80 VF------QSYALYPHLSVAENMSFGLKLAGAKKEEINqrvnQVA--EVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545166817 156 PALLLLDEPLSALD--LNYQFHVMdvVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIH 227
Cdd:PRK11000 152 PSVFLLDEPLSNLDaaLRVQMRIE--ISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYH 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-225 |
8.55e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 103.62 E-value: 8.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSgLTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENLLSLPFARRAEKV 79
Cdd:PRK10851 1 MS-IEIANIKKSFGRTQVLNDISL-DIPSGQMVALLGPSGSGKTTLLRIIAGLeHQTSGHIRFHGTDVSRLHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 80 VFLPQSLPQslpqgvHLQVLESVVVA-------QRASGAGQNQaQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSL 152
Cdd:PRK10851 79 VFQHYALFR------HMTVFDNIAFGltvlprrERPNAAAIKA-KVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 153 IRRPALLLLDEPLSALDLNyqfhvmdvVSRETRR--RNM------VTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQT 224
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQ--------VRKELRRwlRQLheelkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQ 223
|
.
gi 545166817 225 V 225
Cdd:PRK10851 224 V 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-226 |
1.42e-25 |
|
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: 105.30 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 18 IIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPfarraekvvflPQSLPQSL---PQG 93
Cdd:COG2274 490 VLDNISL-TIKPGERVAIVGRSGSGKSTLLKLLLGLYEPtSGRILIDGIDLRQID-----------PASLRRQIgvvLQD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 94 VHLQ---VLESVVVAQrasgAGQNQAQAIALLEELG----IAHLAMNYL-------DSLSGGQKQLVGLAQSLIRRPALL 159
Cdd:COG2274 558 VFLFsgtIRENITLGD----PDATDEEIIEAARLAGlhdfIEALPMGYDtvvgeggSNLSGGQRQRLAIARALLRNPRIL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 160 LLDEPLSALDLNYQFHVMDVVSRETRRRNMVtlVVLHDINIaLRHAAQVIMLKEGKLIDSGDPQTVI 226
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLLKGRTVI--IIAHRLST-IRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-216 |
1.65e-25 |
|
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: 99.94 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNEENLLSLPFARRAEKVVFLPQSLPQslpqgvHLQVLESVVV 104
Cdd:TIGR01277 20 NVADGEIVAIMGPSGAGKSTLLNLIAGfIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFA------HLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 105 AQRASGA--GQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSR 182
Cdd:TIGR01277 94 GLHPGLKlnAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|....
gi 545166817 183 ETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKL 216
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-236 |
1.70e-25 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 100.45 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALaglNR----ASGEAWLNEENLLSLPFARRAEKVVFLPQS---L 86
Cdd:cd03295 12 GGKKAVNNLNL-EIAKGEFLVLIGPSGSGKTTTMKMI---NRliepTSGEIFIDGEDIREQDPVELRRKIGYVIQQiglF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 87 PqslpqgvHLQVLESVVVAQRASGAGQNQAQAIA--LLE--ELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLD 162
Cdd:cd03295 88 P-------HMTVEENIALVPKLLKWPKEKIRERAdeLLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 163 EPLSALdlnyqfhvmDVVSRETRRRNMVTL---------VVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVI---HAES 230
Cdd:cd03295 161 EPFGAL---------DPITRDQLQEEFKRLqqelgktivFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILrspANDF 231
|
....*.
gi 545166817 231 LAQVYG 236
Cdd:cd03295 232 VAEFVG 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-235 |
1.89e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 100.35 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSGLTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENLLSLPFARRAEKV 79
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSL-TVNSGEIVGLLGPNGAGKTTTFYMVVGIvPRDAGNIIIDDEDISLLPLHARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 80 VflpQSLPQSLPQGVHLQV---LESVVVAQRASGAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRP 156
Cdd:PRK10895 80 I---GYLPQEASIFRRLSVydnLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 157 ALLLLDEPLSALDlnyQFHVMDV--VSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESLAQV 234
Cdd:PRK10895 157 KFILLDEPFAGVD---PISVIDIkrIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRV 233
|
.
gi 545166817 235 Y 235
Cdd:PRK10895 234 Y 234
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-222 |
5.02e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 99.37 E-value: 5.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR---ASGEAWLNEENLLSLPFARRAEKVV 80
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNL-TIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyevTSGSILLDGEDILELSPDERARAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 81 FL----PQSLPqslpqGVHL-QVLESVVVAQR--ASGAGQNQAQAIALLEELGiahLAMNYLD-----SLSGGQKQLVGL 148
Cdd:COG0396 80 FLafqyPVEIP-----GVSVsNFLRTALNARRgeELSAREFLKLLKEKMKELG---LDEDFLDryvneGFSGGEKKRNEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 149 AQSLIRRPALLLLDEPLSALDLNyqfhVMDVVSR---ETRRRNMVTLVVLHDINIaLRH--AAQVIMLKEGKLIDSGDP 222
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDID----ALRIVAEgvnKLRSPDRGILIITHYQRI-LDYikPDFVHVLVDGRIVKSGGK 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
29-226 |
1.76e-24 |
|
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: 98.48 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENLLSLPFAR----RAEKVVFLPQS---LPqslpqgvHLQVLE 100
Cdd:cd03294 49 EGEIFVIMGLSGSGKSTLLRCINRLiEPTSGKVLIDGQDIAAMSRKElrelRRKKISMVFQSfalLP-------HRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 101 SVVVAQRASGAGQNQ--AQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALD----LNYQF 174
Cdd:cd03294 122 NVAFGLEVQGVPRAEreERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQD 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545166817 175 HVMDVVSRETRrrnmvTLV-VLHDINIALRHAAQVIMLKEGKLIDSGDPQTVI 226
Cdd:cd03294 202 ELLRLQAELQK-----TIVfITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-216 |
3.10e-24 |
|
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: 96.32 E-value: 3.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 22 LSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSL-----PFARRAEKVVFLPQSLpqsLPqgvH 95
Cdd:cd03292 20 INIS-ISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNGQDVSDLrgraiPYLRRKIGVVFQDFRL---LP---D 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 96 LQVLESVVVAQRASGAGQNQAQ--AIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQ 173
Cdd:cd03292 93 RNVYENVAFALEVTGVPPREIRkrVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 545166817 174 FHVMDVVSRETRRRNMVtLVVLHDINIALRHAAQVIMLKEGKL 216
Cdd:cd03292 173 WEIMNLLKKINKAGTTV-VVATHAKELVDTTRHRVIALERGKL 214
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-228 |
7.03e-24 |
|
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: 97.82 E-value: 7.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGY----GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGL----NRASGEAWLNEENLLSLPFAR- 74
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSF-DVRRGETLGLVGESGSGKSTLARAILGLlpppGITSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 75 ---RAEKVVFLPQ----SLPQSLPqgVHLQVLESVVVAQRASGAgQNQAQAIALLEELGIAHlAMNYLDS----LSGGQK 143
Cdd:COG0444 81 rkiRGREIQMIFQdpmtSLNPVMT--VGDQIAEPLRIHGGLSKA-EARERAIELLERVGLPD-PERRLDRypheLSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 144 QLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQ 223
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVE 236
|
....*
gi 545166817 224 TVIHA 228
Cdd:COG0444 237 ELFEN 241
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-214 |
1.23e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.92 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRASGEAWLNEENLLSLPFARRAekVVFLP 83
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINL-TLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERG--VVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 84 QSLpqsLPQgvhLQVLESVVVAQRASGAGQNQAQAIA--LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLL 161
Cdd:PRK11248 79 EGL---LPW---RNVQDNVAFGLQLAGVEKMQRLEIAhqMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545166817 162 DEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEG 214
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
4-222 |
1.27e-23 |
|
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: 95.41 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR---ASGEAWLNEENLLSLPFARRAEKVV 80
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNL-TVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyevTSGTILFKGQDLLELEPDERARAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 81 FLPQSLPQSLPqGVHLQ-VLESVVVAQRASGaGQNQAQAIALLEELG--IAHLAMN--YLD-----SLSGGQKQLVGLAQ 150
Cdd:TIGR01978 80 FLAFQYPEEIP-GVSNLeFLRSALNARRSAR-GEEPLDLLDFEKLLKekLALLDMDeeFLNrsvneGFSGGEKKRNEILQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545166817 151 SLIRRPALLLLDEPLSALDLNYQFHVMDVVSReTRRRNMVTLVVLHDINIaLRHAA--QVIMLKEGKLIDSGDP 222
Cdd:TIGR01978 158 MALLEPKLAILDEIDSGLDIDALKIVAEGINR-LREPDRSFLIITHYQRL-LNYIKpdYVHVLLDGRIVKSGDV 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
26-221 |
3.40e-23 |
|
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: 94.18 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSL-PFARRAEK----VVFlpqslpqslpQGVHL--- 96
Cdd:cd03258 27 SVPKGEIFGIIGRSGAGKSTLIRCINGLERpTSGSVLVDGTDLTLLsGKELRKARrrigMIF----------QHFNLlss 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 97 -QVLESVVVAQRASGAGQNQ--AQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQ 173
Cdd:cd03258 97 rTVFENVALPLEIAGVPKAEieERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETT 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545166817 174 FHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGD 221
Cdd:cd03258 177 QSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-226 |
3.43e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.26 E-value: 3.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNEENLLSLPFARRAEKVVFLPQSLPQslpqgvHLQVLESVVV--- 104
Cdd:PRK10771 24 RGERVAILGPSGAGKSTLLNLIAGfLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFS------HLTVAQNIGLgln 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 105 -AQRASGAGQNQAQAIAllEELGIahlaMNYLD----SLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDV 179
Cdd:PRK10771 98 pGLKLNAAQREKLHAIA--RQMGI----EDLLArlpgQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545166817 180 VSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVI 226
Cdd:PRK10771 172 VSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
12-225 |
4.21e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 96.55 E-value: 4.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 12 GYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKVVFlpqslpQSL 90
Cdd:PRK09452 23 SFDGKEVISNLDL-TINNGEFLTLLGPSGCGKTTVLRLIAGFETPdSGRIMLDGQDITHVPAENRHVNTVF------QSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 91 PQGVHLQVLESVVVAQRAsgagqnQAQAIALLEELGIAHLAMNYLDS--------LSGGQKQLVGLAQSLIRRPALLLLD 162
Cdd:PRK09452 96 ALFPHMTVFENVAFGLRM------QKTPAAEITPRVMEALRMVQLEEfaqrkphqLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545166817 163 EPLSALDlnYQFHV-MDVVSRETRRRNMVTLV-VLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK09452 170 ESLSALD--YKLRKqMQNELKALQRKLGITFVfVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-228 |
5.52e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.47 E-value: 5.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 12 GYGKRRIIEHLSIS----TLPRGEVTVLLGPNGCGKSTLLRALAGLNRASGEAWLNEENLLS------LPFARRAEkVVF 81
Cdd:PRK15134 290 GILKRTVDHNVVVKnisfTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNlnrrqlLPVRHRIQ-VVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 82 lpQSLPQSL-PQGVHLQVL-ESVVVAQRASGAGQNQAQAIALLEELGI-AHLAMNYLDSLSGGQKQLVGLAQSLIRRPAL 158
Cdd:PRK15134 369 --QDPNSSLnPRLNVLQIIeEGLRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545166817 159 LLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINI--ALRHaaQVIMLKEGKLIDSGDPQTVIHA 228
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVvrALCH--QVIVLRQGEVVEQGDCERVFAA 516
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-229 |
6.20e-23 |
|
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: 97.14 E-value: 6.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 3 GLTINALCAGY--GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKV 79
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSL-TLPPGERVAIVGPSGSGKSTLLALLLRFLDPqSGSITLGGVDLRDLDEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 80 VFLPQSlpqslpqgVHL---QVLESVVVAqrASGAGQnqAQAIALLEELGIAHLAMNY---LDS--------LSGGQKQL 145
Cdd:COG4987 412 AVVPQR--------PHLfdtTLRENLRLA--RPDATD--EELWAALERVGLGDWLAALpdgLDTwlgeggrrLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 146 VGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRnmVTLVVLHDInIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEEL 556
|
....
gi 545166817 226 IHAE 229
Cdd:COG4987 557 LAQN 560
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-222 |
8.69e-23 |
|
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: 92.82 E-value: 8.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPF-ARRAEKVVFLPQSLPQSL 90
Cdd:cd03265 10 YGDFEAVRGVSFR-VRRGEIFGLLGPNGAGKTTTIKMLTTLLKPtSGRATVAGHDVVREPReVRRRIGIVFQDLSVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 91 pqgvhlQVLESVVVAQRASG-AGQNQAQAIA-LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSAL 168
Cdd:cd03265 89 ------TGWENLYIHARLYGvPGAERRERIDeLLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545166817 169 DLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDP 222
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
26-246 |
1.18e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 93.54 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGL---NRASGE--AWLNEENLLSLPFARRAEKVVFLPQSLPQSLPQGVHLQVLE 100
Cdd:PRK09984 26 NIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGShiELLGRTVQREGRLARDIRKSRANTGYIFQQFNLVNRLSVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 101 SVVVAQRASG----------AGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDL 170
Cdd:PRK09984 106 NVLIGALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDP 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 171 NYQFHVMDVVsRETRRRNMVTLVV-LHDINIALRHAAQVIMLKEGKLIDSGDPQTvIHAESLAQVYGVRGRVERCAQ 246
Cdd:PRK09984 186 ESARIVMDTL-RDINQNDGITVVVtLHQVDYALRYCERIVALRQGHVFYDGSSQQ-FDNERFDHLYRSINRVEENAK 260
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-217 |
1.35e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 93.23 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 16 RRIIEHLSIsTLPRGE-VTVLlGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKV--VFlpqslpQSLP 91
Cdd:COG1101 19 KRALDGLNL-TIEEGDfVTVI-GSNGAGKSTLLNAIAGSLPPdSGSILIDGKDVTKLPEYKRAKYIgrVF------QDPM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 92 QGV--HLQVLESVVVAQ-----RASGAGQNQAQaIALLEELgIAHLAM---NYLD----SLSGGQKQLVGLAQSLIRRPA 157
Cdd:COG1101 91 MGTapSMTIEENLALAYrrgkrRGLRRGLTKKR-RELFREL-LATLGLgleNRLDtkvgLLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 158 LLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLI 217
Cdd:COG1101 169 LLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-183 |
2.47e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.64 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 16 RRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEawlneenlLSLPfarRAEKVVFLPQS--LPQ-SLP 91
Cdd:COG4178 376 RPLLEDLSLS-LKPGERLLITGPSGSGKSTLLRAIAGLwPYGSGR--------IARP---AGARVLFLPQRpyLPLgTLR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 92 QgvhlqvlesvVVAQRASGAGQNQAQAIALLEELGIAHLAmNYLDS-------LSGGQKQLVGLAQSLIRRPALLLLDEP 164
Cdd:COG4178 444 E----------ALLYPATAEAFSDAELREALEAVGLGHLA-ERLDEeadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170
....*....|....*....
gi 545166817 165 LSALDLNYQFHVMDVVSRE 183
Cdd:COG4178 513 TSALDEENEAALYQLLREE 531
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-247 |
2.89e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.85 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 9 LCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLN------RASGEAWLNEENLLS----LPFARRAEK 78
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMG-FPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgyRYSGDVLLGGRSIFNyrdvLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 79 VVFLPQSLPQSLPQGVHLQVLESVVVAQRasgagQNQAQAIALLEELGIAHLAMNYL-DS---LSGGQKQLVGLAQSLIR 154
Cdd:PRK14271 106 LFQRPNPFPMSIMDNVLAGVRAHKLVPRK-----EFRGVAQARLTEVGLWDAVKDRLsDSpfrLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 155 RPALLLLDEPLSALDLNYQFHVMDVVSRETRRrnMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVI----HAES 230
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFsspkHAET 258
|
250
....*....|....*..
gi 545166817 231 LAQVYGVRGRVERCAQG 247
Cdd:PRK14271 259 ARYVAGLSGDVKDAKRG 275
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-228 |
3.31e-22 |
|
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: 95.14 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALC----AGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKS----TLLRALA-GLNRASGEAWLNEENLLSLPFAR 74
Cdd:COG4172 7 LSVEDLSvafgQGGGTVEAVKGVSFD-IAAGETLALVGESGSGKSvtalSILRLLPdPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 75 ----RAEKV--VFL-PQSlpqSL-P-QGVHLQVLESVVVAQRASGAgQNQAQAIALLEELGIAHlAMNYLDS----LSGG 141
Cdd:COG4172 86 lrriRGNRIamIFQePMT---SLnPlHTIGKQIAEVLRLHRGLSGA-AARARALELLERVGIPD-PERRLDAyphqLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 142 QKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGD 221
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
....*..
gi 545166817 222 PQTVIHA 228
Cdd:COG4172 241 TAELFAA 247
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-225 |
4.66e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.48 E-value: 4.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEEnllslPFARRA-EKVVFLPQ--SLPQ 88
Cdd:COG4152 11 FGDKTAVDDVSF-TVPKGEIFGLLGPNGAGKTTTIRIILGILAPdSGEVLWDGE-----PLDPEDrRRIGYLPEerGLYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 89 SLPqgvhlqVLESVV-VAQRAsGAGQNQA--QAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPL 165
Cdd:COG4152 85 KMK------VGEQLVyLARLK-GLSKAEAkrRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545166817 166 SALD-LNYQfHVMDVVsRETRRRNmvTLVVL--HDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:COG4152 158 SGLDpVNVE-LLKDVI-RELAAKG--TTVIFssHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-223 |
8.72e-22 |
|
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: 90.26 E-value: 8.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRR--IIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRaekvv 80
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSL-NVYKGEIFGLLGHNGAGKTTTLKMLTGELRPtSGTAYINGYSIRTDRKAAR----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 81 flpQSL---PQSLPQGVHLQVLESVVVAQRASG--AGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRR 155
Cdd:cd03263 75 ---QSLgycPQFDALFDELTVREHLRFYARLKGlpKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545166817 156 PALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMvtLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQ 223
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-221 |
1.60e-21 |
|
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: 89.51 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSISTlPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENLLSLPFARRAEK-VVF 81
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEV-PKGEVTCVLGRNGVGKTTLLKTLMGLlPVKSGSIRLDGEDITKLPPHERARAgIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 82 LPQSlPQSLPQgvhLQVLESVVVAqrASGAGQNQAQAIALLEELGIAHLAMnyLD----SLSGGQKQLVGLAQSLIRRPA 157
Cdd:TIGR03410 80 VPQG-REIFPR---LTVEENLLTG--LAALPRRSRKIPDEIYELFPVLKEM--LGrrggDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545166817 158 LLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGD 221
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-220 |
4.33e-21 |
|
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: 88.04 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFA-RRAEKVVF 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISL-HVKKGEIYGFLGPNGAGKTTTMKIILGLIKPdSGEITFDGKSYQKNIEAlRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 82 LPQSLPqslpqgvHLQVLESVVVAQRASGAGQNQAQAIalLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLL 161
Cdd:cd03268 80 APGFYP-------NLTARENLRLLARLLGIRKKRIDEV--LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545166817 162 DEPLSALDlnyQFHVMDVvsRET----RRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSG 220
Cdd:cd03268 151 DEPTNGLD---PDGIKEL--RELilslRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-237 |
5.70e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.09 E-value: 5.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 15 KRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRASGEA---------WLNEENLLSLpfarrAEKVVFLPQS 85
Cdd:PRK13640 19 KKPALNDISFS-IPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgiTLTAKTVWDI-----REKVGIVFQN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 86 lPQSlpQGVHLQVLESVVVAQRASGAGQNQAQAIA--LLEELGIAhlamNYLDS----LSGGQKQLVGLAQSLIRRPALL 159
Cdd:PRK13640 93 -PDN--QFVGATVGDDVAFGLENRAVPRPEMIKIVrdVLADVGML----DYIDSepanLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545166817 160 LLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIAlRHAAQVIMLKEGKLIDSGDPQTVIHAESLAQVYGV 237
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGL 242
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-214 |
1.37e-20 |
|
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: 87.14 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRASGEAWLNEENLLSLPFARRAekVVFLPQSLpqsLPQgvhLQVLESVVVA 105
Cdd:TIGR01184 7 TIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--VVFQNYSL---LPW---LTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 106 QRASGAGQNQAQAIALLEE----LGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDL----NYQFHVM 177
Cdd:TIGR01184 79 VDRVLPDLSKSERRAIVEEhialVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgNLQEELM 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 545166817 178 DVVSRETRRRNMVTlvvlHDINIALRHAAQVIMLKEG 214
Cdd:TIGR01184 159 QIWEEHRVTVLMVT----HDVDEALLLSDRVVMLTNG 191
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-220 |
4.68e-20 |
|
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: 85.50 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRR----IIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRAS-GEAWLNEENLLSLPFARRAeK 78
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSF-TVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDaGFATVDGFDVVKEPAEARR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 79 VVFLPQSlpqslpQGVH--LQVLESVVVAQRASG-AGQNQAQAI-ALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIR 154
Cdd:cd03266 80 LGFVSDS------TGLYdrLTARENLEYFAGLYGlKGDELTARLeELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545166817 155 RPALLLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSG 220
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFI-RQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
15-216 |
4.96e-20 |
|
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: 85.46 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 15 KRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWL--------NEENLLSLpfaRRAEKVVFLPQS 85
Cdd:TIGR02982 17 RKQVLFDINLEINP-GEIVILTGPSGSGKTTLLTLIGGLRSVqEGSLKVlgqelhgaSKKQLVQL---RRRIGYIFQAHN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 86 LPQSLpqgvhlQVLESVVVA---QRASGAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLD 162
Cdd:TIGR02982 93 LLGFL------TARQNVQMAlelQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545166817 163 EPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIaLRHAAQVIMLKEGKL 216
Cdd:TIGR02982 167 EPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRI-LDVADRILQMEDGKL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-232 |
5.26e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 86.28 E-value: 5.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 8 ALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFA-----RRAEKVVF 81
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLS-LKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVSWRGEPLAKLNRAqrkafRRDIQMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 82 lpqslpQSLPQGVHLQVLESVVVAQ------RASGAGQnQAQAIALLEELGIAHLAMNYL-DSLSGGQKQLVGLAQSLIR 154
Cdd:PRK10419 96 ------QDSISAVNPRKTVREIIREplrhllSLDKAER-LARASEMLRAVDLDDSVLDKRpPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 155 RPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDS---GDPQTVIHAESL 231
Cdd:PRK10419 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETqpvGDKLTFSSPAGR 248
|
.
gi 545166817 232 A 232
Cdd:PRK10419 249 V 249
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-220 |
5.79e-20 |
|
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: 85.40 E-value: 5.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 15 KRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR----ASGEAWLNEENLLSLPFARRaekVVFLPQS---LP 87
Cdd:cd03234 19 YARILNDVSL-HVESGQVMAILGSSGSGKTTLLDAISGRVEgggtTSGQILFNGQPRKPDQFQKC---VAYVRQDdilLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 88 qslpqgvHLQVLESVV-VAQRASGAGQNQAQ-----AIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLL 161
Cdd:cd03234 95 -------GLTVRETLTyTAILRLPRKSSDAIrkkrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545166817 162 DEPLSALDLNYQFHVMDVVSReTRRRNMVTLVVLH----DIniaLRHAAQVIMLKEGKLIDSG 220
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQ-LARRNRIVILTIHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-169 |
8.64e-20 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 85.47 E-value: 8.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLN------RASGEAWLNEENLLS----LPFA 73
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLD-IPENKVTALIGPSGCGKSTLLRCLNRMNdlipgaRVEGEILLDGEDIYDpdvdVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 74 RRaeKV--VF-LPQSLPQSlpqgvhlqVLESVVVAQRASGAgQNQAQAIALLEE-LGIAHL-----------AMnyldSL 138
Cdd:COG1117 91 RR--RVgmVFqKPNPFPKS--------IYDNVAYGLRLHGI-KSKSELDEIVEEsLRKAALwdevkdrlkksAL----GL 155
|
170 180 190
....*....|....*....|....*....|.
gi 545166817 139 SGGQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-171 |
1.04e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLneenllslpfaRRAEKVVFLPQSLPQSLP 91
Cdd:COG0488 8 FGGRPLLDDVSLS-INPGDRIGLVGRNGAGKSTLLKILAGELEPdSGEVSI-----------PKGLRIGYLPQEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 92 QGVHLQVLESV-----VVAQR-------------------------ASGAGQNQAQAIALLEELGIAHLAMNY-LDSLSG 140
Cdd:COG0488 76 LTVLDTVLDGDaelraLEAELeeleaklaepdedlerlaelqeefeALGGWEAEARAEEILSGLGFPEEDLDRpVSELSG 155
|
170 180 190
....*....|....*....|....*....|.
gi 545166817 141 GQKQLVGLAQSLIRRPALLLLDEPLSALDLN 171
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLE 186
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-229 |
2.59e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 82.96 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR---ASGEAWLNEENLLSLPFARRAEKVV 80
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNL-TIKKGEVHALMGPNGSGKSTLAKTIMGHPKyevTEGEILFKGEDITDLPPEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 81 FLPQSLPQSLPqGVHLqvlesvvvaqrasgagqnqaqaialleelgiahlaMNYL----DSLSGGQKQLVGLAQSLIRRP 156
Cdd:cd03217 80 FLAFQYPPEIP-GVKN-----------------------------------ADFLryvnEGFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 157 ALLLLDEPLSALDLNyqfhVMDVVSR---ETRRRNMVTLVVLHDINIA-LRHAAQVIMLKEGKLIDSGDPQTVIHAE 229
Cdd:cd03217 124 DLAILDEPDSGLDID----ALRLVAEvinKLREEGKSVLIITHYQRLLdYIKPDRVHVLYDGRIVKSGDKELALEIE 196
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
26-215 |
4.20e-19 |
|
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: 82.52 E-value: 4.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAG-LNRASG-------------EAWL-NE---ENLL-SLPF-ARRAEKVVFLPQS 85
Cdd:cd03250 27 EVPKGELVAIVGPVGSGKSSLLSALLGeLEKLSGsvsvpgsiayvsqEPWIqNGtirENILfGKPFdEERYEKVIKACAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 86 LP--QSLPQGvhlqvLESVVvaqrasgaGQNqaqaialleelGIahlamnyldSLSGGQKQLVGLAQSLIRRPALLLLDE 163
Cdd:cd03250 107 EPdlEILPDG-----DLTEI--------GEK-----------GI---------NLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 545166817 164 PLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIaLRHAAQVIMLKEGK 215
Cdd:cd03250 154 PLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQL-LPHADQIVVLDNGR 204
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
30-220 |
5.41e-19 |
|
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: 82.64 E-value: 5.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 30 GEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKVVFLPQ-------SLPQSLPQGVHLQVLES 101
Cdd:cd03245 30 GEKVAIIGRVGSGKSTLLKLLAGLYKPtSGSVLLDGTDIRQLDPADLRRNIGYVPQdvtlfygTLRDNITLGAPLADDER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 102 VVVAQRASGAGQ---NQAQAIAL-LEELGiahlamnylDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVM 177
Cdd:cd03245 110 ILRAAELAGVTDfvnKHPNGLDLqIGERG---------RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 545166817 178 DVVSRETRRRNMVtlVVLHDINIaLRHAAQVIMLKEGKLIDSG 220
Cdd:cd03245 181 ERLRQLLGDKTLI--IITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
26-234 |
1.52e-18 |
|
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: 82.50 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLS-----LPFARRaeKV--VF-LPQSlpqslpQGVHL 96
Cdd:TIGR04521 27 TIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPtSGTVTIDGRDITAkkkkkLKDLRK--KVglVFqFPEH------QLFEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 97 QVLESVVVAQRASGAGQNQAQ--AIALLEELGIAHlamNYLD----SLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDL 170
Cdd:TIGR04521 99 TVYKDIAFGPKNLGLSEEEAEerVKEALELVGLDE---EYLErspfELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545166817 171 NYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVI-HAESLAQV 234
Cdd:TIGR04521 176 KGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFsDVDELEKI 240
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
29-218 |
1.67e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.79 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAE----KVVFLPQsLPQSLPQgvhLQVLESVV 103
Cdd:PRK11629 34 EGEMMAIVGSSGSGKSTLLHLLGGLDTpTSGDVIFNGQPMSKLSSAAKAElrnqKLGFIYQ-FHHLLPD---FTALENVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 104 VAQRASGAGQNQAQ--AIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVS 181
Cdd:PRK11629 110 MPLLIGKKKPAEINsrALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLG 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 545166817 182 RETRRRNMVTLVVLHDINIALRHAAQVIMlKEGKLID 218
Cdd:PRK11629 190 ELNRLQGTAFLVVTHDLQLAKRMSRQLEM-RDGRLTA 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-221 |
1.81e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.39 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNE------ENLLSLPFARRAEKVVFLPQSLpqsLPqgvHLQV 98
Cdd:PRK11144 20 TLPAQGITAIFGRSGAGKTSLINAISGLTRPqKGRIVLNGrvlfdaEKGICLPPEKRRIGYVFQDARL---FP---HYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 99 LESVvvaqRASGAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMD 178
Cdd:PRK11144 94 RGNL----RYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 545166817 179 VVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGD 221
Cdd:PRK11144 170 YLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
26-169 |
2.12e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 82.82 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFA--RRAEK---VVFlpqslpqslpQGVHLqvL 99
Cdd:COG1135 27 TIEKGEIFGIIGYSGAGKSTLIRCINLLERPtSGSVLVDGVDLTALSERelRAARRkigMIF----------QHFNL--L 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545166817 100 ESVVVAQ------RASGAGQNQAQAIA--LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:COG1135 95 SSRTVAEnvalplEIAGVPKAEIRKRVaeLLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
26-218 |
2.24e-18 |
|
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: 81.78 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFA-----RRAEKVVFlpQSLPQSL-PQGVHLQV 98
Cdd:TIGR02769 33 SIEEGETVGLLGRSGCGKSTLARLLLGLEKpAQGTVSFRGQDLYQLDRKqrrafRRDVQLVF--QDSPSAVnPRMTVRQI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 99 LESVVVAQRASGAGQNQAQAIALLEELGI-AHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVM 177
Cdd:TIGR02769 111 IGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVIL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 545166817 178 DVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLID 218
Cdd:TIGR02769 191 ELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-239 |
2.26e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.70 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSGL-TINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRASGEAWLNEENLlslpfarraeKV 79
Cdd:PRK09544 1 MTSLvSLENVSVSFGQRRVLSDVSL-ELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL----------RI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 80 VFLPQSLpqslpqgvHLQVLESVVVAQRAS-GAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPAL 158
Cdd:PRK09544 70 GYVPQKL--------YLDTTLPLTVNRFLRlRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 159 LLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEgKLIDSGDPQTV-IHAESLAqVYGV 237
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVsLHPEFIS-MFGP 219
|
..
gi 545166817 238 RG 239
Cdd:PRK09544 220 RG 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
12-227 |
3.09e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.16 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 12 GYGKRRIIEHLSIS--------TLPRGEVTVLLGPNGCGKSTLLRALAGLNRAS-GEAWLNEENLLSLPFAR----RAEK 78
Cdd:PRK10070 28 GLSKEQILEKTGLSlgvkdaslAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTrGQVLIDGVDIAKISDAElrevRRKK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 79 VVFLPQSLPQsLPqgvHLQVLESVVVAQRASG--AGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRP 156
Cdd:PRK10070 108 IAMVFQSFAL-MP---HMTVLDNTAFGMELAGinAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINP 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545166817 157 ALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIH 227
Cdd:PRK10070 184 DILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
26-225 |
4.93e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.43 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLN-------EENLLSLpfaRRAEKVVF-------LPQSLPQSL 90
Cdd:PRK13636 28 NIKKGEVTAILGGNGAGKSTLFQNLNGiLKPSSGRILFDgkpidysRKGLMKL---RESVGMVFqdpdnqlFSASVYQDV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 91 PQGVHLQVLESVVVAQRASGAgqnqaqaialLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDL 170
Cdd:PRK13636 105 SFGAVNLKLPEDEVRKRVDNA----------LKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545166817 171 NYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK13636 175 MGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
26-216 |
5.53e-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: 80.21 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRASGEAWLNEENLLSL---PFARRA------EKVVFlPQSLPQSLPQGVHL 96
Cdd:cd03248 36 TLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehKYLHSKvslvgqEPVLF-ARSLQDNIAYGLQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 97 QVLESVVVAQRASGAGQNqaqaIALLEeLGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHV 176
Cdd:cd03248 115 CSFECVKEAAQKAHAHSF----ISELA-SGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 545166817 177 MDVVSRETRRRNMvtLVVLHDINIaLRHAAQVIMLKEGKL 216
Cdd:cd03248 190 QQALYDWPERRTV--LVIAHRLST-VERADQILVLDGGRI 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-211 |
6.10e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 79.76 E-value: 6.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENLLSLPFARRAEKVVFLPQSlPQSLPQ 92
Cdd:PRK10247 18 GDAKILNNISF-SLRAGEFKLITGPSGCGKSTLLKIVASLiSPTSGTLLFEGEDISTLKPEIYRQQVSYCAQT-PTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 93 GVHLQVLESVVVAQRasgagqnQAQAIALLEELGIAHLAMNYLD----SLSGGQKQLVGLAQSLIRRPALLLLDEPLSAL 168
Cdd:PRK10247 96 TVYDNLIFPWQIRNQ-------QPDPAIFLDDLERFALPDTILTkniaELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 545166817 169 DLNYQFHVMDVVSRETRRRNMVTLVVLHDINiALRHAAQVIML 211
Cdd:PRK10247 169 DESNKHNVNEIIHRYVREQNIAVLWVTHDKD-EINHADKVITL 210
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-225 |
7.19e-18 |
|
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: 80.55 E-value: 7.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAW------LNEENLlslPFARRAEKVVFlpqsl 86
Cdd:TIGR04520 13 SEKPALKNVSLS-IEKGEFVAIIGHNGSGKSTLAKLLNGLLLPtSGKVTvdgldtLDEENL---WEIRKKVGMVF----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 87 pQSlP--QGVHLQVLESVvvaqrASGagqnqaqaialLEELGIAHLAM--------------NYLDS----LSGGQKQLV 146
Cdd:TIGR04520 84 -QN-PdnQFVGATVEDDV-----AFG-----------LENLGVPREEMrkrvdealklvgmeDFRDRephlLSGGQKQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 147 GLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALrHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREI 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-169 |
1.27e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 79.43 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSISTLPRgEVTVLLGPNGCGKSTLLRALAGLN------RASGEAWLNEENLlslpFARRAE 77
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPN-EITALIGPSGSGKSTLLRSINRMNdlnpevTITGSIVYNGHNI----YSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 78 KV--------VFL-PQSLPQSlpqgvhlqVLESVVVAQRASG---------AGQNQAQAIALLEELGiAHLAMNYLdSLS 139
Cdd:PRK14239 81 TVdlrkeigmVFQqPNPFPMS--------IYENVVYGLRLKGikdkqvldeAVEKSLKGASIWDEVK-DRLHDSAL-GLS 150
|
170 180 190
....*....|....*....|....*....|
gi 545166817 140 GGQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-198 |
1.40e-17 |
|
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: 81.75 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAwlnEENLlslpfarraeKVVFLPQSLPQSLPQGVHlQVLESVVVAQR 107
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGvLKPDEGEV---DEDL----------KISYKPQYISPDYDGTVE-EFLRSANTDDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 108 ASGAGQNQaqaiaLLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRR 187
Cdd:COG1245 431 GSSYYKTE-----IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENR 505
|
170
....*....|.
gi 545166817 188 NMVTLVVLHDI 198
Cdd:COG1245 506 GKTAMVVDHDI 516
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-225 |
1.98e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 79.02 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSGLTINALCAGYGKRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALaglnrasgeawlneeNLLSLPFARR----- 75
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKP-GEVVAIIGPSGSGKTTLLRCI---------------NLLEQPEAGTirvgd 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 76 ----AEKVVFLPQSLPQSLPQGV-----------HLQVLESVV---VAQRASGAGQNQAQAIALLEELGIAHLAMNYLDS 137
Cdd:PRK11264 65 itidTARSLSQQKGLIRQLRQHVgfvfqnfnlfpHRTVLENIIegpVIVKGEPKEEATARARELLAKVGLAGKETSYPRR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 138 LSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVV-SRETRRRNMVtlVVLHDINIALRHAAQVIMLKEGKL 216
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIrQLAQEKRTMV--IVTHEMSFARDVADRAIFMDQGRI 222
|
....*....
gi 545166817 217 IDSGDPQTV 225
Cdd:PRK11264 223 VEQGPAKAL 231
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
29-225 |
2.63e-17 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 78.69 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEEnLLSLPFARRAEKVVFLPQSLP----------QSLPQGVHLQ 97
Cdd:COG4598 33 KGDVISIIGSSGSGKSTFLRCINLLETPdSGEIRVGGE-EIRLKPDRDGELVPADRRQLQrirtrlgmvfQSFNLWSHMT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 98 VLESVVVA----QRASGAgQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALD---L 170
Cdd:COG4598 112 VLENVIEApvhvLGRPKA-EAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDpelV 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545166817 171 NYQFHVMDVVSRETrrRNMvtLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:COG4598 191 GEVLKVMRDLAEEG--RTM--LVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-216 |
4.06e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.61 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAGLNRAS-GEAWLNEENLLSL-----PFARRAEKVVFlpqslp 87
Cdd:PRK10908 13 GGRQALQGVTFHMRP-GEMAFLTGHSGAGKSTLLKLICGIERPSaGKIWFSGHDITRLknrevPFLRRQIGMIF------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 88 qslpQGVHL----QVLESVVVAQRASGAGQN--QAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLL 161
Cdd:PRK10908 86 ----QDHHLlmdrTVYDNVAIPLIIAGASGDdiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545166817 162 DEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKL 216
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLF-EEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-233 |
4.18e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.91 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 16 RRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRAS------GE----AWLNEENLLSLpfaRRAEKVVFlpqS 85
Cdd:PRK13634 20 RRALYDVNV-SIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTsgtvtiGErvitAGKKNKKLKPL---RKKVGIVF---Q 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 86 LPQSlpqgvhlQVLESVVVAQRASGA---GQNQAQAIALLEE-LGIAHLAMNYLD----SLSGGQKQLVGLAQSLIRRPA 157
Cdd:PRK13634 93 FPEH-------QLFEETVEKDICFGPmnfGVSEEDAKQKAREmIELVGLPEELLArspfELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 158 LLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVI-HAESLAQ 233
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFaDPDELEA 242
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
29-216 |
4.21e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.51 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAGLNRAS-GEAWLNEENLLSLP----FARRAEKVVFLPQSLpQSLPQgvhLQVLESVV 103
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGSsGEVSLVGQPLHQMDeearAKLRAKHVGFVFQSF-MLIPT---LNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 104 VAQ--RASGAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVS 181
Cdd:PRK10584 111 LPAllRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190
|
170 180 190
....*....|....*....|....*....|....*
gi 545166817 182 RETRRRNMVTLVVLHDINIALRhAAQVIMLKEGKL 216
Cdd:PRK10584 191 SLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
28-201 |
5.60e-17 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 76.69 E-value: 5.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 28 PRGEVTVLLGPNGCGKSTLLRALAGLNRASGEA--WLNEENLLSLPFARRAEKVVFLPQSLPQSlpQGVHLQVLESVVVA 105
Cdd:TIGR01166 16 ERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAvlIDGEPLDYSRKGLLERRQRVGLVFQDPDD--QLFAADVDQDVAFG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 106 QRASGAGQNQAQAIA--LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVsRE 183
Cdd:TIGR01166 94 PLNLGLSEAEVERRVreALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAIL-RR 172
|
170
....*....|....*...
gi 545166817 184 TRRRNMVTLVVLHDINIA 201
Cdd:TIGR01166 173 LRAEGMTVVISTHDVDLA 190
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-225 |
5.73e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 78.13 E-value: 5.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 15 KRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRAS------GEAWLNEENLLSLpfaRRAEKVVFlpQSlPQ 88
Cdd:PRK13635 19 ATYALKDVSFS-VYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEagtitvGGMVLSEETVWDV---RRQVGMVF--QN-PD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 89 SlpQGVHLQVLESVVVAqrasgagqnqaqaialLEELGIAHLAM--------------NYLD----SLSGGQKQLVGLAQ 150
Cdd:PRK13635 92 N--QFVGATVQDDVAFG----------------LENIGVPREEMvervdqalrqvgmeDFLNrephRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545166817 151 SLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRhAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-220 |
7.56e-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: 76.99 E-value: 7.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHL-SIS-TLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEEnllsLPFARRAE-----KVVFLPQS 85
Cdd:cd03267 29 RKYREVEALkGISfTIEKGEIVGFIGPNGAGKTTTLKILSGLLQpTSGEVRVAGL----VPWKRRKKflrriGVVFGQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 86 -LPQSLPqgvhlqVLESVVVAQR-----ASGAGQNQAQAIALLEelgIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALL 159
Cdd:cd03267 105 qLWWDLP------VIDSFYLLAAiydlpPARFKKRLDELSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545166817 160 LLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSG 220
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-235 |
7.62e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.62 E-value: 7.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 2 SGLTINALCAGYGKRRIIEHLSISTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAwlneeNLLSLPF--ARRAEK 78
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRlASGKI-----SILGQPTrqALQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 79 VVFLPQS--LPQSLPqgvhlQVLESVVVAQRASGAG-------QNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLA 149
Cdd:PRK15056 80 VAYVPQSeeVDWSFP-----VLVEDVVMMGRYGHMGwlrrakkRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 150 QSLIRRPALLLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKeGKLIDSGDPQTVIHAE 229
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLL-RELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAE 232
|
....*.
gi 545166817 230 SLAQVY 235
Cdd:PRK15056 233 NLELAF 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-226 |
1.35e-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: 76.11 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENLLSLPFARRAEKVVFLPQS---LPQS 89
Cdd:cd03254 14 EKKPVLKDINFS-IKPGETVAIVGPTGAGKTTLINLLMRFyDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDtflFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 90 lpqgvhlqVLESVvvaqRASGAGQNQAQAIALLEELGIAHLAMNYLD-----------SLSGGQKQLVGLAQSLIRRPAL 158
Cdd:cd03254 93 --------IMENI----RLGRPNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545166817 159 LLLDEPLSALDLNYQFHVMDVVsrETRRRNMVTLVVLHDINIaLRHAAQVIMLKEGKLIDSGDPQTVI 226
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEAL--EKLMKGRTSIIIAHRLST-IKNADKILVLDDGKIIEEGTHDELL 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-225 |
1.47e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.49 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSGLTINALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGL------NRASGEAWLNEENLLSLPFA- 73
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLE-IPDNTITALMGPSGSGKSTLLRVFNRLielypeARVSGEVYLDGQDIFKMDVIe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 74 -RRAEKVVFlpqSLPQSLPqgvHLQVLESVVVAQRASGAGQNQAQAIA----LLEELGIAHLAMNYLD----SLSGGQKQ 144
Cdd:PRK14247 80 lRRRVQMVF---QIPNPIP---NLSIFENVALGLKLNRLVKSKKELQErvrwALEKAQLWDEVKDRLDapagKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 145 LVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRetRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQT 224
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLE--LKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
.
gi 545166817 225 V 225
Cdd:PRK14247 232 V 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-228 |
1.48e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 76.66 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 16 RRIIEHLSIsTLPRGEVTVLLGPNGCGKS-TLLRAL----AGLNRASGEAWLNEENLLslPFARRAEKVVFLPQSlPQSL 90
Cdd:PRK10418 16 QPLVHGVSL-TLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQTAGRVLLDGKPVA--PCALRGRKIATIMQN-PRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 91 PQGVHlQVLESVVVAQRASGAGQNQAQAIALLEELGI---AHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSA 167
Cdd:PRK10418 92 FNPLH-TMHTHARETCLALGKPADDATLTAALEAVGLenaARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545166817 168 LDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHA 228
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-225 |
1.52e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.93 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSISTlPRGEVTVLLGPNGCGKSTLLRALAGLNRAS-GEAWLNEENLlSLPFARRAEKVVFL 82
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQA-NAGDVISIIGSSGSGKSTFLRCINFLEKPSeGSIVVNGQTI-NLVRDKDGQLKVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQSLP----------QSLPQGVHLQVLESVVVAQ-RASGAGQNQAQ--AIALLEELGIAHLAM-NYLDSLSGGQKQLVGL 148
Cdd:PRK10619 84 KNQLRllrtrltmvfQHFNLWSHMTVLENVMEAPiQVLGLSKQEARerAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545166817 149 AQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRR-RNMVtlVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMV--VVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-220 |
1.78e-16 |
|
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: 75.04 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYG--KRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNEENLLSLPFARRaEKVV 80
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSL-ELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGVPVSDLEKALS-SLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 81 FLPQSlpqslpqgVHLqvlesvvvaqrasgagqnqaQAIALLEELGIahlamnyldSLSGGQKQLVGLAQSLIRRPALLL 160
Cdd:cd03247 79 VLNQR--------PYL--------------------FDTTLRNNLGR---------RFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 161 LDEPLSALDLNYQFHVMDVVSRETRRRNMvtLVVLHDInIALRHAAQVIMLKEGKLIDSG 220
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTL--IWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-225 |
1.80e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.14 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENL-LSLPFARRAEKVVFLPQSLpqSL-PqgvHLQVLESV 102
Cdd:COG1129 26 ELRPGEVHALLGENGAGKSTLMKILSGVYQPdSGEILLDGEPVrFRSPRDAQAAGIAIIHQEL--NLvP---NLSVAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 103 VVAQRASGAG-----QNQAQAIALLEELGIAhlamnyLD------SLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLN 171
Cdd:COG1129 101 FLGREPRRGGlidwrAMRRRARELLARLGLD------IDpdtpvgDLSVAQQQLVEIARALSRDARVLILDEPTASLTER 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545166817 172 YQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:COG1129 175 EVERLFRII-RRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-211 |
2.09e-16 |
|
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: 78.10 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEKVVFLPQSlpqslPQ 92
Cdd:TIGR02857 333 GRRPALRPVSF-TVPPGERVALVGPSGAGKSTLLNLLLGFVDpTEGSIAVNGVPLADADADSWRDQIAWVPQH-----PF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 93 GVHLQVLESVVVAQR-ASGAG-QNQAQAIALLE-----ELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPL 165
Cdd:TIGR02857 407 LFAGTIAENIRLARPdASDAEiREALERAGLDEfvaalPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 545166817 166 SALDLNYQFHVMDVVSRETRRRnmVTLVVLHDINIALRhAAQVIML 211
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAAL-ADRIVVL 529
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-197 |
2.19e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.58 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSGLTINALCAGY-GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEK 78
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDL-DVADGEFIVLVGPSGCGKSTLLRMVAGLERiTSGEIWIGGRVVNELEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 79 VVFLPQSL-PqslpqgvHLQVLESVVVAQRASGAGQNQ-----AQAIALLeELGiahlamNYLD----SLSGGQKQLVGL 148
Cdd:PRK11650 80 MVFQNYALyP-------HMSVRENMAYGLKIRGMPKAEieervAEAARIL-ELE------PLLDrkprELSGGQRQRVAM 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 545166817 149 AQSLIRRPALLLLDEPLSALD--LNYQfhvMDVVSRETRRRNMVT-LVVLHD 197
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDakLRVQ---MRLEIQRLHRRLKTTsLYVTHD 194
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-236 |
2.49e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.77 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLS-LPFARRAEKVVflpqslPQSL 90
Cdd:PRK13537 17 YGDKLVVDGLSFH-VQRGECFGLLGPNGAGKTTTLRMLLGLTHpDAGSISLCGEPVPSrARHARQRVGVV------PQFD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 91 PQGVHLQVLESVVVAQRASG--AGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSAL 168
Cdd:PRK13537 90 NLDPDFTVRENLLVFGRYFGlsAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545166817 169 DLNYQfHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAE---SLAQVYG 236
Cdd:PRK13537 170 DPQAR-HLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEigcDVIEIYG 239
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-228 |
3.04e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 76.70 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSGLTINALCAGYGKR----RIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGL----NRASGEAW-LNEENLLSLP 71
Cdd:PRK11022 1 MALLNVDKLSVHFGDEsapfRAVDRISYS-VKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLeFNGQDLQRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 72 FARRAE----KVVFLPQSLPQSLPQ--GVHLQVLESVVVAQRASGAGQNQaQAIALLEELGIAHLAM---NYLDSLSGGQ 142
Cdd:PRK11022 80 EKERRNlvgaEVAMIFQDPMTSLNPcyTVGFQIMEAIKVHQGGNKKTRRQ-RAIDLLNQVGIPDPASrldVYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 143 KQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDP 222
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
....*.
gi 545166817 223 QTVIHA 228
Cdd:PRK11022 239 HDIFRA 244
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
30-228 |
3.60e-16 |
|
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: 77.60 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 30 GEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKVVFLPQ-------SLPQSLPQGVHLQVLES 101
Cdd:TIGR03375 491 GEKVAIIGRIGSGKSTLLKLLLGLYQPtEGSVLLDGVDIRQIDPADLRRNIGYVPQdprlfygTLRDNIALGAPYADDEE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 102 VVVAQRASGAG---QNQAQAIAL-LEELGiahlamnylDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVM 177
Cdd:TIGR03375 571 ILRAAELAGVTefvRRHPDGLDMqIGERG---------RSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFK 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 545166817 178 DVVSRETRRRNMVtlVVLHDINIaLRHAAQVIMLKEGKLIDSGDPQTVIHA 228
Cdd:TIGR03375 642 DRLKRWLAGKTLV--LVTHRTSL-LDLVDRIIVMDNGRIVADGPKDQVLEA 689
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
26-226 |
3.73e-16 |
|
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: 77.48 E-value: 3.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEKVVFLPQS--------------LPQSL 90
Cdd:COG4618 354 SLEPGEVLGVIGPSGSGKSTLARLLVGVWPpTAGSVRLDGADLSQWDREELGRHIGYLPQDvelfdgtiaeniarFGDAD 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 91 PqgvhlqvlESVVVAQRASGAgqnqaqaiallEELgIAHLAMNYlD--------SLSGGQKQLVGLAQSLIRRPALLLLD 162
Cdd:COG4618 434 P--------EKVVAAAKLAGV-----------HEM-ILRLPDGY-DtrigeggaRLSGGQRQRIGLARALYGDPRLVVLD 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545166817 163 EPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIaLRHAAQVIMLKEGKLIDSGDPQTVI 226
Cdd:COG4618 493 EPNSNLDDEGEAALAAAI-RALKARGATVVVITHRPSL-LAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
26-210 |
5.72e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 75.92 E-value: 5.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFA-----RRAEKVVFlpQ----SLPQSLPQGvh 95
Cdd:COG4608 40 DIRRGETLGLVGESGCGKSTLGRLLLRLEEPtSGEILFDGQDITGLSGRelrplRRRMQMVF--QdpyaSLNPRMTVG-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 96 lQVLESVVVAQRASGAGQNQAQAIALLEELGIAHLAMN-YLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQF 174
Cdd:COG4608 116 -DIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADrYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQA 194
|
170 180 190
....*....|....*....|....*....|....*.
gi 545166817 175 HVMDVVSRETRRRNMVTLVVLHDINIaLRHAAQVIM 210
Cdd:COG4608 195 QVLNLLEDLQDELGLTYLFISHDLSV-VRHISDRVA 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-234 |
6.74e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.17 E-value: 6.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 27 LPRGEVTVLLGPNGCGKSTLLRALAGLNRAS-GEAWLNEENLLSLPFA--RRAEKVVFlpqslpqslpQGVHLQVLESVV 103
Cdd:PRK13648 32 IPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKsGEIFYNNQAITDDNFEklRKHIGIVF----------QNPDNQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 104 VAQRASGAgQNQA------QAIA--LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFH 175
Cdd:PRK13648 102 KYDVAFGL-ENHAvpydemHRRVseALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 176 VMDVVSRETRRRNMVTLVVLHDINIALrHAAQVIMLKEGKLIDSGDPQTVI-HAESLAQV 234
Cdd:PRK13648 181 LLDLVRKVKSEHNITIISITHDLSEAM-EADHVIVMNKGTVYKEGTPTEIFdHAEELTRI 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-217 |
7.46e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 73.35 E-value: 7.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 12 GYGKRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAGLN---RASGEAWLNEENLLSLPFARRaekVVFLPQslpq 88
Cdd:cd03213 18 SKSGKQLLKNVSGKAKP-GELTAIMGPSGAGKSTLLNALAGRRtglGVSGEVLINGRPLDKRSFRKI---IGYVPQ---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 89 slpqgvHLQVLESVVVAqrasgagqnqaqaiallEELGIAHLamnyLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSAL 168
Cdd:cd03213 90 ------DDILHPTLTVR-----------------ETLMFAAK----LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545166817 169 DLNYQFHVMDVVSREtRRRNMVTLVVLHDINIALRHAA-QVIMLKEGKLI 217
Cdd:cd03213 143 DSSSALQVMSLLRRL-ADTGRTIICSIHQPSSEIFELFdKLLLLSQGRVI 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
26-169 |
9.30e-16 |
|
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: 74.01 E-value: 9.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEE----NLLSLP----FARRAEKVVFLPQslpqslpqgvHL 96
Cdd:COG4778 33 SVAAGECVALTGPSGAGKSTLLKCIYGNYLPdSGSILVRHDggwvDLAQASpreiLALRRRTIGYVSQ----------FL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 97 QVLESV----VVAQ--RASGAGQNQAQAIA--LLEELGIA-HLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSA 167
Cdd:COG4778 103 RVIPRVsaldVVAEplLERGVDREEARARAreLLARLNLPeRLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTAS 182
|
..
gi 545166817 168 LD 169
Cdd:COG4778 183 LD 184
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-215 |
1.33e-15 |
|
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: 73.98 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 21 HLSIS--TLPRGEVTVLLGPNGCGKSTLLRALAGLNRASGEawlneENLLSLPfarraeKVVFLPQSLPQSLPQGVHlQV 98
Cdd:cd03237 14 TLEVEggSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-----DIEIELD------TVSYKPQYIKADYEGTVR-DL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 99 LESVVvaqraSGAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMD 178
Cdd:cd03237 82 LSSIT-----KDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 545166817 179 VVSRETRRRNMVTLVVLHDInIALRHAAQVIMLKEGK 215
Cdd:cd03237 157 VIRRFAENNEKTAFVVEHDI-IMIDYLADRLIVFEGE 192
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-219 |
1.40e-15 |
|
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: 72.08 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEEnllslpfarraeKVVFLpqslpqslpqgvhlqvleSVVV 104
Cdd:cd03216 22 SVRRGEVHALLGENGAGKSTLMKILSGLYKPdSGEILVDGK------------EVSFA------------------SPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 105 AQRAsgagqnqaqaialleelGIAhlaMNYldSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVsRET 184
Cdd:cd03216 72 ARRA-----------------GIA---MVY--QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI-RRL 128
|
170 180 190
....*....|....*....|....*....|....*
gi 545166817 185 RRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDS 219
Cdd:cd03216 129 RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
22-223 |
1.70e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.00 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 22 LSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRAS-------GEAwLNEENLLSLpfaRRAEKVVFlpqslpqslpQGV 94
Cdd:PRK13647 24 LSLS-IPEGSKTALLGPNGAGKSTLLLHLNGIYLPQrgrvkvmGRE-VNAENEKWV---RSKVGLVF----------QDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 95 HLQVLESVVVAQRASGAGQNQAQAIALLEELGIAHLAMNYLD-------SLSGGQKQLVGLAQSLIRRPALLLLDEPLSA 167
Cdd:PRK13647 89 DDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDfrdkppyHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 545166817 168 LDLNYQFHVMDVVSRETRRRNMVtLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQ 223
Cdd:PRK13647 169 LDPRGQETLMEILDRLHNQGKTV-IVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-216 |
1.88e-15 |
|
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: 71.86 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEKVVFLPQS---LPQS 89
Cdd:cd03246 13 AEPPVLRNVSFS-IEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDPNELGDHVGYLPQDdelFSGS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 90 LpqgvhlqvlesvvvaqrasgagqnqAQAIalleelgiahlamnyldsLSGGQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:cd03246 92 I-------------------------AENI------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545166817 170 LNYQFHVMDVVsRETRRRNMVTLVVLHDINiALRHAAQVIMLKEGKL 216
Cdd:cd03246 129 VEGERALNQAI-AALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-170 |
3.35e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.72 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNeENLlslpfarraeKVVFL 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSL-RIDRGDRIGLIGPNGAGKSTLLKLLAGeLEPDSGTVKLG-ETV----------KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQSLpQSLPqgVHLQVLESVvvaQRASGAGQNQaQAIALLEELGIA-HLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLL 161
Cdd:COG0488 384 DQHQ-EELD--PDKTVLDEL---RDGAPGGTEQ-EVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLL 456
|
....*....
gi 545166817 162 DEPLSALDL 170
Cdd:COG0488 457 DEPTNHLDI 465
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-201 |
3.37e-15 |
|
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: 72.01 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPfARRAEKVVFL 82
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSF-TLNAGEALQVTGPNGIGKTTLLRILAGLLRpDSGEVRWNGTPLAEQR-DEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQsLPQSLPQgvhLQVLESVVVAQRASGAGQNQA-QAIALLEELGIAHLAMNYldsLSGGQKQLVGLAQSLIRRPALLLL 161
Cdd:TIGR01189 79 GH-LPGLKPE---LSALENLHFWAAIHGGAQRTIeDALAAVGLTGFEDLPAAQ---LSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 545166817 162 DEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIA 201
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-201 |
3.48e-15 |
|
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: 71.76 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLlslpfarraekvVFLPQSLPQSLPQ 92
Cdd:cd03231 11 DGRALFSGLSF-TLAAGEALQVTGPNGSGKTTLLRILAGLSPpLAGRVLLNGGPL------------DFQRDSIARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 93 GVHLQVLESVVVAQ------RASGAGQNQAQAIALLEELGIAHLAMNYLdslSGGQKQLVGLAQSLIRRPALLLLDEPLS 166
Cdd:cd03231 78 LGHAPGIKTTLSVLenlrfwHADHSDEQVEEALARVGLNGFEDRPVAQL---SAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|....*
gi 545166817 167 ALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIA 201
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-198 |
4.33e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.76 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSGLTINALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRASGEA-------WLNE---ENLLSL 70
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSME-IYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVrvegrveFFNQniyERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 71 PFARRAEKVVFlPQslPQSLPQGVHLQVLESV-VVAQRAS----GAGQNQAQAIALLEElgIAHLAMNYLDSLSGGQKQL 145
Cdd:PRK14258 84 NRLRRQVSMVH-PK--PNLFPMSVYDNVAYGVkIVGWRPKleidDIVESALKDADLWDE--IKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545166817 146 VGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDI 198
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNL 211
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
26-255 |
4.68e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.61 E-value: 4.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGL----NRASGEAWLNEENLLSLPFAR----RAEKVVFLPQSLPQSL-P-QGVH 95
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSQTAFALMGLlaanGRIGGSATFNGREILNLPEKElnklRAEQISMIFQDPMTSLnPyMRVG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 96 LQVLEsvvVAQRASGAGQNQA--QAIALLEELGI--AHLAMN-YLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDL 170
Cdd:PRK09473 118 EQLME---VLMLHKGMSKAEAfeESVRMLDAVKMpeARKRMKmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 171 NYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESLAQVYGVRGRVERC-AQGRS 249
Cdd:PRK09473 195 TVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPRLdAEGES 274
|
....*.
gi 545166817 250 MVIVDG 255
Cdd:PRK09473 275 LLTIPG 280
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-170 |
7.49e-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: 69.40 E-value: 7.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEawlneenllslpfarraekvvfl 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISL-TINPGDRIGLVGRNGAGKSTLLKLIAGeLEPDEGI----------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 pqslpqslpqgvhLQVLESVVVAqrasgagqnqaqaialleelgiahlamnYLDSLSGGQKQLVGLAQSLIRRPALLLLD 162
Cdd:cd03221 57 -------------VTWGSTVKIG----------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLD 95
|
....*...
gi 545166817 163 EPLSALDL 170
Cdd:cd03221 96 EPTNHLDL 103
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-169 |
9.44e-15 |
|
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: 73.43 E-value: 9.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSISTLPRGEVTVLlGPNGCGKSTLLRALAGLNRA-SGEAWLNEenllslpfarrAEKVVFLPQSlPQSLPQ 92
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVL-GLNGAGKSTLLRIMAGVDKDfNGEARPQP-----------GIKVGYLPQE-PQLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 93 gvhLQVLESVVVAQRASGAGQNQAQAI------------ALLEELG-----IAH-----------LAMNYL--------- 135
Cdd:TIGR03719 83 ---KTVRENVEEGVAEIKDALDRFNEIsakyaepdadfdKLAAEQAelqeiIDAadawdldsqleIAMDALrcppwdadv 159
|
170 180 190
....*....|....*....|....*....|....
gi 545166817 136 DSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-236 |
1.13e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.56 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRASGeawlNEENLLSLPFARRAEKVVFLPQSLPQSLPQ 92
Cdd:PRK13536 51 YGDKAVVNGLSF-TVASGECFGLLGPNGAGKSTIARMILGMTSPDA----GKITVLGVPVPARARLARARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 93 GVHLQVLESVVVAQRASGAGQNQAQAI--ALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDL 170
Cdd:PRK13536 126 DLEFTVRENLLVFGRYFGMSTREIEAVipSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 171 NYQfHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAE---SLAQVYG 236
Cdd:PRK13536 206 HAR-HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHigcQVIEIYG 273
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-198 |
1.56e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.92 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAwlnEENLlslpfarraeKVVFLPQSLPQSLPQGVHlQVLESVvvaqr 107
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGvLKPDEGEV---DPEL----------KISYKPQYIKPDYDGTVE-DLLRSI----- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 108 ASGAGQNQAQAiALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRR 187
Cdd:PRK13409 425 TDDLGSSYYKS-EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEER 503
|
170
....*....|.
gi 545166817 188 NMVTLVVLHDI 198
Cdd:PRK13409 504 EATALVVDHDI 514
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-233 |
1.58e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 72.89 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKVVFLPQSlpqslpq 92
Cdd:COG1132 351 GDRPVLKDISL-TIPPGETVALVGPSGSGKSTLVNLLLRFYDPtSGRILIDGVDIRDLTLESLRRQIGVVPQD------- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 93 gVHL---QVLESVvvaqRASGAGQNQAQAIALLEELGIAHLAMNY---LD--------SLSGGQKQLVGLAQSLIRRPAL 158
Cdd:COG1132 423 -TFLfsgTIRENI----RYGRPDATDEEVEEAAKAAQAHEFIEALpdgYDtvvgergvNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545166817 159 LLLDEPLSALDLNYQFHVMDVVSRETRRRnmVTLVVLHDINiALRHAAQVIMLKEGKLIDSGDpqtviHAESLAQ 233
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLS-TIRNADRILVLDDGRIVEQGT-----HEELLAR 564
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-233 |
1.70e-14 |
|
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: 70.65 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 18 IIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENL--LSLPFARR------AEKVVFlPQSLPQ 88
Cdd:cd03249 18 ILKGLSL-TIPPGKTVALVGSSGCGKSTVVSLLERFyDPTSGEILLDGVDIrdLNLRWLRSqiglvsQEPVLF-DGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 89 SLPQGVHLQVLESVVVAQRASGAgqnqAQAIALLEElGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSAL 168
Cdd:cd03249 96 NIRYGKPDATDEEVEEAAKKANI----HDFIMSLPD-GYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545166817 169 DLNYQFHVMDVVSRetRRRNMVTLVVLHDINiALRHAAQVIMLKEGKLIDSGDpqtviHAESLAQ 233
Cdd:cd03249 171 DAESEKLVQEALDR--AMKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGT-----HDELMAQ 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
13-169 |
2.28e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 71.37 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLS-IS-TLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLP-----FARRAEKVVFlpq 84
Cdd:PRK11153 12 PQGGRTIHALNnVSlHIPAGEIFGVIGASGAGKSTLIRCINLLERpTSGRVLVDGQDLTALSekelrKARRQIGMIF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 85 slpqslpQgvHLQVLESVVVAQ------RASGAGQNQAQA--IALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRP 156
Cdd:PRK11153 89 -------Q--HFNLLSSRTVFDnvalplELAGTPKAEIKArvTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170
....*....|...
gi 545166817 157 ALLLLDEPLSALD 169
Cdd:PRK11153 160 KVLLCDEATSALD 172
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-183 |
3.31e-14 |
|
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: 68.33 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 16 RRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLnrasgeaWLNEENLLSLPfarRAEKVVFLPQsLPQsLPQGVh 95
Cdd:cd03223 14 RVLLKDLSF-EIKPGDRLLITGPSGTGKSSLFRALAGL-------WPWGSGRIGMP---EGEDLLFLPQ-RPY-LPLGT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 96 lqvlesvvvaqrasgagqnqaqaialLEELgiahLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFH 175
Cdd:cd03223 80 --------------------------LREQ----LIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
....*...
gi 545166817 176 VMDVVSRE 183
Cdd:cd03223 130 LYQLLKEL 137
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-169 |
5.08e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLlslpfarRAEKVVFL 82
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNA-GELVQIEGPNGAGKTSLLRILAGLARpDAGEVLWQGEPI-------RRQRDEYH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQSLPQSLPQGVH--LQVLESVVVAQRASGAgQNQAQAIALLEELGIA---HLAMNYldsLSGGQKQLVGLAQSLIRRPA 157
Cdd:PRK13538 74 QDLLYLGHQPGIKteLTALENLRFYQRLHGP-GDDEALWEALAQVGLAgfeDVPVRQ---LSAGQQRRVALARLWLTRAP 149
|
170
....*....|..
gi 545166817 158 LLLLDEPLSALD 169
Cdd:PRK13538 150 LWILDEPFTAID 161
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-233 |
5.39e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.01 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKR--RIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALaglNRA----SGEAWLNEENLLSLPFA--RR 75
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSL-QIKAGEKVALLGRTGCGKSTLLQLL---TRAwdpqQGEILLNGQPIADYSEAalRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 76 AEKVVflpqslpqslPQGVHL---QVLESVVVAQrasgAGQNQAQAIALLEELGIAHLAMNY--LDS--------LSGGQ 142
Cdd:PRK11160 415 AISVV----------SQRVHLfsaTLRDNLLLAA----PNASDEALIEVLQQVGLEKLLEDDkgLNAwlgeggrqLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 143 KQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMvtLVVLHDINiALRHAAQVIMLKEGKLIDSGDp 222
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTV--LMITHRLT-GLEQFDRICVMDNGQIIEQGT- 556
|
250
....*....|.
gi 545166817 223 qtviHAESLAQ 233
Cdd:PRK11160 557 ----HQELLAQ 563
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-169 |
5.71e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.92 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSISTLPRGEVTVLlGPNGCGKSTLLRALAGLNRAS-GEAWLNEenllslpfarrAEKVVFLPQSlPQSLPQ 92
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVL-GLNGAGKSTLLRIMAGVDKEFeGEARPAP-----------GIKVGYLPQE-PQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 93 gvhLQVLESVVVAQRASGAGQNQAQAI------------ALLEELG-----IAHL-----------AMNYL--------- 135
Cdd:PRK11819 85 ---KTVRENVEEGVAEVKAALDRFNEIyaayaepdadfdALAAEQGelqeiIDAAdawdldsqleiAMDALrcppwdakv 161
|
170 180 190
....*....|....*....|....*....|....
gi 545166817 136 DSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
30-223 |
6.62e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 70.91 E-value: 6.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 30 GEVTVLLGPNGCGKSTLLRALAGLNRA-SGE--------AWLNEENLLSLpfarRAEKVVFLPQSLpQSLPqgvHLQVLE 100
Cdd:PRK10535 34 GEMVAIVGASGSGKSTLMNILGCLDKPtSGTyrvagqdvATLDADALAQL----RREHFGFIFQRY-HLLS---HLTAAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 101 SVVVAQRASGAGQNQ--AQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMD 178
Cdd:PRK10535 106 NVEVPAVYAGLERKQrlLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 545166817 179 VVsRETRRRNMVTLVVLHDINIAlRHAAQVIMLKEGKLIDSGDPQ 223
Cdd:PRK10535 186 IL-HQLRDRGHTVIIVTHDPQVA-AQAERVIEIRDGEIVRNPPAQ 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-225 |
6.86e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 69.65 E-value: 6.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 32 VTVLLGPNGCGKSTLLRALAGLNRASGEAWL--------NEENLLSLpfaRRAEKVVFlpqslpQSLPQGVHLQVLES-V 102
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwqgkpldySKRGLLAL---RQQVATVF------QDPEQQIFYTDIDSdI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 103 VVAQRASGAGQNQA-----QAIALLEELGIAHlamNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVM 177
Cdd:PRK13638 100 AFSLRNLGVPEAEItrrvdEALTLVDAQHFRH---QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 545166817 178 DVVSRETRRRNMVtLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK13638 177 AIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-226 |
7.23e-14 |
|
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: 70.84 E-value: 7.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENLLSLPFARRAEKVVFLPQ-------S 85
Cdd:TIGR01842 329 GKKPTLRGISFS-LQAGEALAIIGPSGSGKSTLARLIVGIwPPTSGSVRLDGADLKQWDRETFGKHIGYLPQdvelfpgT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 86 LPQSLPQGVHLQVLESVVVAQRASGAgqnqaqaiallEELgIAHLAMNYlDS--------LSGGQKQLVGLAQSLIRRPA 157
Cdd:TIGR01842 408 VAENIARFGENADPEKIIEAAKLAGV-----------HEL-ILRLPDGY-DTvigpggatLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 158 LLLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINiALRHAAQVIMLKEGKLIDSGDPQTVI 226
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAI-KALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-225 |
7.47e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 69.10 E-value: 7.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRA---LAGLN---RASGEAWLNEENLLSLPF----ARRAEKVVFl 82
Cdd:PRK14267 14 YGSNHVIKGVDLK-IPQNGVFALMGPSGCGKSTLLRTfnrLLELNeeaRVEGEVRLFGRNIYSPDVdpieVRREVGMVF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 pqSLPQSLPqgvHLQVLESVVVAQRASGAGQNQAQ----------AIALLEElgIAHLAMNYLDSLSGGQKQLVGLAQSL 152
Cdd:PRK14267 92 --QYPNPFP---HLTIYDNVAIGVKLNGLVKSKKEldervewalkKAALWDE--VKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545166817 153 IRRPALLLLDEPLSALDLNYQFHVMDVVSRetRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFE--LKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-169 |
8.07e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.36 E-value: 8.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENllsLPFARRAEKVVFL 82
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAA-GEALVLTGPNGSGKTTLLRLIAGLLPpAAGTIKLDGGD---IDDPDVAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 -------PqslpqslpqgvHLQVLESVVVAQRASGAGQNQ-AQAIALLEELGIAHLAMNYldsLSGGQKQLVGLAQSLIR 154
Cdd:PRK13539 79 ghrnamkP-----------ALTVAENLEFWAAFLGGEELDiAAALEAVGLAPLAHLPFGY---LSAGQKRRVALARLLVS 144
|
170
....*....|....*
gi 545166817 155 RPALLLLDEPLSALD 169
Cdd:PRK13539 145 NRPIWILDEPTAALD 159
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-231 |
8.33e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.64 E-value: 8.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRASGEAWLNEENLLSLPFARRAEKVVFLPQSlPQsLPQGvhlQVLESVVVA 105
Cdd:PRK11174 372 TLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESWRKHLSWVGQN-PQ-LPHG---TLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 106 Q-RASGAGQNQAQAIALLEELgIAHLAmNYLDS--------LSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHV 176
Cdd:PRK11174 447 NpDASDEQLQQALENAWVSEF-LPLLP-QGLDTpigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545166817 177 MDVVSRETRRRnmVTLVVLHDINiALRHAAQVIMLKEGKLIDSGDPQTVIHAESL 231
Cdd:PRK11174 525 MQALNAASRRQ--TTLMVTHQLE-DLAQWDQIWVMQDGQIVQQGDYAELSQAGGL 576
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
29-225 |
1.00e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 68.95 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENL----LSLPFARRAEKVVFlpQSLPQSL--PQgvhlqVLES 101
Cdd:PRK13639 27 KGEMVALLGPNGAGKSTLFLHFNGILKpTSGEVLIKGEPIkydkKSLLEVRKTVGIVF--QNPDDQLfaPT-----VEED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 102 VVVAQRASGAGQNQAQ--AIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDV 179
Cdd:PRK13639 100 VAFGPLNLGLSKEEVEkrVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 545166817 180 VSrETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK13639 180 LY-DLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
30-225 |
1.08e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.00 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 30 GEVTVLLGPNGCGKSTLLRALAGLN-RASGEAWLNEENLLS------LPFARRAEKVVFlpqSLPQSlpQGVHLQVLESV 102
Cdd:PRK13649 33 GSYTAFIGHTGSGKSTIMQLLNGLHvPTQGSVRVDDTLITStsknkdIKQIRKKVGLVF---QFPES--QLFEETVLKDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 103 VVAQRASGAGQNQAQAIALlEELGIAHLAMNYLD----SLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMD 178
Cdd:PRK13649 108 AFGPQNFGVSQEEAEALAR-EKLALVGISESLFEknpfELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMT 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545166817 179 VVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK13649 187 LF-KKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-233 |
1.18e-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: 68.41 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGK--RRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENL--LSLPFARRAEK 78
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISL-DIPAGETVALVGPSGSGKSTLVNLIPRFyDVDSGRILIDGHDVrdYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 79 VVflpqslpqslPQGVHL---QVLESVVVAQRasGAGQNQAQAIAlleELGIAHLAMNYLD------------SLSGGQK 143
Cdd:cd03251 80 LV----------SQDVFLfndTVAENIAYGRP--GATREEVEEAA---RAANAHEFIMELPegydtvigergvKLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 144 QLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNmvTLVVLHDINiALRHAAQVIMLKEGKLIDSGDpq 223
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRT--TFVIAHRLS-TIENADRIVVLEDGKIVERGT-- 219
|
250
....*....|
gi 545166817 224 tviHAESLAQ 233
Cdd:cd03251 220 ---HEELLAQ 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-228 |
1.32e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.88 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 19 IEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRASGEAWLNEENLLSlpfaRRAEKVVFLPQslpQSLPQGVHL-- 96
Cdd:PRK10261 32 VRNLSFS-LQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLR----RRSRQVIELSE---QSAAQMRHVrg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 97 ----------------------QVLESVVVAQrasGAGQNQAQAIA--LLEELGIAHLAM---NYLDSLSGGQKQLVGLA 149
Cdd:PRK10261 104 admamifqepmtslnpvftvgeQIAESIRLHQ---GASREEAMVEAkrMLDQVRIPEAQTilsRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 150 QSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHA 228
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-228 |
1.34e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.12 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGK----RRIIEHLSIStLPRGEVTVLLGPNGCGKS----TLLRALAG--LNRASGEAWLNEENLLSLPFA 73
Cdd:PRK15134 6 LAIENLSVAFRQqqtvRTVVNDVSLQ-IEAGETLALVGESGSGKSvtalSILRLLPSppVVYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 74 R----RAEKVVFLPQSLPQSLP--QGVHLQVLEsVVVAQRASGAGQNQAQAIALLEELGIAHLAM---NYLDSLSGGQKQ 144
Cdd:PRK15134 85 TlrgvRGNKIAMIFQEPMVSLNplHTLEKQLYE-VLSLHRGMRREAARGEILNCLDRVGIRQAAKrltDYPHQLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 145 LVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQT 224
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAAT 243
|
....
gi 545166817 225 VIHA 228
Cdd:PRK15134 244 LFSA 247
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-225 |
1.49e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 68.48 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 18 IIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWL--NEENLLSLPFARRAEKVVFlpqslpqslpQGV 94
Cdd:PRK13632 24 ALKNVSF-EINEGEYVAILGHNGSGKSTISKILTGLLKPqSGEIKIdgITISKENLKEIRKKIGIIF----------QNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 95 HLQVLESVVVAQRASG-----AGQNQAQAIalleelgIAHLAM-----NYLD----SLSGGQKQLVGLAQSLIRRPALLL 160
Cdd:PRK13632 93 DNQFIGATVEDDIAFGlenkkVPPKKMKDI-------IDDLAKkvgmeDYLDkepqNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545166817 161 LDEPLSALDLNYQFHVMDVVsRETRRRNMVTLV-VLHDINIALRhAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIM-VDLRKTRKKTLIsITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEI 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-233 |
1.54e-13 |
|
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: 68.03 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 12 GYG-KRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENL--LSLPFARRAEKVVflpqslp 87
Cdd:cd03253 9 AYDpGRPVLKDVSF-TIPAGKKVAIVGPSGSGKSTILRLLFRFyDVSSGSILIDGQDIreVTLDSLRRAIGVV------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 88 qslPQGVhlqVL--ESVVVAQRASGAGQNQAQAIALLEELGIAHLAMNYLDS-----------LSGGQKQLVGLAQSLIR 154
Cdd:cd03253 81 ---PQDT---VLfnDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 155 RPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNmvTLVVLHDINIALrHAAQVIMLKEGKLIDSGDpqtviHAESLAQ 233
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRT--TIVIAHRLSTIV-NADKIIVLKDGRIVERGT-----HEELLAK 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-169 |
1.66e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 68.27 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLN------RASGEAWLNEENLLS-----LPFARRAEKVVF 81
Cdd:PRK14243 20 YGSFLAVKNVWLD-IPKNQITAFIGPSGCGKSTILRCFNRLNdlipgfRVEGKVTFHGKNLYApdvdpVEVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 82 LPQSLPQSlpqgvhlqVLESVVVAQRASGAGQNQAQAI-------ALLEELGiAHLAMNYLdSLSGGQKQLVGLAQSLIR 154
Cdd:PRK14243 99 KPNPFPKS--------IYDNIAYGARINGYKGDMDELVerslrqaALWDEVK-DKLKQSGL-SLSGGQQQRLCIARAIAV 168
|
170
....*....|....*
gi 545166817 155 RPALLLLDEPLSALD 169
Cdd:PRK14243 169 QPEVILMDEPCSALD 183
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
26-222 |
2.81e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.11 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNE----ENLLSLPFARRAEKVVFLPQSLPQslpqgvhLQVLE 100
Cdd:PRK13645 33 TFKKNKVTCVIGTTGSGKSTMIQLTNGLiISETGQTIVGDyaipANLKKIKEVKRLRKEIGLVFQFPE-------YQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 101 SVVVAQRASGA---GQNQAQAIALLEEL-GIAHLAMNYLD----SLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNY 172
Cdd:PRK13645 106 ETIEKDIAFGPvnlGENKQEAYKKVPELlKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545166817 173 QFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDP 222
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-223 |
3.76e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.26 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAG---------LNRASGEAWLNeenLLSLPFAR 74
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYP-GEVLGIVGESGSGKTTLLNALSArlapdagevHYRMRDGQLRD---LYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 75 RAekvvFLPQS----LPQSLPQGVHLQVLESVVVAQRASGAGQN-----QAQAIALLEELGIAhlaMNYLDSL----SGG 141
Cdd:PRK11701 83 RR----RLLRTewgfVHQHPRDGLRMQVSAGGNIGERLMAVGARhygdiRATAGDWLERVEID---AARIDDLpttfSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 142 QKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSG- 220
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGl 235
|
....*....
gi 545166817 221 ------DPQ 223
Cdd:PRK11701 236 tdqvldDPQ 244
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
26-220 |
3.88e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.60 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENLLSLPFARRAEKVVFLPQ-------SLPQSLPQGVHLQ 97
Cdd:TIGR00958 503 TLHPGEVVALVGPSGSGKSTVAALLQNLyQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQepvlfsgSVRENIAYGLTDT 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 98 VLESVVVAQRASGAgqnqAQAIALLEElGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVM 177
Cdd:TIGR00958 583 PDEEIMAAAKAANA----HDFIMEFPN-GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQ 657
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 545166817 178 DVVSRETRrrnmVTLVVLHDINIAlRHAAQVIMLKEGKLIDSG 220
Cdd:TIGR00958 658 ESRSRASR----TVLLIAHRLSTV-ERADQILVLKKGSVVEMG 695
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-164 |
4.04e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 67.06 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 17 RIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEK---------VVFLPQS- 85
Cdd:COG4674 24 KALNDLSL-YVDPGELRVIIGPNGAGKTTLMDVITGKTRpDSGSVLFGGTDLTGLDEHEIARLgigrkfqkpTVFEELTv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 86 ---LPQSLPQGVhlqvleSVVVAQRASGAGQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLD 162
Cdd:COG4674 103 fenLELALKGDR------GVFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLD 176
|
..
gi 545166817 163 EP 164
Cdd:COG4674 177 EP 178
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
30-226 |
4.71e-13 |
|
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: 68.29 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 30 GEVTVLLGPNGCGKSTLLRALAGLNRAS--------GEAWLNEENLLSLPFARRAEKVVFLPQ--------SLPQSLPQG 93
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIAGVLEPTsgevnvrvGDEWVDMTKPGPDGRGRAKRYIGILHQeydlyphrTVLDNLTEA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 94 VHLQ------VLESVVVAQrasGAGQNQAQAIALLEElgiahlamnYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSA 167
Cdd:TIGR03269 390 IGLElpdelaRMKAVITLK---MVGFDEEKAEEILDK---------YPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 168 LDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVI 226
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-200 |
4.96e-13 |
|
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: 67.01 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 28 PR-GEVTVLLGPNGCGKSTLLRALAG-----LNRASGE-AW---LNE--ENLLSLPFARRAE---KVVFLPQSLPQsLPQ 92
Cdd:cd03236 23 PReGQVLGLVGPNGIGKSTALKILAGklkpnLGKFDDPpDWdeiLDEfrGSELQNYFTKLLEgdvKVIVKPQYVDL-IPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 93 GVHLQVLEsvvVAQRASGAGQNQAqaiaLLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNY 172
Cdd:cd03236 102 AVKGKVGE---LLKKKDERGKLDE----LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|....*...
gi 545166817 173 QFHVMDVVSRETRRRNMVtLVVLHDINI 200
Cdd:cd03236 175 RLNAARLIRELAEDDNYV-LVVEHDLAV 201
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
29-227 |
5.61e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.07 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAGLNRAS-GEAWLNEENLLS------LPFARRAEKVVFlpqSLPQSlpQGVHLQVLES 101
Cdd:PRK13643 31 KGSYTALIGHTGSGKSTLLQHLNGLLQPTeGKVTVGDIVVSStskqkeIKPVRKKVGVVF---QFPES--QLFEETVLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 102 VVVAQRASGAGQNQAQAIALlEELGIAHLAMNYLD----SLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVM 177
Cdd:PRK13643 106 VAFGPQNFGIPKEKAEKIAA-EKLEMVGLADEFWEkspfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545166817 178 DVVSRETRRRNMVTLVVlHDINIALRHAAQVIMLKEGKLIDSGDPQTVIH 227
Cdd:PRK13643 185 QLFESIHQSGQTVVLVT-HLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
12-226 |
6.22e-13 |
|
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: 68.23 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 12 GYGkRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKVVFLPQSlpqsl 90
Cdd:TIGR01193 484 GYG-SNILSDISL-TIKMNSKTTIVGMSGSGKSTLAKLLVGFFQArSGEILLNGFSLKDIDRHTLRQFINYLPQE----- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 91 PQGVHLQVLESVVVAQRASGAGQNQAQAIALLE-ELGIAHLAMNYLD-------SLSGGQKQLVGLAQSLIRRPALLLLD 162
Cdd:TIGR01193 557 PYIFSGSILENLLLGAKENVSQDEIWAACEIAEiKDDIENMPLGYQTelseegsSISGGQKQRIALARALLTDSKVLILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545166817 163 EPLSALDLNYQfhvMDVVSRETRRRNMVTLVVLHDINIALRhAAQVIMLKEGKLIDSGDPQTVI 226
Cdd:TIGR01193 637 ESTSNLDTITE---KKIVNNLLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-223 |
8.72e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.33 E-value: 8.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNEENLLSLPFAR--RAEKVVFLpqsLPQSL 90
Cdd:PRK11831 18 GNRCIFDNISL-TVPRGKITAIMGPSGIGKTTLLRLIGGqIAPDHGEILFDGENIPAMSRSRlyTVRKRMSM---LFQSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 91 PQGVHLQVLESVVVAQRAsgagQNQAQAIAL-------LEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDE 163
Cdd:PRK11831 94 ALFTDMNVFDNVAYPLRE----HTQLPAPLLhstvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 164 PLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQ 223
Cdd:PRK11831 170 PFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQ 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
26-178 |
1.01e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 66.53 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFA-----RRAEKVVFlpQSLPQSL-PQGVHLQV 98
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETpTGGELYYQGQDLLKADPEaqkllRQKIQIVF--QNPYGSLnPRKKVGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 99 LESVVVAQRASGAGQNQAQAIALLEELGI-AHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHV- 176
Cdd:PRK11308 115 LEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVl 194
|
....*
gi 545166817 177 ---MD 178
Cdd:PRK11308 195 nlmMD 199
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-221 |
1.13e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRAS-GEAWLNEENLLSLPFARRAEKVVFL 82
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLH-INQGEIVTLIGANGAGKTTLLGTLCGDPRATsGRIVFDGKDITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 pqslpqsLPQGvhLQVLESVVVAQRASGAG-----QNQAQAIALLEEL--GIAHLAMNYLDSLSGGQKQLVGLAQSLIRR 155
Cdd:PRK11614 85 -------VPEG--RRVFSRMTVEENLAMGGffaerDQFQERIKWVYELfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545166817 156 PALLLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLI--DSGD 221
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTI-EQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVleDTGD 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-223 |
1.15e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 66.34 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 19 IEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRAS-GEAWLNEENLLSL---PFARRAEKVVFLPQSLPQSlpqgv 94
Cdd:PRK13646 23 IHDVNT-EFEQGKYYAIVGQTGSGKSTLIQNINALLKPTtGTVTVDDITITHKtkdKYIRPVRKRIGMVFQFPES----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 95 hlQVLESVVVAQRASGAG-------QNQAQAIALLEELGIAHLAMNYLD-SLSGGQKQLVGLAQSLIRRPALLLLDEPLS 166
Cdd:PRK13646 97 --QLFEDTVEREIIFGPKnfkmnldEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 167 ALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQ 223
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPK 231
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
27-214 |
1.34e-12 |
|
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: 65.04 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 27 LPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNEENLLSLPF----ARRAEKVVFLPQSlPQSLPQGVHLQV-LE 100
Cdd:cd03290 24 IPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNKNESEPSFeatrSRNRYSVAYAAQK-PWLLNATVEENItFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 101 SVVVAQRASG-----AGQNQAQAIALLEELGIAHLAMNyldsLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFH 175
Cdd:cd03290 103 SPFNKQRYKAvtdacSLQPDIDLLPFGDQTEIGERGIN----LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 545166817 176 VMDVVSRETRRRNMVTLV-VLHDINIaLRHAAQVIMLKEG 214
Cdd:cd03290 179 LMQEGILKFLQDDKRTLVlVTHKLQY-LPHADWIIAMKDG 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-226 |
1.94e-12 |
|
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: 66.89 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNEEnllslpfarraekVVFLPQslpQSLPQGVHLQvlESVVV 104
Cdd:TIGR00957 660 SIPEGALVAVVGQVGCGKSSLLSALLAeMDKVEGHVHMKGS-------------VAYVPQ---QAWIQNDSLR--ENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 105 A-QRASGAGQNQAQAIALLEELG---------IAHLAMNyldsLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQF 174
Cdd:TIGR00957 722 GkALNEKYYQQVLEACALLPDLEilpsgdrteIGEKGVN----LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 545166817 175 HVMD-VVSRETRRRNMVTLVVLHDINIaLRHAAQVIMLKEGKLIDSGDPQTVI 226
Cdd:TIGR00957 798 HIFEhVIGPEGVLKNKTRILVTHGISY-LPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-194 |
2.45e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 15 KRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLnrasgeawlneenllsLPFARRAEKVVFLPQSLPQSLPqgv 94
Cdd:COG2401 42 ERYVLRDLNL-EIEPGEIVLIVGASGSGKSTLLRLLAGA----------------LKGTPVAGCVDVPDNQFGREAS--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 95 hlqVLESVvvaqrasGAGQNQAQAIALLEELGIAHlAMNYL---DSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLN 171
Cdd:COG2401 102 ---LIDAI-------GRKGDFKDAVELLNAVGLSD-AVLWLrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|...
gi 545166817 172 YQFHVMDVVSRETRRRNmVTLVV 194
Cdd:COG2401 171 TAKRVARNLQKLARRAG-ITLVV 192
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
27-225 |
2.68e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 65.24 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 27 LPRGEVTVLLGPNGCGKSTLLRALAGLNRAS-------GEAWLNEENLLSLPFARRAEKVVFlpqSLPQSlpQGVHLQVL 99
Cdd:PRK13641 30 LEEGSFVALVGHTGSGKSTLMQHFNALLKPSsgtitiaGYHITPETGNKNLKKLRKKVSLVF---QFPEA--QLFENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 100 ESVVVAQRASGAGQNQA--QAIALLEELGIAHLAMNYLD-SLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHV 176
Cdd:PRK13641 105 KDVEFGPKNFGFSEDEAkeKALKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 545166817 177 MDVVSRETRRRNMVTLVVlHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK13641 185 MQLFKDYQKAGHTVILVT-HNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
30-222 |
3.28e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.11 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 30 GEVTVLLGPNGCGKSTLLRALAGLN------------------RASGEAWLNEENLLSLPFARRAEK---------VVFl 82
Cdd:PRK13651 33 GEFIAIIGQTGSGKTTFIEHLNALLlpdtgtiewifkdeknkkKTKEKEKVLEKLVIQKTRFKKIKKikeirrrvgVVF- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 pqslpqslpQGVHLQVLES-----VVVAQRASGAGQNQAQAIALlEELGIAHLAMNYLD----SLSGGQKQLVGLAQSLI 153
Cdd:PRK13651 112 ---------QFAEYQLFEQtiekdIIFGPVSMGVSKEEAKKRAA-KYIELVGLDESYLQrspfELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 154 RRPALLLLDEPLSALDLNYQFHVMDVVSrETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDP 222
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILEIFD-NLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDT 249
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
26-222 |
4.45e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.34 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGL-------NRASGEAwLNEENLLSLpfaRRAEKVVFlpqslpqslpQGVHLQV 98
Cdd:PRK13642 29 SITKGEWVSIIGQNGSGKSTTARLIDGLfeefegkVKIDGEL-LTAENVWNL---RRKIGMVF----------QNPDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 99 LESVVVAQRASGAGQNQAQAIALLEELGIAHLAMNYLD-------SLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLN 171
Cdd:PRK13642 95 VGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDfktrepaRLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 545166817 172 YQFHVMDVVSRETRRRNMVTLVVLHDINIALRhAAQVIMLKEGKLIDSGDP 222
Cdd:PRK13642 175 GRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAP 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
9-231 |
5.61e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.05 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 9 LCAGY-GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNEENLL--SLPFARRAEKVVF--- 81
Cdd:PRK13652 9 LCYSYsGSKEALNNINF-IAPRNSRIAVIGPNGAGKSTLFRHFNGiLKPTSGSVLIRGEPITkeNIREVRKFVGLVFqnp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 82 ----LPQSLPQSLPQGVHLQVLESVVVAQRASGAgqnqaqaialLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPA 157
Cdd:PRK13652 88 ddqiFSPTVEQDIAFGPINLGLDEETVAHRVSSA----------LHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545166817 158 LLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESL 231
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-220 |
5.68e-12 |
|
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: 63.32 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSGLTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEEnlLSLPFarrAEKV 79
Cdd:cd03220 20 LKKLGILGRKGEVGEFWALKDVSF-EVPRGERIGLIGRNGAGKSTLLRLLAGIYPPdSGTVTVRGR--VSSLL---GLGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 80 VFLPQslpqslpqgvhLQVLESVVVAQRASGAGQNQAQA----IALLEELGiahlamNYLDS----LSGGQKQLVGLAQS 151
Cdd:cd03220 94 GFNPE-----------LTGRENIYLNGRLLGLSRKEIDEkideIIEFSELG------DFIDLpvktYSSGMKARLAFAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 152 LIRRPALLLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSG 220
Cdd:cd03220 157 TALEPDILLIDEVLAVGDAAFQEKCQRRL-RELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
30-234 |
6.38e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.91 E-value: 6.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 30 GEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENL----LSLPFARRAEKVVFlpqslpqslpQGVHLQVLESVVV 104
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKPtSGKIIIDGVDItdkkVKLSDIRKKVGLVF----------QYPEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 105 AQRASGA---GQNQAQAIALLEElgiahlAMN--------YLD----SLSGGQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:PRK13637 103 KDIAFGPinlGLSEEEIENRVKR------AMNivgldyedYKDkspfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545166817 170 LNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVI-HAESLAQV 234
Cdd:PRK13637 177 PKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFkEVETLESI 242
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
26-228 |
7.20e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.66 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENLLSLPFARRAEKVVFLPQSLPQSL-PQGVHLQVLESVV 103
Cdd:PRK15112 35 TLREGQTLAIIGENGSGKSTLAKMLAGMiEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTSLnPRQRISQILDFPL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 104 VAQRASGAGQNQAQAIALLEELGI-AHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSR 182
Cdd:PRK15112 115 RLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLE 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 545166817 183 ETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHA 228
Cdd:PRK15112 195 LQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-228 |
1.03e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.67 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGyGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRasgEAW--------LNEENLLSL-PFAR 74
Cdd:PRK15093 9 LTIEFKTSD-GWVKAVDRVSM-TLTEGEIRGLVGESGSGKSLIAKAICGVTK---DNWrvtadrmrFDDIDLLRLsPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 75 RaeKVVFLPQSL----PQSL---PQGVHLQVLESVVVA-------QRAsgaGQNQAQAIALLEELGI-AHLAM--NYLDS 137
Cdd:PRK15093 84 R--KLVGHNVSMifqePQSCldpSERVGRQLMQNIPGWtykgrwwQRF---GWRKRRAIELLHRVGIkDHKDAmrSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 138 LSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLI 217
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250
....*....|.
gi 545166817 218 DSGDPQTVIHA 228
Cdd:PRK15093 239 ETAPSKELVTT 249
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
30-200 |
1.68e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.19 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 30 GEVTVLLGPNGCGKSTLLRALAGLNRAS-GE-AWLNEEnLLSLPFARRAEK-----VVFlpQSLPQSL------------ 90
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKATdGEvAWLGKD-LLGMKDDEWRAVrsdiqMIF--QDPLASLnprmtigeiiae 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 91 PQGVHLQVLESVVVAQRAsgagQNQAQAIALLEELgiahlaMN-YLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:PRK15079 124 PLRTYHPKLSRQEVKDRV----KAMMLKVGLLPNL------INrYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190
....*....|....*....|....*....|.
gi 545166817 170 LNYQFHVMDVVSRETRRRNMVTLVVLHDINI 200
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAV 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
26-225 |
1.70e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.95 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGL----------------NRASGEAWLNEENLLSLPFARRAEKVVFLPQSLPQS 89
Cdd:PRK13631 48 TFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvgdiyigDKKNNHELITNPYSKKIKNFKELRRRVSMVFQFPEY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 90 lpQGVHLQVLESVVVAQRASGAGQNQAQAIA--LLEELGiahLAMNYLD----SLSGGQKQLVGLAQSLIRRPALLLLDE 163
Cdd:PRK13631 128 --QLFKDTIEKDIMFGPVALGVKKSEAKKLAkfYLNKMG---LDDSYLErspfGLSGGQKRRVAIAGILAIQPEILIFDE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545166817 164 PLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK13631 203 PTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-226 |
1.93e-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: 63.67 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR---ASGE-----------AWLNEENLLS 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISF-TIEEGEVLGILGRSGAGKSVLMHVLRGMDQyepTSGRiiyhvalcekcGYVERPSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 70 LPFAR-----RAEKVVF--LPQSLPQSLPQ--GVHLQ----------VLESVVVAQRASGAGQNQA--QAIALLEELGIA 128
Cdd:TIGR03269 80 EPCPVcggtlEPEEVDFwnLSDKLRRRIRKriAIMLQrtfalygddtVLDNVLEALEEIGYEGKEAvgRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 129 HLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQV 208
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*...
gi 545166817 209 IMLKEGKLIDSGDPQTVI 226
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVV 257
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-171 |
2.73e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.97 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAG---LNRASGEAWLNEENLLSLPFARRAEKVV 80
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLS-INKGEIHAIMGPNGSGKSTLSKVIAGhpaYKILEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 81 FLPQSLPQSLPqGVHLQVLESVVVAQRASGAGQNQAQAIALLE----ELGIAHLAMNYL-----DSLSGGQKQLVGLAQS 151
Cdd:CHL00131 87 FLAFQYPIEIP-GVSNADFLRLAYNSKRKFQGLPELDPLEFLEiineKLKLVGMDPSFLsrnvnEGFSGGEKKRNEILQM 165
|
170 180
....*....|....*....|
gi 545166817 152 LIRRPALLLLDEPLSALDLN 171
Cdd:CHL00131 166 ALLDSELAILDETDSGLDID 185
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-231 |
3.55e-11 |
|
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: 61.35 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 18 IIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAGLNRASGEAWL---NEENLLSLPFARRAEKVV-----FLPQSLPQS 89
Cdd:cd03252 17 ILDNISLRIKP-GEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLvdgHDLALADPAWLRRQVGVVlqenvLFNRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 90 LPQGVHLQVLESVVVAQRASGAgqnqAQAIALLEElGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:cd03252 96 IALADPGMSMERVIEAAKLAGA----HDFISELPE-GYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545166817 170 LNYQFHVMDVVSRETRRRNMVtlVVLHDINiALRHAAQVIMLKEGKLIDSGDPQTVIHAESL 231
Cdd:cd03252 171 YESEHAIMRNMHDICAGRTVI--IIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAENGL 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-220 |
3.58e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 62.67 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLralAGLNRA----SGEAWLNEENLLSLPFA--RRAEKVVF-----L 82
Cdd:PRK13657 346 NSRQGVEDVSFEAKP-GQTVAIVGPTGAGKSTLI---NLLQRVfdpqSGRILIDGTDIRTVTRAslRRNIAVVFqdaglF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQSLPQSLPQGVHLQVLESVVVAQRAsgagqnqAQAIALLE--ELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLL 160
Cdd:PRK13657 422 NRSIEDNIRVGRPDATDEEMRAAAER-------AQAHDFIErkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 161 LDEPLSALDLNYQFHVMDVVsrETRRRNMVTLVVLHDINiALRHAAQVIMLKEGKLIDSG 220
Cdd:PRK13657 495 LDEATSALDVETEAKVKAAL--DELMKGRTTFIIAHRLS-TVRNADRILVFDNGRVVESG 551
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-173 |
3.62e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.72 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAGlNRASGEAwlneeNLLSLpFARR----------AEKVVFL 82
Cdd:PRK10938 270 YNDRPILHNLSWQVNP-GEHWQIVGPNGAGKSTLLSLITG-DHPQGYS-----NDLTL-FGRRrgsgetiwdiKKHIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 83 PQSLpqSLPQGVHLQVL--------ESVVVAQRASGAGQNQAQAiaLLEELGI-AHLAMNYLDSLSGGQKQLVGLAQSLI 153
Cdd:PRK10938 342 SSSL--HLDYRVSTSVRnvilsgffDSIGIYQAVSDRQQKLAQQ--WLDILGIdKRTADAPFHSLSWGQQRLALIVRALV 417
|
170 180
....*....|....*....|.
gi 545166817 154 RRPALLLLDEPLSALD-LNYQ 173
Cdd:PRK10938 418 KHPTLLILDEPLQGLDpLNRQ 438
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-231 |
5.92e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.16 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRASGEAWL----NEENLLSLPFARRAEKVVF-------LPQSLPQSLPQGV 94
Cdd:PRK13644 24 VIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgiDTGDFSKLQGIRKLVGIVFqnpetqfVGRTVEEDLAFGP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 95 HLQVLESVVVAQRASGAgqnqaqaialLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQF 174
Cdd:PRK13644 104 ENLCLPPIEIRKRVDRA----------LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 175 HVMDVVSReTRRRNMVTLVVLHDINiALRHAAQVIMLKEGKLIDSGDPQTVIHAESL 231
Cdd:PRK13644 174 AVLERIKK-LHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-200 |
6.76e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 6.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 27 LP---RGEVTVLLGPNGCGKSTLLRALAG-----LNRASGEA-WlnEENL-------LSLPFARRAE---KVVFLPQ--- 84
Cdd:PRK13409 93 LPipkEGKVTGILGPNGIGKTTAVKILSGelipnLGDYEEEPsW--DEVLkrfrgteLQNYFKKLYNgeiKVVHKPQyvd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 85 SLPQSLpQGVHLQVLESVvvaqrasgagqNQAQAI-ALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDE 163
Cdd:PRK13409 171 LIPKVF-KGKVRELLKKV-----------DERGKLdEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....*..
gi 545166817 164 PLSALDLNYQFHVMDVVSRETRRRNMvtLVVLHDINI 200
Cdd:PRK13409 239 PTSYLDIRQRLNVARLIRELAEGKYV--LVVEHDLAV 273
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-225 |
8.36e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.45 E-value: 8.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 16 RRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLN-------RASGEAWLNEENLLSLPFARRAEKVVFLPQSlPQ 88
Cdd:PRK14246 23 KAILKDITIK-IPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQ-PN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 89 SLPqgvHLQVLESVVVAQRASGAgQNQAQAIALLEE----LGIAHLAMNYLDS----LSGGQKQLVGLAQSLIRRPALLL 160
Cdd:PRK14246 101 PFP---HLSIYDNIAYPLKSHGI-KEKREIKKIVEEclrkVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545166817 161 LDEPLSALDLNYQFHVMDVVSRetRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITE--LKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-228 |
9.76e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.10 E-value: 9.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 12 GYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEawlneenllslpfARRAEKVVFLpqsLpqSL 90
Cdd:COG1134 35 RREEFWALKDVSF-EVERGESVGIIGRNGAGKSTLLKLIAGILEPtSGR-------------VEVNGRVSAL---L--EL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 91 PQGVH--LQVLESVvvaqRASGA--GQNQAQAIALLE------ELGiahlamNYLD----SLSGGQKQLVGLAQSLIRRP 156
Cdd:COG1134 96 GAGFHpeLTGRENI----YLNGRllGLSRKEIDEKFDeivefaELG------DFIDqpvkTYSSGMRARLAFAVATAVDP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545166817 157 ALLLLDEPLSALDLNYQFHVMDVVsrETRRRNMVTLV-VLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHA 228
Cdd:COG1134 166 DILLVDEVLAVGDAAFQKKCLARI--RELRESGRTVIfVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-169 |
1.21e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 30 GEVTVLLGPNGCGKSTLLRALAGLNRASG-------------------EAWLNEENLLsLPFARRAEKVVFLPQ-SLPQS 89
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftgtilannrkptkqilkrTGFVTQDDIL-YPHLTVRETLVFCSLlRLPKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 90 LPQGVHLQVLESVVvaqrasgagqnqaqaiallEELGIAH-----LAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEP 164
Cdd:PLN03211 173 LTKQEKILVAESVI-------------------SELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
....*
gi 545166817 165 LSALD 169
Cdd:PLN03211 234 TSGLD 238
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-240 |
1.30e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEEnllSLPFARRAEK----VVFLPQSLpQSLPQgvhLQVLESVV 103
Cdd:PRK11288 29 AGQVHALMGENGAGKSTLLKILSGNYQPdAGSILIDGQ---EMRFASTTAAlaagVAIIYQEL-HLVPE---MTVAENLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 104 VAQRASGAG-----QNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMD 178
Cdd:PRK11288 102 LGQLPHKGGivnrrLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFR 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545166817 179 VVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESLAQ---------VYGVRGR 240
Cdd:PRK11288 182 VI-RELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDRDQLVQamvgreigdIYGYRPR 251
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-221 |
1.59e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.95 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 27 LPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLnEENLLSLP------FARRAEKVVFLPQSLPQSLPQGVHLQVL 99
Cdd:PTZ00243 683 VPRGKLTVVLGATGSGKSTLLQSLLSqFEISEGRVWA-ERSIAYVPqqawimNATVRGNILFFDEEDAARLADAVRVSQL 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 100 ESVVvAQRASGAgqnqaqaialleELGIAHLAMNyldsLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLnyqfHVMDV 179
Cdd:PTZ00243 762 EADL-AQLGGGL------------ETEIGEKGVN----LSGGQKARVSLARAVYANRDVYLLDDPLSALDA----HVGER 820
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 545166817 180 VSRET---RRRNMVTLVVLHDINIaLRHAAQVIMLKEGKLIDSGD 221
Cdd:PTZ00243 821 VVEECflgALAGKTRVLATHQVHV-VPRADYVVALGDGRVEFSGS 864
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-223 |
1.94e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.45 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 30 GEVTVLLGPNGCGKSTLLRALAGLNRA----SGEAWLNEENLLSLPFARRAEKV----VFLPqslpqslpqgvHLQVLES 101
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkgSGSVLLNGMPIDAKEMRAISAYVqqddLFIP-----------TLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 102 VVVA-----QRASGAGQNQAQAIALLEELGI---AHL---AMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDL 170
Cdd:TIGR00955 120 LMFQahlrmPRRVTKKEKRERVDEVLQALGLrkcANTrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545166817 171 NYQFHVMDVVsRETRRRNMVTLVVLHDINIAL-RHAAQVIMLKEGKLIDSGDPQ 223
Cdd:TIGR00955 200 FMAYSVVQVL-KGLAQKGKTIICTIHQPSSELfELFDKIILMAEGRVAYLGSPD 252
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-196 |
2.05e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 60.53 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 18 IIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLnrasgeaWLNEENLLSLPfarRAEKVVFLPQSLPQSLpQGVHLQ 97
Cdd:TIGR00954 467 LIESLSFE-VPSGNNLLICGPNGCGKSSLFRILGEL-------WPVYGGRLTKP---AKGKLFYVPQRPYMTL-GTLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 98 VL--ESVVVAQRAsgaGQNQAQAIALLEELGIAHL--------AM-NYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLS 166
Cdd:TIGR00954 535 IIypDSSEDMKRR---GLSDKDLEQILDNVQLTHIlereggwsAVqDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|
gi 545166817 167 ALDLNyqfhVMDVVSRETRRRNMVTLVVLH 196
Cdd:TIGR00954 612 AVSVD----VEGYMYRLCREFGITLFSVSH 637
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
28-233 |
2.10e-10 |
|
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: 60.50 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 28 PRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENL--LSLPFARRAEKVVflpqslpqslPQGVHLqvLESVVV 104
Cdd:TIGR02203 356 EPGETVALVGRSGSGKSTLVNLIPRFyEPDSGQILLDGHDLadYTLASLRRQVALV----------SQDVVL--FNDTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 105 AQRASGAGQNQAQAiaLLEELGIAHLAMNYLDS---------------LSGGQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:TIGR02203 424 NNIAYGRTEQADRA--EIERALAAAYAQDFVDKlplgldtpigengvlLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545166817 170 LNYQFHVMDVVSRETRRRNmvTLVVLHDINiALRHAAQVIMLKEGKLIDSGdpqtvIHAESLAQ 233
Cdd:TIGR02203 502 NESERLVQAALERLMQGRT--TLVIAHRLS-TIEKADRIVVMDDGRIVERG-----THNELLAR 557
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-222 |
2.75e-10 |
|
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: 60.41 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 16 RRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENL-LSLPFARraekvvflpQSL---PQSL 90
Cdd:TIGR01257 943 RPAVDRLNI-TFYENQITAFLGHNGAGKTTTLSILTGLlPPTSGTVLVGGKDIeTNLDAVR---------QSLgmcPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 91 PQGVHLQVLESVVVAQRASGAGQNQAQ--AIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSAL 168
Cdd:TIGR01257 1013 ILFHHLTVAEHILFYAQLKGRSWEEAQleMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545166817 169 DLNYQFHVMDVVSRETRRRNMVtlVVLHDINIALRHAAQVIMLKEGKLIDSGDP 222
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRSGRTII--MSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-200 |
2.91e-10 |
|
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: 60.18 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 27 LP---RGEVTVLLGPNGCGKSTLLRALAG-----LNRASGEA-WlnEENL-------LSLPFARRAE---KVVFLPQ--- 84
Cdd:COG1245 93 LPvpkKGKVTGILGPNGIGKSTALKILSGelkpnLGDYDEEPsW--DEVLkrfrgteLQDYFKKLANgeiKVAHKPQyvd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 85 SLPQSLpQGVHLQVLESVvvAQRASgagqnqaqAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEP 164
Cdd:COG1245 171 LIPKVF-KGTVRELLEKV--DERGK--------LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....*.
gi 545166817 165 LSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINI 200
Cdd:COG1245 240 SSYLDIYQRLNVARLI-RELAEEGKYVLVVEHDLAI 274
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-197 |
3.29e-10 |
|
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: 59.68 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 3 GLTINALCAGY-GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNEENLLSLPFARRAEKVV 80
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSL-DLPPGERVAILGPSGSGKSTLLATLAGlLDPLQGEVTLDGVPVSSLDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 81 FLPQSlpqslpqgVHL---QVLESVVVAqRASGAGqnqAQAIALLEELGIAHLAMNYLD-----------SLSGGQKQLV 146
Cdd:TIGR02868 413 VCAQD--------AHLfdtTVRENLRLA-RPDATD---EELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 545166817 147 GLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRnmVTLVVLHD 197
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHH 529
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-171 |
3.59e-10 |
|
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: 59.56 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 6 INALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARR----AEKVV 80
Cdd:TIGR03719 325 AENLTKAFGDKLLIDDLSFK-LPPGGIVGVIGPNGAGKSTLFRMITGQEQPdSGTIEIGETVKLAYVDQSRdaldPNKTV 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 81 FlpqslpQSLPQGVHLQVLESVVVAQRA-------SGAGQNQaqaialleelgiahlamnYLDSLSGGQKQLVGLAQSLI 153
Cdd:TIGR03719 404 W------EEISGGLDIIKLGKREIPSRAyvgrfnfKGSDQQK------------------KVGQLSGGERNRVHLAKTLK 459
|
170
....*....|....*...
gi 545166817 154 RRPALLLLDEPLSALDLN 171
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVE 477
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-226 |
6.03e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 58.76 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGlnrASGEAW--------LNEENLLSLPFARRAE------KV 79
Cdd:COG4170 18 GRVKAVDRVSL-TLNEGEIRGLVGESGSGKSLIAKAICG---ITKDNWhvtadrfrWNGIDLLKLSPRERRKiigreiAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 80 VFL-PQS-LPQSLPQGvhlQVLESVVVAQRASG-----AGQNQAQAIALLEELGIA-HLA-MN-YLDSLSGGQKQLVGLA 149
Cdd:COG4170 94 IFQePSScLDPSAKIG---DQLIEAIPSWTFKGkwwqrFKWRKKRAIELLHRVGIKdHKDiMNsYPHELTEGECQKVMIA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 150 QSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVI 226
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQIL 247
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-236 |
6.18e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.07 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAGL---NRASGEAWLNEENLLSLPFARRAEKVV 80
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRP-GECVGLCGENGAGKSTLMKILSGVyphGTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 81 FLpqsLPQSLPQGVHLQVLESVVVAQRASGAGQNQA------QAIALLEELGIAhlAMN---YLDSLSGGQKQLVGLAQS 151
Cdd:TIGR02633 81 VI---IHQELTLVPELSVAENIFLGNEITLPGGRMAynamylRAKNLLRELQLD--ADNvtrPVGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 152 LIRRPALLLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTVIHAESL 231
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDII-RDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDII 234
|
....*
gi 545166817 232 AQVYG 236
Cdd:TIGR02633 235 TMMVG 239
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
29-225 |
6.73e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.18 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRAL-AGLNRASGEAWL------NEENLLSLpfaRRAEKVVFlpqslpqslpQGVHLQVLES 101
Cdd:PRK13633 35 KGEFLVILGRNGSGKSTIAKHMnALLIPSEGKVYVdgldtsDEENLWDI---RNKAGMVF----------QNPDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 102 VVVAQRASGAgqnqaqaiallEELGIA-------------------------HLamnyldsLSGGQKQLVGLAQSLIRRP 156
Cdd:PRK13633 102 IVEEDVAFGP-----------ENLGIPpeeirervdeslkkvgmyeyrrhapHL-------LSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 157 ALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINIALRhAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
29-223 |
9.95e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.82 E-value: 9.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAW-----LNEENLLSLpfaRRAEKVVFlpQSlPQSlpQGVHLQVLESV 102
Cdd:PRK13650 32 QGEWLSIIGHNGSGKSTTVRLIDGLLEAeSGQIIidgdlLTEENVWDI---RHKIGMVF--QN-PDN--QFVGATVEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 103 VVAQRASGAGQNQA-----QAIALLeelGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVM 177
Cdd:PRK13650 104 AFGLENKGIPHEEMkervnEALELV---GMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 545166817 178 DVVSRETRRRNMVTLVVLHDIN-IALrhAAQVIMLKEGKLIDSGDPQ 223
Cdd:PRK13650 181 KTIKGIRDDYQMTVISITHDLDeVAL--SDRVLVMKNGQVESTSTPR 225
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-242 |
1.38e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.38 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGY--GKRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAGLNRASGE------AWlneeNLLSLPFARR 75
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEG-GQRVGLLGRTGSGKSTLLSALLRLLSTEGEiqidgvSW----NSVTLQTWRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 76 AEKVVflpqslpqslPQGVHlqVLESVVVAQRASGAGQNQAQAIALLEELGIAHLAMNYLDSL-----------SGGQKQ 144
Cdd:TIGR01271 1293 AFGVI----------PQKVF--IFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQ 1360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 145 LVGLAQSLIRRPALLLLDEPLSALD-LNYQfhvmdvVSRETRRRNMVTLVVL---HDINiALRHAAQVIMLKEGKLIDSG 220
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDpVTLQ------IIRKTLKQSFSNCTVIlseHRVE-ALLECQQFLVIEGSSVKQYD 1433
|
250 260
....*....|....*....|...
gi 545166817 221 DPQTVIHAESL-AQVYGVRGRVE 242
Cdd:TIGR01271 1434 SIQKLLNETSLfKQAMSAADRLK 1456
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-222 |
1.48e-09 |
|
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: 56.35 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 18 IIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENLLSLPFARRAEKVVFLPQ-------SLPQS 89
Cdd:cd03244 19 VLKNISFSIKP-GEKVGIVGRTGSGKSSLLLALFRLvELSSGSILIDGVDISKIGLHDLRSRISIIPQdpvlfsgTIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 90 L-PQGVH-----LQVLESVvvaqrasgagqNQAQAIALLEELGIAHLAMNYlDSLSGGQKQLVGLAQSLIRRPALLLLDE 163
Cdd:cd03244 98 LdPFGEYsdeelWQALERV-----------GLKEFVESLPGGLDTVVEEGG-ENLSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 164 PLSALDLNYQFHVMDVVsrETRRRNMVTLVVLHDINIALrHAAQVIMLKEGKLIDSGDP 222
Cdd:cd03244 166 ATASVDPETDALIQKTI--REAFKDCTVLTIAHRLDTII-DSDRILVLDKGRVVEFDSP 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
26-225 |
2.46e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.15 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEKVV---FlpqslpqslpQGVHL----Q 97
Cdd:PRK11300 27 EVREQEIVSLIGPNGAGKTTVFNCLTGFYKpTGGTILLRGQHIEGLPGHQIARMGVvrtF----------QHVRLfremT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 98 VLESVVVAQ-RASGAG----------------QNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLL 160
Cdd:PRK11300 97 VIENLLVAQhQQLKTGlfsgllktpafrraesEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545166817 161 LDEPLSAL------DLNyqfHVMDVVSREtrrRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK11300 177 LDEPAAGLnpketkELD---ELIAELRNE---HNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-220 |
2.72e-09 |
|
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: 55.35 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 12 GYGKRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAGL--NRASGEAWLNEENLLSLPFARRAE-KVVFLPQslpq 88
Cdd:cd03233 16 GRSKIPILKDFSGVVKP-GEMVLVLGRPGSGCSTLLKALANRteGNVSVEGDIHYNGIPYKEFAEKYPgEIIYVSE---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 89 slpQGVH---LQVLESVVVAQRASGagqNQaqaialleelgiahlamnYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPL 165
Cdd:cd03233 91 ---EDVHfptLTVRETLDFALRCKG---NE------------------FVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 545166817 166 SALDLNYQFH---VMDVVSRETRRRNMVTLvvLHDINIALRHAAQVIMLKEGKLIDSG 220
Cdd:cd03233 147 RGLDSSTALEilkCIRTMADVLKTTTFVSL--YQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-225 |
2.97e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 19 IEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENLLSLPFA-----RRAEKVVFLPQSLPQSLPQ 92
Cdd:PRK10261 340 VEKVSFDLWP-GETLSLVGESGSGKSTTGRALLRLvESQGGEIIFNGQRIDTLSPGklqalRRDIQFIFQDPYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 93 GVHLQVLESVVVAQRASGAGQnQAQAIALLEELGI-AHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLN 171
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKAA-AARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 545166817 172 YQFHVMDVVSRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-215 |
3.13e-09 |
|
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: 54.89 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAGLNRASGEAwlneenlLSLPFARraekVVFLPQSLpqslpqgvhlqvlesvvvaqra 108
Cdd:cd03222 24 EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN-------DEWDGIT----PVYKPQYI---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 109 sgagqnqaqaialleelgiahlamnyldSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRN 188
Cdd:cd03222 71 ----------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|....*..
gi 545166817 189 MVTLVVLHDInIALRHAAQVIMLKEGK 215
Cdd:cd03222 123 KTALVVEHDL-AVLDYLSDRIHVFEGE 148
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-217 |
4.70e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 55.86 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 15 KRRIIEHLS-IS-TLPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNEENllslPFARRAE-----KVVF----- 81
Cdd:COG4586 31 EYREVEAVDdISfTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVPTSGEVRVLGYV----PFKRRKEfarriGVVFgqrsq 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 82 LPQSLPqslpqgvhlqVLESVVVAQRASGAGQNQ-AQAIALL-EELGIAHLamnyLD----SLSGGQKQLVGLAQSLIRR 155
Cdd:COG4586 107 LWWDLP----------AIDSFRLLKAIYRIPDAEyKKRLDELvELLDLGEL----LDtpvrQLSLGQRMRCELAAALLHR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545166817 156 PALLLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTlVVL--HDIN--IALrhAAQVIMLKEGKLI 217
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFL-KEYNRERGTT-ILLtsHDMDdiEAL--CDRVIVIDHGRII 234
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
30-171 |
9.26e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 9.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 30 GEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENllslpfARRAEKVVFLP--QSLPQSLPQgvhLQVLESV--VV 104
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVeSGQIQIDGKT------ATRGDRSRFMAylGHLPGLKAD---LSTLENLhfLC 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 105 AQRASGAGQNQAQAIALleeLGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLN 171
Cdd:PRK13543 108 GLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
138-211 |
1.19e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 1.19e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545166817 138 LSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVVLHDINiALRHAAQVIML 211
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVL 652
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
30-225 |
1.24e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 30 GEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEKVVFLpqsLPQSLPQGVHLQVLESVVVAQRA 108
Cdd:PRK09700 31 GEIHALLGENGAGKSTLMKVLSGIHEpTKGTITINNINYNKLDHKLAAQLGIGI---IYQELSVIDELTVLENLYIGRHL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 109 SGA--GQN-------QAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSAL---DLNYQFHV 176
Cdd:PRK09700 108 TKKvcGVNiidwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLI 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 545166817 177 MdvvsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDPQTV 225
Cdd:PRK09700 188 M----NQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-231 |
1.74e-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: 54.95 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 18 IIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLPFARRAEKVVFLPQSlpqslpqgvhl 96
Cdd:TIGR00957 1301 VLRHINV-TIHGGEKVGIVGRTGAGKSSLTLGLFRINEsAEGEIIIDGLNIAKIGLHDLRFKITIIPQD----------- 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 97 QVLESVVVAQRASGAGQNQAQAIALLEEL------------GIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEP 164
Cdd:TIGR00957 1369 PVLFSGSLRMNLDPFSQYSDEEVWWALELahlktfvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 165 LSALDLNYQFHVMDVVsrETRRRNMVTLVVLHDINIALRHaAQVIMLKEGKLIDSGDPQTVIHAESL 231
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTI--RTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQQRGI 1512
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-236 |
2.42e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.26 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAGLNR---ASGEAWLNEENLLSLPFARRAEKVV 80
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRP-GEVHAIMGPNGSGKSTLSATLAGREDyevTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 81 FLPQSLPQSLPqGVHLQV-LESVVVAQRA--SGAGQNQAQAIALLEElGIAHLAM--NYLD-----SLSGGQKQLVGLAQ 150
Cdd:PRK09580 81 FMAFQYPVEIP-GVSNQFfLQTALNAVRSyrGQEPLDRFDFQDLMEE-KIALLKMpeDLLTrsvnvGFSGGEKKRNDILQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 151 SLIRRPALLLLDEPLSALDLNYQFHVMDVVSrETRRRNMVTLVVLHDINIaLRHAAQ--VIMLKEGKLIDSGDPQTVIHA 228
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVN-SLRDGKRSFIIVTHYQRI-LDYIKPdyVHVLYQGRIVKSGDFTLVKQL 236
|
....*...
gi 545166817 229 ESlaQVYG 236
Cdd:PRK09580 237 EE--QGYG 242
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-168 |
4.00e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.49 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEEnllSLPF-----ARRAekvvflpqslpqslpqG---VH- 95
Cdd:COG3845 27 TVRPGEIHALLGENGAGKSTLMKILYGLYQPdSGEILIDGK---PVRIrsprdAIAL----------------GigmVHq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 96 -------LQVLESVVVAQRASGAGQ-NQAQAIALLEELgIAHLAMN-----YLDSLSGGQKQLVGLAQSLIRRPALLLLD 162
Cdd:COG3845 88 hfmlvpnLTVAENIVLGLEPTKGGRlDRKAARARIREL-SERYGLDvdpdaKVEDLSVGEQQRVEILKALYRGARILILD 166
|
....*.
gi 545166817 163 EPLSAL 168
Cdd:COG3845 167 EPTAVL 172
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-168 |
4.57e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.52 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKVVFL-PQSlPQSLPqgvHLQVLESVV 103
Cdd:PRK15439 33 TLHAGEVHALLGGNGAGKSTLMKIIAGIVPPdSGTLEIGGNPCARLTPAKAHQLGIYLvPQE-PLLFP---NLSVKENIL 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 104 VAQRASGAGQNQAQaiALLEELGiAHLAmnyLDSLSG----GQKQLVGLAQSLIRRPALLLLDEPLSAL 168
Cdd:PRK15439 109 FGLPKRQASMQKMK--QLLAALG-CQLD---LDSSAGslevADRQIVEILRGLMRDSRILILDEPTASL 171
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-171 |
4.57e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 35 LLGPNGCGKSTLLRALAG-LNRASGEAWlneenllslpfarRAEKV---VFlpqslPQSLPQGVHLQVLESVVVAQRASG 110
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGeLQPSSGTVF-------------RSAKVrmaVF-----SQHHVDGLDLSSNPLLYMMRCFPG 601
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545166817 111 AGQNQAQAiaLLEELGIA-HLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLN 171
Cdd:PLN03073 602 VPEQKLRA--HLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD 661
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
138-233 |
5.67e-08 |
|
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: 53.29 E-value: 5.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 138 LSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNmvTLVvlhdinIALR-----HAAQVIMLK 212
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRT--TLV------IAHRlstivDADEILVLE 566
|
90 100
....*....|....*....|.
gi 545166817 213 EGKLIDSGDpqtviHAESLAQ 233
Cdd:COG5265 567 AGRIVERGT-----HAELLAQ 582
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-171 |
6.29e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNEENLL------SLPFARRA 76
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVP-GSRIGLLGRNGAGKSTLIKLLAGeLAPVSGEIGLAKGIKLgyfaqhQLEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 77 EKVVflpQSLPQSLPQGVHLQVLESVvvaqraSGAGQNQAQAIALLEElgiahlamnyldsLSGGQKQLVGLAQSLIRRP 156
Cdd:PRK10636 392 ESPL---QHLARLAPQELEQKLRDYL------GGFGFQGDKVTEETRR-------------FSGGEKARLVLALIVWQRP 449
|
170
....*....|....*
gi 545166817 157 ALLLLDEPLSALDLN 171
Cdd:PRK10636 450 NLLLLDEPTNHLDLD 464
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-213 |
6.46e-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: 50.82 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAglnrasgeawlneenllslpfarraekVVFLPQSLPQSLPQGVHLQVLESVVVA 105
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDAIG---------------------------LALGGAQSATRRRSGVKAGCIVAAVSA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 106 QRASgagqnqaqaialleelgiahlamnYLDSLSGGQKQLVGLA-----QSLIRRPaLLLLDEPLSALDLNYQFHVMDVV 180
Cdd:cd03227 70 ELIF------------------------TRLQLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAI 124
|
170 180 190
....*....|....*....|....*....|...
gi 545166817 181 SRETRRRNMVtLVVLHDINIALRHAAQVIMLKE 213
Cdd:cd03227 125 LEHLVKGAQV-IVITHLPELAELADKLIHIKKV 156
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-216 |
1.05e-07 |
|
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: 51.78 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGY--GKRRIIEHLSISTLPRGEVTvLLGPNGCGKSTLLRALAGLNRASGEAWLNEENLLSLPFA--RRA--- 76
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVG-LLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQkwRKAfgv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 77 --EKVVFLPQSLPQSL-PQGVH-----LQVLESVVVaqrASGAGQNQAQAIALLEELGIAhlamnyldsLSGGQKQLVGL 148
Cdd:cd03289 82 ipQKVFIFSGTFRKNLdPYGKWsdeeiWKVAEEVGL---KSVIEQFPGQLDFVLVDGGCV---------LSHGHKQLMCL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545166817 149 AQSLIRRPALLLLDEPLSALD-LNYQfhvmdvVSRETRRRNMVTLVVL---HDINiALRHAAQVIMLKEGKL 216
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDpITYQ------VIRKTLKQAFADCTVIlseHRIE-AMLECQRFLVIEENKV 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-164 |
1.22e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.43 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 13 YGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLnRA--SGEAWlneenLLSLPFARRAE------KVVFLPQ 84
Cdd:NF033858 11 YGKTVALDDVSLD-IPAGCMVGLIGPDGVGKSSLLSLIAGA-RKiqQGRVE-----VLGGDMADARHrravcpRIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 85 SLPQSL-PQgvhLQVLESVVVAQRASGAGQNQ-AQAIA-LLEELGIAhlamNYLD----SLSGGQKQLVGLAQSLIRRPA 157
Cdd:NF033858 84 GLGKNLyPT---LSVFENLDFFGRLFGQDAAErRRRIDeLLRATGLA----PFADrpagKLSGGMKQKLGLCCALIHDPD 156
|
....*..
gi 545166817 158 LLLLDEP 164
Cdd:NF033858 157 LLILDEP 163
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
28-231 |
1.30e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 28 PRGEVTVLLGPNGCGKSTLLRALAGLNRAS-GEAWLneenllslpF----------ARRaeKVVFLPQSLpqSLPQgvHL 96
Cdd:NF033858 290 RRGEIFGFLGSNGCGKSTTMKMLTGLLPASeGEAWL---------FgqpvdagdiaTRR--RVGYMSQAF--SLYG--EL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 97 QVLESVVVAQRASGAGQNQAQA-IA-LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALdlnyqf 174
Cdd:NF033858 355 TVRQNLELHARLFHLPAAEIAArVAeMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGV------ 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545166817 175 hvmDVVSR--------ETRRRNMVTLVV-LHDIN-------IALRHAaqvimlkeGKLIDSGDPQTVI---HAESL 231
Cdd:NF033858 429 ---DPVARdmfwrlliELSREDGVTIFIsTHFMNeaercdrISLMHA--------GRVLASDTPAALVaarGAATL 493
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-222 |
1.39e-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: 50.49 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 4 LTINALCAGYGKR--RIIEHLSISTLPRGEVTVLlGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSLPFARRAEKVV 80
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIV-GRTGAGKSTLILALFRFLEAeEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 81 FLPQSlPQSLPQGVHLQV-------LESVVVAQRASGAGQNqaqaialleelgiahlamnyldsLSGGQKQLVGLAQSLI 153
Cdd:cd03369 86 IIPQD-PTLFSGTIRSNLdpfdeysDEEIYGALRVSEGGLN-----------------------LSQGQRQLLCLARALL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545166817 154 RRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTlvvlhdinIALR-----HAAQVIMLKEGKLIDSGDP 222
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILT--------IAHRlrtiiDYDKILVMDAGEVKEYDHP 207
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-171 |
2.10e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 2.10e-07
10 20 30
....*....|....*....|....*....|....*...
gi 545166817 134 YLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLN 171
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1392
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
17-51 |
2.62e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 50.38 E-value: 2.62e-07
10 20 30
....*....|....*....|....*....|....*
gi 545166817 17 RIIEHLSISTLPRGEVTVLLGPNGCGKSTLLRALA 51
Cdd:COG3950 12 RGFEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIA 46
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
136-232 |
2.86e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 136 DSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMvtLVVLHDINIALrHAAQVIMLKEGK 215
Cdd:PLN03232 1370 ENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTM--LVIAHRLNTII-DCDKILVLSSGQ 1446
|
90
....*....|....*..
gi 545166817 216 LIDSGDPQTVIHAESLA 232
Cdd:PLN03232 1447 VLEYDSPQELLSRDTSA 1463
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-164 |
3.08e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.79 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 12 GYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENL-LSLPFARRAEKVVFLPQS---- 85
Cdd:COG1129 261 GLSVGGVVRDVSF-SVRAGEILGIAGLVGAGRTELARALFGADPAdSGEIRLDGKPVrIRSPRDAIRAGIAYVPEDrkge 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 86 ---LPQSLPQGVHLQVLESVVVAQRASGAGQNQAqAIALLEELGI--AHLAMNyLDSLSGGQKQLVGLAQSLIRRPALLL 160
Cdd:COG1129 340 glvLDLSIRENITLASLDRLSRGGLLDRRRERAL-AEEYIKRLRIktPSPEQP-VGNLSGGNQQKVVLAKWLATDPKVLI 417
|
....
gi 545166817 161 LDEP 164
Cdd:COG1129 418 LDEP 421
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
115-220 |
3.15e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.50 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 115 QAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVsRETRRRNMVTLVV 194
Cdd:NF000106 122 RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV-RSMVRDGATVLLT 200
|
90 100
....*....|....*....|....*.
gi 545166817 195 LHDINIALRHAAQVIMLKEGKLIDSG 220
Cdd:NF000106 201 TQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-217 |
4.06e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGL---NRASGEAWLNEENLLSLPFARRAEK-VVFLPQSLpqSLPQgvHLQVLES 101
Cdd:PRK13549 27 KVRAGEIVSLCGENGAGKSTLMKVLSGVyphGTYEGEIIFEGEELQASNIRDTERAgIAIIHQEL--ALVK--ELSVLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 102 VVVAQRASGAG-----QNQAQAIALLEELGI----AHLAMNYldslSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNY 172
Cdd:PRK13549 103 IFLGNEITPGGimdydAMYLRAQKLLAQLKLdinpATPVGNL----GLGQQQLVEIAKALNKQARLLILDEPTASLTESE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 545166817 173 QFHVMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLI 217
Cdd:PRK13549 179 TAVLLDII-RDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
25-171 |
4.64e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 25 STLPRGEVTVLLGPNGCGKSTLLRALAGLNRASGE----------AWLNEEN-LLSLPfarrAEKVVF--------LPQS 85
Cdd:PRK10636 22 ATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGsytfpgnwqlAWVNQETpALPQP----ALEYVIdgdreyrqLEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 86 LPQSLPQG-------VHLQVlesvvvaqRASGAGQNQAQAIALLEELGIAHLAMNY-LDSLSGGQKQLVGLAQSLIRRPA 157
Cdd:PRK10636 98 LHDANERNdghaiatIHGKL--------DAIDAWTIRSRAASLLHGLGFSNEQLERpVSDFSGGWRMRLNLAQALICRSD 169
|
170
....*....|....
gi 545166817 158 LLLLDEPLSALDLN 171
Cdd:PRK10636 170 LLLLDEPTNHLDLD 183
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-234 |
8.34e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 8.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 18 IIEHLSISTlprGEVTVLLGPNGCGKSTLLRALAGlnrasgeawlnEENLLSLPFARRAEKVVFLpqslpqSLPQGVHL- 96
Cdd:PRK10938 20 QLPSLTLNA---GDSWAFVGANGSGKSALARALAG-----------ELPLLSGERQSQFSHITRL------SFEQLQKLv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 97 ----QVLESVVVAQRASGAGQNQAQAI-----------ALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLL 161
Cdd:PRK10938 80 sdewQRNNTDMLSPGEDDTGRTTAEIIqdevkdparceQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 162 DEPLSALDLNYQFHVMDVVSRETRRRNMVTLVV--LHDINIALRHAAqviMLKEGKLIDSGDPQTVI---------HAES 230
Cdd:PRK10938 160 DEPFDGLDVASRQQLAELLASLHQSGITLVLVLnrFDEIPDFVQFAG---VLADCTLAETGEREEILqqalvaqlaHSEQ 236
|
....
gi 545166817 231 LAQV 234
Cdd:PRK10938 237 LEGV 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-216 |
8.34e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.44 E-value: 8.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 15 KRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGL--NRASGEAWLNEENL-LSLPFARRAEKVVFLPQS------ 85
Cdd:TIGR02633 272 HRKRVDDVSFS-LRRGEILGVAGLVGAGRTELVQALFGAypGKFEGNVFINGKPVdIRNPAQAIRAGIAMVPEDrkrhgi 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 86 LPQ-SLPQGVHLQVLESVVVAQRASGAGQNQAqaiaLLEELGIAHLAMNYLD----SLSGGQKQLVGLAQSLIRRPALLL 160
Cdd:TIGR02633 351 VPIlGVGKNITLSVLKSFCFKMRIDAAAELQI----IGSAIQRLKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 545166817 161 LDEPLSALDLNYQFHVMDVVSrETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKL 216
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLIN-QLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-216 |
9.62e-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: 47.81 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENL-LSLPFARRAEKVVFLPQSlpqslpqgvhlqvlesvv 103
Cdd:cd03215 22 EVRAGEIVGIAGLVGNGQTELAEALFGLRPPaSGEITLDGKPVtRRSPRDAIRAGIAYVPED------------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 104 vaqRasgagqnqaQAIALLEELGIAH-LAMNYLdsLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVsR 182
Cdd:cd03215 84 ---R---------KREGLVLDLSVAEnIALSSL--LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLI-R 148
|
170 180 190
....*....|....*....|....*....|....
gi 545166817 183 ETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKL 216
Cdd:cd03215 149 ELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-240 |
1.31e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.95 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSG-LTINALCAGYGK-RRIIEHLSISTLPRGEVTvLLGPNGCGKSTLLRALAGLNRAS-GEAWLNEENLLSLPFarrae 77
Cdd:PRK10790 337 QSGrIDIDNVSFAYRDdNLVLQNINLSVPSRGFVA-LVGHTGSGKSTLASLLMGYYPLTeGEIRLDGRPLSSLSH----- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 78 kvvflpqslpQSLPQGVHLQVLESVVVAQR-----ASGAGQNQAQAIALLEELGIAHLAMNYLD-----------SLSGG 141
Cdd:PRK10790 411 ----------SVLRQGVAMVQQDPVVLADTflanvTLGRDISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 142 QKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVsRETRRRNmvTLVVlhdinIALR-----HAAQVIMLKEGKL 216
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHT--TLVV-----IAHRlstivEADTILVLHRGQA 552
|
250 260
....*....|....*....|....
gi 545166817 217 IDSGDpqtviHAESLAQvygvRGR 240
Cdd:PRK10790 553 VEQGT-----HQQLLAA----QGR 567
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
137-233 |
1.34e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.86 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 137 SLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVsrETRRRNMVTLVVLHDINiALRHAAQVIMLKEGKL 216
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAAL--DELQKNRTSLVIAHRLS-TIEKADEILVVEDGEI 556
|
90
....*....|....*..
gi 545166817 217 IDSGdpqtvIHAESLAQ 233
Cdd:PRK11176 557 VERG-----THAELLAQ 568
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
27-169 |
1.47e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 47.64 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 27 LPRGEVTVLLGPNGCGKSTLLRALAGL-NRASGEAWLNEENLlslpfarRAEKVVFLPQSLPQSLPQGV--HLQVLESVV 103
Cdd:PRK13540 24 LPAGGLLHLKGSNGAGKTTLLKLIAGLlNPEKGEILFERQSI-------KKDLCTYQKQLCFVGHRSGInpYLTLRENCL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545166817 104 VAQRASGAGQNQAQAIALLEelgIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:PRK13540 97 YDIHFSPGAVGITELCRLFS---LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-193 |
2.12e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.93 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLraLAGLnRASGEAWLNEenLLSLPFArraEKVVFLPQslpqslpqgvhLQvlesvvva 105
Cdd:cd03238 17 SIPLNVLVVVTGVSGSGKSTLV--NEGL-YASGKARLIS--FLPKFSR---NKLIFIDQ-----------LQ-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 106 qrasgagqnqaqaiaLLEELGIAHLAMNY-LDSLSGGQKQLVGLAQSLIRRP--ALLLLDEPLSALDLNYQFHVMDVVSR 182
Cdd:cd03238 70 ---------------FLIDVGLGYLTLGQkLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKG 134
|
170
....*....|.
gi 545166817 183 ETRRRNMVTLV 193
Cdd:cd03238 135 LIDLGNTVILI 145
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-171 |
3.35e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 9 LCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNE-----------ENLlslpfarRA 76
Cdd:PRK11819 330 LSKSFGDRLLIDDLSFS-LPPGGIVGIIGPNGAGKSTLFKMITGQEQPdSGTIKIGEtvklayvdqsrDAL-------DP 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 77 EKVVFlpqslpQSLPQGVHLQVLESVVVAQRA-------SGAGQNQaqaialleelgiahlamnYLDSLSGGQKQLVGLA 149
Cdd:PRK11819 402 NKTVW------EEISGGLDIIKVGNREIPSRAyvgrfnfKGGDQQK------------------KVGVLSGGERNRLHLA 457
|
170 180
....*....|....*....|..
gi 545166817 150 QSLIRRPALLLLDEPLSALDLN 171
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLDVE 479
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-169 |
3.49e-06 |
|
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: 48.09 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 19 IEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAWLNEENLLSlPFARRAEKVVFLPQ--SLPQSLPQGVH 95
Cdd:TIGR01257 1955 VDRLCVGVRP-GECFGLLGVNGAGKTTTFKMLTGdTTVTSGDATVAGKSILT-NISDVHQNMGYCPQfdAIDDLLTGREH 2032
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545166817 96 LQVLesvvvaQRASGAGQNQAQAIA--LLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:TIGR01257 2033 LYLY------ARLRGVPAEEIEKVAnwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-169 |
5.23e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.97 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 21 HLSISTLPrGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEENLLSL-PFARRAEKVVFLPQSLPQSlpqGVHLQV 98
Cdd:PRK15439 281 NISLEVRA-GEILGLAGVVGAGRTELAETLYGLRPArGGRIMLNGKEINALsTAQRLARGLVYLPEDRQSS---GLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 99 LES---VVVAQRASGAGQNQAQAIALLEE----LGIAhlaMNYLD----SLSGGQKQLVGLAQSLIRRPALLLLDEPLSA 167
Cdd:PRK15439 357 PLAwnvCALTHNRRGFWIKPARENAVLERyrraLNIK---FNHAEqaarTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
..
gi 545166817 168 LD 169
Cdd:PRK15439 434 VD 435
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-65 |
7.95e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 46.71 E-value: 7.95e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNRA-SGEAWLNEE 65
Cdd:COG4615 354 TIRRGELVFIVGGNGSGKSTLAKLLTGLYRPeSGEILLDGQ 394
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-230 |
1.26e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.27 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 18 IIEHLSISTLPRGEVTVLlGPNGCGKSTLLRALAGL-NRASGEAWLNEENLLSLPFARRAEKVVFLPQSlpqslpqgvhl 96
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIV-GRTGAGKSSMLNALFRIvELERGRILIDGCDISKFGLMDLRKVLGIIPQA----------- 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 97 QVLESVVVaqRASGAGQNQAQAIALLEELGIAHLA----MNYL----------DSLSGGQKQLVGLAQSLIRRPALLLLD 162
Cdd:PLN03130 1322 PVLFSGTV--RFNLDPFNEHNDADLWESLERAHLKdvirRNSLgldaevseagENFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545166817 163 EPLSALDLNYQFHVMDVVSRETRRRNMvtLVVLHDINIALrHAAQVIMLKEGKLIDSGDPQTVIHAES 230
Cdd:PLN03130 1400 EATAAVDVRTDALIQKTIREEFKSCTM--LIIAHRLNTII-DCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-169 |
1.45e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 1 MSGLTINALCAGYGKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALAGlnrasgEAWLNEENLL---SLPFARrae 77
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAEL-HIEDNERVCLVGRNGAGKSTLMKILNG------EVLLDDGRIIyeqDLIVAR--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 78 kvvfLPQSLPQSLPQGVHLQVLE---------------SVVVAQRASGAGQNQ-AQAIALLEELGIAHL----------- 130
Cdd:PRK11147 71 ----LQQDPPRNVEGTVYDFVAEgieeqaeylkryhdiSHLVETDPSEKNLNElAKLQEQLDHHNLWQLenrinevlaql 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 545166817 131 ---AMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:PRK11147 147 gldPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-211 |
1.76e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.52 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAGLnrasgeawlneenllslpFARRAEKVVFLpqSLPQSLPQGVHLQVLESVVVAQRA 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE------------------LGPPGGGVIYI--DGEDILEEVLDQLLLIIVGGKKAS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 109 SGAGQNQAQAIALLEElgiahlamnyldslsggqkqlvglaqsliRRPALLLLDEPLSALD----LNYQFHVMDVVSRET 184
Cdd:smart00382 61 GSGELRLRLALALARK-----------------------------LKPDVLILDEITSLLDaeqeALLLLLEELRLLLLL 111
|
170 180
....*....|....*....|....*..
gi 545166817 185 RRRNMVTLVVLHDINIALRHAAQVIML 211
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-169 |
2.21e-05 |
|
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: 44.16 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAGLNRA---SGEAWLNEEnLLSLPFARRaekVVFLPQslpqsl 90
Cdd:cd03232 18 GKRQLLNNISGYVKP-GTLTALMGESGAGKTTLLDVLAGRKTAgviTGEILINGR-PLDKNFQRS---TGYVEQ------ 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545166817 91 pQGVHLQVLeSVVVAQRASgagqnqaqaiALLEELGIAhlamnyldslsggQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:cd03232 87 -QDVHSPNL-TVREALRFS----------ALLRGLSVE-------------QRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-52 |
3.05e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.88 E-value: 3.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 545166817 4 LTINALCAGYGKRRIIEHLSIStLPRGEVTVLLGPNGCGKSTLLRALAG 52
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLL-LEAGERLAIIGENGVGKTTLLRTLVG 367
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-65 |
3.92e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.22 E-value: 3.92e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 545166817 17 RIIEHLSIStlPRGEVTVLLGPNGCGKSTLLRALAGLNRASGEAWLNEE 65
Cdd:COG3593 12 RSIKDLSIE--LSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEE 58
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
138-226 |
5.00e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 44.32 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 138 LSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVtlVVLHDINiALRHAAQVIMLKEGKLI 217
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVI--ISAHRLS-ALTEASEILVMQHGHIA 528
|
....*....
gi 545166817 218 DSGDPQTVI 226
Cdd:PRK10789 529 QRGNHDQLA 537
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-169 |
5.97e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAGlnR------ASGEAWLNEENLLSlPFARRAEKV----VFLP 83
Cdd:TIGR00956 774 EKRVILNNVDGWVKP-GTLTALMGASGAGKTTLLNVLAE--RvttgviTGGDRLVNGRPLDS-SFQRSIGYVqqqdLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 84 QS-------------LPQSLPQGVHLQVLESVvvaqrasgagqnqaqaIALLEelgiahlaM-NYLDSLSG--------G 141
Cdd:TIGR00956 850 TStvreslrfsaylrQPKSVSKSEKMEYVEEV----------------IKLLE--------MeSYADAVVGvpgeglnvE 905
|
170 180
....*....|....*....|....*....
gi 545166817 142 QKQLVGLAQSLIRRPALLL-LDEPLSALD 169
Cdd:TIGR00956 906 QRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
136-229 |
6.80e-05 |
|
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: 42.97 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 136 DSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVvlHDINIALrHAAQVIMLKEGK 215
Cdd:cd03288 155 ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIA--HRVSTIL-DADLVLVLSRGI 231
|
90
....*....|....
gi 545166817 216 LIDSGDPQTVIHAE 229
Cdd:cd03288 232 LVECDTPENLLAQE 245
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-163 |
9.58e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.42 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSlpfARRAEKvvflpQSLPQSLPQGVHL--QVLESv 102
Cdd:PRK10522 345 TIKRGELLFLIGGNGSGKSTLAMLLTGLYQpQSGEILLDGKPVTA---EQPEDY-----RKLFSAVFTDFHLfdQLLGP- 415
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545166817 103 vvaqraSGAGQNQAQAIALLEELGIAH---LAMNYLD--SLSGGQKQLVGLAQSLIRRPALLLLDE 163
Cdd:PRK10522 416 ------EGKPANPALVEKWLERLKMAHkleLEDGRISnlKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
19-56 |
1.06e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.00 E-value: 1.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 545166817 19 IEHLSIS--------TLPRGEVTVLLGPNGCGKSTLLRALAGLNRA 56
Cdd:COG4637 2 ITRIRIKnfkslrdlELPLGPLTVLIGANGSGKSNLLDALRFLSDA 47
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
137-220 |
1.75e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.66 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 137 SLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVV--LHdiniALRHAAQVIMLKEG 214
Cdd:PLN03232 740 NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTnqLH----FLPLMDRIILVSEG 815
|
....*.
gi 545166817 215 KLIDSG 220
Cdd:PLN03232 816 MIKEEG 821
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
32-60 |
2.46e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 2.46e-04
10 20
....*....|....*....|....*....
gi 545166817 32 VTVLLGPNGCGKSTLLRALAGLNRASGEA 60
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALV 29
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
138-220 |
2.53e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 138 LSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVV--LHdiniALRHAAQVIMLKEGK 215
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTnqLH----FLSQVDRIILVHEGM 816
|
....*
gi 545166817 216 LIDSG 220
Cdd:PLN03130 817 IKEEG 821
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-226 |
2.85e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 137 SLSGGQKQLVGLAQSLIRR---PALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVtLVVLHDINIaLRHAAQVIML-- 211
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTV-VVIEHNLDV-IKTADYIIDLgp 906
|
90
....*....|....*....
gi 545166817 212 ----KEGKLIDSGDPQTVI 226
Cdd:TIGR00630 907 eggdGGGTVVASGTPEEVA 925
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
9-59 |
2.85e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.86 E-value: 2.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 545166817 9 LCAGYGKRRIIEHLSiSTLPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGE 59
Cdd:PRK11147 325 VNYQIDGKQLVKDFS-AQVQRGDKIALIGPNGCGKTTLLKLMLGqLQADSGR 375
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-171 |
3.68e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 14 GKRRIIEHLSIsTLPRGEVTVLLGPNGCGKSTLLRALA---------------------GLNRASGEAWLN---EENLLS 69
Cdd:PLN03073 188 GGRDLIVDASV-TLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqilhveqevvGDDTTALQCVLNtdiERTQLL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 70 LPFARRAEKVVFLPQSLPQSLPQGVHLQVLESVVVAQRAS---------GAGQNQAQAIALLEELGI-AHLAMNYLDSLS 139
Cdd:PLN03073 267 EEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEeiykrleliDAYTAEARAASILAGLSFtPEMQVKATKTFS 346
|
170 180 190
....*....|....*....|....*....|..
gi 545166817 140 GGQKQLVGLAQSLIRRPALLLLDEPLSALDLN 171
Cdd:PLN03073 347 GGWRMRIALARALFIEPDLLLLDEPTNHLDLH 378
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
4-59 |
4.44e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 40.96 E-value: 4.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 4 LTINALcAGYGKRRIIEHLsistlpRGEVTVLLGPNGCGKSTLLRALA-GLNRASGE 59
Cdd:PRK00098 145 LELSAK-EGEGLDELKPLL------AGKVTVLAGQSGVGKSTLLNALApDLELKTGE 194
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
32-58 |
5.54e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 40.13 E-value: 5.54e-04
10 20 30
....*....|....*....|....*....|
gi 545166817 32 VTVLLGPNGCGKSTLLRALA---GLNRASG 58
Cdd:COG3910 39 VTFFVGENGSGKSTLLEAIAvaaGFNPEGG 68
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
27-82 |
6.36e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 39.67 E-value: 6.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 545166817 27 LPRGEVTVLLGPNGCGKSTLLRALAgLNRASGEAWLNEenllslPFARRAEKVVFL 82
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLA-AAVATGKPWLGG------PRVPEQGKVLYV 78
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
18-90 |
7.81e-04 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 39.56 E-value: 7.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545166817 18 IIEHLSISTLPRGEVTVLL--GPNGCGKSTLLRALAGLNRASGEAWLNEENLLSLPFARRAEKVVFLPQSLPQSL 90
Cdd:pfam03215 31 VQEWLDAMFLENAKHRILLisGPSGCGKSTVIKELSKELGPKYREWSNPTSFRSPPNQVTDFRGDCIVNSRFLSQ 105
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
17-50 |
8.65e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.40 E-value: 8.65e-04
10 20 30
....*....|....*....|....*....|....
gi 545166817 17 RIIEHLSIsTLPRGeVTVLLGPNGCGKSTLLRAL 50
Cdd:pfam13476 7 RSFRDQTI-DFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
117-227 |
9.39e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 117 QAIALLEELGIAHLAMNY-LDSLSGGQKQLVGLAQSLI---RRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVtL 192
Cdd:PRK00635 788 EKIHALCSLGLDYLPLGRpLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTV-V 866
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 545166817 193 VVLHDINIaLRHAAQVIML------KEGKLIDSGDPQTVIH 227
Cdd:PRK00635 867 IIEHNMHV-VKVADYVLELgpeggnLGGYLLASCSPEELIH 906
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-223 |
1.01e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.48 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 15 KRRIIEHLSISTLPrGEVTVLLGPNGCGKSTLLRALAG-----------------------LNRASGEAWLNEENLLSLP 71
Cdd:TIGR00956 73 TFDILKPMDGLIKP-GELTVVLGRPGSGCSTLLKTIASntdgfhigvegvitydgitpeeiKKHYRGDVVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 72 FARRAEKVVFL-----PQSLPQSLPQGVHLQVLESVVVAQrasgagqnqaqaialleeLGIAH-----LAMNYLDSLSGG 141
Cdd:TIGR00956 152 HLTVGETLDFAarcktPQNRPDGVSREEYAKHIADVYMAT------------------YGLSHtrntkVGNDFVRGVSGG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 142 QKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMDVVSRETRRRNMVTLVvlhdiniALRHAAQ--------VIMLKE 213
Cdd:TIGR00956 214 ERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLV-------AIYQCSQdayelfdkVIVLYE 286
|
250
....*....|
gi 545166817 214 GKLIDSGDPQ 223
Cdd:TIGR00956 287 GYQIYFGPAD 296
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
16-71 |
1.19e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.08 E-value: 1.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 16 RRIIEHLSISTLPRGeVTVLLGPNGCGKSTLLRALAGLNR-ASGEAWLNEENLLSLP 71
Cdd:PRK13541 13 QKNLFDLSITFLPSA-ITYIKGANGCGKSSLLRMIAGIMQpSSGNIYYKNCNINNIA 68
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
27-214 |
1.50e-03 |
|
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: 39.07 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 27 LPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAwlneenllslpfaRRAEKVVFLPQS---LPQSLPQGVHLQV---- 98
Cdd:cd03291 60 IEKGEMLAITGSTGSGKTSLLMLILGeLEPSEGKI-------------KHSGRISFSSQFswiMPGTIKENIIFGVsyde 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 99 --LESVVVA-QRASGAGQNQAQAIALLEELGIahlamnyldSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFH 175
Cdd:cd03291 127 yrYKSVVKAcQLEEDITKFPEKDNTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 545166817 176 VMD-----VVSRETRRrnMVTLVVLHdiniaLRHAAQVIMLKEG 214
Cdd:cd03291 198 IFEscvckLMANKTRI--LVTSKMEH-----LKKADKILILHEG 234
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
27-65 |
1.65e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 39.11 E-value: 1.65e-03
10 20 30
....*....|....*....|....*....|....*....
gi 545166817 27 LPRGEVTVLLGPNGCGKSTLLRALAgLNRASGEAWLNEE 65
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLA-AAVAAGGPWLGRR 47
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
132-191 |
1.87e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.57 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 132 MNYLDSLSGGQKQLVGLAqsLI-----RRPA-LLLLDEPLSALDL-------------------------NYQFHVMDVV 180
Cdd:pfam02463 1072 VKNLDLLSGGEKTLVALA--LIfaiqkYKPApFYLLDEIDAALDDqnvsrvanllkelsknaqfivislrEEMLEKADKL 1149
|
90
....*....|.
gi 545166817 181 SRETRRRNMVT 191
Cdd:pfam02463 1150 VGVTMVENGVS 1160
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
16-84 |
2.09e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 38.87 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 16 RRIIEHLSISTLPRGE----VTVLLGPNGCGKSTLLRALAGLNRASGEAwLNEENLLSLPFARRAE--------KVVFLP 83
Cdd:COG1106 11 RSFKDELTLSMVASGLrllrVNLIYGANASGKSNLLEALYFLRNLVLNS-SQPGDKLVEPFLLDSEsknepsefEILFLL 89
|
.
gi 545166817 84 Q 84
Cdd:COG1106 90 D 90
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
29-250 |
2.22e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAGLNRA---SGEAWLNEEnLLSLPFARRAEK--VVFLPQSL---PQslpqgvhLQVLE 100
Cdd:NF040905 26 EGEIHALCGENGAGKSTLMKVLSGVYPHgsyEGEILFDGE-VCRFKDIRDSEAlgIVIIHQELaliPY-------LSIAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 101 SVVVA-QRASGA----GQNQAQAIALLEELGIAHLAMNYLDSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFH 175
Cdd:NF040905 98 NIFLGnERAKRGvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545166817 176 VMDVVsRETRRRNMVTLVVLHDINIALRHAAQVIMLKEGKLIDSGDpqtvIHAESLAQVYGVRGRVercaqGRSM 250
Cdd:NF040905 178 LLDLL-LELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLD----CRADEVTEDRIIRGMV-----GRDL 242
|
|
| COG1373 |
COG1373 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
15-51 |
2.35e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440984 [Multi-domain] Cd Length: 405 Bit Score: 38.77 E-value: 2.35e-03
10 20 30
....*....|....*....|....*....|....*..
gi 545166817 15 KRRIIEHLsISTLPRGEVTVLLGPNGCGKSTLLRALA 51
Cdd:COG1373 6 KRKILDKL-LKLLDNRKAVVITGPRQVGKTTLLKQLA 41
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
27-214 |
2.87e-03 |
|
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: 38.74 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 27 LPRGEVTVLLGPNGCGKSTLLRALAG-LNRASGEAwlneenllslpfaRRAEKVVFLPQsLPQSLPQGVHLQVLESVVVA 105
Cdd:TIGR01271 449 LEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEGKI-------------KHSGRISFSPQ-TSWIMPGTIKDNIIFGLSYD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 106 QRASGAGQNQAQA---IALLEELGIAHLAMNYLdSLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHVMD---- 178
Cdd:TIGR01271 515 EYRYTSVIKACQLeedIALFPEKDKTVLGEGGI-TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEsclc 593
|
170 180 190
....*....|....*....|....*....|....*..
gi 545166817 179 -VVSRETRRrnMVTLVVLHdiniaLRHAAQVIMLKEG 214
Cdd:TIGR01271 594 kLMSNKTRI--LVTSKLEH-----LKKADKILLLHEG 623
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
29-59 |
2.93e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.76 E-value: 2.93e-03
10 20 30
....*....|....*....|....*....|..
gi 545166817 29 RGEVTVLLGPNGCGKSTLLRALAG-LNRASGE 59
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPeLVLATGE 115
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
26-60 |
3.33e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 3.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 545166817 26 TLPRGEVTVLLGPNGCGKSTLLRALAGL---------NRASGEA 60
Cdd:pfam13555 18 PIDPRGNTLLTGPSGSGKSTLLDAIQTLlvpakrarfNKAANAG 61
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
135-210 |
4.00e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.51 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545166817 135 LDSLSGGQKQLVGLAQSL------IRRPALLLLDEPLSALDlnyqfhvmdvvsrETRRRNMVTLVVLHdiniaLRHAAQV 208
Cdd:PRK03918 786 LTFLSGGERIALGLAFRLalslylAGNIPLLILDEPTPFLD-------------EERRRKLVDIMERY-----LRKIPQV 847
|
..
gi 545166817 209 IM 210
Cdd:PRK03918 848 II 849
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
138-169 |
4.48e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 38.06 E-value: 4.48e-03
10 20 30
....*....|....*....|....*....|..
gi 545166817 138 LSGGQKQLVGLAQSLIRRPALLLLDEPLSALD 169
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
4-59 |
5.84e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.75 E-value: 5.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 545166817 4 LTINALcAGYGKRRIIEHLsistlpRGEVTVLLGPNGCGKSTLLRALAG-LNRASGE 59
Cdd:pfam03193 87 LFVSAK-TGEGIEALKELL------KGKTTVLAGQSGVGKSTLLNALLPeLDLRTGE 136
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
30-56 |
6.87e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 37.26 E-value: 6.87e-03
10 20
....*....|....*....|....*..
gi 545166817 30 GEVTVLLGPNGCGKSTLLRALAGLNRA 56
Cdd:COG4938 20 KPLTLLIGPNGSGKSTLIQALLLLLQS 46
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
137-176 |
7.76e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 37.40 E-value: 7.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 545166817 137 SLSGGQKQLVGLAQSLIRRPALLLLDEPLSALDLNYQFHV 176
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEI 430
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
135-172 |
9.70e-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: 36.51 E-value: 9.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 545166817 135 LDSLSGGQKQLVGLaqSLIR-----RPA-LLLLDEPLSALDLNY 172
Cdd:cd03273 164 LTELSGGQRSLVAL--SLILalllfKPApMYILDEVDAALDLSH 205
|
|
| |
