|
Name |
Accession |
Description |
Interval |
E-value |
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-258 |
4.32e-73 |
|
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: 223.53 E-value: 4.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYG----GPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTklsRRDKKQF 84
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGES-FGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT---RRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 85 TADVRRVSQDGLAGIgiDPRWTVDRTLSAALKDARRAGRpsGRSVEDLLGDVALDARYAPRTIHSLSGGEKQRVALAVAL 164
Cdd:COG1124 78 RRRVQMVFQDPYASL--HPRHTVDRILAEPLRIHGLPDR--EERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 165 ATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFAgtapG 244
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA----G 229
|
250
....*....|....
gi 1199107692 245 ADHPSVRGLAEAAP 258
Cdd:COG1124 230 PKHPYTRELLAASL 243
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-258 |
2.84e-65 |
|
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: 211.69 E-value: 2.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 1 MSTTTTPILRATGLAAGYGGP-----DVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTK 75
Cdd:COG1123 253 AAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGET-LGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 76 LSRRDKKQFTADVRRVSQDGLAGIgiDPRWTVDRTLSAALKDARRAGRPSGRS-VEDLLGDVALDARYAPRTIHSLSGGE 154
Cdd:COG1123 332 LSRRSLRELRRRVQMVFQDPYSSL--NPRMTVGDIIAEPLRLHGLLSRAERRErVAELLERVGLPPDLADRYPHELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 155 KQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGAL 234
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
250 260
....*....|....*....|....
gi 1199107692 235 RDVFAGTApgadHPSVRGLAEAAP 258
Cdd:COG1123 490 EEVFANPQ----HPYTRALLAAVP 509
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-232 |
1.76e-53 |
|
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: 172.69 E-value: 1.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGYGGPD----VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQ 83
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkALDDVSFSIKKGET-LGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 84 FTADVRRVSQDGLAGIgiDPRWTVDRTLSAALKDARRAGRPS--GRSVEDLLGDVALDARYAPRTIHSLSGGEKQRVALA 161
Cdd:cd03257 80 RRKEIQMVFQDPMSSL--NPRMTIGEQIAEPLRIHGKLSKKEarKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 162 VALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
9-239 |
4.31e-47 |
|
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: 156.34 E-value: 4.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGY-GGPDVVHGIDLDVVPGaPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRD--KK--- 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKG-EFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 83 -------QFTADVrrVSQD---GLAGIGIDPRWTVDRtlsaalkdarragrpsgrsVEDLLGDVALDArYAPRTIHSLSG 152
Cdd:COG1122 80 vfqnpddQLFAPT--VEEDvafGPENLGLPREEIRER-------------------VEEALELVGLEH-LADRPPHELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 153 GEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:COG1122 138 GQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADG 216
|
....*..
gi 1199107692 233 ALRDVFA 239
Cdd:COG1122 217 TPREVFS 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-247 |
5.03e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.79 E-value: 5.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 4 TTTPILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRR---- 79
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEF-VAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 80 ------DKkQFTADVRRVsqdglAGIGIDPRWTVDRTLSAALKDArragrpsgrsVEDLLGDVALDArYAPRTIHSLSGG 153
Cdd:COG1121 81 pqraevDW-DFPITVRDV-----VLMGRYGRRGLFRRPSRADREA----------VDEALERVGLED-LADRPIGELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 154 EKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTV-----HVLADGT- 227
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVlllnrGLVAHGPp 222
|
250 260
....*....|....*....|..
gi 1199107692 228 --FVTSGALRDVFAGTAPGADH 247
Cdd:COG1121 223 eeVLTPENLSRAYGGPVALLAH 244
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-258 |
1.75e-46 |
|
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: 157.52 E-value: 1.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGYGGPD----VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRP---TAGHVTYAGRTVTKLSRRD 80
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvvkAVDGVSFDVRRGET-LGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 81 KKQFTAdvRRVS---QDGLAGIgiDPRWTVDRTLSAALKDARRAGRPSGRS-VEDLLGDVALD--ARYAPRTIHSLSGGE 154
Cdd:COG0444 80 LRKIRG--REIQmifQDPMTSL--NPVMTVGDQIAEPLRIHGGLSKAEARErAIELLERVGLPdpERRLDRYPHELSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 155 KQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGAL 234
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPV 235
|
250 260
....*....|....*....|....
gi 1199107692 235 RDVFAGTApgadHPSVRGLAEAAP 258
Cdd:COG0444 236 EELFENPR----HPYTRALLSSIP 255
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-237 |
4.20e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.07 E-value: 4.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTAdv 88
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEI-FGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 rrVSQDglagIGIDPRWTVDRTLS--AALKDARRAGRPsgRSVEDLLGDVALDARyAPRTIHSLSGGEKQRVALAVALAT 166
Cdd:COG1131 78 --VPQE----PALYPDLTVRENLRffARLYGLPRKEAR--ERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 167 RPRALLLDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDV 237
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-260 |
3.58e-44 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 151.81 E-value: 3.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 2 STTTTPILRATGLAAGY--------GGPDVVH---GIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAG 70
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgglfgRTVGVVKavdGVSFDIRRGET-LGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 71 RTVTKLSRRDKKQFTADVRRVSQDGLAGIgiDPRWTVDRTLSAALK---DARRAGRpsGRSVEDLLGDVALDARYAPRTI 147
Cdd:COG4608 80 QDITGLSGRELRPLRRRMQMVFQDPYASL--NPRMTVGDIIAEPLRihgLASKAER--RERVAELLELVGLRPEHADRYP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 148 HSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGT 227
Cdd:COG4608 156 HEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGK 235
|
250 260 270
....*....|....*....|....*....|...
gi 1199107692 228 FVTSGALRDVFAGTApgadHPSVRGLAEAAPLA 260
Cdd:COG4608 236 IVEIAPRDELYARPL----HPYTQALLSAVPVP 264
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-262 |
4.76e-43 |
|
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: 153.14 E-value: 4.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 6 TPILRATGLAAGY--GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTA---GHVTYAGRTVTKLSRRD 80
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGET-VALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 81 KkqfTADVRRVSQDGLAGIgiDPrWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDARYApRTIHSLSGGEKQRVAL 160
Cdd:COG1123 81 R---GRRIGMVFQDPMTQL--NP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLD-RYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 161 AVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFAG 240
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
250 260
....*....|....*....|..
gi 1199107692 241 TAPGADHPSVRGLAEAAPLAVQ 262
Cdd:COG1123 234 PQALAAVPRLGAARGRAAPAAA 255
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-256 |
7.92e-43 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 146.76 E-value: 7.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 10 RATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTADVR 89
Cdd:PRK10419 14 AHGGLSGKHQHQTVLNNVSLSLKSGET-VALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 90 RVSQDGLAGIgiDPRWTVDRTLS------AALKDARRAGRpsgrsVEDLLGDVALDARYAPRTIHSLSGGEKQRVALAVA 163
Cdd:PRK10419 93 MVFQDSISAV--NPRKTVREIIReplrhlLSLDKAERLAR-----ASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 164 LATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALrdvfaGTAP 243
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPV-----GDKL 240
|
250
....*....|...
gi 1199107692 244 GADHPSVRGLAEA 256
Cdd:PRK10419 241 TFSSPAGRVLQNA 253
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
8-238 |
1.11e-42 |
|
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: 145.96 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDkkqftad 87
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEV-TALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 88 VRR----VSQDGLAGIGIdprwTVDRTLSAALKDARRAGRPSGRS----VEDLLGDVALDArYAPRTIHSLSGGEKQRVA 159
Cdd:COG1120 73 LARriayVPQEPPAPFGL----TVRELVALGRYPHLGLFGRPSAEdreaVEEALERTGLEH-LADRPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 160 LAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVF 238
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-228 |
1.22e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 144.57 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLS----RRDkkqf 84
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGEC-VAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppewRRQ---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 85 tadVRRVSQDglagigidPRWtVDRTLSAALKDAR--RAGRPSGRSVEDLLGDVALDARYAPRTIHSLSGGEKQRVALAV 162
Cdd:COG4619 76 ---VAYVPQE--------PAL-WGGTVRDNLPFPFqlRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199107692 163 ALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTF 228
Cdd:COG4619 144 ALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
23-239 |
2.99e-41 |
|
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: 141.56 E-value: 2.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTADVRRVSQdglaGIGID 102
Cdd:cd03258 20 ALKDVSLSVPKGEI-FGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQ----HFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 103 PRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDARyAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDP 182
Cdd:cd03258 95 SSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDK-ADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199107692 183 AMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:cd03258 174 ETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-232 |
3.07e-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: 140.75 E-value: 3.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 10 RATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRR---------- 79
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEF-LAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigyvpqrrsi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 80 DKkQFTADVRRVsqdglAGIGIDPRWTVDRTLSAALKDArragrpsgrsVEDLLGDVALDArYAPRTIHSLSGGEKQRVA 159
Cdd:cd03235 80 DR-DFPISVRDV-----VLMGLYGHKGLFRRLSKADKAK----------VDEALERVGLSE-LADRQIGELSGGQQQRVL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199107692 160 LAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVhVLADGTFVTSG 232
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-227 |
1.09e-40 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 138.47 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTaDV 88
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEI-VALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR-RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 RRVSQDGlagigidprwtvdrtlsaalkdarraGRPSGRSVEDLLGdvaldaryaprtiHSLSGGEKQRVALAVALATRP 168
Cdd:cd03229 79 GMVFQDF--------------------------ALFPHLTVLENIA-------------LGLSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 169 RALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGT 227
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
23-227 |
1.52e-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: 139.14 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTADV----------RRVS 92
Cdd:cd03225 16 ALDDISLTIKKGEF-VLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVfqnpddqffgPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 93 QD---GLAGIGIDPRWTVDRtlsaalkdarragrpsgrsVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVALATRPR 169
Cdd:cd03225 95 EEvafGLENLGLPEEEIEER-------------------VEEALELVGLEG-LRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199107692 170 ALLLDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADGT 227
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-232 |
1.69e-40 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 139.19 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKkqftaDV 88
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEF-LALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR-----NI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 RRVSQDGlagiGIDPRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDaRYAPRTIHSLSGGEKQRVALAVALATRP 168
Cdd:cd03259 75 GMVFQDY----ALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199107692 169 RALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
24-259 |
1.85e-40 |
|
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: 146.37 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 24 VHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVrPTAGHVTYAGRTVTKLSRRDKKQFTADVRRVSQDGLAGIgiDP 103
Cdd:COG4172 302 VDGVSLTLRRGET-LGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSL--SP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 104 RWTVDRTLS-------AALKDARRAGRpsgrsVEDLLGDVALDARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEP 176
Cdd:COG4172 378 RMTVGQIIAeglrvhgPGLSAAERRAR-----VAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 177 LTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFAgtAPgaDHPSVRGLAEA 256
Cdd:COG4172 453 TSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFD--AP--QHPYTRALLAA 528
|
...
gi 1199107692 257 APL 259
Cdd:COG4172 529 APL 531
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-232 |
4.44e-40 |
|
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: 136.80 E-value: 4.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 10 RATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKkqftadVR 89
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEI-VGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL------AR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 90 RVSqdglagigidprwtvdrTLSAALKDARragrpsgrsVEDLlgdvaldaryAPRTIHSLSGGEKQRVALAVALATRPR 169
Cdd:cd03214 74 KIA-----------------YVPQALELLG---------LAHL----------ADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199107692 170 ALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-232 |
2.91e-39 |
|
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: 135.89 E-value: 2.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 25 HGIDLDVVPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTvtkLSRRDKKQFTADVRRvsqdglaGIGID-- 102
Cdd:cd03297 13 FTLKIDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV---LFDSRKKINLPPQQR-------KIGLVfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 103 -----PRWTVDRTLSAALKDARRagRPSGRSVEDLLGDVALDaRYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPL 177
Cdd:cd03297 83 qyalfPHLNVRENLAFGLKRKRN--REDRISVDELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199107692 178 TAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-251 |
8.08e-39 |
|
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: 135.49 E-value: 8.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 4 TTTPILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQ 83
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEI-LAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 84 ftadVRR----VSQDG-----LagigidprwTVD----------RTLSAALKDARragrpsgrsVEDLLGDVALD--ARY 142
Cdd:COG1127 80 ----LRRrigmLFQGGalfdsL---------TVFenvafplrehTDLSEAEIREL---------VLEKLELVGLPgaADK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 143 APrtiHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHV 222
Cdd:COG1127 138 MP---SELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAV 214
|
250 260
....*....|....*....|....*....
gi 1199107692 223 LADGTFVTSGALRDVFAgtapgADHPSVR 251
Cdd:COG1127 215 LADGKIIAEGTPEELLA-----SDDPWVR 238
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-229 |
5.92e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 132.86 E-value: 5.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 6 TPILRATGLAAGYGGPD----VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDK 81
Cdd:COG1136 2 SPLLELRNLTKSYGTGEgevtALRGVSLSIEAGEF-VAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 82 kqftADVRR-----VSQDGlagiGIDPRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDARyAPRTIHSLSGGEKQ 156
Cdd:COG1136 81 ----ARLRRrhigfVFQFF----NLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDR-LDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199107692 157 RVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERlCPTVHVLADGTFV 229
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIV 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-239 |
8.62e-38 |
|
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: 136.00 E-value: 8.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 26 GIDLDV---VPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTvtkLSRRDKKQFTADVRR----VSQDGLag 98
Cdd:COG4148 13 GFTLDVdftLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV---LQDSARGIFLPPHRRrigyVFQEAR-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 99 igIDPRWTVDRTLSAALKDARRAGRPSGR-SVEDLLGDVALDARYaprtIHSLSGGEKQRVALAVALATRPRALLLDEPL 177
Cdd:COG4148 88 --LFPHLSVRGNLLYGRKRAPRAERRISFdEVVELLGIGHLLDRR----PATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199107692 178 TAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:COG4148 162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
5-211 |
9.95e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 135.61 E-value: 9.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 5 TTPILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLS--RRDkk 82
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEF-VALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPpeKRN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 83 qftadVRRVSQD---------------GLAGIGIDprwtvdrtlsaalKDARRagrpsgRSVEDLLGDVALDArYAPRTI 147
Cdd:COG3842 79 -----VGMVFQDyalfphltvaenvafGLRMRGVP-------------KAEIR------ARVAELLELVGLEG-LADRYP 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199107692 148 HSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLE 211
Cdd:COG3842 134 HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQE 197
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-256 |
1.20e-37 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 133.39 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 6 TPILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFT 85
Cdd:TIGR02769 9 THTYRTGGLFGAKQRAPVLTNVSLSIEEGET-VGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 86 ADVRRVSQDGLAGIgiDPRWTVDRTLS------AALKDARRAGRpsgrsVEDLLGDVALDARYAPRTIHSLSGGEKQRVA 159
Cdd:TIGR02769 88 RDVQLVFQDSPSAV--NPRMTVRQIIGeplrhlTSLDESEQKAR-----IAELLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 160 LAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
250
....*....|....*..
gi 1199107692 240 gtapgADHPSVRGLAEA 256
Cdd:TIGR02769 241 -----FKHPAGRNLQSA 252
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-226 |
3.25e-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: 129.05 E-value: 3.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTAdv 88
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEI-YGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 rrVSQDglagIGIDPRWTVdrtlsaalkdarragrpsgrsvEDLLgdvaldaryaprtihSLSGGEKQRVALAVALATRP 168
Cdd:cd03230 78 --LPEE----PSLYENLTV----------------------RENL---------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199107692 169 RALLLDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADG 226
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
7-226 |
1.50e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 129.79 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLAAGY-GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFT 85
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEF-VALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 86 ADVRRVSQD-GLAG---------IGIDPRWTVDRTLSAALKDARRAGrpsgrsVEDLLGDVALdARYAPRTIHSLSGGEK 155
Cdd:COG3638 80 RRIGMIFQQfNLVPrlsvltnvlAGRLGRTSTWRSLLGLFPPEDRER------ALEALERVGL-ADKAYQRADQLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 156 QRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADG 226
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDG 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-239 |
2.01e-36 |
|
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: 129.77 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 5 TTPILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkkqf 84
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEI-VGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 85 tadVRRVSQDGLA----GIGIDPRWTV------------DRTLSAALKDARRAGRPSGRS---VEDLLGDVALDARyAPR 145
Cdd:COG0411 73 ---PHRIARLGIArtfqNPRLFPELTVlenvlvaaharlGRGLLAALLRLPRARREEREArerAEELLERVGLADR-ADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 146 TIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLAD 225
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF 228
|
250
....*....|....
gi 1199107692 226 GTFVTSGALRDVFA 239
Cdd:COG0411 229 GRVIAEGTPAEVRA 242
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
9-237 |
6.62e-36 |
|
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: 128.05 E-value: 6.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQ--FTA 86
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEI-TGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQigVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 87 DvrrvsqdglaGIGIDPRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDaRYAPRTIHSLSGGEKQRVALAVALAT 166
Cdd:COG4555 81 D----------ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 167 RPRALLLDEPLTAVDPAMRGDVVRRLGdATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDV 237
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILR-ALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
13-251 |
1.37e-35 |
|
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: 126.85 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 13 GLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTADVRRVS 92
Cdd:cd03261 5 GLTKSFGGRTVLKGVDLDVRRGEI-LAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 93 QDGlagigidprwtvdrtlsaALKDA-----------RRAGRPSGRSVEDL----LGDVAL--DARYAPrtiHSLSGGEK 155
Cdd:cd03261 84 QSG------------------ALFDSltvfenvafplREHTRLSEEEIREIvlekLEAVGLrgAEDLYP---AELSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 156 QRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALR 235
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPE 222
|
250
....*....|....*.
gi 1199107692 236 DVFAgtapgADHPSVR 251
Cdd:cd03261 223 ELRA-----SDDPLVR 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
19-233 |
1.83e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 123.62 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 19 GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDkkqfTADVRRvsqdglaG 98
Cdd:COG2884 13 GGREALSDVSLEIEKGEF-VFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRRE----IPYLRR-------R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 99 IGI---D----PRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDARyAPRTIHSLSGGEKQRVALAVALATRPRAL 171
Cdd:COG2884 81 IGVvfqDfrllPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDK-AKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199107692 172 LLDEPLTAVDPAMRGDVVRRLGDAtAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGA 233
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
9-226 |
2.06e-34 |
|
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: 123.37 E-value: 2.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPD----VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKkqf 84
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEF-VAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKEL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 85 tADVRRVSqdglagIGID-------PRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDARyAPRTIHSLSGGEKQR 157
Cdd:cd03255 77 -AAFRRRH------IGFVfqsfnllPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDR-LNHYPSELSGGQQQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 158 VALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHvLADG 226
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIE-LRDG 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-223 |
8.42e-34 |
|
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: 121.81 E-value: 8.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPD----VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRrdkkqf 84
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEF-VALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 85 taDVRRVSQDGLagigIDPRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVAL 164
Cdd:cd03293 74 --DRGYVFQQDA----LLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSG-FENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 165 ATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVL 223
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
23-239 |
9.62e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 124.80 E-value: 9.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDkkqftadVRRVSQDglagIG-- 100
Cdd:COG1135 20 ALDDVSLTIEKGEI-FGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERE-------LRAARRK----IGmi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 101 ------IDPRwTVDRTLSAALK-----DARRAGRpsgrsVEDLLGDVALDAR---YaPRtihSLSGGEKQRVALAVALAT 166
Cdd:COG1135 88 fqhfnlLSSR-TVAENVALPLEiagvpKAEIRKR-----VAELLELVGLSDKadaY-PS---QLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199107692 167 RPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-259 |
1.54e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 124.05 E-value: 1.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 24 VHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTADVRRVSQDGLAgiGIDP 103
Cdd:PRK15079 37 VDGVTLRLYEGET-LGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLA--SLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 104 RWTVDRTLSAALkdarRAGRP--SGRSVED----LLGDVALDARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPL 177
Cdd:PRK15079 114 RMTIGEIIAEPL----RTYHPklSRQEVKDrvkaMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 178 TAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFAGTApgadHPSVRGLAEAA 257
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL----HPYTKALMSAV 265
|
..
gi 1199107692 258 PL 259
Cdd:PRK15079 266 PI 267
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-248 |
1.83e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 124.10 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTV-TKLSRRDkkqftad 87
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGEL-VALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRE------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 88 vRR---VSQD-GLAgigidPRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVA 163
Cdd:COG1118 75 -RRvgfVFQHyALF-----PHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEG-LADRYPSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 164 LATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFagtap 243
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY----- 222
|
....*
gi 1199107692 244 gaDHP 248
Cdd:COG1118 223 --DRP 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-237 |
2.07e-33 |
|
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: 121.39 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkkqftadV 88
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEI-HGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP----------P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 RRVSQDGLA----GIGIDPRWTV----------DRTLSAALKDARRAGRPSGRSVEDLLGDVALDARyAPRTIHSLSGGE 154
Cdd:cd03219 70 HEIARLGIGrtfqIPRLFPELTVlenvmvaaqaRTGSGLLLARARREEREARERAEELLERVGLADL-ADRPAGELSYGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 155 KQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDAtAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGAL 234
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
...
gi 1199107692 235 RDV 237
Cdd:cd03219 228 DEV 230
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-211 |
2.28e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 121.74 E-value: 2.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 3 TTTTPILRATGLAAGYGGPD----VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSR 78
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGggvtALDDVSLTVAAGEF-VALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 79 RdkkqftadvrrvsqdglagIGI---DPR---W-TVDRTLSAALKDARRAGRPSGRSVEDLLGDVALD--ARYAPrtiHS 149
Cdd:COG1116 81 D-------------------RGVvfqEPAllpWlTVLDNVALGLELRGVPKAERRERARELLELVGLAgfEDAYP---HQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199107692 150 LSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLE 211
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVD 200
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-227 |
2.81e-33 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 118.50 E-value: 2.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 10 RATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKqftadvR 89
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEI-VALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR------R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 90 RVSqdglagigidprwtvdrtlsaalkdarragrpsgrsvedllgdvaldaryaprTIHSLSGGEKQRVALAVALATRPR 169
Cdd:cd00267 74 RIG-----------------------------------------------------YVPQLSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199107692 170 ALLLDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADGT 227
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-214 |
3.63e-33 |
|
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: 119.89 E-value: 3.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFta 86
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEA-LALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 87 dvrrvsqdGLAG--IGIDPRWTVDRTLSAALkdARRAGRPSGRSVEDLLGDVALdARYAPRTIHSLSGGEKQRVALAVAL 164
Cdd:COG4133 78 --------AYLGhaDGLKPELTVRENLRFWA--ALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1199107692 165 ATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVE 214
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLELA 195
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-178 |
5.24e-33 |
|
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: 117.75 E-value: 5.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 24 VHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKlsrRDKKQFTADVRRVSQDglagIGIDP 103
Cdd:pfam00005 1 LKNVSLTLNPGEI-LALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD---DERKSLRKEIGYVFQD----PQLFP 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199107692 104 RWTVDRTLSAALKDARRAGRPSGRSVEDLL---GDVALDARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLT 178
Cdd:pfam00005 73 RLTVRENLRLGLLLKGLSKREKDARAEEALeklGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-258 |
8.03e-33 |
|
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: 125.18 E-value: 8.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 4 TTTPILRATGLAAGYGGPD----VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTA----GHVTYAGRTVTK 75
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGgtveAVKGVSFDIAAGET-LALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 76 LSRRDKKQftadVRrvsqdGlAGIGI---------DPRWTVDRTLSAALKDARRAGRPSGRS-VEDLLGDVALDAryaPR 145
Cdd:COG4172 81 LSERELRR----IR-----G-NRIAMifqepmtslNPLHTIGKQIAEVLRLHRGLSGAAARArALELLERVGIPD---PE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 146 TI-----HSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTV 220
Cdd:COG4172 148 RRldaypHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRV 227
|
250 260 270
....*....|....*....|....*....|....*...
gi 1199107692 221 HVLADGTFVTSGALRDVFAgtAPGadHPSVRGLAEAAP 258
Cdd:COG4172 228 AVMRQGEIVEQGPTAELFA--APQ--HPYTRKLLAAEP 261
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
9-233 |
9.25e-33 |
|
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: 119.08 E-value: 9.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkkqftadV 88
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEI-VALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP----------P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 RRVSQDGLA----GIGIDPRWTVDRTLSAALKDARRAGRPsgRSVEDLLGDV-ALDARYAPRTiHSLSGGEKQRVALAVA 163
Cdd:cd03224 70 HERARAGIGyvpeGRRIFPELTVEENLLLGAYARRRAKRK--ARLERVYELFpRLKERRKQLA-GTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 164 LATRPRALLLDEPLTAVDPAMRGDVVRRLGDaTAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGA 233
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRE-LRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-260 |
1.08e-32 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 125.74 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 24 VHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTADVRRVSQDGLAGIgiDP 103
Cdd:PRK10261 340 VEKVSFDLWPGET-LSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASL--DP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 104 RWTVDRTLSAALKDARR-AGRPSGRSVEDLLGDVALDARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDP 182
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199107692 183 AMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFAgtapGADHPSVRGLAEAAPLA 260
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFE----NPQHPYTRKLMAAVPVA 570
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
5-258 |
1.50e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 121.22 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 5 TTPILRATGLAAGY-------GGPDVVH---GIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVT 74
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkrglfKPERLVKaldGVSFTLERGKT-LAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 75 KLSRRDKKQFTADVRRVSQDGLAGIgiDPRWTVDRTLSAAL-------KDARRAgrpsgrSVEDLLGDVALDARYAPRTI 147
Cdd:PRK11308 81 KADPEAQKLLRQKIQIVFQNPYGSL--NPRKKVGQILEEPLlintslsAAERRE------KALAMMAKVGLRPEHYDRYP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 148 HSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGT 227
Cdd:PRK11308 153 HMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGR 232
|
250 260 270
....*....|....*....|....*....|.
gi 1199107692 228 FVTSGALRDVFAgtAPgaDHPSVRGLAEAAP 258
Cdd:PRK11308 233 CVEKGTKEQIFN--NP--RHPYTQALLSATP 259
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-237 |
1.68e-32 |
|
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: 118.93 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 6 TPILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkkqft 85
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEI-VALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLP-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 86 adVRRVSQDGLA----GIGIDPRWTVDRTLSAALKdARRAGRPSGRSVEDLLgdvALDARYAPRtIH----SLSGGEKQR 157
Cdd:COG0410 72 --PHRIARLGIGyvpeGRRIFPSLTVEENLLLGAY-ARRDRAEVRADLERVY---ELFPRLKER-RRqragTLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 158 VALAVALATRPRALLLDEPLTAVDPAMR---GDVVRRLgdatAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGAL 234
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIVeeiFEIIRRL----NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
...
gi 1199107692 235 RDV 237
Cdd:COG0410 221 AEL 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-250 |
2.86e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 118.72 E-value: 2.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQ--- 83
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEV-VAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARrra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 84 ---------FTADVRRVSQDGLAGIGIDPRwTVDRTLSAALKDArragrpsgrsveDLLGdvaldarYAPRTIHSLSGGE 154
Cdd:PRK13548 80 vlpqhsslsFPFTVEEVVAMGRAPHGLSRA-EDDALVAAALAQV------------DLAH-------LAGRDYPQLSGGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 155 KQRVALAVALA------TRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTF 228
Cdd:PRK13548 140 QQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
250 260 270
....*....|....*....|....*....|....*.
gi 1199107692 229 VTSGA---------LRDVF-----AGTAPGADHPSV 250
Cdd:PRK13548 220 VADGTpaevltpetLRRVYgadvlVQPHPETGAPLV 255
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-239 |
3.67e-32 |
|
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: 120.99 E-value: 3.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 25 HGIDLDV-VPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTklSRRDKKQFTADVRRVS---QDGlagiG 100
Cdd:TIGR02142 12 FSLDADFtLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF--DSRKGIFLPPEKRRIGyvfQEA----R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 101 IDPRWTVDRTLSAALKDARRAGRP-SGRSVEDLLGDVALDARYAPRtihsLSGGEKQRVALAVALATRPRALLLDEPLTA 179
Cdd:TIGR02142 86 LFPHLSVRGNLRYGMKRARPSERRiSFERVIELLGIGHLLGRLPGR----LSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 180 VDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-229 |
4.20e-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: 116.97 E-value: 4.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 18 YGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRtVTKLSRRDKKQFTadvrrVSQDgla 97
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEI-IALTGKNGAGKTTLAKILAGLIKESSGSILLNGK-PIKAKERRKSIGY-----VMQD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 98 gigidprwtVDRTL---SAALKDARRAGRPSGRS--VEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVALATRPRALL 172
Cdd:cd03226 80 ---------VDYQLftdSVREELLLGLKELDAGNeqAETVLKDLDLYA-LKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 173 LDEPLTAVDPA-MR--GDVVRRLgdatAELGTAVLLVSHDLELVERLCPTVHVLADGTFV 229
Cdd:cd03226 150 FDEPTSGLDYKnMErvGELIREL----AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-233 |
4.77e-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: 117.78 E-value: 4.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGYGGPDVV-HGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTA 86
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQAlKNINLNINPGEF-VAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 87 DVRRVSQDglagIGIDPRWTV-DRTLSAAL---------------KDARRAgrpsgrsvEDLLGDVALDARYAPRTiHSL 150
Cdd:TIGR02315 80 RIGMIFQH----YNLIERLTVlENVLHGRLgykptwrsllgrfseEDKERA--------LSALERVGLADKAYQRA-DQL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 151 SGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVT 230
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVF 226
|
...
gi 1199107692 231 SGA 233
Cdd:TIGR02315 227 DGA 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-233 |
1.32e-31 |
|
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: 116.90 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPD-VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTAD 87
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEF-VALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 88 VRRVSQDGlagiGIDPRWTV-DRTLSAALkdarrAGRPSGRS------VED------LLGDVALDARYAPRTiHSLSGGE 154
Cdd:cd03256 80 IGMIFQQF----NLIERLSVlENVLSGRL-----GRRSTWRSlfglfpKEEkqralaALERVGLLDKAYQRA-DQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 155 KQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGA 233
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGP 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
9-210 |
1.55e-31 |
|
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: 115.70 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKlSRRDKKQFTADV 88
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEV-VVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 RRVSQ--------DGLAGIGIDPRWTVDRTLSAALKDARragrpsgrsveDLLGDVALDARyAPRTIHSLSGGEKQRVAL 160
Cdd:cd03262 79 GMVFQqfnlfphlTVLENITLAPIKVKGMSKAEAEERAL-----------ELLEKVGLADK-ADAYPAQLSGGQQQRVAI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199107692 161 AVALATRPRALLLDEPLTAVDPAMRG---DVVRRLgdatAELGTAVLLVSHDL 210
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGevlDVMKDL----AEEGMTMVVVTHEM 195
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-245 |
5.89e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.85 E-value: 5.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 27 IDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkkqftADVRRVS---QDG-------L 96
Cdd:COG3840 18 FDLTIAAGER-VAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP--------PAERPVSmlfQENnlfphltV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 97 A---GIGIDPrwtvDRTLSAALKDArragrpsgrsVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVALAtRPRA-LL 172
Cdd:COG3840 89 AqniGLGLRP----GLKLTAEQRAQ----------VEQALERVGLAG-LLDRLPGQLSGGQRQRVALARCLV-RKRPiLL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199107692 173 LDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFAGTAPGA 245
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPA 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
24-239 |
7.96e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 117.21 E-value: 7.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 24 VHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFtadvRRvsqdglaGIG--- 100
Cdd:PRK11153 21 LNNVSLHIPAGEI-FGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA----RR-------QIGmif 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 101 -----IDPRwTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDARyAPRTIHSLSGGEKQRVALAVALATRPRALLLDE 175
Cdd:PRK11153 89 qhfnlLSSR-TVFDNVALPLELAGTPKAEIKARVTELLELVGLSDK-ADRYPAQLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199107692 176 PLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:PRK11153 167 ATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFS 230
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
18-238 |
1.03e-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: 114.26 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 18 YGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRrDKKQFTAdvrrVSQDgla 97
Cdd:cd03300 10 YGGFVALDGVSLDIKEGEF-FTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP-HKRPVNT----VFQN--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 98 gIGIDPRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPL 177
Cdd:cd03300 81 -YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEG-YANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 178 TAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVF 238
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-226 |
1.43e-30 |
|
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: 113.68 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 1 MSTTTTPILRATGLAAGYGGP----DVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKL 76
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTGagelTILKGISLEVEAGES-VAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 77 SRRDKkqftADVRRvsqdglAGIGIdprwtVDR------TLSA----ALKdARRAGRPSGRSV-EDLLGDVALDAR--YA 143
Cdd:COG4181 80 DEDAR----ARLRA------RHVGF-----VFQsfqllpTLTAlenvMLP-LELAGRRDARARaRALLERVGLGHRldHY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 144 PRTihsLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERlCPTVHVL 223
Cdd:COG4181 144 PAQ---LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRL 219
|
...
gi 1199107692 224 ADG 226
Cdd:COG4181 220 RAG 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-237 |
1.72e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 115.21 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 18 YGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKlsrrdkkqftADVRRVsqdgla 97
Cdd:COG4152 11 FGDKTAVDDVSFTVPKGEI-FGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----------EDRRRI------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 98 GI-----GIDPRWTVDRTLS--AALKD-ARRAGRpsgRSVEDLLGDVALdARYAPRTIHSLSGGEKQRVALAVALATRPR 169
Cdd:COG4152 74 GYlpeerGLYPKMKVGEQLVylARLKGlSKAEAK---RRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199107692 170 ALLLDEPLTAVDP----AMRgDVVRRLgdatAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDV 237
Cdd:COG4152 150 LLILDEPFSGLDPvnveLLK-DVIREL----AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
38-238 |
1.86e-30 |
|
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: 114.47 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKqftaDVRR-----------------VSQDglagIG 100
Cdd:TIGR04521 34 VAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLK----DLRKkvglvfqfpehqlfeetVYKD----IA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 101 IDPRwtvdrTLSAALKDARRAgrpsgrsVEDLLGDVALDARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAV 180
Cdd:TIGR04521 106 FGPK-----NLGLSEEEAEER-------VKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199107692 181 DPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVF 238
Cdd:TIGR04521 174 DPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
8-239 |
3.08e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 113.17 E-value: 3.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTklsrrDKKqftAD 87
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEV-VVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-----DSK---KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 88 VRRVSQDglagIGID-------PRWTVDRTLSAALKDARRAGRPSGRSV-EDLLGDVALDAR---YaPrtiHSLSGGEKQ 156
Cdd:COG1126 72 INKLRRK----VGMVfqqfnlfPHLTVLENVTLAPIKVKKMSKAEAEERaMELLERVGLADKadaY-P---AQLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 157 RVALAVALATRPRALLLDEPLTAVDPAMRG---DVVRRLgdatAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGA 233
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPELVGevlDVMRDL----AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGP 219
|
....*.
gi 1199107692 234 LRDVFA 239
Cdd:COG1126 220 PEEFFE 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-232 |
3.10e-30 |
|
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: 112.31 E-value: 3.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkkqftADV 88
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEI-YGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--------EAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 RRVsqdglaGIGID-PRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDARyAPRTIHSLSGGEKQRVALAVALATR 167
Cdd:cd03268 72 RRI------GALIEaPGFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGLKDS-AKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 168 PRALLLDEPLTAVDPA----MRgDVVRRLgdatAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:cd03268 145 PDLLILDEPTNGLDPDgikeLR-ELILSL----RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
18-249 |
6.13e-30 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 112.43 E-value: 6.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 18 YGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKkqftaDVRRVSQDgla 97
Cdd:cd03296 12 FGDFVALDDVSLDIPSGEL-VALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER-----NVGFVFQH--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 98 gIGIDPRWTVDRTLSAALKDARRAGRPSG----RSVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVALATRPRALLL 173
Cdd:cd03296 83 -YALFRHMTVFDNVAFGLRVKPRSERPPEaeirAKVHELLKLVQLDW-LADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 174 DEPLTAVDPAMRGDV---VRRLGDataELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFagtapgaDHPS 249
Cdd:cd03296 161 DEPFGALDAKVRKELrrwLRRLHD---ELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY-------DHPA 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-232 |
3.01e-29 |
|
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: 109.59 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGapPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVtklsRRDKKQFTADV 88
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG--MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 RRVSQDglagIGIDPRWTVDRTL--SAALKDARRAGRPsgRSVEDLLGDVALdARYAPRTIHSLSGGEKQRVALAVALAT 166
Cdd:cd03264 75 GYLPQE----FGVYPNFTVREFLdyIAWLKGIPSKEVK--ARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199107692 167 RPRALLLDEPLTAVDPAMRGDVVRRLGDATAElgTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-231 |
7.35e-29 |
|
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: 107.13 E-value: 7.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQftadv 88
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEV-HALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARR----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 rrvsqdglAGIGidprwtvdrtlsaalkdarragrpsgrsvedllgdvaldaryaprTIHSLSGGEKQRVALAVALATRP 168
Cdd:cd03216 75 --------AGIA---------------------------------------------MVYQLSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199107692 169 RALLLDEPLTAVDPA---MRGDVVRRLGDAtaelGTAVLLVSHDLELVERLCPTVHVLADGTFVTS 231
Cdd:cd03216 102 RLLILDEPTAALTPAeveRLFKVIRRLRAQ----GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
8-232 |
1.27e-28 |
|
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: 109.66 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGyggpdvVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQftad 87
Cdd:cd03294 30 ILKKTGQTVG------VNDVSLDVREGEIFV-IMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRE---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 88 VRR-----VSQDglagIGIDPRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAV 162
Cdd:cd03294 99 LRRkkismVFQS----FALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEG-WEHKYPDELSGGMQQRVGLAR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 163 ALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:cd03294 174 ALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
19-243 |
2.55e-28 |
|
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: 108.16 E-value: 2.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 19 GGPDVVHGIDLDVvPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkkqfTADVRR----VSQD 94
Cdd:cd03295 12 GGKKAVNNLNLEI-AKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD-------PVELRRkigyVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 95 glagIGIDPRWTVDRTLSAALK-----DARRAGRpsgrsVEDLLGDVALD-ARYAPRTIHSLSGGEKQRVALAVALATRP 168
Cdd:cd03295 84 ----IGLFPHMTVEENIALVPKllkwpKEKIRER-----ADELLALVGLDpAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199107692 169 RALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFAGTAP 243
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-232 |
3.09e-28 |
|
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: 107.65 E-value: 3.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLV-----RPTAGHVTYAGRTVtklsrRDKKQ 83
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEI-TALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDI-----YDLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 84 FTADVRRvsqdglaGIGI-----DP-RWTVDRTLSAALKDARRAGRPSGRS-VEDLLGDVALDARYAPRTI-HSLSGGEK 155
Cdd:cd03260 75 DVLELRR-------RVGMvfqkpNPfPGSIYDNVAYGLRLHGIKLKEELDErVEEALRKAALWDEVKDRLHaLGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 156 QRVALAVALATRPRALLLDEPLTAVDPAMRG---DVVRRLGDAtaelgTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAkieELIAELKKE-----YTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-241 |
5.49e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 108.17 E-value: 5.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGYGGPDVVHGIDLDVVPgAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVtKLSRRDKKQFTAD 87
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSL-SPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 88 VRRVSQDGLAGIGIDprwTVDRTLSAALKDARRAGRPSGRSVEDLLgdVALDA-RYAPRTIHSLSGGEKQRVALAVALAT 166
Cdd:PRK13638 79 VATVFQDPEQQIFYT---DIDSDIAFSLRNLGVPEAEITRRVDEAL--TLVDAqHFRHQPIQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199107692 167 RPRALLLDEPLTAVDPAMRGD---VVRRLgdatAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFAGT 241
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQmiaIIRRI----VAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACT 227
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-238 |
8.60e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.12 E-value: 8.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKkqftADV 88
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGEL-TAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWEL----ARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 RRV-SQDGlagigidprwtvdrTLSAALKDA------RRAGRPSGRSVEDLLGDvALD----ARYAPRTIHSLSGGEKQR 157
Cdd:COG4559 77 RAVlPQHS--------------SLAFPFTVEevvalgRAPHGSSAAQDRQIVRE-ALAlvglAHLAGRSYQTLSGGEQQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 158 VALAVALA-------TRPRALLLDEPLTAVDPA-----MRgdVVRRLgdatAELGTAVLLVSHDLELVERLCPTVHVLAD 225
Cdd:COG4559 142 VQLARVLAqlwepvdGGPRWLFLDEPTSALDLAhqhavLR--LARQL----ARRGGGVVAVLHDLNLAAQYADRILLLHQ 215
|
250
....*....|...
gi 1199107692 226 GTFVTSGALRDVF 238
Cdd:COG4559 216 GRLVAQGTPEEVL 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-229 |
1.53e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.54 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYaGRTVtklsrrdkkqfta 86
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDR-IGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 87 dvrRVS-----QDGLagigiDPRWTVDRTLSAALKDARRagrpsgRSVEDLLGDVALDARYAPRTIHSLSGGEKQRVALA 161
Cdd:COG0488 379 ---KIGyfdqhQEEL-----DPDKTVLDELRDGAPGGTE------QEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALA 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 162 VALATRPRALLLDEP---LtavDPAMRgdvvRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFV 229
Cdd:COG0488 445 KLLLSPPNVLLLDEPtnhL---DIETL----EALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-232 |
1.67e-27 |
|
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: 105.28 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPD--VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVtklsRRDKKQfta 86
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEI-FGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 87 dVRRvsqdglaGIGIDP-----------RWTVdrTLSAALKDARRAGRPSgrSVEDLLGDVALDArYAPRTIHSLSGGEK 155
Cdd:cd03263 73 -ARQ-------SLGYCPqfdalfdeltvREHL--RFYARLKGLPKSEIKE--EVELLLRVLGLTD-KANKRARTLSGGMK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 156 QRVALAVALATRPRALLLDEPLTAVDPAMRgdvvRRLGDATAEL--GTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:cd03263 140 RKLSLAIALIGGPSVLLLDEPTSGLDPASR----RAIWDLILEVrkGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-258 |
2.02e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 109.16 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTA 86
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSL-VGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 87 DVrrvSQDGLAGIGIDPRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALdARYAPRTIHSLSGGEKQRVALAVALAT 166
Cdd:PRK09536 81 SV---PQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 167 RPRALLLDEPLTAVD--PAMRG-DVVRRLgdatAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDV------ 237
Cdd:PRK09536 157 ATPVLLLDEPTASLDinHQVRTlELVRRL----VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVltadtl 232
|
250 260
....*....|....*....|....*....
gi 1199107692 238 --------FAGTAPGADHPSVRGLAEAAP 258
Cdd:PRK09536 233 raafdartAVGTDPATGAPTVTPLPDPDR 261
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
19-232 |
3.31e-27 |
|
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: 109.92 E-value: 3.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 19 GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDkkqftadVRR----VSQD 94
Cdd:COG2274 486 DSPPVLDNISLTIKPGER-VAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS-------LRRqigvVLQD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 95 G--LAG-----IGIdprWTVDRTLSAALKDARRAGrpsgrsvedLLGDV-ALDARYAprTI-----HSLSGGEKQRVALA 161
Cdd:COG2274 558 VflFSGtirenITL---GDPDATDEEIIEAARLAG---------LHDFIeALPMGYD--TVvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 162 VALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAelGTAVLLVSHDLELVeRLCPTVHVLADGTFVTSG 232
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDG 691
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-251 |
3.75e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 105.11 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLS--RRDKKqf 84
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEI-VGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhKRARL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 85 tadvrrvsqdglaGIGIDP-------RWTVDRTLSAAL------KDARRagrpsgRSVEDLLGDVALdARYAPRTIHSLS 151
Cdd:COG1137 79 -------------GIGYLPqeasifrKLTVEDNILAVLelrklsKKERE------ERLEELLEEFGI-THLRKSKAYSLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 152 GGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDV---VRRLgdatAELGTAVLLVSHD----LELVERlcptVHVLA 224
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIqkiIRHL----KERGIGVLITDHNvretLGICDR----AYIIS 210
|
250 260
....*....|....*....|....*..
gi 1199107692 225 DGTFVTSGALRDVfagtapgADHPSVR 251
Cdd:COG1137 211 EGKVLAEGTPEEI-------LNNPLVR 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-232 |
5.22e-27 |
|
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: 103.90 E-value: 5.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRD-------- 80
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEI-FGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigylpeer 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 81 ---KKQFTADVRRVSQDgLAGIGIdprwtvdrtlsaalKDARRagrpsgrSVEDLLGDVALdARYAPRTIHSLSGGEKQR 157
Cdd:cd03269 80 glyPKMKVIDQLVYLAQ-LKGLKK--------------EEARR-------RIDEWLERLEL-SEYANKRVEELSKGNQQK 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199107692 158 VALAVALATRPRALLLDEPLTAVDPAMRgDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:cd03269 137 VQFIAAVIHDPELLILDEPFSGLDPVNV-ELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
40-238 |
8.67e-27 |
|
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: 103.95 E-value: 8.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRrDKKQFTAdvrrVSQDglagIGIDPRWTVDRTLSAALKDAR 119
Cdd:cd03299 30 ILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP-EKRDISY----VPQN----YALFPHMTVYKNIAYGLKKRK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 120 RAGRPSGRSVEDLLGDVALDA---RYaPRTihsLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDAT 196
Cdd:cd03299 101 VDKKEIERKVLEIAEMLGIDHllnRK-PET---LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199107692 197 AELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVF 238
Cdd:cd03299 177 KEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-233 |
1.02e-26 |
|
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: 103.22 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 11 ATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRrdkkqftaDVRR 90
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEI-FGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR--------EVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 91 VsqdglagIGIDPRW-TVDRTLSA---ALKDARRAGRPSGR---SVEDLLGDVALdARYAPRTIHSLSGGEKQRVALAVA 163
Cdd:cd03265 74 R-------IGIVFQDlSVDDELTGwenLYIHARLYGVPGAErreRIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 164 LATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGA 233
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGT 215
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-238 |
1.60e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.18 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 3 TTTTPILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKk 82
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEF-LTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 83 qftaDVRRVSQDglagIGIDPRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAV 162
Cdd:PRK09452 87 ----HVNTVFQS----YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEE-FAQRKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199107692 163 ALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVF 238
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIY 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-255 |
2.26e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 105.69 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 6 TPILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKlsrrdkkqfT 85
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEI-FALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH---------V 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 86 ADVRRVSQDGLAGIGIDPRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDaRYAPRTIHSLSGGEKQRVALAVALA 165
Cdd:PRK11607 87 PPYQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 166 TRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFagtapga 245
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY------- 238
|
250
....*....|
gi 1199107692 246 DHPSVRGLAE 255
Cdd:PRK11607 239 EHPTTRYSAE 248
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-237 |
4.24e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.26 E-value: 4.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 5 TTPILRATGLAAGYGGPDVVHGIDLDVVPGAppV-GIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQ 83
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGE--VhALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 84 ftADVRRVSQD-GLAG---------IGIDPR--WTVDRtlSAALKDARRAgrpsgrsVEDLlgDVALDARyapRTIHSLS 151
Cdd:COG1129 79 --AGIAIIHQElNLVPnlsvaenifLGREPRrgGLIDW--RAMRRRAREL-------LARL--GLDIDPD---TPVGDLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 152 GGEKQRVALAVALATRPRALLLDEP---LTAVDPAMRGDVVRRLgdatAELGTAVLLVSHDLELVERLCPTVHVLADGTF 228
Cdd:COG1129 143 VAQQQLVEIARALSRDARVLILDEPtasLTEREVERLFRIIRRL----KAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
....*....
gi 1199107692 229 VTSGALRDV 237
Cdd:COG1129 219 VGTGPVAEL 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-228 |
7.21e-26 |
|
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: 100.20 E-value: 7.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLaagyGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQfta 86
Cdd:cd03215 3 PVLEVRGL----SVKGAVRDVSFEVRAGEI-VGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 87 dvrrvsqdglAGIGIDPRwtvDRtlsaalkdaRRAGRPSGRSVED--LLGdvaldaryaprtiHSLSGGEKQRVALAVAL 164
Cdd:cd03215 75 ----------AGIAYVPE---DR---------KREGLVLDLSVAEniALS-------------SLLSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199107692 165 ATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADGTF 228
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
38-258 |
7.91e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 103.28 E-value: 7.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLV----RPTAGHVTYAGRTVTKLSRRDKKQFT-ADVRRVSQDGLAGIgiDPRWTVDRTLS 112
Cdd:PRK11022 36 VGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERRNLVgAEVAMIFQDPMTSL--NPCYTVGFQIM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 113 AALKDARRAGRPSGRS-VEDLLGDVALDARYAPRTI--HSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVV 189
Cdd:PRK11022 114 EAIKVHQGGNKKTRRQrAIDLLNQVGIPDPASRLDVypHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQII 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 190 RRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFagTAPgaDHPSVRGLAEAAP 258
Cdd:PRK11022 194 ELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF--RAP--RHPYTQALLRALP 258
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
8-239 |
8.28e-26 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 101.58 E-value: 8.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQftad 87
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEI-VGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERAR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 88 vrrvsqdglAGIGIDP-------RWTVDRTLSAAL---KDARRAGRpsGRSVEDLLGDVALdARYAPRTIHSLSGGEKQR 157
Cdd:TIGR04406 76 ---------LGIGYLPqeasifrKLTVEENIMAVLeirKDLDRAER--EERLEALLEEFQI-SHLRDNKAMSLSGGERRR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 158 VALAVALATRPRALLLDEPLTAVDPAMRGDvVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDV 237
Cdd:TIGR04406 144 VEIARALATNPKFILLDEPFAGVDPIAVGD-IKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
..
gi 1199107692 238 FA 239
Cdd:TIGR04406 223 VA 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
18-211 |
8.48e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 103.62 E-value: 8.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 18 YGGPDVVHGIDLDVvPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKK-----QFTADVRRVS 92
Cdd:PRK10851 12 FGRTQVLNDISLDI-PSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKvgfvfQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 93 -QDGLA-GIGIDPRwtVDRTLSAALKdarragrpsgRSVEDLLGDVALdARYAPRTIHSLSGGEKQRVALAVALATRPRA 170
Cdd:PRK10851 91 vFDNIAfGLTVLPR--RERPNAAAIK----------AKVTQLLEMVQL-AHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1199107692 171 LLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLE 211
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQE 198
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-209 |
1.27e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 103.23 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 18 YGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKkqftaDVRRVSQDgla 97
Cdd:COG3839 13 YGGVEALKDIDLDIEDGEF-LVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR-----NIAMVFQS--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 98 gIGIDPRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPL 177
Cdd:COG3839 84 -YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190
....*....|....*....|....*....|..
gi 1199107692 178 TAVDPAMRGDVVRRLGDATAELGTAVLLVSHD 209
Cdd:COG3839 162 SNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
23-239 |
1.37e-25 |
|
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: 101.35 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGrtvtkLSRRDKKQFTaDVRR----VSQD---- 94
Cdd:TIGR04520 17 ALKNVSLSIEKGEF-VAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG-----LDTLDEENLW-EIRKkvgmVFQNpdnq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 95 ------------GLAGIGIDPRWTVDRtlsaalkdarragrpsgrsVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAV 162
Cdd:TIGR04520 90 fvgatveddvafGLENLGVPREEMRKR-------------------VDEALKLVGMED-FRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 163 ALATRPRALLLDEPLTAVDPAMRGDV---VRRLGDataELGTAVLLVSHDLELVErLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVletIRKLNK---EEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFS 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
23-227 |
1.49e-25 |
|
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: 100.59 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTY--AGRTV--TKLSRRDkkqfTADVRR-----VSQ 93
Cdd:COG4778 26 VLDGVSFSVAAGEC-VALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlAQASPRE----ILALRRrtigyVSQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 94 dGLAGIgidPRWTvdrTLSAALKDARRAGRPSGRS---VEDLLGDVALDARY---APRTihsLSGGEKQRVALAVALATR 167
Cdd:COG4778 101 -FLRVI---PRVS---ALDVVAEPLLERGVDREEArarARELLARLNLPERLwdlPPAT---FSGGEQQRVNIARGFIAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 168 PRALLLDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADGT 227
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-226 |
1.62e-25 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 98.61 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 19 GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDkkqftadVRR----VSQD 94
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEK-VAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES-------LRKniayVPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 95 GLagigidprwtvdrtlsaalkdarragrpsgrsvedLLGDvaldaryaprTIHS--LSGGEKQRVALAVALATRPRALL 172
Cdd:cd03228 85 PF-----------------------------------LFSG----------TIREniLSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199107692 173 LDEPLTAVDPAMRGDVVRRLGDATAelGTAVLLVSHDLELVeRLCPTVHVLADG 226
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI-RDADRIIVLDDG 170
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-251 |
6.24e-25 |
|
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: 98.77 E-value: 6.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkkqftadv 88
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEI-VGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 rrVSQDGLAGIGIDP-------RWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALdARYAPRTIHSLSGGEKQRVALA 161
Cdd:cd03218 69 --MHKRARLGIGYLPqeasifrKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 162 VALATRPRALLLDEPLTAVDPAMRGDV---VRRLgdatAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVF 238
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDPIAVQDIqkiIKIL----KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
250
....*....|...
gi 1199107692 239 AgtapgadHPSVR 251
Cdd:cd03218 222 A-------NELVR 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-258 |
7.76e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 100.95 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 1 MSTTTTPILRATGLAAGYGGPD----VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRP---TAGHVTYAGRTV 73
Cdd:PRK09473 5 AQQQADALLDVKDLRVTFSTPDgdvtAVNDLNFSLRAGET-LGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 74 TKLSRRDKKQFTAD-VRRVSQDGLAGIgiDPRWTVDRTLSAALKDARRAGRPSG--RSVEdllgdvALDARYAPRTI--- 147
Cdd:PRK09473 84 LNLPEKELNKLRAEqISMIFQDPMTSL--NPYMRVGEQLMEVLMLHKGMSKAEAfeESVR------MLDAVKMPEARkrm 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 148 ----HSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVL 223
Cdd:PRK09473 156 kmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 235
|
250 260 270
....*....|....*....|....*....|....*
gi 1199107692 224 ADGTFVTSGALRDVFAGTApgadHPSVRGLAEAAP 258
Cdd:PRK09473 236 YAGRTMEYGNARDVFYQPS----HPYSIGLLNAVP 266
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
18-215 |
8.82e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 98.63 E-value: 8.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 18 YGGPDVVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGLVRPTAGHVTYAGrtvtkLSRRDKKqftADVRRVSQDglA 97
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVV-IIGPSGSGKSTLLRCINKLEEITSGDLIVDG-----LKVNDPK---VDERLIRQE--A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 98 GI-----GIDPRWTVDRTLSAALKDARRAGRPSGRSV-EDLLGDVALDARyAPRTIHSLSGGEKQRVALAVALATRPRAL 171
Cdd:PRK09493 80 GMvfqqfYLFPHLTALENVMFGPLRVRGASKEEAEKQaRELLAKVGLAER-AHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1199107692 172 LLDEPLTAVDPAMRGDVVRRLGDaTAELGTAVLLVSHDLELVER 215
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQD-LAEEGMTMVIVTHEIGFAEK 201
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
19-215 |
9.27e-25 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 98.09 E-value: 9.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 19 GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDkkqfTADVRRvsqdglaG 98
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEF-LFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQ----LPLLRR-------R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 99 IGI---DPRWTVDRTLSA----ALKDARRAGRPSGRSVEDLLGDVALDARyAPRTIHSLSGGEKQRVALAVALATRPRAL 171
Cdd:TIGR02673 81 IGVvfqDFRLLPDRTVYEnvalPLEVRGKKEREIQRRVGAALRQVGLEHK-ADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1199107692 172 LLDEPLTAVDPAMRGDVVRRLGDATAeLGTAVLLVSHDLELVER 215
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDR 202
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-226 |
9.31e-25 |
|
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: 98.10 E-value: 9.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKkqftaDV 88
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVV-LLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR-----DI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 RRVSQDglagIGIDPRWTVDRTLSAALKdARRAGRPS----GRSVEDLLGDVALDARYaPRTihsLSGGEKQRVALAVAL 164
Cdd:cd03301 75 AMVFQN----YALYPHMTVYDNIAFGLK-LRKVPKDEiderVREVAELLQIEHLLDRK-PKQ---LSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199107692 165 ATRPRALLLDEPLTAVDP----AMRGDVVRRLgdatAELGTAVLLVSHDLELVERLCPTVHVLADG 226
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAklrvQMRAELKRLQ----QRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-238 |
9.96e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.49 E-value: 9.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 19 GGPDVVHGIDLdVVPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTADVRR-------- 90
Cdd:PRK13652 15 GSKEALNNINF-IAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpddqifs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 91 --VSQD---GLAGIGIDPRwTVDRTLSAALKDArragrpsgrSVEDLLgdvaldaryaPRTIHSLSGGEKQRVALAVALA 165
Cdd:PRK13652 94 ptVEQDiafGPINLGLDEE-TVAHRVSSALHML---------GLEELR----------DRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199107692 166 TRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVF 238
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIF 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-220 |
1.22e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 17 GYGGPDVVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRT----VTKLSRRDKkQFTADVRRVS 92
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTA-VVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvayVPQRSEVPD-SLPLTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 93 QDGlagigidpRWtvdrtlsAALKDARRAGRPSGRSVEDLLGDVALdARYAPRTIHSLSGGEKQRVALAVALATRPRALL 172
Cdd:NF040873 79 AMG--------RW-------ARRGLWRRLTRDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1199107692 173 LDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTV 220
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-233 |
1.96e-24 |
|
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: 101.77 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 5 TTPILRATGLAAGY--GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRrdkk 82
Cdd:COG4987 330 GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGER-VAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE---- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 83 qftADVRR----VSQDG------------LAGIGIDprwtvDRTLSAALKDAR----RAGRPSGrsVEDLLGDvalDARy 142
Cdd:COG4987 405 ---DDLRRriavVPQRPhlfdttlrenlrLARPDAT-----DEELWAALERVGlgdwLAALPDG--LDTWLGE---GGR- 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 143 aprtihSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAelGTAVLLVSHDLELVERlCPTVHV 222
Cdd:COG4987 471 ------RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILV 541
|
250
....*....|.
gi 1199107692 223 LADGTFVTSGA 233
Cdd:COG4987 542 LEDGRIVEQGT 552
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
28-242 |
7.69e-24 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 98.41 E-value: 7.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 28 DLDVVPGAPPVGIV---GESGAGKSTVVRALVGLVRPTAGHVTYAGRTvtkLSRRDKKQFTADVRR----VSQDGLagig 100
Cdd:PRK11144 14 CLTVNLTLPAQGITaifGRSGAGKTSLINAISGLTRPQKGRIVLNGRV---LFDAEKGICLPPEKRrigyVFQDAR---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 101 IDPRWTVDRTLSAALKDARRAgrpSGRSVEDLLGDVALDARYaPrtiHSLSGGEKQRVALAVALATRPRALLLDEPLTAV 180
Cdd:PRK11144 87 LFPHYKVRGNLRYGMAKSMVA---QFDKIVALLGIEPLLDRY-P---GSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199107692 181 DPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFAGTA 242
Cdd:PRK11144 160 DLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-238 |
1.27e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.85 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGYGGPDVVHGIDLDVvPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRdkkQFTAD 87
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSL-PTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR---QLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 88 VRRVSQDGLAGIGIDPRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVALATR 167
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINH-LADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 168 PRALLLDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGA---------LRDVF 238
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTpeevmtpglLRTVF 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-211 |
1.81e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 96.24 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLAAGYGGPD--VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKlsrrdkkQF 84
Cdd:PRK13635 4 EIIRVEHISFRYPDAAtyALKDVSFSVYEGEW-VAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE-------ET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 85 TADVRR-----------------VSQD---GLAGIGIdPRWTVDRTLSAALKDARragrpsgrsVEDllgdvaldarYAP 144
Cdd:PRK13635 76 VWDVRRqvgmvfqnpdnqfvgatVQDDvafGLENIGV-PREEMVERVDQALRQVG---------MED----------FLN 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 145 RTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDV---VRRLGDataELGTAVLLVSHDLE 211
Cdd:PRK13635 136 REPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVletVRQLKE---QKGITVLSITHDLD 202
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-245 |
2.45e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.65 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 28 DLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGR--TVTKLSRR-------DKKQFTAdvRRVSQDglAG 98
Cdd:PRK10771 19 DLTVERGER-VAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRRpvsmlfqENNLFSH--LTVAQN--IG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 99 IGIDPRWTVDRTLSAALKD-ARRAGrpsgrsVEDLLgdvaldaryaPRTIHSLSGGEKQRVALAVALATRPRALLLDEPL 177
Cdd:PRK10771 94 LGLNPGLKLNAAQREKLHAiARQMG------IEDLL----------ARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199107692 178 TAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFAGTAPGA 245
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASAS 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-216 |
2.49e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.88 E-value: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 22 DVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKkqftADVRrvsQDGLAGI-- 99
Cdd:PRK11629 23 DVLHNVSFSIGEGEM-MAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAK----AELR---NQKLGFIyq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 100 --GIDPRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDARYAPRTiHSLSGGEKQRVALAVALATRPRALLLDEPL 177
Cdd:PRK11629 95 fhHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1199107692 178 TAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERL 216
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-247 |
2.60e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.62 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 5 TTPILRATGLAAGY-----------GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRpTAGHVTYAGRTV 73
Cdd:PRK15134 272 ASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGET-LGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 74 TKLSRRDKKQFTADVRRVSQDGLAGIgiDPRWTV-----------DRTLSAALKDARragrpsgrsVEDLLGDVALDARY 142
Cdd:PRK15134 350 HNLNRRQLLPVRHRIQVVFQDPNSSL--NPRLNVlqiieeglrvhQPTLSAAQREQQ---------VIAVMEEVGLDPET 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 143 APRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHV 222
Cdd:PRK15134 419 RHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIV 498
|
250 260
....*....|....*....|....*
gi 1199107692 223 LADGTFVTSGALRDVFAgtAPGADH 247
Cdd:PRK15134 499 LRQGEVVEQGDCERVFA--APQQEY 521
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
9-233 |
2.73e-23 |
|
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: 98.68 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGY-GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRrdkkqftAD 87
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGER-VALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP-------AS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 88 VRRvsqdGLAGIGIDPRWtvdrtLSAALKDARRAGRP--SGRSVEDLLGDVALDA--RYAPRTIHS--------LSGGEK 155
Cdd:COG4988 409 WRR----QIAWVPQNPYL-----FAGTIRENLRLGRPdaSDEELEAALEAAGLDEfvAALPDGLDTplgeggrgLSGGQA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199107692 156 QRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAelGTAVLLVSHDLELVERlCPTVHVLADGTFVTSGA 233
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGT 554
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
38-238 |
3.29e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.50 E-value: 3.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTklsrrDKKQFTADVRRvsQDGLA---------------GIGID 102
Cdd:PRK13637 36 VGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT-----DKKVKLSDIRK--KVGLVfqypeyqlfeetiekDIAFG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 103 PRwtvDRTLSAA--LKDARRAGRPSGRSVEDllgdvaldarYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAV 180
Cdd:PRK13637 109 PI---NLGLSEEeiENRVKRAMNIVGLDYED----------YKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199107692 181 DPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVF 238
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
24-211 |
3.51e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 93.70 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 24 VHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRP---TAGHVTYAGRTVTKLSrrdkkqftADVRRVS---QDGLa 97
Cdd:COG4136 17 LAPLSLTVAPGEI-LTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALP--------AEQRRIGilfQDDL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 98 gigIDPRWTVDRTLSAALkdARRAGRPSGRS-VEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEP 176
Cdd:COG4136 87 ---LFPHLSVGENLAFAL--PPTIGRAQRRArVEQALEEAGLAG-FADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1199107692 177 LTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLE 211
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
39-258 |
4.33e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 96.13 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 39 GIVGESGAGKSTVVRALVGLVRP----TAGHVTYAGRTVTKLSRRDKKQFTA-DVRRVSQDGLAGIgiDPRWTVDRTLSA 113
Cdd:COG4170 37 GLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIIGrEIAMIFQEPSSCL--DPSAKIGDQLIE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 114 ALKDA-------RRAGRPSGRSVEdLLGDV------ALDARYAprtiHSLSGGEKQRVALAVALATRPRALLLDEPLTAV 180
Cdd:COG4170 115 AIPSWtfkgkwwQRFKWRKKRAIE-LLHRVgikdhkDIMNSYP----HELTEGECQKVMIAMAIANQPRLLIADEPTNAM 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 181 DPAMRGDVVRRLgDATAEL-GTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFAGTApgadHPSVRGLAEAAP 258
Cdd:COG4170 190 ESTTQAQIFRLL-ARLNQLqGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPH----HPYTKALLRSMP 263
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-232 |
4.40e-23 |
|
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: 93.71 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 27 IDLDV-VPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKqftadVRRVSQDGlagiGIDPRW 105
Cdd:cd03298 15 MHFDLtFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP-----VSMLFQEN----NLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 106 TVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDARYApRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMR 185
Cdd:cd03298 86 TVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEK-RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199107692 186 GDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:cd03298 165 AEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-237 |
6.73e-23 |
|
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: 93.68 E-value: 6.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 26 GIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkkqftADVRRVSQDglagIGIDPRW 105
Cdd:TIGR01184 3 GVNLTIQQGEF-ISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG--------PDRMVVFQN----YSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 106 TVDRTLSAALKDARRAGRPSGRS--VEDLLGDVALdARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPA 183
Cdd:TIGR01184 70 TVRENIALAVDRVLPDLSKSERRaiVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199107692 184 MRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDV 237
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-229 |
2.75e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.47 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 2 STTTTPILRATGLaagyGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDK 81
Cdd:COG1129 250 AAPGEVVLEVEGL----SVGGVVRDVSFSVRAGEI-LGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 82 KQ-----FTADvRRvsQDGLAgigidPRWTVDRTLS-AALKDARRAGRPSGRS----VEDLLGDVALDARYAPRTIHSLS 151
Cdd:COG1129 325 IRagiayVPED-RK--GEGLV-----LDLSIRENITlASLDRLSRGGLLDRRReralAEEYIKRLRIKTPSPEQPVGNLS 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199107692 152 GGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADGTFV 229
Cdd:COG1129 397 GGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-209 |
2.81e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 92.43 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 6 TPILrATGLAAGYGGPDVVHGIDLDVvPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVtYAGRTVTKLSRRDKKQFT 85
Cdd:PRK11247 11 TPLL-LNAVSKRYGERTVLNQLDLHI-PAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 86 ADVR-----RVSQDglAGIGIDPRWTvdrtlsaalKDARRAgrpsgrsvedlLGDVALDARyAPRTIHSLSGGEKQRVAL 160
Cdd:PRK11247 88 QDARllpwkKVIDN--VGLGLKGQWR---------DAALQA-----------LAAVGLADR-ANEWPAALSGGQKQRVAL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1199107692 161 AVALATRPRALLLDEPLTAVDPAMR---GDVVRRLgdaTAELGTAVLLVSHD 209
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALDALTRiemQDLIESL---WQQHGFTVLLVTHD 193
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-232 |
6.05e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.97 E-value: 6.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 12 TGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQftadVRRV 91
Cdd:PRK13536 45 AGVSKSYGDKAVVNGLSFTVASGEC-FGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR----IGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 92 SQ-DGLagigiDPRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDARYAPRtIHSLSGGEKQRVALAVALATRPRA 170
Cdd:PRK13536 120 PQfDNL-----DLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADAR-VSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199107692 171 LLLDEPLTAVDPAMRGDVVRRLGDATAeLGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-258 |
8.73e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.00 E-value: 8.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 5 TTPILRATGLAAGY--GGPD--VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGL-----VRPTAGHVTYAGRTVTK 75
Cdd:PRK15134 2 TQPLLAIENLSVAFrqQQTVrtVVNDVSLQIEAGET-LALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 76 LSRRDkkqftadVRRVSQDGLAGI------GIDPRWTVDRTLSAALKDARRAGRPSGRS-VEDLLGDVALdaRYAPRTI- 147
Cdd:PRK15134 81 ASEQT-------LRGVRGNKIAMIfqepmvSLNPLHTLEKQLYEVLSLHRGMRREAARGeILNCLDRVGI--RQAAKRLt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 148 ---HSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLA 224
Cdd:PRK15134 152 dypHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQ 231
|
250 260 270
....*....|....*....|....*....|....
gi 1199107692 225 DGTFVTSGALRDVFAgtAPgaDHPSVRGLAEAAP 258
Cdd:PRK15134 232 NGRCVEQNRAATLFS--AP--THPYTQKLLNSEP 261
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
7-232 |
1.30e-21 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 90.66 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRtvtklSRRDKKQFT- 85
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRDVSFDLYPGEV-LGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMR-----SGAELELYQl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 86 --ADVRRVSQDGLAGIGIDPRWTVDRTLSAALKDARR----AGRPSGR---SVEDLLGDVALDARYAPRTIHSLSGGEKQ 156
Cdd:TIGR02323 76 seAERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERlmaiGARHYGNiraTAQDWLEEVEIDPTRIDDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 157 RVALAVALATRPRALLLDEPLTAVDPAMRG---DVVRRLgdaTAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQArllDLLRGL---VRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-260 |
1.34e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.41 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 5 TTPILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQf 84
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGEC-FGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 85 tadVRRVSQ-DGLagigiDPRWTVDRTLsaaLKDARRAGRPSG---RSVEDLLGDVALDARyAPRTIHSLSGGEKQRVAL 160
Cdd:PRK13537 82 ---VGVVPQfDNL-----DPDFTVRENL---LVFGRYFGLSAAaarALVPPLLEFAKLENK-ADAKVGELSGGMKRRLTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 161 AVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFAG 240
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
250 260
....*....|....*....|....*..
gi 1199107692 241 TAP-------GADHPSVRGlaEAAPLA 260
Cdd:PRK13537 229 EIGcdvieiyGPDPVALRD--ELAPLA 253
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-232 |
2.70e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 89.60 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 4 TTTPILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTklsRRDKKQ 83
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEV-LGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQ---LRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 84 FTADVRR---------VSQ---DGL-----AGIGIDPRwtvdrtLSAAlkDARRAGRPSGRSVeDLLGDVALDARY---A 143
Cdd:PRK11701 78 LSEAERRrllrtewgfVHQhprDGLrmqvsAGGNIGER------LMAV--GARHYGDIRATAG-DWLERVEIDAARiddL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 144 PRTihsLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRG---DVVRRLgdaTAELGTAVLLVSHDLELVERLCPTV 220
Cdd:PRK11701 149 PTT---FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQArllDLLRGL---VRELGLAVVIVTHDLAVARLLAHRL 222
|
250
....*....|..
gi 1199107692 221 HVLADGTFVTSG 232
Cdd:PRK11701 223 LVMKQGRVVESG 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-239 |
3.18e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 90.29 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 20 GPDVVHGIDLdVVPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVtKLSRR----------------DKKQ 83
Cdd:PRK13636 18 GTHALKGINI-NIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmklresvgmvfqdpDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 84 FTADVRRVSQDGLAGIGIdPRWTVDRTLSAALKdarRAGrpsgrsVEDLlgdvaldaRYAPrtIHSLSGGEKQRVALAVA 163
Cdd:PRK13636 96 FSASVYQDVSFGAVNLKL-PEDEVRKRVDNALK---RTG------IEHL--------KDKP--THCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199107692 164 LATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-211 |
5.32e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.15 E-value: 5.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLAAGYGGPD----VVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkk 82
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVV-ALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 83 qftADVRRVSQ-DGLAgigidPRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDArYAPRTIHSLSGGEKQRVALA 161
Cdd:COG4525 76 ---ADRGVVFQkDALL-----PWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLAD-FARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1199107692 162 VALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLE 211
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVE 196
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-232 |
5.73e-21 |
|
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: 91.79 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLAAGY-----GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTY-AGRT---VTKLS 77
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEI-FGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEwvdMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 78 RRDKKQFTADVRRVSQDglagIGIDPRWTVDRTLSAA----LKD--ARRagrpsgRSVEdLLGDVALDARYA----PRTI 147
Cdd:TIGR03269 357 PDGRGRAKRYIGILHQE----YDLYPHRTVLDNLTEAigleLPDelARM------KAVI-TLKMVGFDEEKAeeilDKYP 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 148 HSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGT 227
Cdd:TIGR03269 426 DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGK 505
|
....*
gi 1199107692 228 FVTSG 232
Cdd:TIGR03269 506 IVKIG 510
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
38-215 |
5.78e-21 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 87.67 E-value: 5.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFtadvRR-----VSQD-GLagigIDPRwTVDRTL 111
Cdd:TIGR03608 27 YAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKF----RReklgyLFQNfAL----IENE-TVEENL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 112 SAALKDARRAGRPSGRSVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRgDVVRR 191
Cdd:TIGR03608 98 DLGLKYKKLSKKEKREKKKEALEKVGLNL-KLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNR-DEVLD 175
|
170 180
....*....|....*....|....
gi 1199107692 192 LGDATAELGTAVLLVSHDLELVER 215
Cdd:TIGR03608 176 LLLELNDEGKTIIIVTHDPEVAKQ 199
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-226 |
7.93e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.62 E-value: 7.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 19 GGPDVVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDkkqfTADVRRvsQDGLag 98
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAF-LTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRE----VPFLRR--QIGM-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 99 IGIDPRWTVDRT----LSAALKDARRAGRPSGRSVEDLLGDVAL--DARYAPRtihSLSGGEKQRVALAVALATRPRALL 172
Cdd:PRK10908 84 IFQDHHLLMDRTvydnVAIPLIIAGASGDDIRRRVSAALDKVGLldKAKNFPI---QLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1199107692 173 LDEPLTAVDPAMRGDVVrRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADG 226
Cdd:PRK10908 161 ADEPTGNLDDALSEGIL-RLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
25-226 |
9.34e-21 |
|
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: 87.46 E-value: 9.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 25 HGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTADVRRVSQDGLagigIDPR 104
Cdd:cd03292 18 DGINISISAGEF-VFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQDFR----LLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 105 WTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDARYapRTIHS-LSGGEKQRVALAVALATRPRALLLDEPLTAVDPA 183
Cdd:cd03292 93 RNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKH--RALPAeLSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1199107692 184 MRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADG 226
Cdd:cd03292 171 TTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-239 |
1.66e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 87.72 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGaPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVT-------KLSRRDK 81
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAG-DVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 82 KQFTADVRRVSQdGLAGIGIDPRWTV-DRTLSAALKDARRAGRPSGRSVEDLLGDVALDARYAPRTIHSLSGGEKQRVAL 160
Cdd:PRK10619 85 NQLRLLRTRLTM-VFQHFNLWSHMTVlENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 161 AVALATRPRALLLDEPLTAVDPAMRGDVVRRLgDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIM-QQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-211 |
2.25e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.45 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGYGGPDVVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTAD 87
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLV-VLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 88 VRRVSQDGLAGIGIDPRwtvdrtLSAALKDARRAgrpsgrSVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVALATR 167
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQ------LAGVEKMQRLE------IAHQMLKKVGLEG-AEKRYIWQLSGGQRQRVGIARALAAN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1199107692 168 PRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLE 211
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIE 190
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
13-239 |
3.69e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 86.73 E-value: 3.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 13 GLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTklSRRDKKQFTADVRRVS 92
Cdd:PRK11264 8 NLVKKFHGQTVLHGIDLEVKPGEV-VAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITID--TARSLSQQKGLIRQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 93 QDG---LAGIGIDPRWTV-DRTLSAAL---KDARRAGRPSGRSvedLLGDVALDAR---YAPRtihsLSGGEKQRVALAV 162
Cdd:PRK11264 85 QHVgfvFQNFNLFPHRTVlENIIEGPVivkGEPKEEATARARE---LLAKVGLAGKetsYPRR----LSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199107692 163 ALATRPRALLLDEPLTAVDPAMRGDVVRRLgDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTI-RQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
23-232 |
4.24e-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: 85.88 E-value: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRrdkkqftaDVRRVSQDGLAGIGID 102
Cdd:cd03266 20 AVDGVSFTVKPGEV-TGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA--------EARRRLGFVSDSTGLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 103 PRWTVDRTLS-----AALKDARRAGRpsgrsVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPL 177
Cdd:cd03266 91 DRLTARENLEyfaglYGLKGDELTAR-----LEELADRLGMEE-LLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 178 TAVD----PAMRgDVVRRLgdatAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:cd03266 165 TGLDvmatRALR-EFIRQL----RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-226 |
4.51e-20 |
|
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: 84.58 E-value: 4.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGG--PDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFta 86
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGES-LAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 87 dVRRVSQDglagigidprwtvDRTLSAALKDArragrpsgrsvedllgdvaldaryaprtIhsLSGGEKQRVALAVALAT 166
Cdd:cd03246 78 -VGYLPQD-------------DELFSGSIAEN----------------------------I--LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199107692 167 RPRALLLDEPLTAVDPAmrGDvvRRLGDATAEL---GTAVLLVSHDLELVERlCPTVHVLADG 226
Cdd:cd03246 114 NPRILVLDEPNSHLDVE--GE--RALNQAIAALkaaGATRIVIAHRPETLAS-ADRILVLEDG 171
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
8-239 |
1.84e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.13 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGY-GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVtklsRRDKKQFTA 86
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEM-VALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI----KYDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 87 dVRRVsqdglagIGI---DPrwtvDRTLSAALKDARRAGRPSG---------RSVEDLLGDVALDArYAPRTIHSLSGGE 154
Cdd:PRK13639 76 -VRKT-------VGIvfqNP----DDQLFAPTVEEDVAFGPLNlglskeeveKRVKEALKAVGMEG-FENKPPHHLSGGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 155 KQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGAL 234
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
....*
gi 1199107692 235 RDVFA 239
Cdd:PRK13639 222 KEVFS 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-238 |
1.86e-19 |
|
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: 84.75 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 6 TPILRATGLAAGYGGPDVVHGIDLDVVPG---AppvgIVGESGAGKSTVVRALVGLVRPTAG-HVTYAGRTVTKLSRRD- 80
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGehwA----ILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWEl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 81 KK-----------QFTAD--VRRVSQDGL-AGIGIDPRWTVDrtlsaalkDARRAgrpsgrsvEDLLGDVALDArYAPRT 146
Cdd:COG1119 77 RKriglvspalqlRFPRDetVLDVVLSGFfDSIGLYREPTDE--------QRERA--------RELLELLGLAH-LADRP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 147 IHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDlelVERLCPTV-HV--L 223
Cdd:COG1119 140 FGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHH---VEEIPPGItHVllL 216
|
250
....*....|....*
gi 1199107692 224 ADGTFVTSGALRDVF 238
Cdd:COG1119 217 KDGRVVAAGPKEEVL 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-238 |
1.94e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.56 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 27 IDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdKKQFTADVRRvsqdglaGIGIDPRWT 106
Cdd:PRK13643 25 IDLEVKKGSY-TALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS---KQKEIKPVRK-------KVGVVFQFP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 107 VDRTLS-AALKDARRAGRPSGRSVEDL-------LGDVALDARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLT 178
Cdd:PRK13643 94 ESQLFEeTVLKDVAFGPQNFGIPKEKAekiaaekLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 179 AVDPAMRGDVVrRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVF 238
Cdd:PRK13643 174 GLDPKARIEMM-QLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
39-258 |
2.06e-19 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 86.01 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 39 GIVGESGAGKSTVVRALVGLV----RPTAGHVTYAGRTVTKLSRRDKKQFTA-DVRRVSQDGLAGIgiDPRWTVDRTLSA 113
Cdd:PRK15093 37 GLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRERRKLVGhNVSMIFQEPQSCL--DPSERVGRQLMQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 114 ALKDARRAGR-------PSGRSVEdLLGDVAL-DARYAPRTI-HSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAM 184
Cdd:PRK15093 115 NIPGWTYKGRwwqrfgwRKRRAIE-LLHRVGIkDHKDAMRSFpYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTT 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199107692 185 RGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFagTAPgaDHPSVRGLAEAAP 258
Cdd:PRK15093 194 QAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELV--TTP--HHPYTQALIRAIP 263
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
38-239 |
2.28e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.07 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVT------KLSRRDKK-----QFtADVRRVSQDGLAGIGIDPRwt 106
Cdd:PRK13634 36 VAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKvgivfQF-PEHQLFEETVEKDICFGPM-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 107 vdrTLSAALKDARRAGRpsgrsveDLLGDVALDARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRG 186
Cdd:PRK13634 113 ---NFGVSEEDAKQKAR-------EMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199107692 187 DVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFA 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-232 |
2.45e-19 |
|
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: 83.74 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkkqftadv 88
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGER-IGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG----------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 rrvsqdglAGIGIDPRWTVdrtlsaaLKDARRAGRPSGRSVEDL------------LGDvALDARYapRTihsLSGGEKQ 156
Cdd:cd03220 91 --------LGGGFNPELTG-------RENIYLNGRLLGLSRKEIdekideiiefseLGD-FIDLPV--KT---YSSGMKA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199107692 157 RVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLgDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:cd03220 150 RLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRL-RELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-239 |
4.34e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.59 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLsrrdkkqftadvrrvsqdGLAGiGID 102
Cdd:COG1134 41 ALKDVSFEVERGES-VGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL------------------ELGA-GFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 103 PRWTVdR---TLSAALKDARRAgrpsgrSVEDLLGDVA----L-DARYAPrtIHSLSGGEKQRVALAVALATRPRALLLD 174
Cdd:COG1134 101 PELTG-ReniYLNGRLLGLSRK------EIDEKFDEIVefaeLgDFIDQP--VKTYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199107692 175 EPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:COG1134 172 EVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
18-232 |
6.42e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 83.14 E-value: 6.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 18 YGGPDVVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTV---TKLSRRDKKQFTADVRRVSQD 94
Cdd:COG4161 12 YGSHQALFDINLECPSGETLV-LLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 95 glagIGIDPRWTVDRTLSAA----LKDARRAGRPSGrsvEDLLGDVALDaRYAPRTIHSLSGGEKQRVALAVALATRPRA 170
Cdd:COG4161 91 ----YNLWPHLTVMENLIEApckvLGLSKEQAREKA---MKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199107692 171 LLLDEPLTAVDPAMRGDVV---RRLgdatAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVeiiREL----SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-254 |
7.77e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.60 E-value: 7.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTyagrtVTKLSRRDKKQfTADVRR------------ 90
Cdd:PRK13633 25 ALDDVNLEVKKGEF-LVILGRNGSGKSTIAKHMNALLIPSEGKVY-----VDGLDTSDEEN-LWDIRNkagmvfqnpdnq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 91 -----VSQD---GLAGIGIDP---RWTVDRTLsaalkdaRRAGRPSGRsvedllgdvaldaRYAPrtiHSLSGGEKQRVA 159
Cdd:PRK13633 98 ivatiVEEDvafGPENLGIPPeeiRERVDESL-------KKVGMYEYR-------------RHAP---HLLSGGQKQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 160 LAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDL-ELVErlCPTVHVLADGTFVTSGALRDVF 238
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMeEAVE--ADRIIVMDSGKVVMEGTPKEIF 232
|
250 260
....*....|....*....|
gi 1199107692 239 AGT----APGADHPSVRGLA 254
Cdd:PRK13633 233 KEVemmkKIGLDVPQVTELA 252
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
5-232 |
1.10e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.73 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 5 TTPILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSR------ 78
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEI-VSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqiarm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 79 ---------RDKKQFT-------ADVRRVSQDGLAGIGIDPRWtvdrtlsaalkdaRRAGRPSGRSVEDLLGDVALDArY 142
Cdd:PRK11300 81 gvvrtfqhvRLFREMTvienllvAQHQQLKTGLFSGLLKTPAF-------------RRAESEALDRAATWLERVGLLE-H 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 143 APRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHV 222
Cdd:PRK11300 147 ANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYV 226
|
250
....*....|
gi 1199107692 223 LADGTFVTSG 232
Cdd:PRK11300 227 VNQGTPLANG 236
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-232 |
1.22e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 84.83 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 19 GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRrdkkqftADVRR----VSQD 94
Cdd:COG1132 351 GDRPVLKDISLTIPPGET-VALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTL-------ESLRRqigvVPQD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 95 ------------GLAGIGIDprwtvDRTLSAALKDARragrpsgrsVEDLLgdVALDARYAprTI-----HSLSGGEKQR 157
Cdd:COG1132 423 tflfsgtireniRYGRPDAT-----DEEVEEAAKAAQ---------AHEFI--EALPDGYD--TVvgergVNLSGGQRQR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199107692 158 VALAVALATRPRALLLDEPLTAVDPAmrgdVVRRLGDATAEL--GTAVLLVSHDLELVeRLCPTVHVLADGTFVTSG 232
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTE----TEALIQEALERLmkGRTTIVIAHRLSTI-RNADRILVLDDGRIVEQG 556
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-237 |
1.27e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.69 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 4 TTTPILRATGLAAGYGGpdVV--HGIDLDVVPGAppV-GIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrd 80
Cdd:COG3845 1 MMPPALELRGITKRFGG--VVanDDVSLTVRPGE--IhALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRS--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 81 kkqfTADVRRvsqdglAGIG---------------------IDPRWTVDRTLSAALKDARRagrpsgrsVEDLLG-DVAL 138
Cdd:COG3845 74 ----PRDAIA------LGIGmvhqhfmlvpnltvaenivlgLEPTKGGRLDRKAARARIRE--------LSERYGlDVDP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 139 DARyaprtIHSLSGGEKQRVALAVALATRPRALLLDEPlTAV-DPA-----MRgdVVRRLgdatAELGTAVLLVSHDLEL 212
Cdd:COG3845 136 DAK-----VEDLSVGEQQRVEILKALYRGARILILDEP-TAVlTPQeadelFE--ILRRL----AAEGKSIIFITHKLRE 203
|
250 260
....*....|....*....|....*
gi 1199107692 213 VERLCPTVHVLADGTFVTSGALRDV 237
Cdd:COG3845 204 VMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
8-227 |
1.29e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.75 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLV---RPTAGHVTYAGRTVTKLSR--RDKK 82
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEM-VALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGRlaRDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 83 QFTAD----------VRRVS--QDGLAG-IGIDPRW-TVDRTLSAALKdaRRAGRPSGRsvedllgdVALdARYAPRTIH 148
Cdd:PRK09984 83 KSRANtgyifqqfnlVNRLSvlENVLIGaLGSTPFWrTCFSWFTREQK--QRALQALTR--------VGM-VHFAHQRVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 149 SLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTV------HV 222
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIvalrqgHV 231
|
....*
gi 1199107692 223 LADGT 227
Cdd:PRK09984 232 FYDGS 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-232 |
1.36e-18 |
|
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: 81.03 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGL--VRPTAGHVTYAGRTVTKLSrrdkkqfta 86
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHA-LMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLP--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 87 dvrrVSQDGLAGIGIDPRWTVdrtlsaalkdarragRPSGRSVEDLLGDVALdaryaprtihSLSGGEKQRVALAVALAT 166
Cdd:cd03217 71 ----PEERARLGIFLAFQYPP---------------EIPGVKNADFLRYVNE----------GFSGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 167 RPRALLLDEPLTAVD-PAMR--GDVVRRLgdatAELGTAVLLVSHDLELVERLCPT-VHVLADGTFVTSG 232
Cdd:cd03217 122 EPDLAILDEPDSGLDiDALRlvAEVINKL----REEGKSVLIITHYQRLLDYIKPDrVHVLYDGRIVKSG 187
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
40-239 |
2.51e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 81.76 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRALVGLVRPTAGHVTYAGRtvtKLSRRDKKQFTADVRRVSQDglAGIGIDPRWTVDRTLSAALK-DA 118
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLHFGDYSYRSQRIRMIFQD--PSTSLNPRQRISQILDFPLRlNT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 119 RRAGRPSGRSVEDLLGDVALDARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAE 198
Cdd:PRK15112 119 DLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEK 198
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1199107692 199 LGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:PRK15112 199 QGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-242 |
2.53e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.54 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGyggpdvVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkkqfTAD 87
Cdd:PRK10070 34 ILEKTGLSLG------VKDASLAIEEGEIFV-IMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIS-------DAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 88 VRRVSQDGLAGI----GIDPRWTVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDaRYAPRTIHSLSGGEKQRVALAVA 163
Cdd:PRK10070 100 LREVRRKKIAMVfqsfALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 164 LATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFAGTA 242
Cdd:PRK10070 179 LAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
38-258 |
3.17e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.75 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRD---KKQFTADVRRVSQDGLAGI------GIDPRWTVD 108
Cdd:PRK10261 45 LAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVielSEQSAAQMRHVRGADMAMIfqepmtSLNPVFTVG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 109 RTLSAALKDARRAGRPSG-RSVEDLLGDVALDARYA--PRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMR 185
Cdd:PRK10261 125 EQIAESIRLHQGASREEAmVEAKRMLDQVRIPEAQTilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQ 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199107692 186 GDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFagTAPgaDHPSVRGLAEAAP 258
Cdd:PRK10261 205 AQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIF--HAP--QHPYTRALLAAVP 273
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
18-238 |
3.97e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 82.46 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 18 YGGPDVVHGIDLdVVPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKkqftaDVRRVSQDgla 97
Cdd:PRK11432 16 FGSNTVIDNLNL-TIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR-----DICMVFQS--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 98 gIGIDPRWTVDRTLSAALKdarRAGRPSG---RSVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVALATRPRALLLD 174
Cdd:PRK11432 87 -YALFPHMSLGENVGYGLK---MLGVPKEerkQRVKEALELVDLAG-FEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199107692 175 EPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVF 238
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
40-238 |
3.98e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 81.34 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTADVRRVSQDGLAGIgidprwTVDRTLSAALKDAR 119
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQFVGS------IVKYDVAFGLENHA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 120 RAGRPSGRSVEDLLGDVALDAR--YAPrtiHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATA 197
Cdd:PRK13648 114 VPYDEMHRRVSEALKQVDMLERadYEP---NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKS 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199107692 198 ELGTAVLLVSHDL-ELVErlCPTVHVLADGTFVTSGALRDVF 238
Cdd:PRK13648 191 EHNITIISITHDLsEAME--ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-232 |
4.01e-18 |
|
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: 80.84 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTADVRRVSQ--------D 94
Cdd:cd03267 36 ALKGISFTIEKGEI-VGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQlwwdlpviD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 95 GLAGI----GIDP---RWTVDRtLSAALKdarragrpsgrsVEDLLgdvaldarYAPrtIHSLSGGEKQRVALAVALATR 167
Cdd:cd03267 115 SFYLLaaiyDLPParfKKRLDE-LSELLD------------LEELL--------DTP--VRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199107692 168 PRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-238 |
6.32e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 80.59 E-value: 6.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 5 TTPILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRAL--VGLVRP---TAGHVTYAGRTVTKlSRR 79
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEI-TALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYS-PRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 80 DKKQFTADVRRVSQD--------------GLAGIGIDPRWTVDRTLSAALKDARragrpSGRSVEDLLGDVALdaryapr 145
Cdd:PRK14239 80 DTVDLRKEIGMVFQQpnpfpmsiyenvvyGLRLKGIKDKQVLDEAVEKSLKGAS-----IWDEVKDRLHDSAL------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 146 tihSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRL----GDATaelgtaVLLVSHDLELVERLCPTVH 221
Cdd:PRK14239 148 ---GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLlglkDDYT------MLLVTRSMQQASRISDRTG 218
|
250
....*....|....*..
gi 1199107692 222 VLADGTFVTSGALRDVF 238
Cdd:PRK14239 219 FFLDGDLIEYNDTKQMF 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
9-239 |
7.13e-18 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 82.87 E-value: 7.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPD--VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGrtvtklsrrdkkqftA 86
Cdd:COG4618 331 LSVENLTVVPPGSKrpILRGVSFSLEPGEV-LGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG---------------A 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 87 DVRRVSQDGLAG-IG----------------------IDPRwtvdrtlsAALKDARRAGrpsgrsVEDLLG------DVA 137
Cdd:COG4618 395 DLSQWDREELGRhIGylpqdvelfdgtiaeniarfgdADPE--------KVVAAAKLAG------VHEMILrlpdgyDTR 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 138 LDARYAPrtihsLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAmrGDvvRRLGDATAEL---GTAVLLVSHDLELVe 214
Cdd:COG4618 461 IGEGGAR-----LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDE--GE--AALAAAIRALkarGATVVVITHRPSLL- 530
|
250 260
....*....|....*....|....*
gi 1199107692 215 RLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:COG4618 531 AAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-229 |
1.09e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.00 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGL-AAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQft 85
Cdd:COG3845 256 VVLEVENLsVRDDRGVPALKDVSLEVRAGEI-LGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRR-- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 86 ADVRRVSQDGLaGIGIDPRWTVdrTLSAALKDARRAGRPSG-----RSVEDLLGDVAldARYAPRT------IHSLSGGE 154
Cdd:COG3845 333 LGVAYIPEDRL-GRGLVPDMSV--AENLILGRYRRPPFSRGgfldrKAIRAFAEELI--EEFDVRTpgpdtpARSLSGGN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 155 KQRVALAVALATRPRALLLDEPlTavdpamRG-DV-----VRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTF 228
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQP-T------RGlDVgaiefIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
.
gi 1199107692 229 V 229
Cdd:COG3845 481 V 481
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
26-238 |
1.35e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.17 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 26 GIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSR-RDKKQFTADVRRVSQDGLAGIgidpr 104
Cdd:PRK13649 25 DVNLTIEDGSY-TAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQIRKKVGLVFQFPESQL----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 105 wtVDRTLsaaLKDARRAGRPSGRSVEDL-------LGDVALDARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPL 177
Cdd:PRK13649 99 --FEETV---LKDVAFGPQNFGVSQEEAealarekLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 178 TAVDPAMRGDVVrRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVF 238
Cdd:PRK13649 174 AGLDPKGRKELM-TLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-222 |
1.53e-17 |
|
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: 81.56 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLAAGYGGPD-VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTklsrrdkkQFT 85
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRpALRPVSFTVPPGER-VALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA--------DAD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 86 ADVRRvsqDGLAGIGIDPrWTVDRTLSAALKDARRAGrpSGRSVEDLLGDVALD--ARYAPRTIHS--------LSGGEK 155
Cdd:TIGR02857 391 ADSWR---DQIAWVPQHP-FLFAGTIAENIRLARPDA--SDAEIREALERAGLDefVAALPQGLDTpigeggagLSGGQA 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199107692 156 QRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAelGTAVLLVSHDLELVERLCPTVHV 222
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
38-239 |
1.55e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.26 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVT-KLSRRDKKQFTADVRRVSQ---------DGLAGIGIDPR--- 104
Cdd:PRK13641 36 VALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKKLRKKVSLVFQfpeaqlfenTVLKDVEFGPKnfg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 105 WTVDRTLSAALKDARRAGRPsgrsvEDLLGDVALDaryaprtihsLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAM 184
Cdd:PRK13641 116 FSEDEAKEKALKWLKKVGLS-----EDLISKSPFE----------LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199107692 185 RGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:PRK13641 181 RKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
9-232 |
1.63e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 79.34 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPG---AppvgIVGESGAGKSTVVRALVGL--VRPTAGHVTYAGRTVTKLSrrdkkq 83
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGevhA----IMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELS------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 84 ftADVRrvsqdGLAGI-----------GIdprwTVDRTLSAALKdARRAGRPSGRS----VEDLLGDVALDARYAPRTIH 148
Cdd:COG0396 71 --PDER-----ARAGIflafqypveipGV----SVSNFLRTALN-ARRGEELSAREflklLKEKMKELGLDEDFLDRYVN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 149 -SLSGGEKQRVALAVALATRPRALLLDEPLTAVDPamrgDVVRRLGDATAEL---GTAVLLVSHDLELVERLCPT-VHVL 223
Cdd:COG0396 139 eGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDI----DALRIVAEGVNKLrspDRGILIITHYQRILDYIKPDfVHVL 214
|
....*....
gi 1199107692 224 ADGTFVTSG 232
Cdd:COG0396 215 VDGRIVKSG 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-211 |
3.19e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.59 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLS--RRdkkqfTADVRRVSQDGLAGIG 100
Cdd:COG1101 21 ALDGLNLTIEEGDF-VTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPeyKR-----AKYIGRVFQDPMMGTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 101 idPRWTVD------------RTLSAALKDARRAG-----RPSGRSVEDLLGDValdaryaprtIHSLSGGEKQRVALAVA 163
Cdd:COG1101 95 --PSMTIEenlalayrrgkrRGLRRGLTKKRRELfrellATLGLGLENRLDTK----------VGLLSGGQRQALSLLMA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1199107692 164 LATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLE 211
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNME 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-235 |
3.77e-17 |
|
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: 80.64 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGlVRPTA---GHVTYAGRTVTKLSRRDKKQf 84
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGEC-VGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLKASNIRDTER- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 85 tadvrrvsqdglAGIGI-DPRWTVDRTLSAA----------LKDARRAGRPSGRSVEDLLGDVALDARYAPRTIHSLSGG 153
Cdd:TIGR02633 78 ------------AGIVIiHQELTLVPELSVAeniflgneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 154 EKQRVALAVALATRPRALLLDEP---LTAVDPAMRGDVVRRLgdatAELGTAVLLVSHDLELVERLCPTVHVLADGTFVT 230
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPsssLTEKETEILLDIIRDL----KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVA 221
|
....*
gi 1199107692 231 SGALR 235
Cdd:TIGR02633 222 TKDMS 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-227 |
3.91e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.90 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLdVVPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTA-DVRRVSQDGLAGIGI 101
Cdd:PRK10584 25 ILTGVEL-VVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAkHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 102 DPRWTVDrtLSAALKDARRagRPSGRSVEDLLGDVALDAR--YAPRtihSLSGGEKQRVALAVALATRPRALLLDEPlta 179
Cdd:PRK10584 104 NALENVE--LPALLRGESS--RQSRNGAKALLEQLGLGKRldHLPA---QLSGGEQQRVALARAFNGRPDVLFADEP--- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199107692 180 vdpamRGDVVRRLGDATAEL--------GTAVLLVSHDLELVERlCPTVHVLADGT 227
Cdd:PRK10584 174 -----TGNLDRQTGDKIADLlfslnrehGTTLILVTHDLQLAAR-CDRRLRLVNGQ 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
9-212 |
4.72e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.15 E-value: 4.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVtklsRRDKKQFTADv 88
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGEL-VQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI----RRQRDEYHQD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 rrvsqdgLAGIG----IDPRWTVDRTLSAALKDARRAGRpsgRSVEDLLGDVALdARYAPRTIHSLSGGEKQRVALAVAL 164
Cdd:PRK13538 76 -------LLYLGhqpgIKTELTALENLRFYQRLHGPGDD---EALWEALAQVGL-AGFEDVPVRQLSAGQQRRVALARLW 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1199107692 165 ATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLEL 212
Cdd:PRK13538 145 LTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPV 192
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
40-239 |
4.78e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 78.62 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKK------------QFT-ADVRRVSQDGLAGIGIDPRWT 106
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRhkigmvfqnpdnQFVgATVEDDVAFGLENKGIPHEEM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 107 VDRTLSAAlkdarragrpsgrsveDLLGDVALDARYAPRtihsLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRG 186
Cdd:PRK13650 118 KERVNEAL----------------ELVGMQDFKEREPAR----LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199107692 187 DVVRRLGDATAELGTAVLLVSHDLELVErLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:PRK13650 178 ELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFS 229
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-226 |
5.06e-17 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 80.21 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 6 TPILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTyagrtvtkLSRRDKKQFT 85
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSR-IGLLGRNGAGKSTLIKLLAGELAPVSGEIG--------LAKGIKLGYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 86 AdvrrvsQDGLAGIGIDPrwtvdrtlSAALKDARRAGRPSGRSVEDLLGDVALDARYAPRTIHSLSGGEKQRVALAVALA 165
Cdd:PRK10636 381 A------QHQLEFLRADE--------SPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVW 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 166 TRPRALLLDEPLTAVDPAMRgdvvRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADG 226
Cdd:PRK10636 447 QRPNLLLLDEPTNHLDLDMR----QALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDG 503
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
40-239 |
5.58e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 78.67 E-value: 5.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTklsRRDKKQFTADVRR----VSQDGLAGIGIDprwTVDRTLSAAL 115
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIT---HKTKDKYIRPVRKrigmVFQFPESQLFED---TVEREIIFGP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 116 KDARRAGRPSGRSVEDLLGDVALdaryaPRTIHSLS-----GGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVR 190
Cdd:PRK13646 112 KNFKMNLDEVKNYAHRLLMDLGF-----SRDVMSQSpfqmsGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMR 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1199107692 191 RLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:PRK13646 187 LLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-236 |
6.16e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 78.98 E-value: 6.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 24 VHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTAdvrrV----SQ------ 93
Cdd:COG4586 38 VDDISFTIEPGEI-VGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGV----VfgqrSQlwwdlp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 94 --DG---LAGI-GIDPRW---TVDRtLSAALkdarragrpsgrSVEDLLGdvaldaryapRTIHSLSGGEKQRVALAVAL 164
Cdd:COG4586 113 aiDSfrlLKAIyRIPDAEykkRLDE-LVELL------------DLGELLD----------TPVRQLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199107692 165 ATRPRALLLDEPLTAVDPAMRgDVVRR-LGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRD 236
Cdd:COG4586 170 LHRPKILFLDEPTIGLDVVSK-EAIREfLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEE 241
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
26-232 |
7.15e-17 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 77.30 E-value: 7.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 26 GIDLDVVPGAPpVGIVGESGAGKSTVVRALVG--LVRPTAGHVTYAGRTVTKLS---RRDKKQFTAdvrrvSQDGLAGIG 100
Cdd:TIGR01978 18 GVNLTVKKGEI-HAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDLLELEpdeRARAGLFLA-----FQYPEEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 101 IdprwTVDRTLSAALkDARRAGRPSG--------RSVEDLLGDVALDARYAPRTIH-SLSGGEKQRVALAVALATRPRAL 171
Cdd:TIGR01978 92 V----SNLEFLRSAL-NARRSARGEEpldlldfeKLLKEKLALLDMDEEFLNRSVNeGFSGGEKKRNEILQMALLEPKLA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199107692 172 LLDEPLTAVD-PAMRG--DVVRRLgdatAELGTAVLLVSHDLELVERLCP-TVHVLADGTFVTSG 232
Cdd:TIGR01978 167 ILDEIDSGLDiDALKIvaEGINRL----REPDRSFLIITHYQRLLNYIKPdYVHVLLDGRIVKSG 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-217 |
7.58e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.72 E-value: 7.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 18 YGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGR-TVTKLSRRDKKQFTADVRRVSQDGL 96
Cdd:COG0488 8 FGGRPLLDDVSLSINPGDR-IGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlRIGYLPQEPPLDDDLTVLDTVLDGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 97 AGIG--IDPRWTVDRTLSAALKDARRAGRPSGR-----------SVEDLLGDVALDARYAPRTIHSLSGGEKQRVALAVA 163
Cdd:COG0488 87 AELRalEAELEELEAKLAEPDEDLERLAELQEEfealggweaeaRAEEILSGLGFPEEDLDRPVSELSGGWRRRVALARA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 164 LATRPRALLLDEP---LtavdpamrgDV--VRRLGDATAELGTAVLLVSHDLELVERLC 217
Cdd:COG0488 167 LLSEPDLLLLDEPtnhL---------DLesIEWLEEFLKNYPGTVLVVSHDRYFLDRVA 216
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
9-226 |
7.82e-17 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 77.05 E-value: 7.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVvPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRtvtKLSRRDKKQFTADV 88
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTV-PKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGH---PWTRKDLHKIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 RR-------VSQDGLAgigidprwtvDRTLSAALKDARragrpsgrsVEDLLGDVALDaRYAPRTIHSLSGGEKQRVALA 161
Cdd:TIGR03740 77 ESpplyenlTARENLK----------VHTTLLGLPDSR---------IDEVLNIVDLT-NTGKKKAKQFSLGMKQRLGIA 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199107692 162 VALATRPRALLLDEPLTAVDPAMRGDvVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADG 226
Cdd:TIGR03740 137 IALLNHPKLLILDEPTNGLDPIGIQE-LRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEG 200
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
38-238 |
8.91e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 77.72 E-value: 8.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRD--KK----------QFtadvrrvsqdglagIGIdprw 105
Cdd:PRK13632 38 VAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKigiifqnpdnQF--------------IGA---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 106 TVDRTLSAALKDARRAGRPSGRSVEDLLGDVALDaRYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMR 185
Cdd:PRK13632 100 TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199107692 186 GDVVRRLGDATAELGTAVLLVSHDLELVeRLCPTVHVLADGTFVTSGALRDVF 238
Cdd:PRK13632 179 REIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
40-238 |
9.44e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.35 E-value: 9.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRALVGLVRPTAG-----------HVTYAGRTVTKLSRRDK--KQFTADVRRVSQDglagigidPRW- 105
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdKKNNHELITNPYSKKIKnfKELRRRVSMVFQF--------PEYq 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 106 ----TVDRTLS---AALKDARRAGRPSGRSVEDLLGdvaLDARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLT 178
Cdd:PRK13631 129 lfkdTIEKDIMfgpVALGVKKSEAKKLAKFYLNKMG---LDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTA 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 179 AVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVF 238
Cdd:PRK13631 206 GLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
39-208 |
9.66e-17 |
|
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: 76.93 E-value: 9.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 39 GIVGESGAGKSTVVRALVGLVRP---TAGHVTYAGRtvtklsRRDKKQFTADVRRVSQDGLagigIDPRWTVDRTL--SA 113
Cdd:cd03234 37 AILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQ------PRKPDQFQKCVAYVRQDDI----LLPGLTVRETLtyTA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 114 ALKDARRA--GRPSGRSVEDLLGDVAlDARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRR 191
Cdd:cd03234 107 ILRLPRKSsdAIRKKRVEDVLLRDLA-LTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVST 185
|
170
....*....|....*..
gi 1199107692 192 LGDaTAELGTAVLLVSH 208
Cdd:cd03234 186 LSQ-LARRNRIVILTIH 201
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-234 |
1.25e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 6 TPILRATGLAaGYGGPDvvhgIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQ-- 83
Cdd:PRK15439 266 APVLTVEDLT-GEGFRN----ISLEVRAGEI-LGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLArg 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 84 --FTADVRRVSqdglaGIGIDP--RWTV------DRTL-------SAALKDARRAgrpsgrsvedlLGDVALDARYAPRT 146
Cdd:PRK15439 340 lvYLPEDRQSS-----GLYLDAplAWNVcalthnRRGFwikpareNAVLERYRRA-----------LNIKFNHAEQAART 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 147 ihsLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDaTAELGTAVLLVSHDLELVERLCPTVHVLADG 226
Cdd:PRK15439 404 ---LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRS-IAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
....*...
gi 1199107692 227 TFvtSGAL 234
Cdd:PRK15439 480 EI--SGAL 485
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
8-239 |
1.28e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.86 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkkqFTAD 87
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEI-VGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP------LHAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 88 VRRvsqdglaGIGIDP-------RWTVDRTLSAAL---KDARRAGRPSgrSVEDLLGDVALdARYAPRTIHSLSGGEKQR 157
Cdd:PRK10895 76 ARR-------GIGYLPqeasifrRLSVYDNLMAVLqirDDLSAEQRED--RANELMEEFHI-EHLRDSMGQSLSGGERRR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 158 VALAVALATRPRALLLDEPLTAVDPAMRGDvVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDV 237
Cdd:PRK10895 146 VEIARALAANPKFILLDEPFAGVDPISVID-IKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
..
gi 1199107692 238 FA 239
Cdd:PRK10895 225 LQ 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-227 |
1.31e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 6 TPILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGhvtyagrtvtKLSRRDKKQft 85
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKI-LTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKRNGKLR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 86 advrrvsqdglagIGIDP-RWTVDRTLSAALKDARRAgRPSGRSvEDLLGdvALDARYAPRTI----HSLSGGEKQRVAL 160
Cdd:PRK09544 69 -------------IGYVPqKLYLDTTLPLTVNRFLRL-RPGTKK-EDILP--ALKRVQAGHLIdapmQKLSGGETQRVLL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199107692 161 AVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELV-----ERLCPTVHVLADGT 227
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmaktdEVLCLNHHICCSGT 203
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3-237 |
2.61e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.18 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 3 TTTTPILRATGLAAGYGGPDVVHGIDLDVvPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKk 82
Cdd:PRK10253 2 TESVARLRGEQLTLGYGKYTVAENLTVEI-PDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 83 qftadVRRVSQdgLAGIGIDPRwtvDRTLSAALKDARRAGRP---SGRSVEDLLGDVALDA----RYAPRTIHSLSGGEK 155
Cdd:PRK10253 80 -----ARRIGL--LAQNATTPG---DITVQELVARGRYPHQPlftRWRKEDEEAVTKAMQAtgitHLADQSVDTLSGGQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 156 QRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALR 235
Cdd:PRK10253 150 QRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPK 229
|
..
gi 1199107692 236 DV 237
Cdd:PRK10253 230 EI 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-235 |
3.27e-16 |
|
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: 78.13 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 6 TPILRATGLAAGYGGPD--VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTklsrrdkkq 83
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTSspAVDRLCVGVRPGEC-FGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL--------- 2004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 84 ftADVRRVSQDglagIGIDPRW-TVDRTLSAA---LKDARRAGRPSgRSVEDL----LGDVALDArYAPRTIHSLSGGEK 155
Cdd:TIGR01257 2005 --TNISDVHQN----MGYCPQFdAIDDLLTGRehlYLYARLRGVPA-EEIEKVanwsIQSLGLSL-YADRLAGTYSGGNK 2076
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 156 QRVALAVALATRPRALLLDEPLTAVDPAMRgdvvRRLGDATAEL---GTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:TIGR01257 2077 RKLSTAIALIGCPPLVLLDEPTTGMDPQAR----RMLWNTIVSIireGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLG 2152
|
...
gi 1199107692 233 ALR 235
Cdd:TIGR01257 2153 TIQ 2155
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-224 |
3.41e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 77.67 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYaGRTVtKLSRRDKkqftad 87
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGI-VGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-KLAYVDQ------ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 88 vrrvSQDGLagigiDPRWTVDRTLSAALKDARragrpsgrsvedlLGDVALDAR-YAPR----------TIHSLSGGEKQ 156
Cdd:TIGR03719 393 ----SRDAL-----DPNKTVWEEISGGLDIIK-------------LGKREIPSRaYVGRfnfkgsdqqkKVGQLSGGERN 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199107692 157 RVALAVALATRPRALLLDEPLTAVDPamrgDVVRRLGDATAELGTAVLLVSHDLELVERLCptVHVLA 224
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHDRWFLDRIA--THILA 512
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
9-214 |
4.03e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.45 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVtklsrrdkkqftADV 88
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEA-LQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL------------DFQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 RRVSQDGLAGIGIDPrwTVDRTLSAaLKDARRAGRPSGRS-VEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVALATR 167
Cdd:cd03231 68 RDSIARGLLYLGHAP--GIKTTLSV-LENLRFWHADHSDEqVEEALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199107692 168 PRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVE 214
Cdd:cd03231 144 RPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSE 190
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-215 |
4.26e-16 |
|
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: 75.22 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 20 GPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRtvtKLSRRDKKQFTADVRRVSQDGL--- 96
Cdd:cd03252 14 GPVILDNISLRIKPGEV-VGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGH---DLALADPAWLRRQVGVVLQENVlfn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 97 ----AGIGI-DPRWTVDRTLSAA-LKDARRAGRPSGRSVEDLLGDVALdaryaprtihSLSGGEKQRVALAVALATRPRA 170
Cdd:cd03252 90 rsirDNIALaDPGMSMERVIEAAkLAGAHDFISELPEGYDTIVGEQGA----------GLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199107692 171 LLLDEPLTAVDPAMRGDVVRRLGDATAelGTAVLLVSHDLELVER 215
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-237 |
5.15e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.13 E-value: 5.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 5 TTPILRATGLAAGYGGPDVVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQF 84
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHA-LLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 85 tadvrrvsqdglaGIG--------IDP----------RWTVDRTLSAALKDARRAgRPSGRSVEDLLG-DVALDARYApr 145
Cdd:PRK09700 81 -------------GIGiiyqelsvIDEltvlenlyigRHLTKKVCGVNIIDWREM-RVRAAMMLLRVGlKVDLDEKVA-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 146 tihSLSGGEKQRVALAVALATRPRALLLDEP---LTAVDPAMRGDVVRRLGDAtaelGTAVLLVSHDLELVERLCPTVHV 222
Cdd:PRK09700 145 ---NLSISHKQMLEIAKTLMLDAKVIIMDEPtssLTNKEVDYLFLIMNQLRKE----GTAIVYISHKLAEIRRICDRYTV 217
|
250
....*....|....*
gi 1199107692 223 LADGTFVTSGALRDV 237
Cdd:PRK09700 218 MKDGSSVCSGMVSDV 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
32-238 |
1.00e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.92 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 32 VPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRrdkKQFTADVRRVSQdglagigidprwtVDRTL 111
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ---KNLVAYVPQSEE-------------VDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 112 SAALKDA------------RRAGRPSGRSVEDLLGDV-ALDARYapRTIHSLSGGEKQRVALAVALATRPRALLLDEPLT 178
Cdd:PRK15056 94 PVLVEDVvmmgryghmgwlRRAKKRDRQIVTAALARVdMVEFRH--RQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 179 AVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVhVLADGTFVTSGALRDVF 238
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTF 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-209 |
1.07e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.98 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 3 TTTTPILRATGLAAGYGGPDVVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKK 82
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKL-ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 83 Q-----------FTADVRrvsqDGLagigIDPrWTVdrtlsaalkdarRAGRPSGRSVEDLLGDVALDARYAPRTIHSLS 151
Cdd:PRK10247 81 QqvsycaqtptlFGDTVY----DNL----IFP-WQI------------RNQQPDPAIFLDDLERFALPDTILTKNIAELS 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 152 GGEKQRVALAVALATRPRALLLDEPLTAVDPAMR---GDVVRRLgdaTAELGTAVLLVSHD 209
Cdd:PRK10247 140 GGEKQRISLIRNLQFMPKVLLLDEITSALDESNKhnvNEIIHRY---VREQNIAVLWVTHD 197
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
40-241 |
1.13e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.84 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRALVGLVRPTA---GHVTYAGRTVTKLSRRDKKQFTADVRRVSQDGLAGIgidprwTVDRTLSAALK 116
Cdd:PRK13640 38 LIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREKVGIVFQNPDNQFVGA------TVGDDVAFGLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 117 DaRRAGRPSGRS-VEDLLGDVALdARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDA 195
Cdd:PRK13640 112 N-RAVPRPEMIKiVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199107692 196 TAELGTAVLLVSHDLELVErLCPTVHVLADGTFVTSGALRDVFAGT 241
Cdd:PRK13640 190 KKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-233 |
1.19e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.77 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 20 GPDVVHGIDLdVVPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKlsrRDKKQFTADVRRVSQdglagi 99
Cdd:PRK13647 17 GTKALKGLSL-SIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA---ENEKWVRSKVGLVFQ------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 100 giDPRwtvDRTLSAALKD--------ARRAGRPSGRSVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVALATRPRAL 171
Cdd:PRK13647 87 --DPD---DQVFSSTVWDdvafgpvnMGLDKDEVERRVEEALKAVRMWD-FRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199107692 172 LLDEPLTAVDPAMRgDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGA 233
Cdd:PRK13647 161 VLDEPMAYLDPRGQ-ETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-216 |
1.23e-15 |
|
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: 73.78 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 22 DVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRrdkkqftADVRRvsqdglaGIGI 101
Cdd:cd03245 18 PALDNVSLTIRAGEK-VAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP-------ADLRR-------NIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 102 DPRwtvDRTL-SAALKDARRAGRPSGRSVEDL----LGDVALDARYAPRTI--------HSLSGGEKQRVALAVALATRP 168
Cdd:cd03245 83 VPQ---DVTLfYGTLRDNITLGAPLADDERILraaeLAGVTDFVNKHPNGLdlqigergRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 169 RALLLDEPLTAVDPAMRGDVVRRLGDATAelGTAVLLVSHD---LELVERL 216
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRpslLDLVDRI 208
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-217 |
1.24e-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: 71.71 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTvtklsrrdkkqftaDV 88
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDR-IGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV--------------KI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 RRVSQdglagigidprwtvdrtlsaalkdarragrpsgrsvedllgdvaldaryaprtihsLSGGEKQRVALAVALATRP 168
Cdd:cd03221 66 GYFEQ--------------------------------------------------------LSGGEKMRLALAKLLLENP 89
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1199107692 169 RALLLDEPLTAVDPAMrgdvVRRLGDATAELGTAVLLVSHDLELVERLC 217
Cdd:cd03221 90 NLLLLDEPTNHLDLES----IEALEEALKEYPGTVILVSHDRYFLDQVA 134
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-216 |
1.48e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.30 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLAAGYGGPDVVHGIDLDVVPgAPPVGIVGESGAGKSTVVRAL------VGLVRpTAGHVTYAGRTV------- 73
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQ-SKVTAIIGPSGCGKSTFLKCLnrmnelESEVR-VEGRVEFFNQNIyerrvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 74 TKLSRR------DKKQFTADVRRVSQDGLAGIGIDPRWTVDRTLSAALKDARRAGRpsgrsVEDLLGDVALDaryaprti 147
Cdd:PRK14258 84 NRLRRQvsmvhpKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDE-----IKHKIHKSALD-------- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 148 hsLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERL 216
Cdd:PRK14258 151 --LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRL 217
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
39-232 |
1.56e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.05 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 39 GIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTvtkLSRRDKKQFTADVRRVSQDGLAGIGIDPRWTVDRTLSAALKDA 118
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQP---LESWSSKAFARKVAYLPQQLPAAEGMTVRELVAIGRYPWHGAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 119 RRAGRPSGRSVEDLLGDVALDArYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAE 198
Cdd:PRK10575 118 GRFGAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQE 196
|
170 180 190
....*....|....*....|....*....|....
gi 1199107692 199 LGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:PRK10575 197 RGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
22-232 |
1.82e-15 |
|
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: 72.58 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 22 DVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTA--GHVTYAGRtvtklsRRDKKQFTADVRRVSQDGLagi 99
Cdd:cd03213 23 QLLKNVSGKAKPGEL-TAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGR------PLDKRSFRKIIGYVPQDDI--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 100 gIDPRWTVDRTL--SAALKdarragrpsgrsvedllgdvaldaryaprtihSLSGGEKQRVALAVALATRPRALLLDEPL 177
Cdd:cd03213 93 -LHPTLTVRETLmfAAKLR--------------------------------GLSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 178 TAVDPAMRGDVV---RRLgdatAELGTAVLLVSHDL-ELVERLCPTVHVLADGTFVTSG 232
Cdd:cd03213 140 SGLDSSSALQVMsllRRL----ADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
18-232 |
2.06e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 73.51 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 18 YGGPDVVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQftadVRRVSQDgla 97
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLV-LLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKA----IRELRRN--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 98 gIGID-------PRWTVDRTLSAALKDARRAGRPSGRS-VEDLLGDVALdARYAPRTIHSLSGGEKQRVALAVALATRPR 169
Cdd:PRK11124 84 -VGMVfqqynlwPHLTVQQNLIEAPCRVLGLSKDQALArAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199107692 170 ALLLDEPLTAVDPAMRGDVV---RRLgdatAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVsiiREL----AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-243 |
2.12e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.54 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 32 VPGAPPVGIVGESGAGKSTVVRALVGLVR------PTAGHVTYAGRTVTKLsrrDKKQFTADVRRVSQDGlagiGIDPRW 105
Cdd:PRK14246 33 IPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQI---DAIKLRKEVGMVFQQP----NPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 106 TVDRTLSAALKD-ARRAGRPSGRSVEDLLGDVAL-----DARYAPRTihSLSGGEKQRVALAVALATRPRALLLDEPLTA 179
Cdd:PRK14246 106 SIYDNIAYPLKShGIKEKREIKKIVEECLRKVGLwkevyDRLNSPAS--QLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199107692 180 VDPAMRGDVVRRLGDATAELgtAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFagTAP 243
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF--TSP 243
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
38-233 |
2.13e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.47 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGlvRPTAGhVTYAGRTVTKLSRRDKKQFTADVRRVSQDGLagigIDPRWTVDRTL--SAAL 115
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNALAF--RSPKG-VKGSGSVLLNGMPIDAKEMRAISAYVQQDDL----FIPTLTVREHLmfQAHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 116 KDARRAGRPSGRS-VEDLLGDVAL-DARY----APRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVV 189
Cdd:TIGR00955 127 RMPRRVTKKEKRErVDEVLQALGLrKCANtrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1199107692 190 RRLGDaTAELGTAVLLVSHD-----LELVERLCptvhVLADGTFVTSGA 233
Cdd:TIGR00955 207 QVLKG-LAQKGKTIICTIHQpsselFELFDKII----LMAEGRVAYLGS 250
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
18-238 |
2.19e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.58 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 18 YGGPDVVHGIDLDVVPGappvGI---VGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDkkqfTAdvRRVS-- 92
Cdd:COG4604 11 YGGKVVLDDVSLTIPKG----GItalIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRE----LA--KRLAil 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 93 -QDglagIGIDPRWTVdRTL--------SAalkdarraGRPSG---RSVEDLLGDVALDArYAPRTIHSLSGGEKQRVAL 160
Cdd:COG4604 81 rQE----NHINSRLTV-RELvafgrfpySK--------GRLTAedrEIIDEAIAYLDLED-LADRYLDELSGGQRQRAFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 161 AVALATRPRALLLDEPLTAVDPA-----MRgdVVRRLGDataELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGA-- 233
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDMKhsvqmMK--LLRRLAD---ELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTpe 221
|
250
....*....|..
gi 1199107692 234 -------LRDVF 238
Cdd:COG4604 222 eiitpevLSDIY 233
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
40-239 |
2.53e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.89 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRALVGLVrptaghVTYAGRTVT---KLSRRDKKqfTADVRRVSQDglagIGID---PRW-----TVD 108
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLI------ISETGQTIVgdyAIPANLKK--IKEVKRLRKE----IGLVfqfPEYqlfqeTIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 109 RTLSAALKDARRAGRPSGRSVEDLLGDVALDARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDV 188
Cdd:PRK13645 110 KDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDF 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 189 VRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:PRK13645 190 INLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
23-237 |
3.96e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.58 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHV-----------------TYAGRTVTKLSRRDKKQFT 85
Cdd:PRK13651 22 ALDNVSVEINQGEF-IAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekeKVLEKLVIQKTRFKKIKKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 86 ADVRR-----------------VSQD---GLAGIGIDPRwtvdrtlsAALKDARragrpsgrsveDLLGDVALDARYAPR 145
Cdd:PRK13651 101 KEIRRrvgvvfqfaeyqlfeqtIEKDiifGPVSMGVSKE--------EAKKRAA-----------KYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 146 TIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLAD 225
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250
....*....|....*.
gi 1199107692 226 GTFVTSG----ALRDV 237
Cdd:PRK13651 241 GKIIKDGdtydILSDN 256
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
19-209 |
5.48e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 73.72 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 19 GGPDVVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKkqftaDVRRVSQDglag 98
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIV-LVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR-----DIAMVFQN---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 99 IGIDPRWTVDRTLSAALKDaRRAGRP--------SGRSVEdlLGDVaLDARyaPRtihSLSGGEKQRVALAVALATRPRA 170
Cdd:PRK11650 85 YALYPHMSVRENMAYGLKI-RGMPKAeieervaeAARILE--LEPL-LDRK--PR---ELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1199107692 171 LLLDEPLTAVDP----AMRGDvVRRLgdaTAELGTAVLLVSHD 209
Cdd:PRK11650 156 FLFDEPLSNLDAklrvQMRLE-IQRL---HRRLKTTSLYVTHD 194
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-227 |
6.83e-15 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 71.35 E-value: 6.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 20 GPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGR-------------TVtklsrRDKKQFTA 86
Cdd:cd03250 17 TSFTLKDINLEVPKGEL-VAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiayvsqepwiqngTI-----RENILFGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 87 DvrrvsqdglagigIDPRWtVDRTLSA-ALKdarragrpsgrsvEDL----LGDvaldaryapRTI-----HSLSGGEKQ 156
Cdd:cd03250 91 P-------------FDEER-YEKVIKAcALE-------------PDLeilpDGD---------LTEigekgINLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199107692 157 RVALAVALATRPRALLLDEPLTAVDPamrgDVVRRL-----GDATAELGTaVLLVSHDLELVERlCPTVHVLADGT 227
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDA----HVGRHIfenciLGLLLNNKT-RILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-210 |
9.16e-15 |
|
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: 73.55 E-value: 9.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLAAGY-GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDkkqFT 85
Cdd:TIGR02868 333 PTLELRDLSAGYpGAPPVLDGVSLDLPPGER-VAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE---VR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 86 ADVRRVSQDGlagigidprwtvdRTLSAALKDARRAGRP--SGRSVEDLLGDVALdARYAPRTIH-----------SLSG 152
Cdd:TIGR02868 409 RRVSVCAQDA-------------HLFDTTVRENLRLARPdaTDEELWAALERVGL-ADWLRALPDgldtvlgeggaRLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199107692 153 GEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAelGTAVLLVSHDL 210
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-183 |
1.42e-14 |
|
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: 70.60 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 19 GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRdkkqftaDVRR----VSQD 94
Cdd:cd03244 15 NLPPVLKNISFSIKPGEK-VGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLH-------DLRSrisiIPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 95 GLAGIG-----IDP--RWTvDRTLSAALKDARRAGRpsgrsVEDLLGdvALDARYAPRTIHsLSGGEKQRVALAVALATR 167
Cdd:cd03244 87 PVLFSGtirsnLDPfgEYS-DEELWQALERVGLKEF-----VESLPG--GLDTVVEEGGEN-LSVGQRQLLCLARALLRK 157
|
170
....*....|....*.
gi 1199107692 168 PRALLLDEPLTAVDPA 183
Cdd:cd03244 158 SKILVLDEATASVDPE 173
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-208 |
1.51e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.92 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTY-AGRTVTKLSRR------DKKQ---FTADVRRVS 92
Cdd:COG4178 378 LLEDLSLSLKPGER-LLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPQRpylplgTLREallYPATAEAFS 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 93 qdglagigidprwtvDRTLSAALKDARragrpsgrsVEDLLGDVALDARYAprtiHSLSGGEKQRVALAVALATRPRALL 172
Cdd:COG4178 457 ---------------DAELREALEAVG---------LGHLAERLDEEADWD----QVLSLGEQQRLAFARLLLHKPDWLF 508
|
170 180 190
....*....|....*....|....*....|....*..
gi 1199107692 173 LDEPLTAVDPAMRGDVVRRLgdaTAEL-GTAVLLVSH 208
Cdd:COG4178 509 LDEATSALDEENEAALYQLL---REELpGTTVISVGH 542
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
9-256 |
2.25e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.88 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPdVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGL----VRPTAGHVTYAGRTVTKLSRRDKKqf 84
Cdd:PRK10418 5 IELRNIALQAAQP-LVHGVSLTLQRGRV-LALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVAPCALRGRK-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 85 tadvrrvsqdgLAGIGIDPRWTVD--RTLSA-ALKDARRAGRPSGRSV-EDLLGDVALD--ARYAPRTIHSLSGGEKQRV 158
Cdd:PRK10418 81 -----------IATIMQNPRSAFNplHTMHThARETCLALGKPADDATlTAALEAVGLEnaARVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 159 ALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVF 238
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
250
....*....|....*...
gi 1199107692 239 AgtAPgaDHPSVRGLAEA 256
Cdd:PRK10418 230 N--AP--KHAVTRSLVSA 243
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
38-209 |
2.87e-14 |
|
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: 70.13 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTADVRRVSQDGLAGIGIDPRWTVDrtLSAALKd 117
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRDLLSSITKDFYTHPYFKTE--IAKPLQ- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 118 arragrpsgrsVEDLLgdvaldaryaPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMR---GDVVRRL-- 192
Cdd:cd03237 105 -----------IEQIL----------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmaSKVIRRFae 163
|
170
....*....|....*...
gi 1199107692 193 -GDATAelgtavLLVSHD 209
Cdd:cd03237 164 nNEKTA------FVVEHD 175
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-239 |
2.98e-14 |
|
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: 72.14 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGL--VRPTAGHVTY------------------ 68
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEV-LGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 69 -----AGRTVTK----LSRRDKKQFTADVRRVS---QDGLAGIGIDprwTVDRTLSAALKDARRAGRPSGRSVEDLLGDV 136
Cdd:TIGR03269 80 epcpvCGGTLEPeevdFWNLSDKLRRRIRKRIAimlQRTFALYGDD---TVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 137 ALDARYApRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERL 216
Cdd:TIGR03269 157 QLSHRIT-HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|...
gi 1199107692 217 CPTVHVLADGTFVTSGALRDVFA 239
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-182 |
4.93e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 69.68 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 2 STTTTPILRATGLAAGYGGPDVVHGIDLDVVPGAppV-GIVGESGAGKSTVVRA------LVGLVRpTAGHVTYAGRTVt 74
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGDKQALKDINLDIPENK--VtALIGPSGCGKSTLLRClnrmndLIPGAR-VEGEILLDGEDI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 75 klsrRDKKQFTADVRR----VSQ----------D----GLAGIGIDPRWTVD----RTL-SAALKDarragrpsgrSVED 131
Cdd:COG1117 81 ----YDPDVDVVELRRrvgmVFQkpnpfpksiyDnvayGLRLHGIKSKSELDeiveESLrKAALWD----------EVKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 132 LLGDVALdaryaprtihSLSGGEKQRVALAVALATRPRALLLDEPLTAVDP 182
Cdd:COG1117 147 RLKKSAL----------GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDP 187
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
22-232 |
5.61e-14 |
|
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: 69.18 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 22 DVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRtvtklsrrdkkqftaDVRRVSQDGL-AGIG 100
Cdd:cd03253 15 PVLKDVSFTIPAGKK-VAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ---------------DIREVTLDSLrRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 101 IDPRWTVdrTLSAALKDARRAGRPSGrSVEDLLgDVALDARYAPRTIHS--------------LSGGEKQRVALAVALAT 166
Cdd:cd03253 79 VVPQDTV--LFNDTIGYNIRYGRPDA-TDEEVI-EAAKAAQIHDKIMRFpdgydtivgerglkLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199107692 167 RPRALLLDEPLTAVDPAMRGDVVRRLGDATAelGTAVLLVSHDLELVERlCPTVHVLADGTFVTSG 232
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-181 |
1.17e-13 |
|
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: 70.23 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 25 HGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRtvtklsrrdkkqftaDVRRVSQDGL-AGIGIDP 103
Cdd:COG5265 375 KGVSFEVPAGKT-VAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ---------------DIRDVTQASLrAAIGIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 104 RWTV---DrTLSAALkdarRAGRPsGRSVEdllgDVALDARYAprTIHS-------------------LSGGEKQRVALA 161
Cdd:COG5265 439 QDTVlfnD-TIAYNI----AYGRP-DASEE----EVEAAARAA--QIHDfieslpdgydtrvgerglkLSGGEKQRVAIA 506
|
170 180
....*....|....*....|
gi 1199107692 162 VALATRPRALLLDEPLTAVD 181
Cdd:COG5265 507 RTLLKNPPILIFDEATSALD 526
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-236 |
1.43e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 3 TTTTPILRATGLAAGYGGPDVVHGIDLDVVPGAPPvGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKK 82
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVH-ALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 83 QFtaDVRRVSQDGLagigIDPRWTVDRTLSAALkdARRAGrpSGRSVEDLLGDVA----LDARYAprtihSLSGGEKQRV 158
Cdd:PRK15439 85 QL--GIYLVPQEPL----LFPNLSVKENILFGL--PKRQA--SMQKMKQLLAALGcqldLDSSAG-----SLEVADRQIV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199107692 159 ALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLgDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRD 236
Cdd:PRK15439 150 EILRGLMRDSRILILDEPTASLTPAETERLFSRI-RELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-232 |
1.44e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.14 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLsrrDKKQFTADVRRVSQDGLA----- 97
Cdd:TIGR00958 496 VLKGLTFTLHPGEV-VALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY---DHHYLHRQVALVGQEPVLfsgsv 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 98 --GIGIDPRWTVDRTLSAALKDArragrpsgrSVEDLLGDValdaryaPRTIHS--------LSGGEKQRVALAVALATR 167
Cdd:TIGR00958 572 reNIAYGLTDTPDEEIMAAAKAA---------NAHDFIMEF-------PNGYDTevgekgsqLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199107692 168 PRALLLDEPLTAVDPAmrgdVVRRLGDATAELGTAVLLVSHDLELVERlCPTVHVLADGTFVTSG 232
Cdd:TIGR00958 636 PRVLILDEATSALDAE----CEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
23-232 |
1.57e-13 |
|
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: 68.02 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRrdkKQFTADVRRVSQDGLagigid 102
Cdd:cd03254 18 VLKDINFSIKPGET-VAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISR---KSLRSMIGVVLQDTF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 103 prwtvdrTLSAALKDARRAGRPSGRSVEDLLGDVALDARYAPRTI------------HSLSGGEKQRVALAVALATRPRA 170
Cdd:cd03254 88 -------LFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLpngydtvlgengGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199107692 171 LLLDEPLTAVDPAMRgdvvRRLGDATAEL--GTAVLLVSHDLELVERlCPTVHVLADGTFVTSG 232
Cdd:cd03254 161 LILDEATSNIDTETE----KLIQEALEKLmkGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-231 |
1.95e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 5 TTPILRATGLAAGYGGPDVVHGIDLDVVPGAppV-GIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKkq 83
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQ--VhALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 84 FTADVRRVSQDglagIGIDPRWTVDRTL-------SAALKDARRAGRPSGRSVEDLLGDVALDARyaprtIHSLSGGEKQ 156
Cdd:PRK11288 77 LAAGVAIIYQE----LHLVPEMTVAENLylgqlphKGGIVNRRLLNYEAREQLEHLGVDIDPDTP-----LKYLSIGQRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 157 RVALAVALATRPRALLLDEP---LTA--VDPAMRgdVVRRLGDAtaelGTAVLLVSHDLELVERLCPTVHVLADGTFVTS 231
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPtssLSAreIEQLFR--VIRELRAE----GRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
24-239 |
2.14e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.20 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 24 VHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTADVRRVSQDGLAGIgidp 103
Cdd:PRK13642 23 LNGVSFSITKGEW-VSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFVGA---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 104 rwTVDRTLSAALKDArraGRPS----GRSVEDLLGDVALDarYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTA 179
Cdd:PRK13642 98 --TVEDDVAFGMENQ---GIPReemiKRVDEALLAVNMLD--FKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 180 VDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERlCPTVHVLADGTFVTSGALRDVFA 239
Cdd:PRK13642 171 LDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-238 |
2.15e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.02 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVvPGAPPVGIVGESGAGKSTVVRALVGLVR--PTA---GHVTYAGRTVTKLsrrDKKQ 83
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEI-PDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKM---DVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 84 FTADVRRVSQ--DGLAGIGIDPRWTVDRTLSAALKDARRAGRPSGRSVEDL-LGDVALDARYAPRTihSLSGGEKQRVAL 160
Cdd:PRK14247 80 LRRRVQMVFQipNPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAqLWDEVKDRLDAPAG--KLSGGQQQRLCI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199107692 161 AVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELgtAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVF 238
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-231 |
3.06e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 5 TTPILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGlVRPTA---GHVTYAGRTVTKLSRRDK 81
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEI-VSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIFEGEELQASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 82 KQftadvrrvsqdglAGIGI-DPRWTVDRTLSAAL-----KDARRAGRPSGRSV----EDLLGDVALDARYAPRTIHsLS 151
Cdd:PRK13549 80 ER-------------AGIAIiHQELALVKELSVLEniflgNEITPGGIMDYDAMylraQKLLAQLKLDINPATPVGN-LG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 152 GGEKQRVALAVALATRPRALLLDEP---LTAVDPAMRGDVVRRLGDAtaelGTAVLLVSHDLELVERLCPTVHVLADGTF 228
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPtasLTESETAVLLDIIRDLKAH----GIACIYISHKLNEVKAISDTICVIRDGRH 221
|
...
gi 1199107692 229 VTS 231
Cdd:PRK13549 222 IGT 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
38-255 |
3.33e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.70 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRrdkkqfTADVRRvsqdgLAGIGIDPRWT--VDRTLSAAL 115
Cdd:PRK13644 31 IGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK------LQGIRK-----LVGIVFQNPETqfVGRTVEEDL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 116 kdarrAGRPSG---------RSVEDLLGDVALDaRYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRG 186
Cdd:PRK13644 100 -----AFGPENlclppieirKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199107692 187 DVVRRLgDATAELGTAVLLVSHDLELVErLCPTVHVLADGTFVTSGALRDVFA-------GTAPgadhPSVRGLAE 255
Cdd:PRK13644 174 AVLERI-KKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVLSdvslqtlGLTP----PSLIELAE 243
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-236 |
4.27e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 5 TTPILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDkkqf 84
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRV-MALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 85 tadvrrvSQDglAGIGID-------PRWTVDRTLSAALKDARRAGRPSGR----SVEDLLGdvALDARYAPRT-IHSLSG 152
Cdd:PRK10762 76 -------SQE--AGIGIIhqelnliPQLTIAENIFLGREFVNRFGRIDWKkmyaEADKLLA--RLNLRFSSDKlVGELSI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 153 GEKQRVALAVALATRPRALLLDEP---LTAVDPAMRGDVVRRLGDAtaelGTAVLLVSHDLELVERLCPTVHVLADGTFV 229
Cdd:PRK10762 145 GEQQMVEIAKVLSFESKVIIMDEPtdaLTDTETESLFRVIRELKSQ----GRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
....*..
gi 1199107692 230 TSGALRD 236
Cdd:PRK10762 221 AEREVAD 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
40-263 |
4.61e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRALVGLVrPTAGHVTYAGRTVTKLSRRDKKQFTAdvrRVSQDGLAGIGIDprwtVDRTLSAALKDAR 119
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRA---YLSQQQTPPFAMP----VFQYLTLHQPDKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 120 RAGRPSGRsVEDLLGDVALDARYaPRTIHSLSGGEKQRVALA-VALATRPRA------LLLDEPLTAVDPAMRGdVVRRL 192
Cdd:PRK03695 99 RTEAVASA-LNEVAEALGLDDKL-GRSVNQLSGGEWQRVRLAaVVLQVWPDInpagqlLLLDEPMNSLDVAQQA-ALDRL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 193 GDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFagtapgadhpSVRGLAEAAPLAVQR 263
Cdd:PRK03695 176 LSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL----------TPENLAQVFGVNFRR 236
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
38-223 |
5.20e-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: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTYAG--RTVTKLSRRDKKQ--FTadvrRVSQDGLAGIgIDPRW------TV 107
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwDEILDEFRGSELQnyFT----KLLEGDVKVI-VKPQYvdlipkAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 108 DRTLSAALKdarragRPSGRSVEDLLGDVaLDARYA-PRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMR- 185
Cdd:cd03236 104 KGKVGELLK------KKDERGKLDELVDQ-LELRHVlDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRl 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1199107692 186 --GDVVRRLgdatAELGTAVLLVSHDLELVERLCPTVHVL 223
Cdd:cd03236 177 naARLIREL----AEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
23-232 |
6.20e-13 |
|
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: 65.41 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTADVRRVsqdglagigid 102
Cdd:cd03247 17 VLKNLSLELKQGEK-IALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRP----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 103 prWTVDRTLSAALkdarraGRPsgrsvedllgdvaldaryaprtihsLSGGEKQRVALAVALATRPRALLLDEPLTAVDP 182
Cdd:cd03247 85 --YLFDTTLRNNL------GRR-------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1199107692 183 AMRGDVVRRLGDATAElgTAVLLVSHDLELVERLcPTVHVLADGTFVTSG 232
Cdd:cd03247 132 ITERQLLSLIFEVLKD--KTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-209 |
7.85e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.65 E-value: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYA-GRTVTKLSRRDKKQFTADVRRVSQDGLAGIgi 101
Cdd:TIGR03719 20 ILKDISLSFFPGAK-IGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGYLPQEPQLDPTKTVRENVEEGVAEI-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 102 dpRWTVDR--TLSAALKD--------ARRAGRpsgrsVEDLLG-----------DVALDA-RYAP--RTIHSLSGGEKQR 157
Cdd:TIGR03719 97 --KDALDRfnEISAKYAEpdadfdklAAEQAE-----LQEIIDaadawdldsqlEIAMDAlRCPPwdADVTKLSGGERRR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1199107692 158 VALAVALATRPRALLLDEPLTAVDpamrGDVVRRLGDATAELGTAVLLVSHD 209
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
7-229 |
9.99e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.06 E-value: 9.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkkqfTA 86
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEI-VTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQ-------TA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 87 DVRRvsqdglAGIGIDP-------RWTVDRTLS-AALKDARRAGRPSGRSVEDLLGdvALDARYAPRTiHSLSGGEKQRV 158
Cdd:PRK11614 76 KIMR------EAVAIVPegrrvfsRMTVEENLAmGGFFAERDQFQERIKWVYELFP--RLHERRIQRA-GTMSGGEQQML 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199107692 159 ALAVALATRPRALLLDEPLTAVDPAmrgdVVRRLGDATAEL---GTAVLLVSHDLELVERLCPTVHVLADGTFV 229
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAPI----IIQQIFDTIEQLreqGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-239 |
1.83e-12 |
|
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: 66.66 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 3 TTTTPILRATG------LAAGYGGPD--VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVT 74
Cdd:TIGR02203 319 TGTRAIERARGdvefrnVTFRYPGRDrpALDSISLVIEPGET-VALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 75 KLSRRDKKqftADVRRVSQDGLagigidprwTVDRTLSAALKDARRAGRPSGRsVEDllgdvALDARYA-------PRTI 147
Cdd:TIGR02203 398 DYTLASLR---RQVALVSQDVV---------LFNDTIANNIAYGRTEQADRAE-IER-----ALAAAYAqdfvdklPLGL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 148 HS--------LSGGEKQRVALAVALATRPRALLLDEPLTAVDpamrGDVVRRLGDATAEL--GTAVLLVSHDLELVERlC 217
Cdd:TIGR02203 460 DTpigengvlLSGGQRQRLAIARALLKDAPILILDEATSALD----NESERLVQAALERLmqGRTTLVIAHRLSTIEK-A 534
|
250 260
....*....|....*....|..
gi 1199107692 218 PTVHVLADGTFVTSGALRDVFA 239
Cdd:TIGR02203 535 DRIVVMDDGRIVERGTHNELLA 556
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-254 |
3.62e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 64.73 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLAAGYGGPDVVHGIDLDVvPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGH-----VTYAGRTVtkLSRRDK 81
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGF-PARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSI--FNYRDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 82 KQFTADVRRVSQDGlagiGIDPRWTVDRTLsAALKDARRAGRPSGRSV-EDLLGDVALDARYAPRTIHS---LSGGEKQR 157
Cdd:PRK14271 97 LEFRRRVGMLFQRP----NPFPMSIMDNVL-AGVRAHKLVPRKEFRGVaQARLTEVGLWDAVKDRLSDSpfrLSGGQQQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 158 VALAVALATRPRALLLDEPLTAVDPAMRGDV---VRRLGDAtaelgTAVLLVSHDLELVERLCPTVHVLADGTFVTSGAL 234
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIeefIRSLADR-----LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPT 246
|
250 260
....*....|....*....|
gi 1199107692 235 RDVFAGTAPGADHPSVRGLA 254
Cdd:PRK14271 247 EQLFSSPKHAETARYVAGLS 266
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
8-237 |
6.82e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 6.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVG-LVRPTA-------GHVTYAGRTVTKLSRR 79
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRV-TALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 80 DKKQFTADVRRVSQDGLAgigidprWTVDR-TLSAALKDARRAGRPSGRSVE------DLLGDVALDARyaprTIHSLSG 152
Cdd:PRK13547 80 RLARLRAVLPQAAQPAFA-------FSAREiVLLGRYPHARRAGALTHRDGEiawqalALAGATALVGR----DVTTLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 153 GEKQRVALAVALA---------TRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVL 223
Cdd:PRK13547 149 GELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAML 228
|
250
....*....|....
gi 1199107692 224 ADGTFVTSGALRDV 237
Cdd:PRK13547 229 ADGAIVAHGAPADV 242
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
32-243 |
8.24e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 63.63 E-value: 8.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 32 VPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTADVRRVSQDGlagiGIDPRWTVDRTL 111
Cdd:PRK11831 30 VPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSG----ALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 112 SAALKDARRAGRPSGRSVEdLLGDVALDARYAPRTIHS-LSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVR 190
Cdd:PRK11831 106 AYPLREHTQLPAPLLHSTV-MMKLEAVGLRGAAKLMPSeLSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199107692 191 RLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFAGTAP 243
Cdd:PRK11831 185 LISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP 237
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
38-232 |
8.78e-12 |
|
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: 63.33 E-value: 8.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDkkqftadVRR----VSQDglagigidPrwtvdrTL-S 112
Cdd:cd03249 32 VALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRW-------LRSqiglVSQE--------P------VLfD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 113 AALKDARRAGRPSGRSVEDLlgDVALDAryaprTIHS-------------------LSGGEKQRVALAVALATRPRALLL 173
Cdd:cd03249 91 GTIAENIRYGKPDATDEEVE--EAAKKA-----NIHDfimslpdgydtlvgergsqLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 174 DEPLTAVDPAMRGDVVRRLGDATaeLGTAVLLVSHDLELVeRLCPTVHVLADGTFVTSG 232
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQG 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
38-223 |
9.95e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 9.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVT-----------YAGRTV----TKLSRRDKK-----QFTADVRRVsqdgla 97
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDYEeepswdevlkrFRGTELqnyfKKLYNGEIKvvhkpQYVDLIPKV------ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 98 gigidprwtVDRTLSAALKDARRAGRPsgRSVEDLLG-DVALDaryapRTIHSLSGGEKQRVALAVALATRPRALLLDEP 176
Cdd:PRK13409 176 ---------FKGKVRELLKKVDERGKL--DEVVERLGlENILD-----RDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1199107692 177 LTAVDPAMR---GDVVRRLGDataelGTAVLLVSHDLELVERLCPTVHVL 223
Cdd:PRK13409 240 TSYLDIRQRlnvARLIRELAE-----GKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-238 |
1.01e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 63.32 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 18 YGGPDVVHGIDLDVvPGAPPVGIVGESGAGKSTVVRALVGLVR--PTA---GHVTYAGRTVTKlSRRDKKQFTADVRRVS 92
Cdd:PRK14267 14 YGSNHVIKGVDLKI-PQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYS-PDVDPIEVRREVGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 93 Q-----------DGLAgIGI------DPRWTVDRTLSAALKDArragrPSGRSVEDLLGDVAldaryaprtiHSLSGGEK 155
Cdd:PRK14267 92 QypnpfphltiyDNVA-IGVklnglvKSKKELDERVEWALKKA-----ALWDEVKDRLNDYP----------SNLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 156 QRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELgtAVLLVSHDLELVERLCPTVHVLADGTFVTSGALR 235
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR 233
|
...
gi 1199107692 236 DVF 238
Cdd:PRK14267 234 KVF 236
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
38-223 |
1.85e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.65 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVT-----------YAGRTV----TKLSRRDKK-----QFTADVRRVsqdgla 97
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDeepswdevlkrFRGTELqdyfKKLANGEIKvahkpQYVDLIPKV------ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 98 gigidprwtVDRTLSAALKDARRAGRpsGRSVEDLLG-DVALDaryapRTIHSLSGGEKQRVALAVALATRPRALLLDEP 176
Cdd:COG1245 176 ---------FKGTVRELLEKVDERGK--LDELAEKLGlENILD-----RDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1199107692 177 LTAVDPAMR---GDVVRRLgdatAELGTAVLLVSHDLELVERLCPTVHVL 223
Cdd:COG1245 240 SSYLDIYQRlnvARLIREL----AEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
7-226 |
1.88e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 63.73 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 7 PILRATGLAAGY-GGP----DVVHGIDLDvvpgaPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTyagrtvtklsrRDK 81
Cdd:PLN03073 507 PIISFSDASFGYpGGPllfkNLNFGIDLD-----SRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSA 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 82 KQFTADVRRVSQDGLaGIGIDPRWTVDRTLSAALKDARRAGrpsgrsvedlLGDVALDARYAPRTIHSLSGGEKQRVALA 161
Cdd:PLN03073 571 KVRMAVFSQHHVDGL-DLSSNPLLYMMRCFPGVPEQKLRAH----------LGSFGVTGNLALQPMYTLSGGQKSRVAFA 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199107692 162 VALATRPRALLLDEPLTAVDPamrgDVVRRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADG 226
Cdd:PLN03073 640 KITFKKPHILLLDEPSNHLDL----DAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEG 700
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
40-238 |
2.11e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.17 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRALVGLVrPTAGHVTYAGRTVTKLSRRDKKQFTAdvrRVSQDGLAGIGIdPRWTV-DRTLSAALKDA 118
Cdd:COG4138 27 LIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRA---YLSQQQSPPFAM-PVFQYlALHQPAGASSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 119 RRAGRpsgrsVEDLLGDVALDARYaPRTIHSLSGGEKQRVALA-VALATRPRA------LLLDEPLTAVDPAMRGdVVRR 191
Cdd:COG4138 102 AVEQL-----LAQLAEALGLEDKL-SRPLTQLSGGEWQRVRLAaVLLQVWPTInpegqlLLLDEPMNSLDVAQQA-ALDR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199107692 192 LGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVF 238
Cdd:COG4138 175 LLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-215 |
2.85e-11 |
|
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: 61.72 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 21 PD--VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTvtkLSRRDKKQFTADVRRVSQ----- 93
Cdd:cd03248 25 PDtlVLQDVSFTLHPGEV-TALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKP---ISQYEHKYLHSKVSLVGQepvlf 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 94 -----DGLA-GIGIDPRWTVDRTLSAALKDARRAGRPSGRSVEdllgdvaldaryAPRTIHSLSGGEKQRVALAVALATR 167
Cdd:cd03248 101 arslqDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTE------------VGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1199107692 168 PRALLLDEPLTAVDPAMRGDVVRRLGDATAElgTAVLLVSHDLELVER 215
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER 214
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-204 |
3.36e-11 |
|
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: 61.12 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 17 GYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTA---GHVTYAGRTVTKlsrrDKKQFTADVRRVSQ 93
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEM-VLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKE----FAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 94 DGLAgigiDPRWTVDRTLSAALKdarragrpsgrsvedLLGDvaldaryapRTIHSLSGGEKQRVALAVALATRPRALLL 173
Cdd:cd03233 91 EDVH----FPTLTVRETLDFALR---------------CKGN---------EFVRGISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190
....*....|....*....|....*....|.
gi 1199107692 174 DEPLTAVDPAMRGDVVRRLGDATAELGTAVL 204
Cdd:cd03233 143 DNSTRGLDSSTALEILKCIRTMADVLKTTTF 173
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
9-183 |
3.57e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.04 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGLVRPTAGHVTYAGrtvtklsrrdKKQFTADV 88
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALV-LTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG----------GDIDDPDV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 RRVS-----QDGLagigiDPRWTVDRTLS--AALKDARRagrpsgRSVEDLLGDVALdARYAPRTIHSLSGGEKQRVALA 161
Cdd:PRK13539 72 AEAChylghRNAM-----KPALTVAENLEfwAAFLGGEE------LDIAAALEAVGL-APLAHLPFGYLSAGQKRRVALA 139
|
170 180
....*....|....*....|..
gi 1199107692 162 VALATRPRALLLDEPLTAVDPA 183
Cdd:PRK13539 140 RLLVSNRPIWILDEPTAALDAA 161
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-215 |
4.45e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 61.34 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 2 STTTTPILRATGLAAGYGGPDVVHGIDLDVvPGAPPVGIVGESGAGKSTVVRA---LVGLVrPTA---GHVTYAGRTVTk 75
Cdd:PRK14243 4 LNGTETVLRTENLNVYYGSFLAVKNVWLDI-PKNQITAFIGPSGCGKSTILRCfnrLNDLI-PGFrveGKVTFHGKNLY- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 76 lsrrDKKQFTADVRR----VSQ----------DGLA------GIGIDPRWTVDRTL-SAALKDarragrpsgrSVEDLLG 134
Cdd:PRK14243 81 ----APDVDPVEVRRrigmVFQkpnpfpksiyDNIAygarinGYKGDMDELVERSLrQAALWD----------EVKDKLK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 135 DVALdaryaprtihSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMrgdvVRRLGDATAELGT--AVLLVSHDLEL 212
Cdd:PRK14243 147 QSGL----------SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPIS----TLRIEELMHELKEqyTIIIVTHNMQQ 212
|
...
gi 1199107692 213 VER 215
Cdd:PRK14243 213 AAR 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
13-213 |
4.59e-11 |
|
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: 60.50 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 13 GLAAGYGG--PDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRdkkqftaDVRR 90
Cdd:cd03369 11 NLSVRYAPdlPPVLKNVSFKVKAGEK-IGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE-------DLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 91 vsqdglaGIGIDPRwtvDRTL-SAALKdarragrpSGRSVEDLLGDVALdarYAPRTIHS----LSGGEKQRVALAVALA 165
Cdd:cd03369 83 -------SLTIIPQ---DPTLfSGTIR--------SNLDPFDEYSDEEI---YGALRVSEgglnLSQGQRQLLCLARALL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1199107692 166 TRPRALLLDEPLTAVDPAMRGDVVRRLGDATAelGTAVLLVSHDLELV 213
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTI 187
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
38-213 |
4.67e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.49 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTyagrTVTKLSRrdKKQFtadvrrVSQDglagigidprwtVDRTLSAALKD 117
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEVD----EDLKISY--KPQY------ISPD------------YDGTVEEFLRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 118 ARRAGRPSGRSVEDLLGDVALDARYApRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMR---GDVVRRLgd 194
Cdd:COG1245 425 ANTDDFGSSYYKTEIIKPLGLEKLLD-KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavAKAIRRF-- 501
|
170
....*....|....*....
gi 1199107692 195 aTAELGTAVLLVSHDLELV 213
Cdd:COG1245 502 -AENRGKTAMVVDHDIYLI 519
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-224 |
7.14e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.06 E-value: 7.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 8 ILRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYaGRTVtKLSRRDKkqftad 87
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGI-VGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-KLAYVDQ------ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 88 vrrvSQDGLagigiDPRWTVDRTLSAALkdarragrpsgrsveDL--LGDVALDAR-YAPR----------TIHSLSGGE 154
Cdd:PRK11819 395 ----SRDAL-----DPNKTVWEEISGGL---------------DIikVGNREIPSRaYVGRfnfkggdqqkKVGVLSGGE 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 155 KQRVALAVALATRPRALLLDEPLTAVDPamrgDVVRRLGDATAELGTAVLLVSHDLELVERLCptVHVLA 224
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDV----ETLRALEEALLEFPGCAVVISHDRWFLDRIA--THILA 514
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-239 |
7.51e-11 |
|
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: 62.27 E-value: 7.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 19 GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGrTVTKLSRRDKKQFTAdvrrVSQDGLAG 98
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGAL-VAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVPQQAWIQNDS----LRENILFG 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 99 IGIDPRWtVDRTLSAALKDARRAGRPSGRSVEdlLGDVALDaryaprtihsLSGGEKQRVALAVALATRPRALLLDEPLT 178
Cdd:TIGR00957 723 KALNEKY-YQQVLEACALLPDLEILPSGDRTE--IGEKGVN----------LSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199107692 179 AVDPAMRGDVVRR-LGDATAELGTAVLLVSHDLELVERLcPTVHVLADGTFVTSGALRDVFA 239
Cdd:TIGR00957 790 AVDAHVGKHIFEHvIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
38-210 |
9.78e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 9.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTyagrTVTKLSRrdKKQFtadvrrvsqdglagIGIDPRWTVDRTLSAALKD 117
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVD----PELKISY--KPQY--------------IKPDYDGTVEDLLRSITDD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 118 ----------ARRAGrpsgrsVEDLLGdvaldaryapRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMR-- 185
Cdd:PRK13409 428 lgssyykseiIKPLQ------LERLLD----------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRla 491
|
170 180
....*....|....*....|....*.
gi 1199107692 186 -GDVVRRLgdaTAELGTAVLLVSHDL 210
Cdd:PRK13409 492 vAKAIRRI---AEEREATALVVDHDI 514
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
40-263 |
1.01e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkkqFTADVRRVSQDglagigidprWTVDRT--LSAALKD 117
Cdd:PRK10938 34 FVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS------FEQLQKLVSDE----------WQRNNTdmLSPGEDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 118 ArraGRPSGRSVEDLLGDVALDARYA---------PRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDV 188
Cdd:PRK10938 98 T---GRTTAEIIQDEVKDPARCEQLAqqfgitallDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 189 VRRLGDATAELGTAVLLVS--HDL-ELVERlcptVHVLADGTFVTSGALRDVFA--------------GTA-PGADHPSV 250
Cdd:PRK10938 175 AELLASLHQSGITLVLVLNrfDEIpDFVQF----AGVLADCTLAETGEREEILQqalvaqlahseqleGVQlPEPDEPSA 250
|
250
....*....|....
gi 1199107692 251 R-GLAEAAPLAVQR 263
Cdd:PRK10938 251 RhALPANEPRIVLN 264
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-209 |
1.46e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 61.28 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 16 AGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDkkqfTADVRRvSQDG 95
Cdd:PRK10535 16 SGEEQVEVLKGISLDIYAGEM-VAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADA----LAQLRR-EHFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 96 LagigIDPRWTVDRTLSAAL------------KDARRAgrpsgRSVEdLLGDVALDAR--YAPrtiHSLSGGEKQRVALA 161
Cdd:PRK10535 90 F----IFQRYHLLSHLTAAQnvevpavyagleRKQRLL-----RAQE-LLQRLGLEDRveYQP---SQLSGGQQQRVSIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1199107692 162 VALATRPRALLLDEPLTAVDpAMRGDVVRRLGDATAELGTAVLLVSHD 209
Cdd:PRK10535 157 RALMNGGQVILADEPTGALD-SHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
18-209 |
1.50e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.81 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 18 YGGPDVVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKkqftadvrrvsqdgla 97
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVV-FVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER---------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 98 GIG-------IDPRWTVDRTLSAALKDARRAGRPSGRSVEDLlGDVALDARYAPRTIHSLSGGEKQRVALAVALATRPRA 170
Cdd:PRK11000 76 GVGmvfqsyaLYPHLSVAENMSFGLKLAGAKKEEINQRVNQV-AEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1199107692 171 LLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHD 209
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
13-237 |
1.59e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.52 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 13 GLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAG--KSTVVRALVGlvrPTAGHVTYagRTVTKLSRRDKKQFTADVRR 90
Cdd:NF000106 18 GLVKHFGEVKAVDGVDLDVREGTV-LGVLGP*GAA**RGALPAHV*G---PDAGRRPW--RF*TWCANRRALRRTIG*HR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 91 VSQDGL--AGIGIDPRWTVDRTLSAALKDARRagrpsgrSVEDLLGDVALdARYAPRTIHSLSGGEKQRVALAVALATRP 168
Cdd:NF000106 92 PVR*GRreSFSGRENLYMIGR*LDLSRKDARA-------RADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 169 RALLLDEPLTAVDPAMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDV 237
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
38-232 |
1.78e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.63 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVrPTAGHVTYAGrtvTKLSRRDKKQFtadvRRvsqdGLAGIGIDPRwtvdrTLSAALKD 117
Cdd:PRK11174 379 IALVGPSGAGKTSLLNALLGFL-PYQGSLKING---IELRELDPESW----RK----HLSWVGQNPQ-----LPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 118 ARRAGRPSGrSVEDLlgDVALDARYAPRTIHS---------------LSGGEKQRVALAVALATRPRALLLDEPLTAVDP 182
Cdd:PRK11174 442 NVLLGNPDA-SDEQL--QQALENAWVSEFLPLlpqgldtpigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1199107692 183 AMRGDVVRRLGDATAelGTAVLLVSHDLELVERlCPTVHVLADGTFVTSG 232
Cdd:PRK11174 519 HSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
17-239 |
1.82e-10 |
|
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: 60.91 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 17 GYGGPdVVHGIDLDVvPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFtadVRRVSQDgl 96
Cdd:TIGR01193 484 GYGSN-ILSDISLTI-KMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF---INYLPQE-- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 97 agigidPRWTVDRTLSAALKDARRagrpsGRSVEDLLGDVAL-----DARYAPRTIH--------SLSGGEKQRVALAVA 163
Cdd:TIGR01193 557 ------PYIFSGSILENLLLGAKE-----NVSQDEIWAACEIaeikdDIENMPLGYQtelseegsSISGGQKQRIALARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 164 LATRPRALLLDEPLTAVDPAMRGDVVRRL---GDATaelgtaVLLVSHDLELVERlCPTVHVLADGTFVTSGALRDVFA 239
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLlnlQDKT------IIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLD 697
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-218 |
1.86e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRptaghvtyagrtvtklSRRDKKQFTADVRRVSQDgLAGI-GI 101
Cdd:COG2401 45 VLRDLNLEIEPGEI-VLIVGASGSGKSTLLRLLAGALK----------------GTPVAGCVDVPDNQFGRE-ASLIdAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 102 DPRWTVDrtlsAALKDARRAGrpsgrsvedlLGDVAL-DARYaprtiHSLSGGEKQRVALAVALATRPRALLLDEPLTAV 180
Cdd:COG2401 107 GRKGDFK----DAVELLNAVG----------LSDAVLwLRRF-----KELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1199107692 181 DPAMRGDVVRRLGDATAELGTAVLLVSHDLELVERLCP 218
Cdd:COG2401 168 DRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQP 205
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-232 |
9.10e-10 |
|
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: 57.24 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 17 GYGG--PDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkkqfTADVRR---- 90
Cdd:cd03251 9 RYPGdgPPVLRDISLDIPAGET-VALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT-------LASLRRqigl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 91 VSQDGLAGIGidprwTVDR-----TLSAALKDARRAGRPSGRS--VEDLlgDVALDARYAPRTIhSLSGGEKQRVALAVA 163
Cdd:cd03251 81 VSQDVFLFND-----TVAEniaygRPGATREEVEEAARAANAHefIMEL--PEGYDTVIGERGV-KLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 164 LATRPRALLLDEPLTAVDpamrGDVVRRLGDATAEL--GTAVLLVSHDLELVERlCPTVHVLADGTFVTSG 232
Cdd:cd03251 153 LLKDPPILILDEATSALD----TESERLVQAALERLmkNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-226 |
9.41e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 9.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAagygGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKkqftadV 88
Cdd:PRK11288 258 LRLDGLK----GPGLREPISFSVRAGEI-VGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDA------I 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 RrvsqdglAGI----------GIDPRWTVDRTLSAAlkdARRAGRPSG---------RSVEDLLGDVALDARYAPRTIHS 149
Cdd:PRK11288 327 R-------AGImlcpedrkaeGIIPVHSVADNINIS---ARRHHLRAGclinnrweaENADRFIRSLNIKTPSREQLIMN 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199107692 150 LSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDaTAELGTAVLLVSHDLELVERLCPTVHVLADG 226
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYE-LAAQGVAVLFVSSDLPEVLGVADRIVVMREG 472
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
150-208 |
1.08e-09 |
|
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: 56.01 E-value: 1.08e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 150 LSGGEKQRVALAVALATRPRALLLDEPLTAVDPamrgDVVRRLGDATAELGTAVLLVSH 208
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESEDRLYQLLKELGITVISVGH 146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-181 |
1.65e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.06 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 19 GGPDVVHGIDLDVVPgAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSrrdkkqfTADVRRVSQ----- 93
Cdd:PLN03232 1247 GLPPVLHGLSFFVSP-SEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG-------LTDLRRVLSiipqs 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 94 ----DGLAGIGIDP-RWTVDRTLSAALKDARragrpsgrsVEDLL--GDVALDARYAPRTiHSLSGGEKQRVALAVALAT 166
Cdd:PLN03232 1319 pvlfSGTVRFNIDPfSEHNDADLWEALERAH---------IKDVIdrNPFGLDAEVSEGG-ENFSVGQRQLLSLARALLR 1388
|
170
....*....|....*
gi 1199107692 167 RPRALLLDEPLTAVD 181
Cdd:PLN03232 1389 RSKILVLDEATASVD 1403
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
146-230 |
1.88e-09 |
|
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: 55.44 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 146 TIHSLSGGEKQRVALAVALA---TRPRAL-LLDEPLTAVDPamrgDVVRRLGDATAEL---GTAVLLVSHDLELVERLCP 218
Cdd:cd03227 74 TRLQLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDP----RDGQALAEAILEHlvkGAQVIVITHLPELAELADK 149
|
90
....*....|..
gi 1199107692 219 TVHVLADGTFVT 230
Cdd:cd03227 150 LIHIKKVITGVY 161
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
23-181 |
2.79e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.04 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 23 VVHGIDLDVvPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQftaDVRRVSQDGLagigid 102
Cdd:PRK10790 356 VLQNINLSV-PSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ---GVAMVQQDPV------ 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 103 prwtvdrTLSAALKDARRAGRP-SGRSVEDLLGDVALD--ARYAPRTIHS--------LSGGEKQRVALAVALATRPRAL 171
Cdd:PRK10790 426 -------VLADTFLANVTLGRDiSEEQVWQALETVQLAelARSLPDGLYTplgeqgnnLSVGQKQLLALARVLVQTPQIL 498
|
170
....*....|
gi 1199107692 172 LLDEPLTAVD 181
Cdd:PRK10790 499 ILDEATANID 508
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-181 |
2.97e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.44 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 21 PDVVHGIDLDVVPgAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQ-----------FTADVR 89
Cdd:PLN03130 1252 PPVLHGLSFEISP-SEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKvlgiipqapvlFSGTVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 90 rvsqdglagIGIDP--------RW-TVDRtlsAALKDARRagRPSgrsvedlLGdvaLDARYAPRTiHSLSGGEKQRVAL 160
Cdd:PLN03130 1331 ---------FNLDPfnehndadLWeSLER---AHLKDVIR--RNS-------LG---LDAEVSEAG-ENFSVGQRQLLSL 1385
|
170 180
....*....|....*....|.
gi 1199107692 161 AVALATRPRALLLDEPLTAVD 181
Cdd:PLN03130 1386 ARALLRRSKILVLDEATAAVD 1406
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
41-232 |
3.12e-09 |
|
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: 57.33 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 41 VGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVtklsrrdkkQFTADVRRVSqdglagIGIDPRWTV-DRTLSAA---LK 116
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---------ETNLDAVRQS------LGMCPQHNIlFHHLTVAehiLF 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 117 DARRAGRPSGRS---VEDLLGDVALDARYAPRTiHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRgdvvRRLG 193
Cdd:TIGR01257 1027 YAQLKGRSWEEAqleMEAMLEDTGLHHKRNEEA-QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR----RSIW 1101
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1199107692 194 DATAEL--GTAVLLVSHDLELVERLCPTVHVLADGTFVTSG 232
Cdd:TIGR01257 1102 DLLLKYrsGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
38-210 |
3.47e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVtklsrrdkkqftadVRRVSQDGLA-GI----------GIDPRWT 106
Cdd:PRK10762 281 LGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV--------------VTRSPQDGLAnGIvyisedrkrdGLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 107 VDRTLS-AALKD-ARRAGRPSGRS----VEDLLGDVALDARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAV 180
Cdd:PRK10762 347 VKENMSlTALRYfSRAGGSLKHADeqqaVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190
....*....|....*....|....*....|
gi 1199107692 181 DPAMRGDVVRRLGDATAElGTAVLLVSHDL 210
Cdd:PRK10762 427 DVGAKKEIYQLINQFKAE-GLSIILVSSEM 455
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
27-176 |
1.14e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 27 IDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYA-GRTVTKLSRRDKKQFTADVRRVSQDGLAGIgidpRW 105
Cdd:PRK11819 26 ISLSFFPGAK-IGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKVGYLPQEPQLDPEKTVRENVEEGVAEV----KA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 106 TVDR--TLSAALKD--------ARRAGRpsgrsVEDLLG-----------DVALDA-RYAPR--TIHSLSGGEKQRVALA 161
Cdd:PRK11819 101 ALDRfnEIYAAYAEpdadfdalAAEQGE-----LQEIIDaadawdldsqlEIAMDAlRCPPWdaKVTKLSGGERRRVALC 175
|
170
....*....|....*
gi 1199107692 162 VALATRPRALLLDEP 176
Cdd:PRK11819 176 RLLLEKPDMLLLDEP 190
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
40-214 |
1.23e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRALVGLVRPTAGHVtyagRTVTKLSRRDKKQFTADvrrvsqdglagigIDPRWTVDRTLSAALKDAR 119
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLEVAYFDQHRAE-------------LDPEKTVMDNLAEGKQEVM 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 120 RAGRPsgRSVEDLLGDVALDARYAPRTIHSLSGGEKQRVALAvALATRPRALL-LDEPLTAVDPamrgdvvrrlgdATAE 198
Cdd:PRK11147 413 VNGRP--RHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLA-RLFLKPSNLLiLDEPTNDLDV------------ETLE 477
|
170 180
....*....|....*....|....*
gi 1199107692 199 L---------GTaVLLVSHDLELVE 214
Cdd:PRK11147 478 LleelldsyqGT-VLLVSHDRQFVD 501
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
38-226 |
2.14e-08 |
|
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: 54.45 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGlvrptaghvTYAGRTVTKLSRrDKKQFtaDVRRVSQDGLAGI----------GIDPRWTV 107
Cdd:TIGR02633 289 LGVAGLVGAGRTELVQALFG---------AYPGKFEGNVFI-NGKPV--DIRNPAQAIRAGIamvpedrkrhGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 108 DRTLS-AALKDARRAGRPSGRSVEDLLGD----VALDARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDP 182
Cdd:TIGR02633 357 GKNITlSVLKSFCFKMRIDAAAELQIIGSaiqrLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1199107692 183 AMRGDVVRRLGDATAElGTAVLLVSHDLELVERLCPTVHVLADG 226
Cdd:TIGR02633 437 GAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
40-209 |
3.07e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.82 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRD-KKQFTA---DVrrvsqdglagigidprWTVDRTLSaal 115
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyRKLFSAvftDF----------------HLFDQLLG--- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 116 kdarragrPSGRSVEDLLGDVALDARYAPRTIH---------SLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRG 186
Cdd:PRK10522 415 --------PEGKPANPALVEKWLERLKMAHKLEledgrisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
170 180
....*....|....*....|...
gi 1199107692 187 DVVRRLGDATAELGTAVLLVSHD 209
Cdd:PRK10522 487 EFYQVLLPLLQEMGKTIFAISHD 509
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
24-181 |
3.88e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 53.81 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 24 VHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRrdkkqftADVRR----VSQDglAGI 99
Cdd:PRK13657 351 VEDVSFEAKPGQT-VAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR-------ASLRRniavVFQD--AGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 100 gidprwtVDRTLSaalkDARRAGRPSGRSVEDLLgdvALDARYAPRTI---------------HSLSGGEKQRVALAVAL 164
Cdd:PRK13657 421 -------FNRSIE----DNIRVGRPDATDEEMRA---AAERAQAHDFIerkpdgydtvvgergRQLSGGERQRLAIARAL 486
|
170
....*....|....*..
gi 1199107692 165 ATRPRALLLDEPLTAVD 181
Cdd:PRK13657 487 LKDPPILILDEATSALD 503
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
131-211 |
5.68e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 131 DLLGdvaLDARYAPRTIHSLSGGEkQRVALAV-ALATRPRALLLDEPLTAVDPAMRgDVVRRLGDA-TAELGTAVLLVSH 208
Cdd:PRK10938 386 DILG---IDKRTADAPFHSLSWGQ-QRLALIVrALVKHPTLLILDEPLQGLDPLNR-QLVRRFVDVlISEGETQLLFVSH 460
|
...
gi 1199107692 209 DLE 211
Cdd:PRK10938 461 HAE 463
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
42-212 |
6.58e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.49 E-value: 6.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 42 GESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQFTADVRRVsqdglagiGIDPRWTVDRTLSAALKDARRA 121
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRS--------GINPYLTLRENCLYDIHFSPGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 122 grpsgRSVEDLLGDVALDaRYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAElGT 201
Cdd:PRK13540 106 -----VGITELCRLFSLE-HLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAK-GG 178
|
170
....*....|..
gi 1199107692 202 AVLLVSH-DLEL 212
Cdd:PRK13540 179 AVLLTSHqDLPL 190
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
38-223 |
7.10e-08 |
|
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: 51.03 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTklsrrdkkqftadvrrvsqdglagigidprwtvdrtlsaalkd 117
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 118 arragrpsgrsvedllgdvaldarYAPRTIhSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATA 197
Cdd:cd03222 65 ------------------------YKPQYI-DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170 180
....*....|....*....|....*.
gi 1199107692 198 ELGTAVLLVSHDLELVERLCPTVHVL 223
Cdd:cd03222 120 EGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-216 |
7.97e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 9 LRATGLAAGYGGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRtvtklsrrdkkqftADV 88
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGER-LAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN--------------ANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 RRVSQDGLAgigidpRWTVDRTLSAALKDARRAGRPSgRSVEDLLGDVALDARYAPRTIHSLSGGEKQRVALAVALATRP 168
Cdd:PRK15064 385 GYYAQDHAY------DFENDLTLFDWMSQWRQEGDDE-QAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKP 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1199107692 169 RALLLDEPLTAVDpaMrgDVVRRLGDATAELGTAVLLVSHDLELVERL 216
Cdd:PRK15064 458 NVLVMDEPTNHMD--M--ESIESLNMALEKYEGTLIFVSHDREFVSSL 501
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
38-239 |
1.08e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.57 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRptaGHvTYAGrTVTKLSRRDKKQFTADVRRVSQDGLagigIDPRWTVDRTL--SAAL 115
Cdd:PLN03211 97 LAVLGPSGSGKSTLLNALAGRIQ---GN-NFTG-TILANNRKPTKQILKRTGFVTQDDI----LYPHLTVRETLvfCSLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 116 KDARRAGRPSGRSV-EDLLGDVAL----DARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVR 190
Cdd:PLN03211 168 RLPKSLTKQEKILVaESVISELGLtkceNTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1199107692 191 RLGDATAELGTAVLLVSHDLELVERLCPTVHVLADGTFVTSGALRDVFA 239
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
38-226 |
2.08e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.32 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRD--KK--QFTADVRRVSqdglagiGIDPRWTVDRTLSA 113
Cdd:PRK09700 292 LGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavKKgmAYITESRRDN-------GFFPNFSIAQNMAI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 114 A--LKDARRAG-------RPSGRSVEDLLGDVALDARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAM 184
Cdd:PRK09700 365 SrsLKDGGYKGamglfheVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGA 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199107692 185 RGD---VVRRLgdatAELGTAVLLVSHDLELVERLCPTVHVLADG 226
Cdd:PRK09700 445 KAEiykVMRQL----ADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-208 |
2.69e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.85 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 4 TTTPILRATGLAAGYGGPDVVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTklsRRDKKQ 83
Cdd:PRK13543 7 TAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALL-VQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT---RGDRSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 84 FTADVRRvsqdgLAGIGIDPRWTVDRTLSAALKdARRAGRPSGRSvedlLGDVALdARYAPRTIHSLSGGEKQRVALAVA 163
Cdd:PRK13543 83 FMAYLGH-----LPGLKADLSTLENLHFLCGLH-GRRAKQMPGSA----LAIVGL-AGYEDTLVRQLSAGQKKRLALARL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199107692 164 LATRPRALLLDEPLTAVDPAMRgDVVRRLGDATAELGTAVLLVSH 208
Cdd:PRK13543 152 WLSPAPLWLLDEPYANLDLEGI-TLVNRMISAHLRGGGAALVTTH 195
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
27-216 |
5.37e-07 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 49.19 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 27 IDLDVVPGAPPVGIVGESGAGKSTVVRAlvglvrptaghVTYA--GRTvtklsRRDKKQFTADVRRVSQDGLAGIGID-- 102
Cdd:cd03279 20 IDFTGLDNNGLFLICGPTGAGKSTILDA-----------ITYAlyGKT-----PRYGRQENLRSVFAPGEDTAEVSFTfq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 103 ---PRWTVDRTLSAALKDARRAG-RPSGRSvedllgdvaldARYAPRTIHSLSGGEKQRVALAVALA----------TRP 168
Cdd:cd03279 84 lggKKYRVERSRGLDYDQFTRIVlLPQGEF-----------DRFLARPVSTLSGGETFLASLSLALAlsevlqnrggARL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1199107692 169 RALLLDEPLTAVDPAMRgDVVRRLGDATAELGTAVLLVSHDLELVERL 216
Cdd:cd03279 153 EALFIDEGFGTLDPEAL-EAVATALELIRTENRMVGVISHVEELKERI 199
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
12-211 |
9.28e-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: 49.08 E-value: 9.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 12 TGLAAGY--GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRpTAGHVTYAGRTVTKLSRRD-KKQFTADV 88
Cdd:cd03289 6 KDLTAKYteGGNAVLENISFSISPGQR-VGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKwRKAFGVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 89 RRVSQ-DGLAGIGIDP--RWTvDRTLsaaLKDARRAGRPSG-RSVEDLLGDVALDARYAprtihsLSGGEKQRVALAVAL 164
Cdd:cd03289 84 QKVFIfSGTFRKNLDPygKWS-DEEI---WKVAEEVGLKSViEQFPGQLDFVLVDGGCV------LSHGHKQLMCLARSV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199107692 165 ATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAelGTAVLLVSHDLE 211
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRIE 198
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
147-226 |
1.33e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 147 IHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVrRLGDATAELGTAVLLVSHDLELVERLCPTVHVLADG 226
Cdd:PRK13549 403 IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIY-KLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
145-215 |
1.74e-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: 1.74e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199107692 145 RTIHSLSGGEKQRVALAVALATRP-RAL-LLDEPLTAVDPAMRG---DVVRRLGDataeLGTAVLLVSHDLELVER 215
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELFSEPpGTLfILDEPSTGLHQQDINqllEVIKGLID----LGNTVILIEHNLDVLSS 154
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
38-176 |
2.72e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 38 VGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGR-TVTKLSRRDKKQFTADVRRVSQDGLAGIG--------------ID 102
Cdd:PRK11147 32 VCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlIVARLQQDPPRNVEGTVYDFVAEGIEEQAeylkryhdishlveTD 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 103 PRwtvDRTLS--AALK---DARRAGRPSGRsVEDLLGDVALDARyAPRTihSLSGGEKQRVALAVALATRPRALLLDEP 176
Cdd:PRK11147 112 PS---EKNLNelAKLQeqlDHHNLWQLENR-INEVLAQLGLDPD-AALS--SLSGGWLRKAALGRALVSNPDVLLLDEP 183
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-211 |
4.84e-06 |
|
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: 46.17 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 20 GPDVVHGIDLDV-VPGAPPVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAgrtvtklSRRDKKQFTADVRRVSQDGLAG 98
Cdd:cd03290 11 GSGLATLSNINIrIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS-------NKNESEPSFEATRSRNRYSVAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 99 IGIDPrWTVDRTLSAALKDARRAGRPSGRSVED---LLGDVAL-----DARYAPRTIhSLSGGEKQRVALAVALATRPRA 170
Cdd:cd03290 84 AAQKP-WLLNATVEENITFGSPFNKQRYKAVTDacsLQPDIDLlpfgdQTEIGERGI-NLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1199107692 171 LLLDEPLTAV-----DPAMRGDVVRRLGDATaelgTAVLLVSHDLE 211
Cdd:cd03290 162 VFLDDPFSALdihlsDHLMQEGILKFLQDDK----RTLVLVTHKLQ 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
149-215 |
4.91e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 4.91e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199107692 149 SLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVER 215
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR 1424
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-232 |
5.84e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.17 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 2 STTTTPILRATGLAAGYGGPDVVHGIDLDVVPGAPPVgIVGESGAGKSTVVRALVGlvRP----TAGHVTYAGRTVTKLs 77
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHA-IMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 78 rrdkkqfTADVRrvSQDG--LA---GIGIdPRWTVDRTLSAALKDARRA-GRPSGRSVEDL------LGDVALDARYAPR 145
Cdd:CHL00131 77 -------EPEER--AHLGifLAfqyPIEI-PGVSNADFLRLAYNSKRKFqGLPELDPLEFLeiinekLKLVGMDPSFLSR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 146 TIHS-LSGGEKQRVA-LAVALaTRPRALLLDEPLTAVD-PAMR--GDVVRRLGDATaelgTAVLLVSHDLELVERLCPT- 219
Cdd:CHL00131 147 NVNEgFSGGEKKRNEiLQMAL-LDSELAILDETDSGLDiDALKiiAEGINKLMTSE----NSIILITHYQRLLDYIKPDy 221
|
250
....*....|...
gi 1199107692 220 VHVLADGTFVTSG 232
Cdd:CHL00131 222 VHVMQNGKIIKTG 234
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-232 |
5.98e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 47.13 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 4 TTTPILRATGLAAGY--GGPDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDK 81
Cdd:PRK11160 334 ADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEK-VALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 82 KQFTADV-RRVS------QDGLAgIGiDPRWTvDRTLSAALkdaRRAGrpsgrsVEDLL-GDVALDA------Ryaprti 147
Cdd:PRK11160 413 RQAISVVsQRVHlfsatlRDNLL-LA-APNAS-DEALIEVL---QQVG------LEKLLeDDKGLNAwlgeggR------ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 148 hSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAelGTAVLLVSHDLELVERLcPTVHVLADGT 227
Cdd:PRK11160 475 -QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQ 550
|
....*
gi 1199107692 228 FVTSG 232
Cdd:PRK11160 551 IIEQG 555
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-239 |
1.62e-05 |
|
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: 45.77 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 133 LGDVALDARYAPRTIHSLSGGEKQRVALAVALATRPRALL--LDEP---LTAVDPAMRGDVVRRLGDataeLGTAVLLVS 207
Cdd:TIGR00630 472 LIDVGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPsigLHQRDNRRLINTLKRLRD----LGNTLIVVE 547
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1199107692 208 HDLELVErlcptvhvLAD-------------GTFVTSGALRDVFA 239
Cdd:TIGR00630 548 HDEDTIR--------AADyvidigpgagehgGEVVASGTPEEILA 584
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
27-86 |
1.79e-05 |
|
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: 45.56 E-value: 1.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 27 IDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLSRRDKKQ-FTA 86
Cdd:COG4615 351 IDLTIRRGEL-VFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQlFSA 410
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
40-205 |
2.03e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRAL----VGLVRPTAGHVTYAGRTVTKLsrrdKKQFTADVRRVSQDglagigiD---PRWTVDRTLS 112
Cdd:TIGR00956 92 VLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEI----KKHYRGDVVYNAET-------DvhfPHLTVGETLD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 113 AALKDARRAGRPSGRSVEDL---LGDVAL---------DARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAV 180
Cdd:TIGR00956 161 FAARCKTPQNRPDGVSREEYakhIADVYMatyglshtrNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGL 240
|
170 180
....*....|....*....|....*
gi 1199107692 181 DPAMRGDVVRRLGDATAELGTAVLL 205
Cdd:TIGR00956 241 DSATALEFIRALKTSANILDTTPLV 265
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
39-185 |
2.34e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 39 GIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVT--KLSRRdkkqftadvRRV---SQD-GLAGigidpRWTVDR--T 110
Cdd:NF033858 296 GFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDagDIATR---------RRVgymSQAfSLYG-----ELTVRQnlE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 111 LSAAL---KDARRAGRpsgrsVEDL-----LGDVAlDARYAprtihSLSGGEKQRVALAVALATRPRALLLDEPLTAVDP 182
Cdd:NF033858 362 LHARLfhlPAAEIAAR-----VAEMlerfdLADVA-DALPD-----SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP 430
|
...
gi 1199107692 183 AMR 185
Cdd:NF033858 431 VAR 433
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-209 |
5.68e-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: 42.36 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 37 PVGIVGESGAGKSTVVRALVGLVRPTAGHVtyagrtvtklsrrdkkqftadvrrvsqdglagIGIDPRWTVDRTLSAALK 116
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------IYIDGEDILEEVLDQLLL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 117 DarragrpsgrsvedllgdvaldarYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDV-----VRR 191
Cdd:smart00382 52 I------------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRL 107
|
170
....*....|....*...
gi 1199107692 192 LGDATAELGTAVLLVSHD 209
Cdd:smart00382 108 LLLLKSEKNLTVILTTND 125
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
150-208 |
6.27e-05 |
|
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: 43.97 E-value: 6.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 150 LSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGdvvrRLGDATAELGTAVLLVSH 208
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG----YMYRLCREFGITLFSVSH 637
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-228 |
7.55e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.96 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 27 IDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTA-GHVTYAGRT--VTKLSRrdkkQFTADVRrvsQDGLAGIGIDP 103
Cdd:PLN03130 636 INLDVPVGSL-VAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVayVPQVSW----IFNATVR---DNILFGSPFDP 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 104 -RWtvDRTLSAALKDARRAGRPSGRSVEdlLGDVALDaryaprtihsLSGGEKQRVALAVALATRPRALLLDEPLTAVDp 182
Cdd:PLN03130 708 eRY--ERAIDVTALQHDLDLLPGGDLTE--IGERGVN----------ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD- 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1199107692 183 amrGDVVRRLGDA--TAELG--TAVLLVS--HDLELVERLCpTVH---VLADGTF 228
Cdd:PLN03130 773 ---AHVGRQVFDKciKDELRgkTRVLVTNqlHFLSQVDRII-LVHegmIKEEGTY 823
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
131-214 |
7.85e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.63 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 131 DLLGDVALDARYAPRTIHSLSGGEKQRVALAVALATRPRALL--LDEPLTAVDPAMRG---DVVRRLGDataeLGTAVLL 205
Cdd:cd03270 119 GFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDrliETLKRLRD----LGNTVLV 194
|
....*....
gi 1199107692 206 VSHDLELVE 214
Cdd:cd03270 195 VEHDEDTIR 203
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
20-232 |
9.87e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 20 GPDVVHGIDLDVVPGAPPvGIVGESGAGKSTVVRALVGL--VRPTAGHVTYAGRTVTKLSRRDKK--------QFTADVR 89
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVH-AIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAgegifmafQYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 90 RVSQDGLagigidprwtvdrtLSAALKDAR--RAGRPSGR-SVEDLLGD----VALDARYAPRTIH-SLSGGEKQRVALA 161
Cdd:PRK09580 92 GVSNQFF--------------LQTALNAVRsyRGQEPLDRfDFQDLMEEkialLKMPEDLLTRSVNvGFSGGEKKRNDIL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199107692 162 VALATRPRALLLDEpltaVDPAMRGDVVRRLGDATAEL---GTAVLLVSHDLELVERLCPT-VHVLADGTFVTSG 232
Cdd:PRK09580 158 QMAVLEPELCILDE----SDSGLDIDALKIVADGVNSLrdgKRSFIIVTHYQRILDYIKPDyVHVLYQGRIVKSG 228
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-213 |
1.20e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 1.20e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199107692 145 RTIHSLSGGEKQRVALAVALATRPRAL--LLDEP---LTAVDPAMRGDVVRRLGDAtaelGTAVLLVSHDLELV 213
Cdd:PRK00635 472 RALATLSGGEQERTALAKHLGAELIGItyILDEPsigLHPQDTHKLINVIKKLRDQ----GNTVLLVEHDEQMI 541
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
124-213 |
1.86e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.83 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 124 PSGRSVEDLLGDVALDarYAP--RTIHSLSGGEKQRVALAVAL---ATRPRALLLDEPLTAV---DPAMRGDVVRRLgda 195
Cdd:cd03271 144 PKIARKLQTLCDVGLG--YIKlgQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLhfhDVKKLLEVLQRL--- 218
|
90
....*....|....*...
gi 1199107692 196 tAELGTAVLLVSHDLELV 213
Cdd:cd03271 219 -VDKGNTVVVIEHNLDVI 235
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
150-225 |
1.98e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 1.98e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199107692 150 LSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRRLGDATAELGTAVLLVSHDLELVeRLCPTVHVLAD 225
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVLSN 654
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
149-213 |
2.01e-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: 42.31 E-value: 2.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 149 SLSGGEKQRVALAVAL---ATRPRALLLDEPLTAV---DPAMRGDVVRRLGDAtaelGTAVLLVSHDLELV 213
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLhfdDIKKLLEVLQRLVDK----GNTVVVIEHNLDVI 895
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
150-241 |
2.35e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.46 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 150 LSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRGDVVRR--LGdatAELGTAVLLVSHDLELVERlCPTVHVLADGT 227
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEcfLG---ALAGKTRVLATHQVHVVPR-ADYVVALGDGR 858
|
90
....*....|....
gi 1199107692 228 FVTSGALRDvFAGT 241
Cdd:PTZ00243 859 VEFSGSSAD-FMRT 871
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
136-216 |
3.30e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 136 VALDARYAPRTIHSLSGGEKQRVALAVALA----------TRPRALLLDEPLTAVDPAMRGDVVRRLgDATAELGTAVLL 205
Cdd:TIGR00618 937 VADAYTGSVRPSATLSGGETFLASLSLALAladllstsggTVLDSLFIDEGFGSLDEDSLDRAIGIL-DAIREGSKMIGI 1015
|
90
....*....|.
gi 1199107692 206 VSHDLELVERL 216
Cdd:TIGR00618 1016 ISHVPEFRERI 1026
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
40-216 |
4.98e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 40.28 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRALV----GLVRPTaghvTYAGRTVTKLSRrdKKQFTADVR---RVSQDGlagigidpRWTVDRTLS 112
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyaltGELPPN----SKGGAHDPKLIR--EGEVRAQVKlafENANGK--------KYTITRSLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 113 AAlkdarragrpsgRSV-----EDLlgdvaldARYAPRTIHSLSGGEKQ------RVALAVALATRPRALLLDEPLTAVD 181
Cdd:cd03240 93 IL------------ENVifchqGES-------NWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 1199107692 182 PAMRGDVVRRLGDATAELGT-AVLLVSHDLELVERL 216
Cdd:cd03240 154 EENIEESLAEIIEERKSQKNfQLIVITHDEELVDAA 189
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
149-229 |
5.66e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 149 SLSGGEKQRVALAVALATRPRALLLDEPltavdpaMRG-DV---------VRRLgdatAELGTAVLLVSHdlELVERL-- 216
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEP-------TRGiDVgakyeiytiINEL----AAEGKGVIVISS--ELPELLgm 470
|
90
....*....|...
gi 1199107692 217 CPTVHVLADGTFV 229
Cdd:NF040905 471 CDRIYVMNEGRIT 483
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
40-229 |
7.88e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRALVGlVRPtagHVTYAGRTVTKLSRRdkkQFtADVRRVSQDG-------LA--------------- 97
Cdd:NF040905 32 LCGENGAGKSTLMKVLSG-VYP---HGSYEGEILFDGEVC---RF-KDIRDSEALGiviihqeLAlipylsiaeniflgn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 98 -----GIgIDprWtvDRTLsaalkdaRRAgrpsgrsvEDLLGDVALDAryAPRT-IHSLSGGEKQRVALAVALATRPRAL 171
Cdd:NF040905 104 erakrGV-ID--W--NETN-------RRA--------RELLAKVGLDE--SPDTlVTDIGVGKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199107692 172 LLDEPlTAvdpAMRGDVVRRLGDATAEL---GTAVLLVSHDLELVERLCPTVHVLADGTFV 229
Cdd:NF040905 162 ILDEP-TA---ALNEEDSAALLDLLLELkaqGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
150-182 |
8.01e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 8.01e-04
10 20 30
....*....|....*....|....*....|...
gi 1199107692 150 LSGGEKQRVALAVALATRPRALLLDEPLTAVDP 182
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
40-208 |
8.19e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.60 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 40 IVGESGAGKSTVVRALVGlvRPTAGHVtyagRTVTKLSRRDKKQFTadVRRVS----QDGLAgigiDPRWTVDRTL--SA 113
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAG--RKTGGYI----EGDIRISGFPKKQET--FARISgyceQNDIH----SPQVTVRESLiySA 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 114 ALKDARRAGRPSG-RSVEDLLGDVAL----DARYAPRTIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVDpAMRGDV 188
Cdd:PLN03140 979 FLRLPKEVSKEEKmMFVDEVMELVELdnlkDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD-ARAAAI 1057
|
170 180
....*....|....*....|
gi 1199107692 189 VRRLGDATAELGTAVLLVSH 208
Cdd:PLN03140 1058 VMRTVRNTVDTGRTVVCTIH 1077
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-181 |
1.04e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 40.08 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 21 PDVVHGIDLDVVPGAPpVGIVGESGAGKSTVVRALVGLVRPTAGHVTYAGRTVTKLsRRDkkQFTADVRRVSQ------D 94
Cdd:PRK10789 328 HPALENVNFTLKPGQM-LGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL-QLD--SWRSRLAVVSQtpflfsD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199107692 95 GLAGigidprwtvdrtlSAALkdarraGRPSGRSVE----DLLGDVALDARYAPRTIHS--------LSGGEKQRVALAV 162
Cdd:PRK10789 404 TVAN-------------NIAL------GRPDATQQEiehvARLASVHDDILRLPQGYDTevgergvmLSGGQKQRISIAR 464
|
170
....*....|....*....
gi 1199107692 163 ALATRPRALLLDEPLTAVD 181
Cdd:PRK10789 465 ALLLNAEILILDDALSAVD 483
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
146-181 |
1.31e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 1.31e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1199107692 146 TIHSLSGGEKQRVALAVALATRPRALLLDEPLTAVD 181
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
149-215 |
3.54e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 38.46 E-value: 3.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199107692 149 SLSGGEKQRVALAVALATRPRALLLDEPLTAVDPAMRgdvvRRLGDATAEL--GTAVLLVSHDLELVER 215
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTESE----RAIQAALDELqkNRTSLVIAHRLSTIEK 544
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
150-213 |
5.73e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 5.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199107692 150 LSGGEKQRVALAVALATR--PRAL-LLDEPLTavdpamrG----------DVVRRLgdatAELGTAVLLVSHDLELV 213
Cdd:COG0178 827 LSGGEAQRVKLASELSKRstGKTLyILDEPTT-------GlhfhdirkllEVLHRL----VDKGNTVVVIEHNLDVI 892
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
150-178 |
9.12e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.36 E-value: 9.12e-03
10 20 30
....*....|....*....|....*....|..
gi 1199107692 150 LSGGEKQRVALAVALATRP--RAL-LLDEPLT 178
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgKTLyILDEPTT 862
|
|
| |
