|
Name |
Accession |
Description |
Interval |
E-value |
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-261 |
1.19e-153 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 428.49 E-value: 1.19e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENLRFDNCHGKRWQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHY 80
Cdd:COG4167 1 MSALLEVRNLSKTFKYRTGLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 81 DNKHRVLNIRMVFQNSNESLNPGITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQRQRVAL 160
Cdd:COG4167 81 DYKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 161 ARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHW 240
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240
|
250 260
....*....|....*....|.
gi 495265151 241 PKDEYTKKLVHAHQALINGQS 261
Cdd:COG4167 241 PQHEVTKRLIESHFGEALTAD 261
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-252 |
5.72e-100 |
|
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: 301.05 E-value: 5.72e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLRFDncHGKRwqNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNK 83
Cdd:COG1123 260 LLEVRNLSKR--YPVR--GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 HRVL---NIRMVFQNSNESLNPGITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQRQRVAL 160
Cdd:COG1123 336 SLRElrrRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 161 ARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHW 240
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
250
....*....|..
gi 495265151 241 PKDEYTKKLVHA 252
Cdd:COG1123 496 PQHPYTRALLAA 507
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-252 |
3.60e-97 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 287.78 E-value: 3.60e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLRfdnchgKRWQNKGSKFTLGP--------INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNER 75
Cdd:COG4608 7 LLEVRDLK------KHFPVRGGLFGRTVgvvkavdgVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 76 KLEHYDN---KHRVLNIRMVFQNSNESLNPGITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSD 152
Cdd:COG4608 81 DITGLSGrelRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 153 GQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250 260
....*....|....*....|
gi 495265151 233 KTDVIFHWPKDEYTKKLVHA 252
Cdd:COG4608 241 PRDELYARPLHPYTQALLSA 260
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
29-252 |
1.02e-94 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 281.47 E-value: 1.02e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDN---KHRVLNIRMVFQNSNESLNPGIT 105
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQNPYGSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 106 LGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVR 185
Cdd:PRK11308 111 VGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495265151 186 SQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLVHA 252
Cdd:PRK11308 191 AQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSA 257
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-252 |
6.40e-92 |
|
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: 271.29 E-value: 6.40e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENL--RFDNCHGKRwqnkgskFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYD 81
Cdd:COG1124 1 MLEVRNLsvSYGQGGRRV-------PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 82 NKHRVLNIRMVFQNSNESLNPGITLGSILEEPLKLNTRLDNQARIAKVeqtLKLVGLLPEHRFFYRHMLSDGQRQRVALA 161
Cdd:COG1124 74 RKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREERIAEL---LEQVGLPPSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 162 RAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWP 241
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
250
....*....|.
gi 495265151 242 KDEYTKKLVHA 252
Cdd:COG1124 231 KHPYTRELLAA 241
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-252 |
4.41e-89 |
|
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: 266.53 E-value: 4.41e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLR--FDnchgkrwQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQP---DSGSIYLNERKLE 78
Cdd:COG0444 1 LLEVRNLKvyFP-------TRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 79 HYD----NKHRVLNIRMVFQNSNESLNPGITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEHRFF--YRHMLSD 152
Cdd:COG0444 74 KLSekelRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLdrYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 153 GQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250 260
....*....|....*....|
gi 495265151 233 KTDVIFHWPKDEYTKKLVHA 252
Cdd:COG0444 234 PVEELFENPRHPYTRALLSS 253
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-232 |
4.80e-88 |
|
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: 260.90 E-value: 4.80e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLRFDNCHGKRWQnkgskFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNK 83
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSV-----KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 HRVL---NIRMVFQNSNESLNPGITLGSILEEPLKLNTRLDNQARI-AKVEQTLKLVGLLPEHRFFYRHMLSDGQRQRVA 159
Cdd:cd03257 76 LRKIrrkEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARkEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495265151 160 LARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-253 |
8.77e-88 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 261.65 E-value: 8.77e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENL----RFDNCHGKRWQNKGSKftlgPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERK 76
Cdd:PRK15112 1 VETLLEVRNLsktfRYRTGWFRRQTVEAVK----PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 77 LEHYDNKHRVLNIRMVFQNSNESLNPGITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQRQ 156
Cdd:PRK15112 77 LHFGDYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 157 RVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDV 236
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
250
....*....|....*..
gi 495265151 237 IFHWPKDEYTKKLVHAH 253
Cdd:PRK15112 237 VLASPLHELTKRLIAGH 253
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
32-252 |
1.52e-82 |
|
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: 256.54 E-value: 1.52e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLeQPDSGSIYLNERKLEHYDNKH-RVL--NIRMVFQNSNESLNPGITLGS 108
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAlRPLrrRMQVVFQDPFGSLSPRMTVGQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ILEEPLKL-NTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQ 187
Cdd:COG4172 384 IIAEGLRVhGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 188 TVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLVHA 252
Cdd:COG4172 464 ILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAA 528
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-252 |
2.75e-70 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 219.19 E-value: 2.75e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLR--FDNCHGKR--WQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSI-YLNE--RK 76
Cdd:PRK15079 8 LLEVADLKvhFDIKDGKQwfWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLGKdlLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 77 LEHYDNKHRVLNIRMVFQNSNESLNPGITLGSILEEPLKL-NTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQR 155
Cdd:PRK15079 88 MKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 156 QRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTD 235
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 247
|
250
....*....|....*..
gi 495265151 236 VIFHWPKDEYTKKLVHA 252
Cdd:PRK15079 248 EVYHNPLHPYTKALMSA 264
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-252 |
7.53e-69 |
|
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: 221.10 E-value: 7.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLR--FDnchgkrwQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPD----SGSIYLNERKL 77
Cdd:COG4172 6 LLSVEDLSvaFG-------QGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 78 EHYD----NKHRVLNIRMVFQNSNESLNPGITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLL-PEHRF-FYRHMLS 151
Cdd:COG4172 79 LGLSerelRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPdPERRLdAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 152 DGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVES 231
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
250 260
....*....|....*....|.
gi 495265151 232 GKTDVIFHWPKDEYTKKLVHA 252
Cdd:COG4172 239 GPTAELFAAPQHPYTRKLLAA 259
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-242 |
9.61e-67 |
|
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: 215.15 E-value: 9.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENLRFDNCHGKRWqnkgskfTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPD---SGSIYLNERKL 77
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVP-------AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 78 EHYDNKHRVLNIRMVFQNSNESLNPgITLGSILEEPLkLNTRLDNQARIAKVEQTLKLVGLlpEHRFF-YRHMLSDGQRQ 156
Cdd:COG1123 74 LELSEALRGRRIGMVFQDPMTQLNP-VTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGL--ERRLDrYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 157 RVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDV 236
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
....*.
gi 495265151 237 IFHWPK 242
Cdd:COG1123 230 ILAAPQ 235
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
32-252 |
1.14e-57 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 193.92 E-value: 1.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHY-DNKHRVL--NIRMVFQNSNESLNPGITLGS 108
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLsPGKLQALrrDIQFIFQDPYASLDPRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ILEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQT 188
Cdd:PRK10261 423 SIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495265151 189 VNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLVHA 252
Cdd:PRK10261 503 INLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAA 566
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-239 |
3.11e-56 |
|
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: 179.84 E-value: 3.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRFdnchgkRWQnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLehydNKH 84
Cdd:COG1122 1 IELENLSF------SYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI----TKK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 85 RVLNIR----MVFQNSNESL-NPgitlgSILEE----PLklNTRLDNQARIAKVEQTLKLVGLlpEHrffYR----HMLS 151
Cdd:COG1122 69 NLRELRrkvgLVFQNPDDQLfAP-----TVEEDvafgPE--NLGLPREEIRERVEEALELVGL--EH---LAdrppHELS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 152 DGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVES 231
Cdd:COG1122 137 GGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
....*...
gi 495265151 232 GKTDVIFH 239
Cdd:COG1122 216 GTPREVFS 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
32-239 |
7.50e-56 |
|
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: 179.02 E-value: 7.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRV---LNIRMVFQNSN--ESLNpgitl 106
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRIGMLFQGGAlfDSLT----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 gsiLEE----PLKLNTRLDNQARIAKVEQTLKLVGlLPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDP 182
Cdd:COG1127 99 ---VFEnvafPLREHTDLSEAEIRELVLEKLELVG-LPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 183 sVRSQTVN-LLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFH 239
Cdd:COG1127 175 -ITSAVIDeLIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-230 |
2.53e-55 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 178.73 E-value: 2.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLRFDNCHGKRWQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNK 83
Cdd:PRK10419 3 LLNVSGLSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 HRVL---NIRMVFQNSNESLNPGITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQRQRVAL 160
Cdd:PRK10419 83 QRKAfrrDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 161 ARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVE 230
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
4-245 |
5.12e-54 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 177.98 E-value: 5.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLRfdnchgKRWqnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNK 83
Cdd:COG3842 5 ALELENVS------KRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 HRvlNIRMVFQNsnESLNPGITLGSILEEPLKLNtRLDNQARIAKVEQTLKLVGLLP-EHRffYRHMLSDGQRQRVALAR 162
Cdd:COG3842 76 KR--NVGMVFQD--YALFPHLTVAENVAFGLRMR-GVPKAEIRARVAELLELVGLEGlADR--YPHQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 163 AIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHN----LGivrhISDKILVMKQGKVVESGKTDVIF 238
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRIEQVGTPEEIY 224
|
....*..
gi 495265151 239 HWPKDEY 245
Cdd:COG3842 225 ERPATRF 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-234 |
1.40e-53 |
|
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: 174.22 E-value: 1.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLRFDNCHGKRWQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNK 83
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 HRVL---NIRMVFQNSNESLNPGITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQRQRVAL 160
Cdd:TIGR02769 82 QRRAfrrDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495265151 161 ARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKT 234
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDV 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-249 |
3.77e-53 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 179.90 E-value: 3.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLR--FDNCHGKRWQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLeQPDSGSIYLNERKLEHYD 81
Cdd:PRK15134 275 LLDVEQLQvaFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL-INSQGEIWFDGQPLHNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 82 NK------HRvlnIRMVFQNSNESLNPGITLGSILEEPLKLNTR-LDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQ 154
Cdd:PRK15134 354 RRqllpvrHR---IQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPtLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 155 RQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKT 234
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDC 510
|
250
....*....|....*
gi 495265151 235 DVIFHWPKDEYTKKL 249
Cdd:PRK15134 511 ERVFAAPQQEYTRQL 525
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-230 |
2.12e-52 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 169.84 E-value: 2.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENLRfdnchgKRWQNKGSKFT-LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEH 79
Cdd:COG1136 1 MSPLLELRNLT------KSYGTGEGEVTaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 80 YDNKHRVL----NIRMVFQNSNesLNPGITlgsILEE---PLKLNtRLDNQARIAKVEQTLKLVGLlpEHRFFYR-HMLS 151
Cdd:COG1136 75 LSERELARlrrrHIGFVFQFFN--LLPELT---ALENvalPLLLA-GVSRKERRERARELLERVGL--GDRLDHRpSQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 152 DGQRQRVALARAIILNPQVIVADEPFAALDpSVRSQTV-NLLMELQRELGLGFIFISHNLGIVRHiSDKILVMKQGKVVE 230
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLD-SKTGEEVlELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
24-239 |
2.75e-52 |
|
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: 169.99 E-value: 2.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKL----EHYDNKHRvLNIRMVFQNSneS 99
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLR-RRMGMLFQSG--A 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 100 LNPGITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEHRFfYRHMLSDGQRQRVALARAIILNPQVIVADEPFAA 179
Cdd:cd03261 88 LFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDL-YPAELSGGMKKRVALARALALDPELLLYDEPTAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 180 LDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFH 239
Cdd:cd03261 167 LDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
10-232 |
4.90e-52 |
|
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: 168.47 E-value: 4.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 10 LRFDNCHgKRWqnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRvlNI 89
Cdd:cd03259 1 LELKGLS-KTY---GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR--NI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 90 RMVFQNSneSLNPGITLGSILEEPLKLNtRLDNQARIAKVEQTLKLVGLLP-EHRffYRHMLSDGQRQRVALARAIILNP 168
Cdd:cd03259 75 GMVFQDY--ALFPHLTVAENIAFGLKLR-GVPKAEIRARVRELLELVGLEGlLNR--YPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495265151 169 QVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-252 |
7.16e-52 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 171.83 E-value: 7.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENLR--FDNchgkrwqNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPD---SGSIYLNER 75
Cdd:PRK09473 9 ADALLDVKDLRvtFST-------PDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 76 KL----EHYDNKHRVLNIRMVFQNSNESLNPGITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLlPEHR---FFYRH 148
Cdd:PRK09473 82 EIlnlpEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKM-PEARkrmKMYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 149 MLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKV 228
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 240
|
250 260
....*....|....*....|....
gi 495265151 229 VESGKTDVIFHWPKDEYTKKLVHA 252
Cdd:PRK09473 241 MEYGNARDVFYQPSHPYSIGLLNA 264
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
17-242 |
2.30e-51 |
|
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: 167.37 E-value: 2.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 17 GKRWQNKGSKFT-LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVL---NIRMV 92
Cdd:cd03258 8 SKVFGDTGGKVTaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKarrRIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 93 FQNSNeSLNPGITLGSIlEEPLKLnTRLDNQARIAKVEQTLKLVGLlPEHRFFYRHMLSDGQRQRVALARAIILNPQVIV 172
Cdd:cd03258 88 FQHFN-LLSSRTVFENV-ALPLEI-AGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 173 ADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPK 242
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-227 |
1.84e-50 |
|
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: 164.56 E-value: 1.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 6 SVENLRFDnchgkrwQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHR 85
Cdd:cd03225 1 ELKNLSFS-------YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 86 VLNIRMVFQNSNESLnpgitLGSILEEPLK---LNTRLDNQARIAKVEQTLKLVGL--LPEHRFfyrHMLSDGQRQRVAL 160
Cdd:cd03225 74 RRKVGLVFQNPDDQF-----FGPTVEEEVAfglENLGLPEEEIEERVEEALELVGLegLRDRSP---FTLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495265151 161 ARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGK 227
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-251 |
1.78e-49 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 165.64 E-value: 1.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRfdnchgKRWQNKGSKFT-LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNK 83
Cdd:COG1135 2 IELENLS------KTFPTKGGPVTaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 HRVL---NIRMVFQNSNeslnpgitlgsILEE---------PLKLnTRLDNQARIAKVEQTLKLVGLlPEHRFFYRHMLS 151
Cdd:COG1135 76 ELRAarrKIGMIFQHFN-----------LLSSrtvaenvalPLEI-AGVPKAEIRKRVAELLELVGL-SDKADAYPSQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 152 DGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVES 231
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
|
250 260
....*....|....*....|
gi 495265151 232 GKTDVIFHWPKDEYTKKLVH 251
Cdd:COG1135 223 GPVLDVFANPQSELTRRFLP 242
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-228 |
6.01e-49 |
|
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: 160.73 E-value: 6.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRfdnchgKRWQNKGSKFT-LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNK 83
Cdd:cd03255 1 IELKNLS------KTYGGGGEKVQaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 HRVL----NIRMVFQNSNesLNPGITLGSILEEPLKLNTRLDNQARiAKVEQTLKLVGLlpEHRFFYR-HMLSDGQRQRV 158
Cdd:cd03255 75 ELAAfrrrHIGFVFQSFN--LLPDLTALENVELPLLLAGVPKKERR-ERAEELLERVGL--GDRLNHYpSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 159 ALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHiSDKILVMKQGKV 228
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
24-242 |
2.05e-47 |
|
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: 157.40 E-value: 2.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRvlNIRMVFQNSneSLNPG 103
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR--PVNTVFQNY--ALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 ITLGSILEEPLKLNtRLDNQARIAKVEQTLKLVGLLpEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPS 183
Cdd:cd03300 87 LTVFENIAFGLRLK-KLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 184 VRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPK 242
Cdd:cd03300 165 LRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
29-246 |
2.27e-47 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 160.70 E-value: 2.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLehYDNKH-RVLNIRMVFQN----------SN 97
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL--FTNLPpRERRVGFVFQHyalfphmtvaEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 98 eslnpgITLGsileeplkLNTRLDNQARI-AKVEQTLKLVGLL-PEHRffYRHMLSDGQRQRVALARAIILNPQVIVADE 175
Cdd:COG1118 96 ------IAFG--------LRVRPPSKAEIrARVEELLELVQLEgLADR--YPSQLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495265151 176 PFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYT 246
Cdd:COG1118 160 PFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFV 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-230 |
2.79e-47 |
|
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: 156.48 E-value: 2.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRfdnchgKRWQNKGSKFT-LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNK 83
Cdd:cd03293 1 LEVRNVS------KTYGGGGGAVTaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 hrvlnIRMVFQNSneSLNPGITlgsILEE---PLKLNtRLDNQARIAKVEQTLKLVGLLP-EHRffYRHMLSDGQRQRVA 159
Cdd:cd03293 75 -----RGYVFQQD--ALLPWLT---VLDNvalGLELQ-GVPKAEARERAEELLELVGLSGfENA--YPHQLSGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495265151 160 LARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQ--GKVVE 230
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-237 |
6.63e-47 |
|
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: 156.74 E-value: 6.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLRFDnchgkrwqnKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNK 83
Cdd:COG1120 1 MLEAENLSVG---------YGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 HRVLNIRMVFQNSneSLNPGIT------LGSIleePLKLNTRLDNQARIAKVEQTLKLVGLLP-EHRFFyrHMLSDGQRQ 156
Cdd:COG1120 72 ELARRIAYVPQEP--PAPFGLTvrelvaLGRY---PHLGLFGRPSAEDREAVEEALERTGLEHlADRPV--DELSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 157 RVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKT-D 235
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPeE 224
|
..
gi 495265151 236 VI 237
Cdd:COG1120 225 VL 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
32-248 |
1.95e-46 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 154.77 E-value: 1.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEhyDNKHRVLNIR----MVFQNSNesLNPGIT-L 106
Cdd:COG1126 20 ISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT--DSKKDINKLRrkvgMVFQQFN--LFPHLTvL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 GSILEEPLKLNTRLDNQARiAKVEQTLKLVGLLpEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRS 186
Cdd:COG1126 96 ENVTLAPIKVKKMSKAEAE-ERAMELLERVGLA-DKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495265151 187 QTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKK 248
Cdd:COG1126 174 EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-245 |
2.18e-46 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 157.93 E-value: 2.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRfdnchgKRWqnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKH 84
Cdd:COG3839 4 LELENVS------KSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 85 RvlNIRMVFQNSneSLNPGIT----LGSileePLKLNtRLDNQARIAKVEQTLKLVGLlpEHrFFYRH--MLSDGQRQRV 158
Cdd:COG3839 75 R--NIAMVFQSY--ALYPHMTvyenIAF----PLKLR-KVPKAEIDRRVREAAELLGL--ED-LLDRKpkQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 159 ALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHN------LGivrhisDKILVMKQGKVVESG 232
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveamtLA------DRIAVMNDGRIQQVG 216
|
250
....*....|...
gi 495265151 233 KTDVIFHWPKDEY 245
Cdd:COG3839 217 TPEELYDRPANLF 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
32-252 |
2.31e-46 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 161.80 E-value: 2.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLA-KLLVGLEQPD----SGSIYLNERKLEHYDNKH----RVLNIRMVFQNSNESLNP 102
Cdd:PRK15134 28 VSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPPvvypSGDIRFHGESLLHASEQTlrgvRGNKIAMIFQEPMVSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 103 GITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEHRFF--YRHMLSDGQRQRVALARAIILNPQVIVADEPFAAL 180
Cdd:PRK15134 108 LHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLtdYPHQLSGGERQRVMIAMALLTRPELLIADEPTTAL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495265151 181 DPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLVHA 252
Cdd:PRK15134 188 DVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLNS 259
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
32-250 |
2.52e-46 |
|
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: 155.49 E-value: 2.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKhRVLNIR-----MVFQNSneSLNPGITL 106
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRK-ELRELRrkkisMVFQSF--ALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 GSILEEPLKLNTrLDNQARIAKVEQTLKLVGLLP-EHRffYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVR 185
Cdd:cd03294 120 LENVAFGLEVQG-VPRAEREERAAEALELVGLEGwEHK--YPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIR 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 186 SQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLV 250
Cdd:cd03294 197 REMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
24-227 |
3.02e-46 |
|
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: 152.34 E-value: 3.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVL--NIRMVFQNSNesLN 101
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrRIGMVFQDFA--LF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 102 PGITLGSILEEPLklntrldnqariakveqtlklvgllpehrffyrhmlSDGQRQRVALARAIILNPQVIVADEPFAALD 181
Cdd:cd03229 89 PHLTVLENIALGL------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495265151 182 PSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGK 227
Cdd:cd03229 133 PITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-230 |
3.56e-46 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 154.86 E-value: 3.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLrfdnchGKRWQNKGSKFT-LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDN 82
Cdd:COG1116 7 ALELRGV------SKRFPTGGGGVTaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 83 KhrvlnIRMVFQNSneSL--------NpgITLGsileepLKLnTRLDNQARIAKVEQTLKLVGLLP-EHRffYRHMLSDG 153
Cdd:COG1116 81 D-----RGVVFQEP--ALlpwltvldN--VALG------LEL-RGVPKAERRERARELLELVGLAGfEDA--YPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 154 QRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLG-IVRhISDKILVMKQ--GKVVE 230
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVF-LADRVVVLSArpGRIVE 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-238 |
3.60e-46 |
|
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: 155.28 E-value: 3.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRFdnchgkRWQNkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLehyDNKH 84
Cdd:TIGR04520 1 IEVENVSF------SYPE-SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT---LDEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 85 RVLNIR----MVFQNSNESLnpgitLGSILEEPLKL---NTRLDNQARIAKVEQTLKLVGLLpEHRFFYRHMLSDGQRQR 157
Cdd:TIGR04520 71 NLWEIRkkvgMVFQNPDNQF-----VGATVEDDVAFgleNLGVPREEMRKRVDEALKLVGME-DFRDREPHLLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 158 VALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHiSDKILVMKQGKVVESGKTDVI 237
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREI 223
|
.
gi 495265151 238 F 238
Cdd:TIGR04520 224 F 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
32-232 |
7.22e-46 |
|
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: 163.08 E-value: 7.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQNsneslnpgITL--GSI 109
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQD--------VFLfsGTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 110 LEeplklNTRLDN-QARIAKVEQTLKLVGLlpeHRFFYRH-------------MLSDGQRQRVALARAIILNPQVIVADE 175
Cdd:COG2274 566 RE-----NITLGDpDATDEEIIEAARLAGL---HDFIEALpmgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495265151 176 PFAALDPSVRSQTVNLLMELQRELGLgfIFISHNLGIVRHiSDKILVMKQGKVVESG 232
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLKGRTV--IIIAHRLSTIRL-ADRIIVLDKGRIVEDG 691
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-252 |
4.32e-45 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 160.02 E-value: 4.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 2 NDLLSVENLRFdnchgkRWQNKGSKF-TLGPINFSIQAGETLAIVGANGSGKSLLA-KLLVGLEQP----DSGSIYLNER 75
Cdd:PRK10261 10 RDVLAVENLNI------AFMQEQQKIaAVRNLSFSLQRGETLAIVGESGSGKSVTAlALMRLLEQAgglvQCDKMLLRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 76 KLEHYD---------NKHRVLNIRMVFQNSNESLNPGITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVgLLPEHRFF- 145
Cdd:PRK10261 84 SRQVIElseqsaaqmRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQV-RIPEAQTIl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 146 --YRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVM 223
Cdd:PRK10261 163 srYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
250 260
....*....|....*....|....*....
gi 495265151 224 KQGKVVESGKTDVIFHWPKDEYTKKLVHA 252
Cdd:PRK10261 243 YQGEAVETGSVEQIFHAPQHPYTRALLAA 271
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
18-232 |
2.97e-44 |
|
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: 148.56 E-value: 2.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 18 KRWqnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRvlNIRMVFQNSn 97
Cdd:cd03301 8 KRF---GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR--DIAMVFQNY- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 98 eSLNPGITLGSILEEPLKLN--TRLDNQARIAKVEQTLKLVGLLpeHRffYRHMLSDGQRQRVALARAIILNPQVIVADE 175
Cdd:cd03301 82 -ALYPHMTVYDNIAFGLKLRkvPKDEIDERVREVAELLQIEHLL--DR--KPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495265151 176 PFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
32-252 |
4.44e-44 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 151.43 E-value: 4.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGL-EQPD---SGSIYLNERKLEHYDNKHRV----LNIRMVFQNSNESLNPG 103
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPGrvmAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPMTSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 ITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLL-PEHRF-FYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALD 181
Cdd:PRK11022 106 YTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPdPASRLdVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495265151 182 PSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLVHA 252
Cdd:PRK11022 186 VTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRA 256
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-232 |
4.60e-44 |
|
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: 146.81 E-value: 4.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 6 SVENLRFDNchgkrwqnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHR 85
Cdd:cd03214 1 EVENLSVGY---------GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 86 vlnirmvfqnsneslnpgitlgsileeplklntrldnqAR-IAKVEQTLKLVGLLP-EHRFFyrHMLSDGQRQRVALARA 163
Cdd:cd03214 72 --------------------------------------ARkIAYVPQALELLGLAHlADRPF--NELSGGERQRVLLARA 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 164 IILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:cd03214 112 LAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
22-238 |
1.14e-43 |
|
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: 149.14 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 22 NKGSKF---TLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVlNIR----MVFQ 94
Cdd:TIGR04521 11 QPGTPFekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLK-DLRkkvgLVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 95 NSNESL--------------NPGITLGSILEeplklntrldnqariaKVEQTLKLVGLLPEhrFFYRH--MLSDGQRQRV 158
Cdd:TIGR04521 90 FPEHQLfeetvykdiafgpkNLGLSEEEAEE----------------RVKEALELVGLDEE--YLERSpfELSGGQMRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 159 ALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIF 238
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
32-237 |
1.87e-43 |
|
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: 146.94 E-value: 1.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGL-----EQPDSGSIYLNERKLehYDNKHRVLNIR----MVFQNSNesLNP 102
Cdd:cd03260 19 ISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDI--YDLDVDVLELRrrvgMVFQKPN--PFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 103 GitlgSILEE---PLKLNTRLDNQARIAKVEQTLKLVGLLPE-HRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFA 178
Cdd:cd03260 95 G----SIYDNvayGLRLHGIKLKEELDERVEEALRKAALWDEvKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 179 ALDPSVRSQTVNLLMELQRELGLgfIFISHNLGIVRHISDKILVMKQGKVVESGKTDVI 237
Cdd:cd03260 171 ALDPISTAKIEELIAELKKEYTI--VIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-229 |
1.98e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 147.51 E-value: 1.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLrfdnchGKRWqnKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHydNK 83
Cdd:COG3638 2 MLELRNL------SKRY--PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTA--LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 HRVL-----NIRMVFQNSNesLNPGIT---------LG--SILEEPLKLNTRLDnqarIAKVEQTLKLVGLLpeHRFFYR 147
Cdd:COG3638 72 GRALrrlrrRIGMIFQQFN--LVPRLSvltnvlagrLGrtSTWRSLLGLFPPED----RERALEALERVGLA--DKAYQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 148 -HMLSDGQRQRVALARAIILNPQVIVADEPFAALDPsVRSQTV-NLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQ 225
Cdd:COG3638 144 aDQLSGGQQQRVAIARALVQEPKLILADEPVASLDP-KTARQVmDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD 222
|
....
gi 495265151 226 GKVV 229
Cdd:COG3638 223 GRVV 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-228 |
3.32e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.03 E-value: 3.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRFDNCHGKRwqnkgskftLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYD-NK 83
Cdd:COG4619 1 LELEGLSFRVGGKPI---------LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPpPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 HRVLnIRMVFQNSneSLNPGiTLGSILEEPLKLNTRLDNQARIAKVeqtLKLVGLLPE--HRFFYRhmLSDGQRQRVALA 161
Cdd:COG4619 72 WRRQ-VAYVPQEP--ALWGG-TVRDNLPFPFQLRERKFDRERALEL---LERLGLPPDilDKPVER--LSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495265151 162 RAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKV 228
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
11-252 |
1.08e-41 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 145.71 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 11 RFDNCHgKRWQNKGSKFT-LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVL-- 87
Cdd:PRK11153 3 ELKNIS-KVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 88 -NIRMVFQN----SNESLNPGITLgsileePLKLNTRldNQARI-AKVEQTLKLVGLlPEHRFFYRHMLSDGQRQRVALA 161
Cdd:PRK11153 82 rQIGMIFQHfnllSSRTVFDNVAL------PLELAGT--PKAEIkARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 162 RAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWP 241
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
250
....*....|.
gi 495265151 242 KDEYTKKLVHA 252
Cdd:PRK11153 233 KHPLTREFIQS 243
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
23-256 |
2.95e-41 |
|
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: 141.67 E-value: 2.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 23 KGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQNSneSLNP 102
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQI--GLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 103 GITLGSILEEPLKLNtRLDNQARIAKVEQTLKLVGLLPEH-RFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALD 181
Cdd:cd03295 89 HMTVEENIALVPKLL-KWPKEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 182 PSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLVHAHQAL 256
Cdd:cd03295 168 PITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGADRLL 242
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-235 |
3.51e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 141.35 E-value: 3.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRfdnchgKRWqnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEhyDNKH 84
Cdd:COG1131 1 IEVRGLT------KRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA--RDPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 85 RVL-NIRMVFQNSNesLNPGITLGSILEEPLKLNtRLDNQARIAKVEQTLKLVGLLPEHRFFYRHmLSDGQRQRVALARA 163
Cdd:COG1131 70 EVRrRIGYVPQEPA--LYPDLTVRENLRFFARLY-GLPRKEARERIDELLELFGLTDAADRKVGT-LSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495265151 164 IILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTD 235
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-227 |
7.68e-41 |
|
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: 138.28 E-value: 7.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRFdnchgkRWQNKGsKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKH 84
Cdd:cd03228 1 IEFKNVSF------SYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 85 RVLNIRMVFQNsneslnPGITLGSILEeplklntrldNqariakveqtlklvgllpehrffyrhMLSDGQRQRVALARAI 164
Cdd:cd03228 74 LRKNIAYVPQD------PFLFSGTIRE----------N--------------------------ILSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 165 ILNPQVIVADEPFAALDPsvrsQTVNLLMELQRELGLG--FIFISHNLGIVRHiSDKILVMKQGK 227
Cdd:cd03228 112 LRDPPILILDEATSALDP----ETEALILEALRALAKGktVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
9-238 |
7.93e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 140.28 E-value: 7.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 9 NLRFDNChgkRWQNKGSKFTlgpINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRvlN 88
Cdd:COG3840 1 MLRLDDL---TYRYGDFPLR---FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER--P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 89 IRMVFQNSNesLNPGIT------LGsileepLKLNTRLDNQARiAKVEQTLKLVGL------LPEHrffyrhmLSDGQRQ 156
Cdd:COG3840 73 VSMLFQENN--LFPHLTvaqnigLG------LRPGLKLTAEQR-AQVEQALERVGLaglldrLPGQ-------LSGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 157 RVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDV 236
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
..
gi 495265151 237 IF 238
Cdd:COG3840 217 LL 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
29-178 |
9.83e-41 |
|
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: 137.39 E-value: 9.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQNSNesLNPGITLGS 108
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQ--LFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495265151 109 ILEEPLKL--NTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFA 178
Cdd:pfam00005 79 NLRLGLLLkgLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
24-228 |
1.09e-40 |
|
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: 139.20 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLehYDNKHRVLNIR----MVFQNSNes 99
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL--TDDKKNINELRqkvgMVFQQFN-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 100 LNPGIT-LGSILEEPLKLNTRLDNQARiAKVEQTLKLVGLLpEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFA 178
Cdd:cd03262 87 LFPHLTvLENITLAPIKVKGMSKAEAE-ERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495265151 179 ALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKV 228
Cdd:cd03262 165 ALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-238 |
2.34e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.45 E-value: 2.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENLRFDncHGKRWqnkgskfTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHY 80
Cdd:COG1121 3 MMPAIELENLTVS--YGGRP-------VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 81 DNKhrvlnIRMVFQNSneSLNPG--------ITLGSILEEPLklnTRLDNQARIAKVEQTLKLVGLLPehrffYRH---- 148
Cdd:COG1121 74 RRR-----IGYVPQRA--EVDWDfpitvrdvVLMGRYGRRGL---FRRPSRADREAVDEALERVGLED-----LADrpig 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 149 MLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGkV 228
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-L 216
|
250
....*....|
gi 495265151 229 VESGKTDVIF 238
Cdd:COG1121 217 VAHGPPEEVL 226
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-233 |
3.43e-40 |
|
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: 145.67 E-value: 3.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 10 LRFDNCHgkrWQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNI 89
Cdd:COG4988 337 IELEDVS---FSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 90 RMVFQNsneslnPGITLGSILEeplklNTRLDN-QARIAKVEQTLKLVGLlpeHRFFYR-------------HMLSDGQR 155
Cdd:COG4988 414 AWVPQN------PYLFAGTIRE-----NLRLGRpDASDEELEAALEAAGL---DEFVAAlpdgldtplgeggRGLSGGQA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 156 QRVALARAIILNPQVIVADEPFAALDPsvrsQTVNLLMELQRELGLG--FIFISHNLGIVRHiSDKILVMKQGKVVESGK 233
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDA----ETEAEILQALRRLAKGrtVILITHRLALLAQ-ADRILVLDDGRIVEQGT 554
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
32-245 |
3.99e-40 |
|
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: 138.63 E-value: 3.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRvlNIRMVFQNSneSLNPGITLGSILE 111
Cdd:cd03296 21 VSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER--NVGFVFQHY--ALFRHMTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 112 EPLKLNTRLD--NQARI-AKVEQTLKLVGLLP-EHRffYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQ 187
Cdd:cd03296 97 FGLRVKPRSErpPEAEIrAKVHELLKLVQLDWlADR--YPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 188 TVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEY 245
Cdd:cd03296 175 LRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
29-229 |
5.41e-40 |
|
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: 136.02 E-value: 5.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKH-RVLNIRMVFQnsneslnpgitlg 107
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 sileeplklntrldnqariakveqtlklvgllpehrffyrhmLSDGQRQRVALARAIILNPQVIVADEPFAALDPsvrSQ 187
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTP---AE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495265151 188 TVNLL--MELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVV 229
Cdd:cd03216 118 VERLFkvIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
32-233 |
6.69e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 137.49 E-value: 6.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKhRVLNIR----MVFQN----SNESLNPG 103
Cdd:COG2884 21 VSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRR-EIPYLRrrigVVFQDfrllPDRTVYEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 ITLgsileePLKLNTRLDNQARiAKVEQTLKLVGLLpEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPS 183
Cdd:COG2884 100 VAL------PLRVTGKSRKEIR-RRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495265151 184 VRSQTVNLLMELQReLGLGFIFISHNLGIVRHISDKILVMKQGKVVESGK 233
Cdd:COG2884 172 TSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-238 |
7.58e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 138.99 E-value: 7.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENLRFdnchgkRWQNKgSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLehy 80
Cdd:PRK13635 2 KEEIIRVEHISF------RYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 81 dNKHRVLNIR----MVFQNSNESLnpgitLGSILEEPLKLNtrLDNQA-----RIAKVEQTLKLVGLLPehrFFYR--HM 149
Cdd:PRK13635 72 -SEETVWDVRrqvgMVFQNPDNQF-----VGATVQDDVAFG--LENIGvpreeMVERVDQALRQVGMED---FLNRepHR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 150 LSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHiSDKILVMKQGKVV 229
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
....*....
gi 495265151 230 ESGKTDVIF 238
Cdd:PRK13635 220 EEGTPEEIF 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-237 |
8.46e-40 |
|
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: 138.07 E-value: 8.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLRFdnchgkrwqNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNK 83
Cdd:COG4555 1 MIEVENLSK---------KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 HRvLNIRMVFQNSNesLNPGITLGSILE--EPLKLNTRLDNQARIAKVEQTLKLVGLLpEHRFfyrHMLSDGQRQRVALA 161
Cdd:COG4555 72 AR-RQIGVLPDERG--LYDRLTVRENIRyfAELYGLFDEELKKRIEELIELLGLEEFL-DRRV---GELSTGMKKKVALA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495265151 162 RAIILNPQVIVADEPFAALDPSVRSQTVNLLMELqRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVI 237
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-250 |
9.32e-40 |
|
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: 137.85 E-value: 9.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRfdnchgKRWQNkgskFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKH 84
Cdd:cd03299 1 LKVENLS------KDWKE----FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 85 RvlNIRMVFQNsnESLNPGITLGSILEEPLKLntRLDNQARI-AKVEQTLKLVG---LLpeHRffYRHMLSDGQRQRVAL 160
Cdd:cd03299 71 R--DISYVPQN--YALFPHMTVYKNIAYGLKK--RKVDKKEIeRKVLEIAEMLGidhLL--NR--KPETLSGGEQQRVAI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 161 ARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHW 240
Cdd:cd03299 141 ARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
250
....*....|
gi 495265151 241 PKDEYTKKLV 250
Cdd:cd03299 221 PKNEFVAEFL 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
24-244 |
1.61e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 137.45 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSG--SIYLNERKLEHYDNKHRVLNIR----MVFQNSN 97
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlNIAGNHFDFSKTPSDKAIRELRrnvgMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 98 esLNPGIT-LGSILEEPLKLnTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHmLSDGQRQRVALARAIILNPQVIVADEP 176
Cdd:PRK11124 93 --LWPHLTvQQNLIEAPCRV-LGLSKDQALARAEKLLERLRLKPYADRFPLH-LSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 177 FAALDPSVRSQTVNLLMELQrELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDViFHWPKDE 244
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTE 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
24-227 |
3.15e-39 |
|
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: 133.91 E-value: 3.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQnsneslnpg 103
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 itlgsileeplklntrldnqariakveqtlklvgllpehrffyrhmLSDGQRQRVALARAIILNPQVIVADEPFAALDPS 183
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495265151 184 VRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGK 227
Cdd:cd00267 115 SRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-228 |
3.65e-39 |
|
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: 134.06 E-value: 3.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRfdnchgKRWqnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNErklehydnkh 84
Cdd:cd03230 1 IEVRNLS------KRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG---------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 85 rvlnirmvfqnsneslnpgitlGSILEEPlklntrldnqariakvEQTLKLVGLLPEHRFFYRHM-------LSDGQRQR 157
Cdd:cd03230 62 ----------------------KDIKKEP----------------EEVKRRIGYLPEEPSLYENLtvrenlkLSGGMKQR 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495265151 158 VALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKV 228
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
29-230 |
3.77e-39 |
|
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: 136.02 E-value: 3.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDN----KHRVLNIRMVFQnsNESLNPGI 104
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdaraRLRARHVGFVFQ--SFQLLPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 105 TlgsILEE---PLKLNTRLDNQARiAKVEqtLKLVGLlpEHRFfyRHM---LSDGQRQRVALARAIILNPQVIVADEPFA 178
Cdd:COG4181 106 T---ALENvmlPLELAGRRDARAR-ARAL--LERVGL--GHRL--DHYpaqLSGGEQQRVALARAFATEPAILFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495265151 179 ALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHiSDKILVMKQGKVVE 230
Cdd:COG4181 176 NLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
10-235 |
1.34e-38 |
|
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: 135.00 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 10 LRFDNChGKRWqnKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNE---RKLEHYDNKHRV 86
Cdd:cd03256 1 IEVENL-SKTY--PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdiNKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 87 LNIRMVFQNSN--------ESLNPGiTLG--SILEEPLKLNTRLDNQARIAKVEQtlklVGLLPehrFFYRHM--LSDGQ 154
Cdd:cd03256 78 RQIGMIFQQFNlierlsvlENVLSG-RLGrrSTWRSLFGLFPKEEKQRALAALER----VGLLD---KAYQRAdqLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 155 RQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKT 234
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPP 229
|
.
gi 495265151 235 D 235
Cdd:cd03256 230 A 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
24-244 |
2.17e-38 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 134.37 E-value: 2.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNErklEHYD-----NKHRVLNIR----MVFQ 94
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAG---HQFDfsqkpSEKAIRLLRqkvgMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 95 NSNesLNPGIT-LGSILEEPLKLnTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHmLSDGQRQRVALARAIILNPQVIVA 173
Cdd:COG4161 90 QYN--LWPHLTvMENLIEAPCKV-LGLSKEQAREKAMKLLARLRLTDKADRFPLH-LSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495265151 174 DEPFAALDPSVRSQTVNLLMELQrELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDvIFHWPKDE 244
Cdd:COG4161 166 DEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPQTE 234
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
44-245 |
2.48e-38 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 136.47 E-value: 2.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 44 IVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNirMVFQNSneSLNPGITLGSILEEPLKLNtRLDNQ 123
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHIN--MVFQSY--ALFPHMTVEENVAFGLKMR-KVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 124 ARIAKVEQTLKLVGLlPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGF 203
Cdd:TIGR01187 76 EIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495265151 204 IFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEY 245
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-249 |
5.17e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 134.44 E-value: 5.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENLRFdnCHGKRWQNKgSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNerKLEHY 80
Cdd:PRK13633 1 MNEMIKCKNVSY--KYESNEEST-EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVD--GLDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 81 DNKHrVLNIR----MVFQNSNESLnpgitLGSILEEPLKL---NTRLDNQARIAKVEQTLKLVGLLpEHRFFYRHMLSDG 153
Cdd:PRK13633 76 DEEN-LWDIRnkagMVFQNPDNQI-----VATIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGMY-EYRRHAPHLLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 154 QRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHiSDKILVMKQGKVVESGK 233
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGT 227
|
250
....*....|....*.
gi 495265151 234 TDVIFhwPKDEYTKKL 249
Cdd:PRK13633 228 PKEIF--KEVEMMKKI 241
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
32-228 |
1.75e-37 |
|
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: 131.12 E-value: 1.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKhrvlnIRMVFQNSNESLNPGIT----LG 107
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYVPQRRSIDRDFPISvrdvVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 SILEEPLKLNTRLdNQARIAKVEQTLKLVGL--LPEHRFfyrHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVR 185
Cdd:cd03235 93 MGLYGHKGLFRRL-SKADKAKVDEALERVGLseLADRQI---GELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495265151 186 SQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKV 228
Cdd:cd03235 169 EDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
24-250 |
2.62e-37 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 135.07 E-value: 2.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNirMVFQNSneSLNPG 103
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVN--TVFQSY--ALFPH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 ITLGSILEEPLKLNTRldNQARIAK-VEQTLKLVGLlpEHrFFYR--HMLSDGQRQRVALARAIILNPQVIVADEPFAAL 180
Cdd:PRK09452 101 MTVFENVAFGLRMQKT--PAAEITPrVMEALRMVQL--EE-FAQRkpHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 181 DPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLV 250
Cdd:PRK09452 176 DYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFI 245
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
32-237 |
3.80e-37 |
|
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: 131.02 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNkHRV--LNIRMVFQNSN--ESL----NPG 103
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP-HEIarLGIGRTFQIPRlfPELtvleNVM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 ITLGSILEEPLKLNTRLDNQARI-AKVEQTLKLVGLLPehrffYRHM----LSDGQRQRVALARAIILNPQVIVADEPFA 178
Cdd:cd03219 98 VAAQARTGSGLLLARARREEREArERAEELLERVGLAD-----LADRpageLSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 179 ALDPSVRSQTVNLLMELqRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVI 237
Cdd:cd03219 173 GLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-238 |
5.14e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 131.41 E-value: 5.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 27 FTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQNSNESLnpgitL 106
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQF-----V 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 GSILEEPLKLNtrLDNQA-----RIAKVEQTLKLVGLLpEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALD 181
Cdd:PRK13648 98 GSIVKYDVAFG--LENHAvpydeMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495265151 182 PSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHiSDKILVMKQGKVVESGKTDVIF 238
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
32-232 |
6.00e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 137.22 E-value: 6.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDnkHRVL--NIRMVFQNSneslnpgiTL--G 107
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT--LESLrrQIGVVPQDT--------FLfsG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 SILEeplklNTRL-DNQARIAKVEQTLKLVGLlpeHRFFYR-------------HMLSDGQRQRVALARAIILNPQVIVA 173
Cdd:COG1132 429 TIRE-----NIRYgRPDATDEEVEEAAKAAQA---HEFIEAlpdgydtvvgergVNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495265151 174 DEPFAALDPsvRSQtvnllMELQREL-----GLGFIFISHNLGIVRHiSDKILVMKQGKVVESG 232
Cdd:COG1132 501 DEATSALDT--ETE-----ALIQEALerlmkGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
32-250 |
7.49e-37 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 134.08 E-value: 7.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKhRVLNIR-----MVFQNsneslnpgitL 106
Cdd:COG4175 46 ASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKK-ELRELRrkkmsMVFQH----------F 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 G-----SILEE---PLKLNtRLDNQARIAKVEQTLKLVGLLP-EHRffYRHMLSDGQRQRVALARAIILNPQVIVADEPF 177
Cdd:COG4175 115 AllphrTVLENvafGLEIQ-GVPKAERRERAREALELVGLAGwEDS--YPDELSGGMQQRVGLARALATDPDILLMDEAF 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495265151 178 AALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLV 250
Cdd:COG4175 192 SALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFV 264
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
32-256 |
1.32e-36 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 130.20 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSL-----LAKLLVGLEQPdSGSIYLNERKLEHYDNKHRvlNIRMVFQNSNESLNPGITL 106
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLtcaaaLGILPAGVRQT-AGRVLLDGKPVAPCALRGR--KIATIMQNPRSAFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 GSILEEPLKLNTRLDNQARIAkveQTLKLVGLLPEHRFFYRH--MLSDGQRQRVALARAIILNPQVIVADEPFAALDPSV 184
Cdd:PRK10418 99 HTHARETCLALGKPADDATLT---AALEAVGLENAARVLKLYpfEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495265151 185 RSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLVHAHQAL 256
Cdd:PRK10418 176 QARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAHLAL 247
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-233 |
2.72e-36 |
|
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: 135.28 E-value: 2.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRFdnchgkRWQNkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKH 84
Cdd:COG4987 334 LELEDVSF------RYPG-AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 85 RVLNIRMVFQNsneslnPGITLGSILEeplklNTRL-DNQARIAKVEQTLKLVGLLPehrfFYRHM-------------- 149
Cdd:COG4987 407 LRRRIAVVPQR------PHLFDTTLRE-----NLRLaRPDATDEELWAALERVGLGD----WLAALpdgldtwlgeggrr 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 150 LSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLgfIFISHNLGIVRHIsDKILVMKQGKVV 229
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLERM-DRILVLEDGRIV 548
|
....
gi 495265151 230 ESGK 233
Cdd:COG4987 549 EQGT 552
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
31-232 |
6.49e-36 |
|
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: 127.22 E-value: 6.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 31 PINFSIQ--AGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRvlNIRMVFQNSNE----SLNPGI 104
Cdd:cd03298 14 PMHFDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR--PVSMLFQENNLfahlTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 105 TLGsiLEEPLKLNTrlDNQARIAKVEQTLKLVGL---LPEHrffyrhmLSDGQRQRVALARAIILNPQVIVADEPFAALD 181
Cdd:cd03298 92 GLG--LSPGLKLTA--EDRQAIEVALARVGLAGLekrLPGE-------LSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495265151 182 PSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:cd03298 161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-250 |
7.07e-36 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 128.12 E-value: 7.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENLrfdnchGKRWqnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIylnerkleHY 80
Cdd:PRK11701 3 DQPLLSVRGL------TKLY---GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV--------HY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 81 DNKHRVL---------NIRM--------VFQNSNESLNPGITLGSILEEPLKL-------NTRLDNQARIAKVEQTLKLV 136
Cdd:PRK11701 66 RMRDGQLrdlyalseaERRRllrtewgfVHQHPRDGLRMQVSAGGNIGERLMAvgarhygDIRATAGDWLERVEIDAARI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 137 GLLPehRFFyrhmlSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHI 216
Cdd:PRK11701 146 DDLP--TTF-----SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLL 218
|
250 260 270
....*....|....*....|....*....|....
gi 495265151 217 SDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLV 250
Cdd:PRK11701 219 AHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLLV 252
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-234 |
7.20e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 128.70 E-value: 7.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENLRFdnchgkRWQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHy 80
Cdd:PRK13650 1 MSNIIEVKNLTF------KYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 81 DNkhrVLNIR----MVFQNSNESLnpgitLGSILEEPLKL---NTRLDNQARIAKVEQTLKLVGLLpehRFFYRH--MLS 151
Cdd:PRK13650 74 EN---VWDIRhkigMVFQNPDNQF-----VGATVEDDVAFgleNKGIPHEEMKERVNEALELVGMQ---DFKEREpaRLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 152 DGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRhISDKILVMKQGKvVES 231
Cdd:PRK13650 143 GGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQ-VES 220
|
...
gi 495265151 232 GKT 234
Cdd:PRK13650 221 TST 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
28-232 |
7.44e-36 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 127.34 E-value: 7.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 28 TLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQnsneslNPGITLG 107
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQ------DTFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 SILEeplklNTRL-DNQARIAKVEQTLKLVGLlpeHRFFYR-------------HMLSDGQRQRVALARAIILNPQVIVA 173
Cdd:cd03254 92 TIME-----NIRLgRPNATDEEVIEAAKEAGA---HDFIMKlpngydtvlgengGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 174 DEPFAALDPSVRSQTVNLLMELQRelGLGFIFISHNLGIVRHiSDKILVMKQGKVVESG 232
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
39-232 |
1.28e-35 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 126.26 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 39 GETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNK-----HRvLNIRMVFQNSneSLNPGITLGSILEEP 113
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinlppQQ-RKIGLVFQQY--ALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 114 LKLNTRLDNQARIAKVEQTLKLVGLLpehrFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLM 193
Cdd:cd03297 100 LKRKRNREDRISVDELLDLLGLDHLL----NRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 495265151 194 ELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:cd03297 176 QIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-230 |
2.44e-35 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 125.93 E-value: 2.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLrfdnchGKRWQNKGSKF-TLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHY-D 81
Cdd:TIGR02211 1 LLKCENL------GKRYQEGKLDTrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLsS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 82 NKHRVL-NIRMVFQNSNESLNPGITlgsILEE---PLkLNTRLDNQARIAKVEQTLKLVGLlpEHRFFYR-HMLSDGQRQ 156
Cdd:TIGR02211 75 NERAKLrNKKLGFIYQFHHLLPDFT---ALENvamPL-LIGKKSVKEAKERAYEMLEKVGL--EHRINHRpSELSGGERQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495265151 157 RVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHIsDKILVMKQGKVVE 230
Cdd:TIGR02211 149 RVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
32-237 |
2.80e-35 |
|
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: 126.69 E-value: 2.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNkHRVLNIRMV--FQNSNesLNPGITL--- 106
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIArtFQNPR--LFPELTVlen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 ----------GSILEEPLKLNTRLDNQARI-AKVEQTLKLVGLLPehrffYRHM----LSDGQRQRVALARAIILNPQVI 171
Cdd:COG0411 100 vlvaaharlgRGLLAALLRLPRARREEREArERAEELLERVGLAD-----RADEpagnLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495265151 172 VADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVI 237
Cdd:COG0411 175 LLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
32-252 |
9.94e-35 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 126.94 E-value: 9.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLeQPDSGSI-----YLNERKLEHYDNKHR--VL--NIRMVFQNSNESLNP 102
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVtadrfRWNGIDLLKLSPRERrkIIgrEIAMIFQEPSSCLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 103 GITLGSILEEPLkLNTRLDN------QARIAKVEQTLKLVGLlPEHRFF---YRHMLSDGQRQRVALARAIILNPQVIVA 173
Cdd:COG4170 105 SAKIGDQLIEAI-PSWTFKGkwwqrfKWRKKRAIELLHRVGI-KDHKDImnsYPHELTEGECQKVMIAMAIANQPRLLIA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 174 DEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLVHA 252
Cdd:COG4170 183 DEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKALLRS 261
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
32-248 |
6.74e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 122.94 E-value: 6.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNE------RKLEHYDNKHRVL--NIRMVFQNSNesLNPG 103
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtaRSLSQQKGLIRQLrqHVGFVFQNFN--LFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 IT-LGSILEEPLKLNTRLDNQArIAKVEQTLKLVGLLPEHRFFYRHmLSDGQRQRVALARAIILNPQVIVADEPFAALDP 182
Cdd:PRK11264 100 RTvLENIIEGPVIVKGEPKEEA-TARARELLAKVGLAGKETSYPRR-LSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495265151 183 SVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKK 248
Cdd:PRK11264 178 ELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-239 |
7.16e-34 |
|
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: 125.21 E-value: 7.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 27 FTLGpINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVL----NIRMVFQNSneSLNP 102
Cdd:COG4148 14 FTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPphrrRIGYVFQEA--RLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 103 GITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLpeHRffYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDP 182
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLL--DR--RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495265151 183 SVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFH 239
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
32-235 |
1.52e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.67 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKH-RVLNIRMVFQNSNesLNPGIT----- 105
Cdd:COG1129 23 VSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELN--LVPNLSvaeni 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 106 -LGsilEEPLKLNtRLDNQARIAKVEQTLKLVGL-LPEHRffyrhMLSD---GQRQRVALARAIILNPQVIVADEPFAAL 180
Cdd:COG1129 101 fLG---REPRRGG-LIDWRAMRRRARELLARLGLdIDPDT-----PVGDlsvAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 181 DPSvrsqTVNLLMELQREL---GLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTD 235
Cdd:COG1129 172 TER----EVERLFRIIRRLkaqGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVA 225
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-234 |
3.51e-33 |
|
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: 120.87 E-value: 3.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLrfdnchGKRWQNkgSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKL----EH 79
Cdd:TIGR02315 1 MLEVENL------SKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 80 YDNKHRVlNIRMVFQNSNEslnpgITLGSILEEplKLNTRLDNQ------------ARIAKVEQTLKLVGLLpEHRFFYR 147
Cdd:TIGR02315 73 KLRKLRR-RIGMIFQHYNL-----IERLTVLEN--VLHGRLGYKptwrsllgrfseEDKERALSALERVGLA-DKAYQRA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 148 HMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGK 227
Cdd:TIGR02315 144 DQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGE 223
|
....*..
gi 495265151 228 VVESGKT 234
Cdd:TIGR02315 224 IVFDGAP 230
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
29-208 |
3.51e-33 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 121.12 E-value: 3.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVlnirmVFQNsnESLNPGITLGS 108
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGV-----VFQK--DALLPWLNVLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ILEEPLKLNtRLDNQARIAKVEQTLKLVGLLP-EHRFFYRhmLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQ 187
Cdd:COG4525 96 NVAFGLRLR-GVPKAERRARAEELLALVGLADfARRRIWQ--LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQ 172
|
170 180
....*....|....*....|.
gi 495265151 188 TVNLLMELQRELGLGFIFISH 208
Cdd:COG4525 173 MQELLLDVWQRTGKGVFLITH 193
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
33-235 |
5.09e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 120.07 E-value: 5.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 33 NFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNerklehyDNKHRVLN-----IRMVFQNSNesLNPGITLG 107
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLN-------GQDHTTTPpsrrpVSMLFQENN--LFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 SILEEPLKLNTRLDNQARiAKVEQTLKLVGLlpeHRFFYR--HMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVR 185
Cdd:PRK10771 90 QNIGLGLNPGLKLNAAQR-EKLHAIARQMGI---EDLLARlpGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495265151 186 SQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTD 235
Cdd:PRK10771 166 QEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTD 215
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-235 |
1.05e-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: 122.14 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 27 FTLgPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLehYDNKHRVL------NIRMVFQNSneSL 100
Cdd:TIGR02142 12 FSL-DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL--FDSRKGIFlppekrRIGYVFQEA--RL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 101 NPGITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEhrffYRHMLSDGQRQRVALARAIILNPQVIVADEPFAAL 180
Cdd:TIGR02142 87 FPHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGR----LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 181 DPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTD 235
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIA 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-238 |
1.16e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 120.54 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 22 NKGSKF---TLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNErkLEHYDNKHRVLNIR----MVFQ 94
Cdd:PRK13637 13 MEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDITDKKVKLSDIRkkvgLVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 95 NSN-----ESLNPGITLGsileePLKLNtrLDNQARIAKVEQTLKLVGLLPEHrffYRHM----LSDGQRQRVALARAII 165
Cdd:PRK13637 91 YPEyqlfeETIEKDIAFG-----PINLG--LSEEEIENRVKRAMNIVGLDYED---YKDKspfeLSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495265151 166 LNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIF 238
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
32-235 |
1.32e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 124.37 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKH-RVLNIRMVFQNSN--ESL----NpgI 104
Cdd:COG3845 24 VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGMVHQHFMlvPNLtvaeN--I 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 105 TLGSileEPLKLnTRLDNQARIAKVEQTLKLVGL-LPEHRffYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPs 183
Cdd:COG3845 102 VLGL---EPTKG-GRLDRKAARARIRELSERYGLdVDPDA--KVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTP- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 184 vrsQTVNLLMELQREL---GLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTD 235
Cdd:COG3845 175 ---QEADELFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
10-233 |
1.90e-32 |
|
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: 118.87 E-value: 1.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 10 LRFDNCHgkrWQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNI 89
Cdd:cd03253 1 IEFENVT---FAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 90 RMVFQNS---NESLNPGITLGsileeplKLNTRLDNQARIAKVEQTLKLVGLLPEHrffYRH-------MLSDGQRQRVA 159
Cdd:cd03253 78 GVVPQDTvlfNDTIGYNIRYG-------RPDATDEEVIEAAKAAQIHDKIMRFPDG---YDTivgerglKLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495265151 160 LARAIILNPQVIVADEPFAALDpsvrSQTVNLLMELQRELGLG--FIFISHNLGIVRHiSDKILVMKQGKVVESGK 233
Cdd:cd03253 148 IARAILKNPPILLLDEATSALD----THTEREIQAALRDVSKGrtTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
24-255 |
1.95e-32 |
|
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: 124.48 E-value: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNkhrvlnirmvfqnsnESLNP- 102
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR---------------EELGRh 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 103 ------GITL--GSILEeplklN-TRLDnQARIAKVEQTLKLVGL------LPEHrffYR-------HMLSDGQRQRVAL 160
Cdd:COG4618 408 igylpqDVELfdGTIAE-----NiARFG-DADPEKVVAAAKLAGVhemilrLPDG---YDtrigeggARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 161 ARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELqRELGLGFIFISHNLGIVRHiSDKILVMKQGKVVESGktdvifhw 240
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFG-------- 548
|
250
....*....|....*
gi 495265151 241 PKDEYTKKLVHAHQA 255
Cdd:COG4618 549 PRDEVLARLARPAAA 563
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
32-238 |
4.20e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.03 E-value: 4.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEhYDNKhRVLNIR----MVFQNSNESLNPGITLG 107
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKK-SLLEVRktvgIVFQNPDDQLFAPTVEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 SILEEPLKLNTRLDNQARiaKVEQTLKLVGLL------PEHrffyrhmLSDGQRQRVALARAIILNPQVIVADEPFAALD 181
Cdd:PRK13639 99 DVAFGPLNLGLSKEEVEK--RVKEALKAVGMEgfenkpPHH-------LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495265151 182 PSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIF 238
Cdd:PRK13639 170 PMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-208 |
6.52e-32 |
|
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: 116.42 E-value: 6.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLRFDncHGKRWqnkgskfTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNK 83
Cdd:COG4133 2 MLEAENLSCR--RGERL-------LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 HRvLNIRMVFQNSneSLNPGITlgsiLEEPLKLNTRLDN-QARIAKVEQTLKLVGLLP-EHRFFyrHMLSDGQRQRVALA 161
Cdd:COG4133 73 YR-RRLAYLGHAD--GLKPELT----VRENLRFWAALYGlRADREAIDEALEAVGLAGlADLPV--RQLSAGQKRRVALA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495265151 162 RAIILNPQVIVADEPFAALDPsvrsQTVNLLMEL---QRELGLGFIFISH 208
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDA----AGVALLAELiaaHLARGGAVLLTTH 189
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
24-245 |
6.93e-32 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 119.82 E-value: 6.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRvlNIRMVFQNSneSLNPG 103
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR--DICMVFQSY--ALFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 ITLGSILEEPLKLNTRlDNQARIAKVEQTLKLVGLLP-EHRffYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDP 182
Cdd:PRK11432 93 MSLGENVGYGLKMLGV-PKEERKQRVKEALELVDLAGfEDR--YVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495265151 183 SVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEY 245
Cdd:PRK11432 170 NLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
29-238 |
7.52e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 118.41 E-value: 7.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHydNKHRVLNIR----MVFQNSNESLNPGI 104
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDY--SRKGLMKLResvgMVFQDPDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 105 TLGSILEEPLKLNTRLDNQARiaKVEQTLKLVGLLP-EHRffYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPS 183
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRK--RVDNALKRTGIEHlKDK--PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 184 VRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIF 238
Cdd:PRK13636 176 GVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-238 |
8.10e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.17 E-value: 8.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 6 SVENLRFDnchgkrwQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLehydNKHR 85
Cdd:PRK13632 9 KVENVSFS-------YPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI----SKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 86 VLNIR----MVFQNSNESLnpgitLGSILEEPLKL---NTRLDNQARIAKVEQTLKLVGLLpEHRFFYRHMLSDGQRQRV 158
Cdd:PRK13632 78 LKEIRkkigIIFQNPDNQF-----IGATVEDDIAFgleNKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 159 ALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRhISDKILVMKQGKVVESGKTDVIF 238
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEIL 230
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
29-223 |
2.35e-31 |
|
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: 121.24 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQNsneslnPGITLGS 108
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQH------PFLFAGT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ILEeplklNTRL-DNQARIAKVEQTLKLVGL------LPE--HRFFYRH--MLSDGQRQRVALARAIILNPQVIVADEPF 177
Cdd:TIGR02857 412 IAE-----NIRLaRPDASDAEIREALERAGLdefvaaLPQglDTPIGEGgaGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495265151 178 AALDPsvrsQTVNLLMELQRELGLG--FIFISHNLGiVRHISDKILVM 223
Cdd:TIGR02857 487 AHLDA----ETEAEVLEALRALAQGrtVLLVTHRLA-LAALADRIVVL 529
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
32-243 |
4.50e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.66 E-value: 4.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLE-HYDNKH-RVL--NIRMVFQNSNESLNPGITLG 107
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKlKPLrkKVGIVFQFPEHQLFEETVEK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 SILEEPLKLNTRLDNQARIAKveQTLKLVGLLPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQ 187
Cdd:PRK13634 106 DICFGPMNFGVSEEDAKQKAR--EMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495265151 188 TVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKD 243
Cdd:PRK13634 184 MMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
20-212 |
9.02e-31 |
|
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: 113.48 E-value: 9.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 20 WQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIR----MVFQN 95
Cdd:TIGR03608 5 SKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRReklgYLFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 96 ----SNESLNPGITLGSILEeplKLNTRLDNQariaKVEQTLKLVGL-LPEHRFFYRhmLSDGQRQRVALARAIILNPQV 170
Cdd:TIGR03608 85 faliENETVEENLDLGLKYK---KLSKKEKRE----KKKEALEKVGLnLKLKQKIYE--LSGGEQQRVALARAILKPPPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495265151 171 IVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGI 212
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEV 196
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-242 |
1.12e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 114.68 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 2 NDLLSVENLRfdnchgKRWqnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNER------ 75
Cdd:PRK10619 3 ENKLNVIDLH------KRY---GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 76 ----KLEHYDNKH-RVLNIR--MVFQNSNesLNPGIT-LGSILEEPLKLNTRLDNQARiAKVEQTLKLVGLLPEHRFFYR 147
Cdd:PRK10619 74 dkdgQLKVADKNQlRLLRTRltMVFQHFN--LWSHMTvLENVMEAPIQVLGLSKQEAR-ERAVKYLAKVGIDERAQGKYP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 148 HMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGK 227
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGK 229
|
250
....*....|....*
gi 495265151 228 VVESGKTDVIFHWPK 242
Cdd:PRK10619 230 IEEEGAPEQLFGNPQ 244
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
32-232 |
1.96e-30 |
|
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: 112.98 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNerklEHYDNKHRVL---NIRMVFQNSneSLNPGITlgs 108
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN----GYSIRTDRKAarqSLGYCPQFD--ALFDELT--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 iLEEPLKLNTRL---DNQARIAKVEQTLKLVGLLPehrffYRH----MLSDGQRQRVALARAIILNPQVIVADEPFAALD 181
Cdd:cd03263 92 -VREHLRFYARLkglPKSEIKEEVELLLRVLGLTD-----KANkrarTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495265151 182 PSVRSQTVNLLMELQRelGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:cd03263 166 PASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-232 |
2.76e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 113.67 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLRFdnchgkrwqNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDN- 82
Cdd:COG4559 1 MLEAENLSV---------RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPw 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 83 ---KHR-VLNirmvfQNSneSLNPGIT------LGSIleePLKLNTRLDNQAriakVEQTLKLVGLLP-EHRFFyrHMLS 151
Cdd:COG4559 72 elaRRRaVLP-----QHS--SLAFPFTveevvaLGRA---PHGSSAAQDRQI----VREALALVGLAHlAGRSY--QTLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 152 DGQRQRVALARAI--ILNPQVIVA-----DEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMK 224
Cdd:COG4559 136 GGEQQRVQLARVLaqLWEPVDGGPrwlflDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLH 214
|
....*...
gi 495265151 225 QGKVVESG 232
Cdd:COG4559 215 QGRLVAQG 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-241 |
3.20e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.13 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 13 DNCHgkrwQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMV 92
Cdd:PRK13652 8 DLCY----SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 93 FQNSNESLNPGITLGSILEEPLKLNtrLDNQARIAKVEQTLKLVGLlPEHRFFYRHMLSDGQRQRVALARAIILNPQVIV 172
Cdd:PRK13652 84 FQNPDDQIFSPTVEQDIAFGPINLG--LDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 173 ADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWP 241
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-244 |
3.31e-30 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 113.36 E-value: 3.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRfdnchgKRWqnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKH 84
Cdd:COG4598 9 LEVRDLH------KSF---GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 85 ---------RVLNIR----MVFQNSNesLNPGIT-LGSILEEPLKLNTRLDNQArIAKVEQTLKLVGLlPEHRFFYRHML 150
Cdd:COG4598 80 gelvpadrrQLQRIRtrlgMVFQSFN--LWSHMTvLENVIEAPVHVLGRPKAEA-IERAEALLAKVGL-ADKRDAYPAHL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 151 SDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVE 230
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEE 234
|
250
....*....|....
gi 495265151 231 SGKTDVIFHWPKDE 244
Cdd:COG4598 235 QGPPAEVFGNPKSE 248
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
22-241 |
5.77e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 114.80 E-value: 5.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 22 NKGSKF-----TLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRvlNIRMVFQNS 96
Cdd:PRK10851 6 ANIKKSfgrtqVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR--KVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 97 N--------ESLNPGITLgsileepLKLNTRLDNQARIAKVEQTLKLVGLlpEH---RffYRHMLSDGQRQRVALARAII 165
Cdd:PRK10851 84 AlfrhmtvfDNIAFGLTV-------LPRRERPNAAAIKAKVTQLLEMVQL--AHladR--YPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495265151 166 LNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWP 241
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
24-237 |
1.62e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.40 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDN----KHR-VLNirmvfQNSne 98
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPaelaRRRaVLP-----QHS-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 99 slnpgiTLG---SILE------EPLKLNTRLDNQAriakVEQTLKLVGLLP-EHRFFyrHMLSDGQRQRVALARAiiL-- 166
Cdd:PRK13548 86 ------SLSfpfTVEEvvamgrAPHGLSRAEDDAL----VAAALAQVDLAHlAGRDY--PQLSGGEQQRVQLARV--Laq 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 167 ------NPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGK-TDVI 237
Cdd:PRK13548 152 lwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTpAEVL 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
32-250 |
2.84e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.39 E-value: 2.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNirMVFQNSneSLNPGITLGSILE 111
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPIN--MMFQSY--ALFPHMTVEQNIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 112 EPLKLNtRLDNQARIAKVEQTLKLVGLlpeHRFFYR--HMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTV 189
Cdd:PRK11607 114 FGLKQD-KLPKAEIASRVNEMLGLVHM---QEFAKRkpHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQ 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495265151 190 NLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLV 250
Cdd:PRK11607 190 LEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
32-235 |
3.03e-29 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 109.83 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRV-LNIRMVFQNSNesLNPGITLgsil 110
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERArAGIGYVPEGRR--IFPELTV---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 111 EEPLKL----NTRLDNQARIAKVeqtlklVGLLPEHRFFYRHM---LSDGQRQRVALARAIILNPQVIVADEPFAALDPS 183
Cdd:cd03224 93 EENLLLgayaRRRAKRKARLERV------YELFPRLKERRKQLagtLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495265151 184 VRSQTVNLLMELqRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTD 235
Cdd:cd03224 167 IVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
23-229 |
7.84e-29 |
|
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: 108.50 E-value: 7.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 23 KGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEhydNKHRVLNIRMVFQNSNESLnp 102
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQDVDYQL-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 103 giTLGSILEEpLKLNTRL--DNQARIAKVEQTLKLVGLLPEHRffyrHMLSDGQRQRVALARAIILNPQVIVADEPFAAL 180
Cdd:cd03226 85 --FTDSVREE-LLLGLKEldAGNEQAETVLKDLDLYALKERHP----LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495265151 181 DPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVV 229
Cdd:cd03226 158 DYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-243 |
1.16e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.80 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENLRFdnchgkRWQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHY 80
Cdd:PRK13642 1 MNKILEVENLVF------KYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 81 DNKHRVLNIRMVFQNSNESLnpgitLGSILEEPLKL---NTRLDNQARIAKVEQTLKLVGLLpEHRFFYRHMLSDGQRQR 157
Cdd:PRK13642 75 NVWNLRRKIGMVFQNPDNQF-----VGATVEDDVAFgmeNQGIPREEMIKRVDEALLAVNML-DFKTREPARLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 158 VALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHiSDKILVMKQGKVVESGKTDVI 237
Cdd:PRK13642 149 VAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
....*.
gi 495265151 238 FHWPKD 243
Cdd:PRK13642 228 FATSED 233
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
32-232 |
1.17e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.03 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEhyDNKHRVLNIR----MVFQNSNesLNPGIT-L 106
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN--DPKVDERLIRqeagMVFQQFY--LFPHLTaL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 GSILEEPLKLNTRLDNQARiAKVEQTLKLVGLlPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRS 186
Cdd:PRK09493 96 ENVMFGPLRVRGASKEEAE-KQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRH 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495265151 187 QTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:PRK09493 174 EVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
28-232 |
1.32e-28 |
|
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: 108.06 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 28 TLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDnkHRVL--NIRMVFQNS---NESLNP 102
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD--PADLrrNIGYVPQDVtlfYGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 103 GITLGSileePLKLNTRLDNQARIAKVEQtlkLVGLLP--------EHRFFyrhmLSDGQRQRVALARAIILNPQVIVAD 174
Cdd:cd03245 97 NITLGA----PLADDERILRAAELAGVTD---FVNKHPngldlqigERGRG----LSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 175 EPFAALDPSVRSQTVNLLMELQRELGLgfIFISHNLGIVRhISDKILVMKQGKVVESG 232
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGDKTL--IIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-228 |
1.37e-28 |
|
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: 106.92 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRFDNCHGKRWQNKGskftlgpINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKH 84
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRN-------VSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 85 RVLNIRMVFQNsneslnpgITL--GSILEeplklntrldnqariakveqtlklvgllpehrffyrHMLSDGQRQRVALAR 162
Cdd:cd03246 74 LGDHVGYLPQD--------DELfsGSIAE------------------------------------NILSGGQRQRLGLAR 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495265151 163 AIILNPQVIVADEPFAALDPSvRSQTVNLLMELQRELGLGFIFISHNLGIVRhISDKILVMKQGKV 228
Cdd:cd03246 110 ALYGNPRILVLDEPNSHLDVE-GERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-250 |
1.89e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.59 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENLRFdnchgkrWQnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGL--EQPD---SGSIYLNER 75
Cdd:COG1117 8 LEPKIEVRNLNV-------YY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 76 KLehYDNKHRVLNIR----MVFQNSNesLNPGitlgSILEE---PLKLNTRLDNQARIAKVEQTLKLVGLLPE--HRFfy 146
Cdd:COG1117 79 DI--YDPDVDVVELRrrvgMVFQKPN--PFPK----SIYDNvayGLRLHGIKSKSELDEIVEESLRKAALWDEvkDRL-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 147 rHM----LSDGQRQRVALARAIILNPQVIVADEPFAALDPsVRSQTV-NLLMELQRELGLgfIFISHNLGIVRHISDKIL 221
Cdd:COG1117 149 -KKsalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDP-ISTAKIeELILELKKDYTI--VIVTHNMQQAARVSDYTA 224
|
250 260
....*....|....*....|....*....
gi 495265151 222 VMKQGKVVESGKTDVIFHWPKDEYTKKLV 250
Cdd:COG1117 225 FFYLGELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
32-227 |
2.29e-28 |
|
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: 107.33 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVL---NIRMVFQNSNesLNPGITLGS 108
Cdd:TIGR02673 21 VSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLlrrRIGVVFQDFR--LLPDRTVYE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ILEEPLKLNTRLDNQARIaKVEQTLKLVGLLPEHRFFyRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQT 188
Cdd:TIGR02673 99 NVALPLEVRGKKEREIQR-RVGAALRQVGLEHKADAF-PEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERI 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 495265151 189 VNLLMELQReLGLGFIFISHNLGIVRHISDKILVMKQGK 227
Cdd:TIGR02673 177 LDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
33-234 |
4.05e-28 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 106.87 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 33 NFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRvlNIRMVFQNSNesLNPGIT----LGS 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQR--PVSMLFQENN--LFAHLTvrqnIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ILEEPLKLNTrLDNQariaKVEQTLKLVGL------LPEHrffyrhmLSDGQRQRVALARAIILNPQVIVADEPFAALDP 182
Cdd:TIGR01277 94 GLHPGLKLNA-EQQE----KVVDAAQQVGIadyldrLPEQ-------LSGGQRQRVALARCLVRPNPILLLDEPFSALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495265151 183 SVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKT 234
Cdd:TIGR01277 162 LLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
32-209 |
7.85e-28 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 105.20 E-value: 7.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEhYDNK----HRVlNIRMVFQNSNESLNPGITLG 107
Cdd:TIGR01166 11 LNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLD-YSRKglleRRQ-RVGLVFQDPDDQLFAADVDQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 SILEEPLKLNTRlDNQARiAKVEQTLKLVGLLP-EHRFFyrHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRS 186
Cdd:TIGR01166 89 DVAFGPLNLGLS-EAEVE-RRVREALTAVGASGlRERPT--HCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGRE 164
|
170 180
....*....|....*....|...
gi 495265151 187 QTVNLLMELqRELGLGFIFISHN 209
Cdd:TIGR01166 165 QMLAILRRL-RAEGMTVVISTHD 186
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
32-235 |
1.01e-27 |
|
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: 106.42 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQNS---NESLNPGITLGs 108
Cdd:cd03252 21 ISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENvlfNRSIRDNIALA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ileeplklntrlDNQARIAKVEQTLKLVGllpEHRFF------YRHM-------LSDGQRQRVALARAIILNPQVIVADE 175
Cdd:cd03252 100 ------------DPGMSMERVIEAAKLAG---AHDFIselpegYDTIvgeqgagLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495265151 176 PFAALDpsvrSQTVNLLMELQREL--GLGFIFISHNLGIVRHiSDKILVMKQGKVVESGKTD 235
Cdd:cd03252 165 ATSALD----YESEHAIMRNMHDIcaGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHD 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
32-243 |
1.11e-27 |
|
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: 106.01 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVlnirmVFQNSneSLNPGITL-GSIL 110
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV-----VFQNY--SLLPWLTVrENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 111 EEPLKLNTRLDNQARIAKVEQTLKLVGLlPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVN 190
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495265151 191 LLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKT-DVIFHWPKD 243
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQIlEVPFPRPRD 209
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
28-249 |
1.59e-27 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 110.73 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 28 TLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYL---NERKLEHYDNKHrvlNIRMVFQNsneslnPGI 104
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLdgvDIRQIDPADLRR---NIGYVPQD------PRL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 105 TLGSiLEEPLKLNTRLDNQARIAKVeqtLKLVGLlpeHRFFYRH-------------MLSDGQRQRVALARAIILNPQVI 171
Cdd:TIGR03375 551 FYGT-LRDNIALGAPYADDEEILRA---AELAGV---TEFVRRHpdgldmqigergrSLSGGQRQAVALARALLRDPPIL 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 172 VADEPFAALDPSVRSQtvnLLMELQREL-GLGFIFISHNLGIVRhISDKILVMKQGKVVESGktdvifhwPKDEYTKKL 249
Cdd:TIGR03375 624 LLDEPTSAMDNRSEER---FKDRLKRWLaGKTLVLVTHRTSLLD-LVDRIIVMDNGRIVADG--------PKDQVLEAL 690
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
29-235 |
2.10e-27 |
|
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: 105.31 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQnsneslNPGITLGS 108
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQ------EPVLFDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ILEeplklNTRL-DNQARIAKVEQTLKLVGLlpeHRFF------YRHM-------LSDGQRQRVALARAIILNPQVIVAD 174
Cdd:cd03249 93 IAE-----NIRYgKPDATDEEVEEAAKKANI---HDFImslpdgYDTLvgergsqLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495265151 175 EPFAALDPSVRSQ---TVNLLMElqrelGLGFIFISHNLGIVRHiSDKILVMKQGKVVESGKTD 235
Cdd:cd03249 165 EATSALDAESEKLvqeALDRAMK-----GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHD 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-208 |
2.16e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.87 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRFdnchgkrwqNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPD---SGSIYLNERKLEHYD 81
Cdd:COG4136 2 LSLENLTI---------TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 82 NKHRvlNIRMVFQNsnESLNPGITLGSILeePLKLNTRLDNQARIAKVEQTLKLVGLlpeHRFFYRH--MLSDGQRQRVA 159
Cdd:COG4136 73 AEQR--RIGILFQD--DLLFPHLSVGENL--AFALPPTIGRAQRRARVEQALEEAGL---AGFADRDpaTLSGGQRARVA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495265151 160 LARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISH 208
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-228 |
2.34e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 105.28 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 18 KRWQN-KGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYD--NKHRVLNIRMVFQ 94
Cdd:PRK11629 13 KRYQEgSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaAKAELRNQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 95 NSNESLNPGITLGSILEEPLKLNTRLDNQARiAKVEQTLKLVGLlpEHRFFYRHM-LSDGQRQRVALARAIILNPQVIVA 173
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPLLIGKKKPAEIN-SRALEMLAAVGL--EHRANHRPSeLSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 174 DEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKiLVMKQGKV 228
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ-LEMRDGRL 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-228 |
3.40e-27 |
|
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: 103.28 E-value: 3.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLRFDNchgkrwqnkgskfTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNK 83
Cdd:cd03215 4 VLEVRGLSVKG-------------AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 HRV-LNIRMVfqnsneslnPG--ITLGSILEEPLKLNTRLdnqariakveqtlklvgllpehrffyRHMLSDGQRQRVAL 160
Cdd:cd03215 71 DAIrAGIAYV---------PEdrKREGLVLDLSVAENIAL--------------------------SSLLSGGNQQKVVL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 161 ARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKV 228
Cdd:cd03215 116 ARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
32-245 |
5.61e-27 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 107.04 E-value: 5.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRvlNIRMVFQNSneSLNPGITLGSILE 111
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER--GVGMVFQSY--ALYPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 112 EPLKLN--TRLDNQARIAKVEQTLKLVGLL---PEhrffyrhMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRS 186
Cdd:PRK11000 98 FGLKLAgaKKEEINQRVNQVAEVLQLAHLLdrkPK-------ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 187 QTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEY 245
Cdd:PRK11000 171 QMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRF 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
33-247 |
6.20e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.43 E-value: 6.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 33 NFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKH----RVLNIRMVFQNSneSLNPGITLGS 108
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevRRKKIAMVFQSF--ALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ILEEPLKLnTRLDNQARIAKVEQTLKLVGLlPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQT 188
Cdd:PRK10070 126 NTAFGMEL-AGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 189 VNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTK 247
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
24-237 |
6.29e-27 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 108.59 E-value: 6.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDnkhrvlniRMVFQNSNESLNPG 103
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWD--------RETFGKHIGYLPQD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 ITL--GSILEEPLKLNTRLDNQARI--AKVEQTLKLVGLLPEHrffYRHM-------LSDGQRQRVALARAIILNPQVIV 172
Cdd:TIGR01842 401 VELfpGTVAENIARFGENADPEKIIeaAKLAGVHELILRLPDG---YDTVigpggatLSGGQRQRIALARALYGDPKLVV 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 173 ADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHIsDKILVMKQGKVVESGKTDVI 237
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCV-DKILVLQDGRIARFGERDEV 540
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-230 |
7.54e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 106.47 E-value: 7.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRfdnchgKRWQNKgsKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKH 84
Cdd:PRK11650 4 LKLQAVR------KSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 85 RvlNIRMVFQNSneSLNPGITLGSILEEPLKlNTRLDN---QARIAKVEQTLKLVGLL---PEHrffyrhmLSDGQRQRV 158
Cdd:PRK11650 76 R--DIAMVFQNY--ALYPHMSVRENMAYGLK-IRGMPKaeiEERVAEAARILELEPLLdrkPRE-------LSGGQRQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 159 ALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHN------LGivrhisDKILVMKQGkVVE 230
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDqveamtLA------DRVVVMNGG-VAE 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-232 |
9.67e-27 |
|
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: 103.07 E-value: 9.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 14 NCHGKRWqnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKlehYDNKHRVLNirmvf 93
Cdd:cd03268 4 NDLTKTY---GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS---YQKNIEALR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 94 qnsneslnpgiTLGSILEEP-----------LKLNTRLdNQARIAKVEQTLKLVGL-LPEHRFFyrHMLSDGQRQRVALA 161
Cdd:cd03268 73 -----------RIGALIEAPgfypnltarenLRLLARL-LGIRKKRIDEVLDVVGLkDSAKKKV--KGFSLGMKQRLGIA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495265151 162 RAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-210 |
1.32e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 104.01 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVlnirmVFQNsnESLNPG 103
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGV-----VFQN--EGLLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 ITLGSILEEPLKLnTRLDNQARIAKVEQTLKLVGLL-PEHRFFYRhmLSDGQRQRVALARAIILNPQVIVADEPFAALDP 182
Cdd:PRK11248 85 RNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEgAEKRYIWQ--LSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180
....*....|....*....|....*...
gi 495265151 183 SVRSQTVNLLMELQRELGLGFIFISHNL 210
Cdd:PRK11248 162 FTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
32-237 |
1.45e-26 |
|
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: 107.58 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLN------ERKLEHYDNKHRVLN-IRMVFQNSneSLNPGI 104
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvDMTKPGPDGRGRAKRyIGILHQEY--DLYPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 105 TLGSILEEPLKLNtrLDNQARIAKVEQTLKLVG--------LLPEhrffYRHMLSDGQRQRVALARAIILNPQVIVADEP 176
Cdd:TIGR03269 381 TVLDNLTEAIGLE--LPDELARMKAVITLKMVGfdeekaeeILDK----YPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495265151 177 FAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVI 237
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
29-228 |
3.53e-26 |
|
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: 101.72 E-value: 3.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVL---NIRMVFQNS------NES 99
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrrKIGVVFQDFrllpdrNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 100 LNPGITLGSILEEPLKLNTRldnqariakVEQTLKLVGLLPEHRFFYRHmLSDGQRQRVALARAIILNPQVIVADEPFAA 179
Cdd:cd03292 97 ENVAFALEVTGVPPREIRKR---------VPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495265151 180 LDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKV 228
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-238 |
3.70e-26 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 102.24 E-value: 3.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRFDncHGKRWQNKGskftlgpINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKH 84
Cdd:cd03218 1 LRAENLSKR--YGKRKVVNG-------VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 85 RV-LNIRMVFQNSneSLNPGIT----LGSILEEplklnTRLDNQARIAKVEQTLKLVGLLP-EHRFFYRhmLSDGQRQRV 158
Cdd:cd03218 72 RArLGIGYLPQEA--SIFRKLTveenILAVLEI-----RGLSKKEREEKLEELLEEFHITHlRKSKASS--LSGGERRRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 159 ALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELqRELGLGFIFISHNlgiVRH---ISDKILVMKQGKVVESGKTD 235
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHN---VREtlsITDRAYIIYEGKVLAEGTPE 218
|
...
gi 495265151 236 VIF 238
Cdd:cd03218 219 EIA 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
32-233 |
4.01e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 106.73 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNK--HRvlNIRMVFQNS---NESLNPGITL 106
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHR--QVALVGQEPvlfSGSVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 GsileeplkLNTRLDNQAR-IAKVEQTLKLVGLLP--------EHRFFyrhmLSDGQRQRVALARAIILNPQVIVADEPF 177
Cdd:TIGR00958 578 G--------LTDTPDEEIMaAAKAANAHDFIMEFPngydtevgEKGSQ----LSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495265151 178 AALDPSVrSQTVNLLMELQrelGLGFIFISHNLGIVRHiSDKILVMKQGKVVESGK 233
Cdd:TIGR00958 646 SALDAEC-EQLLQESRSRA---SRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGT 696
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
32-249 |
6.89e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.57 E-value: 6.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGS--------IYLNERKLehYDNKHRVlniRMVFQNSNESLnPG 103
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTV--WDIREKV---GIVFQNPDNQF-VG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 ITLGSILEEPLKlNTRLDNQARIAKVEQTLKLVGLL------PEHrffyrhmLSDGQRQRVALARAIILNPQVIVADEPF 177
Cdd:PRK13640 100 ATVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLdyidsePAN-------LSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495265151 178 AALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHiSDKILVMKQGKVVESGKTDVIFhwPKDEYTKKL 249
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIF--SKVEMLKEI 240
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-232 |
8.85e-26 |
|
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: 100.35 E-value: 8.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENL--RFDNCHGkrwqnkgskftLGPINFSIQAGeTLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERK-LEHYD 81
Cdd:cd03264 1 LQLENLtkRYGKKRA-----------LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDvLKQPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 82 NKHRVLNirmvFQNSNESLNPGITLGSILEEPLKLNTRLDNQARiAKVEQTLKLVGLLpEHRFFYRHMLSDGQRQRVALA 161
Cdd:cd03264 69 KLRRRIG----YLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVK-ARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495265151 162 RAIILNPQVIVADEPFAALDPSVRSQTVNLLmelqRELGLGFIFI--SHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLL----SELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-250 |
9.91e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 101.53 E-value: 9.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGL-----EQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQNSNE 98
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 99 ----SLNPGITLGsileepLKLNTRLDNQARI-AKVEQTLKLVGLLPEHRFFYRH---MLSDGQRQRVALARAIILNPQV 170
Cdd:PRK14247 94 ipnlSIFENVALG------LKLNRLVKSKKELqERVRWALEKAQLWDEVKDRLDApagKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 171 IVADEPFAALDPSVRSQTVNLLMELQRELGLgfIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLV 250
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYV 245
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
32-235 |
4.28e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 103.21 E-value: 4.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYD-NKHRVLNIRMVFQN----SNESLNPGITL 106
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEpllfPNLSVKENILF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 GsiLEEPLKLNTRLdnQARIAKVEQTLKLvgllpehrffyrHM----LSDGQRQRVALARAIILNPQVIVADEPFAALDP 182
Cdd:PRK15439 110 G--LPKRQASMQKM--KQLLAALGCQLDL------------DSsagsLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 183 svrSQTVNLLMELQ--RELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTD 235
Cdd:PRK15439 174 ---AETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTA 225
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
32-232 |
4.50e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 99.37 E-value: 4.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLE--QPDSGSIYLNERKLEHYDNKHRV-LNIRMVFQNSNESlnPGITLGS 108
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERArAGIFLAFQYPVEI--PGVSVSN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ILEEPL--KLNTRLDNQARIAKVEQTLKLVGLLPEhrFFYRHM---LSDGQRQRVALARAIILNPQVIVADEPFAALD-P 182
Cdd:COG0396 97 FLRTALnaRRGEELSAREFLKLLKEKMKELGLDED--FLDRYVnegFSGGEKKRNEILQMLLLEPKLAILDETDSGLDiD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495265151 183 SVR--SQTVNLLmelqRELGLGFIFISHNLGIVRHIS-DKILVMKQGKVVESG 232
Cdd:COG0396 175 ALRivAEGVNKL----RSPDRGILIITHYQRILDYIKpDFVHVLVDGRIVKSG 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
8-245 |
7.51e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.90 E-value: 7.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 8 ENLRFDNCHGKRWQNKGskftLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVL 87
Cdd:PRK13641 6 ENVDYIYSPGTPMEKKG----LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 88 NIR----MVFQNSNESLNPGITLGSILEEPLKLNTRlDNQARIAKVeQTLKLVGL---LPEHRFFYrhmLSDGQRQRVAL 160
Cdd:PRK13641 82 KLRkkvsLVFQFPEAQLFENTVLKDVEFGPKNFGFS-EDEAKEKAL-KWLKKVGLsedLISKSPFE---LSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 161 ARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIF-- 238
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFsd 235
|
....*...
gi 495265151 239 -HWPKDEY 245
Cdd:PRK13641 236 kEWLKKHY 243
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-238 |
8.56e-25 |
|
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: 99.00 E-value: 8.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 10 LRFDNCHGKRwqnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSG-SIYLNERKLEHYDnkhrVLN 88
Cdd:COG1119 4 LELRNVTVRR----GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGED----VWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 89 IR----MVfqnSNE---SLNPGITL---------GSI--LEEPlklntrldNQARIAKVEQTLKLVGL--LPEHRFfyrH 148
Cdd:COG1119 76 LRkrigLV---SPAlqlRFPRDETVldvvlsgffDSIglYREP--------TDEQRERARELLELLGLahLADRPF---G 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 149 MLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLG-IVRHISdKILVMKQGK 227
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGIT-HVLLLKDGR 220
|
250
....*....|.
gi 495265151 228 VVESGKTDVIF 238
Cdd:COG1119 221 VVAAGPKEEVL 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-235 |
9.44e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 98.62 E-value: 9.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENL------------RFDNCHGKRWQNKGSKFT-LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDS 67
Cdd:COG1134 1 MSSMIEVENVsksyrlyhepsrSLKELLLRRRRTRREEFWaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 68 GSIYLNERK---LE-----HYDnkhrvL----NIRMVfqnsneslnpGITLGSILEEPlklntrldnQARIAKVEQtlkL 135
Cdd:COG1134 81 GRVEVNGRVsalLElgagfHPE-----LtgreNIYLN----------GRLLGLSRKEI---------DEKFDEIVE---F 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 136 VGLlpeHRFFYR--HMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIV 213
Cdd:COG1134 134 AEL---GDFIDQpvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAV 209
|
250 260
....*....|....*....|..
gi 495265151 214 RHISDKILVMKQGKVVESGKTD 235
Cdd:COG1134 210 RRLCDRAIWLEKGRLVMDGDPE 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
32-232 |
1.62e-24 |
|
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: 96.23 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLnirmvfqnsneslnpgitLGSILE 111
Cdd:cd03247 21 LSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL------------------ISVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 112 EPLKLNTRLDNQariakveqtlklVGLlpehRFfyrhmlSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNL 191
Cdd:cd03247 83 RPYLFDTTLRNN------------LGR----RF------SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495265151 192 LMELQRELGLgfIFISHNLGIVRHIsDKILVMKQGKVVESG 232
Cdd:cd03247 141 IFEVLKDKTL--IWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
32-238 |
2.45e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 98.31 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIR----MVFQNSNESLNPGITLG 107
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRkrigMVFQFPESQLFEDTVER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 SILEEPLKLNTRLDNQAriAKVEQTLKLVGllpehrfFYRHML-------SDGQRQRVALARAIILNPQVIVADEPFAAL 180
Cdd:PRK13646 106 EIIFGPKNFKMNLDEVK--NYAHRLLMDLG-------FSRDVMsqspfqmSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 181 DPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIF 238
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
32-232 |
2.94e-24 |
|
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: 96.83 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERklehydnkhrvlnIRMVFqNSNESLNPGITlGsilE 111
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-------------VSSLL-GLGGGFNPELT-G---R 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 112 EPLKLNTRL---DNQARIAKVEQTLKLVGLlpeHRFFYRHM--LSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRS 186
Cdd:cd03220 103 ENIYLNGRLlglSRKEIDEKIDEIIEFSEL---GDFIDLPVktYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495265151 187 QTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:cd03220 180 KCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
32-214 |
5.13e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.38 E-value: 5.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIylnerklehydnkHRVLNIRMVF--QNS--NESLnP----- 102
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------------RRAGGARVAYvpQRSevPDSL-Pltvrd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 103 GITLGsiLEEPLKLNTRLDNQARiAKVEQTLKLVGLLP-EHRFFyrHMLSDGQRQRVALARAIILNPQVIVADEPFAALD 181
Cdd:NF040873 77 LVAMG--RWARRGLWRRLTRDDR-AAVDDALERVGLADlAGRQL--GELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|...
gi 495265151 182 PSVRSQTVNLLMELQRElGLGFIFISHNLGIVR 214
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
24-228 |
6.37e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 96.67 E-value: 6.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNkhrvlNIRMVFQNSN----ES 99
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE-----DTRLMFQDARllpwKK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 100 LNPGITLGsileepLKLNTRldnqariAKVEQTLKLVGLlPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAA 179
Cdd:PRK11247 98 VIDNVGLG------LKGQWR-------DAALQALAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495265151 180 LDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKV 228
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
10-232 |
7.51e-24 |
|
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: 95.51 E-value: 7.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 10 LRFDNCHgKRWQNKGSKF-TLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIylnerKLEHYDNKH--RV 86
Cdd:cd03266 2 ITADALT-KRFRDVKKTVqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA-----TVDGFDVVKepAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 87 LNIRMVFQNSNESLNPGITLGSILEEPLKLNTrLDNQARIAKVEqtlKLVGLLPEHRFFYRHM--LSDGQRQRVALARAI 164
Cdd:cd03266 76 ARRRLGFVSDSTGLYDRLTARENLEYFAGLYG-LKGDELTARLE---ELADRLGMEELLDRRVggFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 165 ILNPQVIVADEPFAALDpSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:cd03266 152 VHDPPVLLLDEPTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
32-235 |
8.14e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 95.82 E-value: 8.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRV-LNI------RMVFqnsneslnPGI 104
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArLGIgyvpegRRIF--------PSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 105 TLgsilEEPLKL--NTRLDNQARIAKVEQTLKLVGLLPEHRffyRHM---LSDGQRQRVALARAIILNPQVIVADEPFAA 179
Cdd:COG0410 94 TV----EENLLLgaYARRDRAEVRADLERVYELFPRLKERR---RQRagtLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495265151 180 LDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTD 235
Cdd:COG0410 167 LAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAA 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-232 |
1.42e-23 |
|
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: 94.65 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRfdnchgKRWqnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEhYDNKH 84
Cdd:cd03269 1 LEVENVT------KRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-IAARN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 85 RvlnirMVFQNSNESLNPGITLGSILEEPLKLNTRLDNQARiAKVEQTLKLVGLlPEHRFFYRHMLSDGQRQRVALARAI 164
Cdd:cd03269 71 R-----IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEAR-RRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 165 ILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
1.94e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.96 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENLRFDNCHGKRwqnkgskfTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLeHY 80
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTK--------ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV-NA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 81 DNKHRVLN-IRMVFQNSNESLNPGITLGSILEEPLklNTRLDNQARIAKVEQTLKLVGLLpEHRFFYRHMLSDGQRQRVA 159
Cdd:PRK13647 72 ENEKWVRSkVGLVFQDPDDQVFSSTVWDDVAFGPV--NMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495265151 160 LARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
32-232 |
2.38e-23 |
|
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: 94.60 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQNS---NESLNPGITLGs 108
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVflfNDTVAENIAYG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ileeplklntRLDnqARIAKVEQTLKLVGLlpeHRFF------YRHM-------LSDGQRQRVALARAIILNPQVIVADE 175
Cdd:cd03251 100 ----------RPG--ATREEVEEAARAANA---HEFImelpegYDTVigergvkLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 176 PFAALDpsvrSQTVNLLMELQRELGLG--FIFISHNLGIVRHiSDKILVMKQGKVVESG 232
Cdd:cd03251 165 ATSALD----TESERLVQAALERLMKNrtTFVIAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-251 |
2.99e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.56 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLeHYDNKHRV--------LNIRM------VF--Qn 95
Cdd:COG4152 20 VSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-DPEDRRRIgylpeergLYPKMkvgeqlVYlaR- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 96 snesLNpGITLGSILEEPLKLNTRLDNQARIA-KVEQtlklvgllpehrffyrhmLSDGQRQRVALARAIILNPQVIVAD 174
Cdd:COG4152 98 ----LK-GLSKAEAKRRADEWLERLGLGDRANkKVEE------------------LSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 175 EPFAALDPsVrsqTVNLLMELQREL---GLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIfhwpKDEYTKKLVH 251
Cdd:COG4152 155 EPFSGLDP-V---NVELLKDVIRELaakGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI----RRQFGRNTLR 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
32-235 |
6.31e-23 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 93.20 E-value: 6.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNerkleHYDNKHRVLNIR----MVFQNSneSLNPGITLg 107
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVA-----GHDVVREPREVRrrigIVFQDL--SVDDELTG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 silEEPLKLNTRL---DNQARIAKVEQTLKLVGLLpEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSV 184
Cdd:cd03265 91 ---WENLYIHARLygvPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495265151 185 RSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTD 235
Cdd:cd03265 167 RAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-232 |
7.05e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 94.06 E-value: 7.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENLRFdnchgkrwqNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHY 80
Cdd:PRK11831 4 VANLVDMRGVSF---------TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 81 dNKHRVLNIR----MVFQNSneSLNPGITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGL------LPEHrffyrhmL 150
Cdd:PRK11831 75 -SRSRLYTVRkrmsMLFQSG--ALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLrgaaklMPSE-------L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 151 SDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVE 230
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVA 224
|
..
gi 495265151 231 SG 232
Cdd:PRK11831 225 HG 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
32-235 |
1.05e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.95 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIY--------LNERKLEHydnkhrvlNIRMVFQNS---NESL 100
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgtdirtVTRASLRR--------NIAVVFQDAglfNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 101 NPGITLGS--------------------ILEEPLKLNTRLDNQARiakveqtlklvgllpehrffyrhMLSDGQRQRVAL 160
Cdd:PRK13657 426 EDNIRVGRpdatdeemraaaeraqahdfIERKPDGYDTVVGERGR-----------------------QLSGGERQRLAI 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 161 ARAIILNPQVIVADEPFAALDpSVRSQTVNLLMELQRELGLGFIfISHNLGIVRHiSDKILVMKQGKVVESGKTD 235
Cdd:PRK13657 483 ARALLKDPPILILDEATSALD-VETEAKVKAALDELMKGRTTFI-IAHRLSTVRN-ADRILVFDNGRVVESGSFD 554
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
29-235 |
1.55e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 92.98 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLeQPDSGSIYLNERKLEHYD----NKHR---------VLNIRmVFQN 95
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSaaelARHRaylsqqqspPFAMP-VFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 96 sneslnpgITLGSileePLKLNTRLDNQArIAKVEQTLKLVGLLPehrffyRHM--LSDGQRQRVALARAII-----LNP 168
Cdd:COG4138 90 --------LALHQ----PAGASSEAVEQL-LAQLAEALGLEDKLS------RPLtqLSGGEWQRVRLAAVLLqvwptINP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495265151 169 --QVIVADEPFAALDpsVRSQTV--NLLMELqRELGLGFIFISHNLG-IVRHiSDKILVMKQGKVVESGKTD 235
Cdd:COG4138 151 egQLLLLDEPMNSLD--VAQQAAldRLLREL-CQQGITVVMSSHDLNhTLRH-ADRVWLLKQGKLVASGETA 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
32-237 |
1.56e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.13 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNkHRVLNIRMV--FQN-------------- 95
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG-HQIARMGVVrtFQHvrlfremtvienll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 96 --SNESLNPGItLGSILEEPlklNTRLDNQARIAKVEQTLKLVGLLPehrFFYRHM--LSDGQRQRVALARAIILNPQVI 171
Cdd:PRK11300 103 vaQHQQLKTGL-FSGLLKTP---AFRRAESEALDRAATWLERVGLLE---HANRQAgnLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495265151 172 VADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVI 237
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
32-252 |
1.69e-22 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 94.48 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQpDSGSIYLNERKLEHYD-------NKHRVL--NIRMVFQNSNESLNP 102
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDIDllrlsprERRKLVghNVSMIFQEPQSCLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 103 GITLGSILEEPLKLNT-------RLDNQARIAKveQTLKLVGlLPEHRFF---YRHMLSDGQRQRVALARAIILNPQVIV 172
Cdd:PRK15093 105 SERVGRQLMQNIPGWTykgrwwqRFGWRKRRAI--ELLHRVG-IKDHKDAmrsFPYELTEGECQKVMIAIALANQPRLLI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 173 ADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLVHA 252
Cdd:PRK15093 182 ADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQALIRA 261
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
33-238 |
1.96e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.53 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 33 NFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSG-------SIYLNERKLEHYDNKHRvlNIRMVFQNSNESLNPGIT 105
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyAIPANLKKIKEVKRLRK--EIGLVFQFPEYQLFQETI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 106 LGSILEEPLKLNTrlDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVR 185
Cdd:PRK13645 109 EKDIAFGPVNLGE--NKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495265151 186 SQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIF 238
Cdd:PRK13645 187 EDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-237 |
2.58e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 92.01 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENL--RFdnchGKRWQNKGskftlgpINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDN 82
Cdd:COG1137 4 LEAENLvkSY----GKRTVVKD-------VSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 83 KHRVlniRM----------------VFQNsneslnpgitLGSILEEplklnTRLDNQARIAKVEQTLKLVGLlpEHRffy 146
Cdd:COG1137 73 HKRA---RLgigylpqeasifrkltVEDN----------ILAVLEL-----RKLSKKEREERLEELLEEFGI--THL--- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 147 RH----MLSDGQRQRVALARAIILNPQVIVADEPFAALDP-SVRS-QtvNLLMELqRELGLGfIFIS-HN----LGIVrh 215
Cdd:COG1137 130 RKskaySLSGGERRRVEIARALATNPKFILLDEPFAGVDPiAVADiQ--KIIRHL-KERGIG-VLITdHNvretLGIC-- 203
|
250 260
....*....|....*....|..
gi 495265151 216 isDKILVMKQGKVVESGKTDVI 237
Cdd:COG1137 204 --DRAYIISEGKVLAEGTPEEI 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
32-232 |
2.92e-22 |
|
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: 95.66 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERklehydnkhrvlNIRMVFQNS--------------- 96
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ------------DIRDVTQASlraaigivpqdtvlf 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 97 NESL-------NPGITLGSILEeplklntrldnQARIAKVEQtlkLVGLLPEHrffYRHM-------LSDGQRQRVALAR 162
Cdd:COG5265 445 NDTIayniaygRPDASEEEVEA-----------AARAAQIHD---FIESLPDG---YDTRvgerglkLSGGEKQRVAIAR 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495265151 163 AIILNPQVIVADEPFAALDpsvrSQTVNLLMELQRELGLG--FIFISHNLGIVRHiSDKILVMKQGKVVESG 232
Cdd:COG5265 508 TLLKNPPILIFDEATSALD----SRTERAIQAALREVARGrtTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
27-230 |
3.28e-22 |
|
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: 95.25 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 27 FTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERK-----LEHYDNkhrvlNIRMVFqnSN---- 97
Cdd:COG4615 346 FTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPvtadnREAYRQ-----LFSAVF--SDfhlf 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 98 ESLnpgitLGsileeplklntrLDNQARIAKVEQTLKLVGL-----LPEHRFFYRHmLSDGQRQRVALARAIILNPQVIV 172
Cdd:COG4615 419 DRL-----LG------------LDGEADPARARELLERLELdhkvsVEDGRFSTTD-LSQGQRKRLALLVALLEDRPILV 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 173 ADEpFAA-LDPSVR----SQtvnLLMELqRELGLGFIFISHNlgiVR--HISDKILVMKQGKVVE 230
Cdd:COG4615 481 FDE-WAAdQDPEFRrvfyTE---LLPEL-KARGKTVIAISHD---DRyfDLADRVLKMDYGKLVE 537
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
32-238 |
4.37e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.36 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLneRKLEHYDNKhRVLNIR----MVFQNSNESLnpgitLG 107
Cdd:PRK13644 21 INLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV--SGIDTGDFS-KLQGIRklvgIVFQNPETQF-----VG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 SILEEPLKL---NTRLDNQARIAKVEQTLKLVGlLPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSV 184
Cdd:PRK13644 93 RTVEEDLAFgpeNLCLPPIEIRKRVDRALAEIG-LEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495265151 185 RSQTVNLLMELQRElGLGFIFISHNLGIVrHISDKILVMKQGKVVESGKTDVIF 238
Cdd:PRK13644 172 GIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
29-232 |
6.45e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 94.53 E-value: 6.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLeQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQnsneslNPGITLGS 108
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWRKHLSWVGQ------NPQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ILEeplklNTRLDN-QARIAKVEQTLKLVGLlpeHRFFYRHM-------------LSDGQRQRVALARAIILNPQVIVAD 174
Cdd:PRK11174 439 LRD-----NVLLGNpDASDEQLQQALENAWV---SEFLPLLPqgldtpigdqaagLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 175 EPFAALDpsvrSQTVNLLME-LQRE-LGLGFIFISHNLGIVRHIsDKILVMKQGKVVESG 232
Cdd:PRK11174 511 EPTASLD----AHSEQLVMQaLNAAsRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQG 565
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
32-238 |
1.15e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.34 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIR----MVFQNSNESLNPGITLG 107
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRkkvgLVFQFPESQLFEETVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 SILEEPLKLNTRLDNQARIAKveQTLKLVGLLPEhrFFYRH--MLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVR 185
Cdd:PRK13649 106 DVAFGPQNFGVSQEEAEALAR--EKLALVGISES--LFEKNpfELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495265151 186 SQTVNLLMELQrELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIF 238
Cdd:PRK13649 182 KELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-227 |
1.16e-21 |
|
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: 89.45 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRFdnchgkRWQNKG--SKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERklehydn 82
Cdd:cd03250 1 ISVEDASF------TWDSGEqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 83 khrvlnIRMVFQNS---NESLNPGITLGSILEEPlklntrldnqariaKVEQTLKLVGLLPEHRFFYRH----------M 149
Cdd:cd03250 68 ------IAYVSQEPwiqNGTIRENILFGKPFDEE--------------RYEKVIKACALEPDLEILPDGdlteigekgiN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 150 LSDGQRQRVALARAIILNPQVIVADEPFAALDpsvrSQTVNLLME--LQRELGLG--FIFISHNLGIVRHiSDKILVMKQ 225
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVD----AHVGRHIFEncILGLLLNNktRILVTHQLQLLPH-ADQIVVLDN 202
|
..
gi 495265151 226 GK 227
Cdd:cd03250 203 GR 204
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-233 |
1.47e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 93.63 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRFDNCHGKRwqnkgskfTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYdnKH 84
Cdd:PRK10790 341 IDIDNVSFAYRDDNL--------VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL--SH 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 85 RVL--NIRMVFQNS---NESLNPGITLGSILEEplklntrldnqariAKVEQTLKLVGLLPehrfFYRHM---------- 149
Cdd:PRK10790 411 SVLrqGVAMVQQDPvvlADTFLANVTLGRDISE--------------EQVWQALETVQLAE----LARSLpdglytplge 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 150 ----LSDGQRQRVALARAIILNPQVIVADEPFAALDpSVRSQTVNLLMELQRElGLGFIFISHNLG-IVRhiSDKILVMK 224
Cdd:PRK10790 473 qgnnLSVGQKQLLALARVLVQTPQILILDEATANID-SGTEQAIQQALAAVRE-HTTLVVIAHRLStIVE--ADTILVLH 548
|
....*....
gi 495265151 225 QGKVVESGK 233
Cdd:PRK10790 549 RGQAVEQGT 557
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-229 |
1.50e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.16 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLrfdnCHGKRwqnkgskftLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLehydnk 83
Cdd:COG1129 256 VLEVEGL----SVGGV---------VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV------ 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 hRVLNIRmvfqnsnESLNPGI--------TLGSILEEPLKLNTRLDNQARIAKVeqtlklvGLLP---EHRFFYRHM--- 149
Cdd:COG1129 317 -RIRSPR-------DAIRAGIayvpedrkGEGLVLDLSIRENITLASLDRLSRG-------GLLDrrrERALAEEYIkrl 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 150 -------------LSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHI 216
Cdd:COG1129 382 riktpspeqpvgnLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGL 460
|
250
....*....|...
gi 495265151 217 SDKILVMKQGKVV 229
Cdd:COG1129 461 SDRILVMREGRIV 473
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-234 |
1.57e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 91.86 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLehYDNKHRVL------NIRMVFQNSNesLNPGIT 105
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL--FDAEKGIClppekrRIGYVFQDAR--LFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 106 LgsilEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEhrffYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVR 185
Cdd:PRK11144 93 V----RGNLRYGMAKSMVAQFDKIVALLGIEPLLDR----YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495265151 186 SQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKT 234
Cdd:PRK11144 165 RELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-238 |
2.51e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.07 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAgeTLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHydNKHRVLNIRM----VFQNSNESLNPGITLG 107
Cdd:PRK13638 22 LDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY--SKRGLLALRQqvatVFQDPEQQIFYTDIDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 SILEEPLKLNTRLDNQARiaKVEQTLKLVGllPEHrffYRHM----LSDGQRQRVALARAIILNPQVIVADEPFAALDPS 183
Cdd:PRK13638 98 DIAFSLRNLGVPEAEITR--RVDEALTLVD--AQH---FRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 184 VRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIF 238
Cdd:PRK13638 171 GRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-250 |
4.46e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 89.34 E-value: 4.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 26 KFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIR------MVFQNSNES 99
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKlrkevgMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 100 lnPGITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEhrfFYRHM------LSDGQRQRVALARAIILNPQVIVA 173
Cdd:PRK14246 103 --PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKE---VYDRLnspasqLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 174 DEPFAALDpSVRSQTV-NLLMELQRELGLgfIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLV 250
Cdd:PRK14246 178 DEPTSMID-IVNSQAIeKLITELKNEIAI--VIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
32-228 |
6.46e-21 |
|
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: 87.91 E-value: 6.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNK--HR---------VLNIRMVFQNSNESL 100
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSkvslvgqepVLFARSLQDNIAYGL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 101 nPGITLGSILEEPLKLNTRlDNQARIAKVEQTLklVGLLPEhrffyrhMLSDGQRQRVALARAIILNPQVIVADEPFAAL 180
Cdd:cd03248 113 -QSCSFECVKEAAQKAHAH-SFISELASGYDTE--VGEKGS-------QLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495265151 181 DPSVRSQTVNLLMELQRELGLgfIFISHNLGIVRHiSDKILVMKQGKV 228
Cdd:cd03248 182 DAESEQQVQQALYDWPERRTV--LVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
32-181 |
9.81e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.78 E-value: 9.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDnkhrvlnirmvfqnsnESLN---------P 102
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR----------------DEYHqdllylghqP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 103 GITlgSIL--EEPLKLNTRLDNQARIAKVEQTLKLVGL-----LPEHRffyrhmLSDGQRQRVALARAIILNPQVIVADE 175
Cdd:PRK13538 84 GIK--TELtaLENLRFYQRLHGPGDDEALWEALAQVGLagfedVPVRQ------LSAGQQRRVALARLWLTRAPLWILDE 155
|
....*.
gi 495265151 176 PFAALD 181
Cdd:PRK13538 156 PFTAID 161
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-250 |
1.11e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.12 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 23 KGSKFTLG--------PINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQ 94
Cdd:PRK10253 9 RGEQLTLGygkytvaeNLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 95 NSNeslNPG-ITL------GSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEHrffyRHMLSDGQRQRVALARAIILN 167
Cdd:PRK10253 89 NAT---TPGdITVqelvarGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQS----VDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 168 PQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKtdvifhwPKDEYTK 247
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA-------PKEIVTA 234
|
...
gi 495265151 248 KLV 250
Cdd:PRK10253 235 ELI 237
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-229 |
2.03e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 87.45 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKL----EHYdnkhRVLNIRMVFQnsneslNPgiTLG 107
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpEYK----RAKYIGRVFQ------DP--MMG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 -----SILE---------EPLKLNTRLdNQARIAKVEQTLKLVGLLPEHRFFYR-HMLSDGQRQRVALARAIILNPQVIV 172
Cdd:COG1101 93 tapsmTIEEnlalayrrgKRRGLRRGL-TKKRRELFRELLATLGLGLENRLDTKvGLLSGGQRQALSLLMATLTKPKLLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495265151 173 ADEPFAALDPsvrsQTVNLLMELQREL----GLGFIFISHNLgivRH---ISDKILVMKQGKVV 229
Cdd:COG1101 172 LDEHTAALDP----KTAALVLELTEKIveenNLTTLMVTHNM---EQaldYGNRLIMMHEGRII 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
32-232 |
2.18e-20 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 86.39 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDnkHRVLNIRMVFqnsneslnpgitlgsILE 111
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG--LHDLRSRISI---------------IPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 112 EP------LKLNtrLD--NQARIAKVEQTLKLVGLLPEHRFFYRHM----------LSDGQRQRVALARAIILNPQVIVA 173
Cdd:cd03244 86 DPvlfsgtIRSN--LDpfGEYSDEELWQALERVGLKEFVESLPGGLdtvveeggenLSVGQRQLLCLARALLRKSKILVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495265151 174 DEPFAALDPsvrsQTVNLLMELQRElglGF-----IFISHNLGIVRHiSDKILVMKQGKVVESG 232
Cdd:cd03244 164 DEATASVDP----ETDALIQKTIRE---AFkdctvLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-229 |
2.21e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.17 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENLRfdnchgKRWQN-KGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEH 79
Cdd:PRK10535 1 MTALLELKDIR------RSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 80 YDN----KHRVLNIRMVFQNSNesLNPGITLGSILEEPlKLNTRLDNQARIAKVEQTLKLVGLlpEHRFFYR-HMLSDGQ 154
Cdd:PRK10535 75 LDAdalaQLRREHFGFIFQRYH--LLSHLTAAQNVEVP-AVYAGLERKQRLLRAQELLQRLGL--EDRVEYQpSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 155 RQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELqRELGLGFIFISHNLGIVRHiSDKILVMKQGKVV 229
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
34-238 |
2.74e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 87.25 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 34 FSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLnerkLEHYDNKHRVLNIRMVFQNSNE---SLnpgitlgSIL 110
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI----LGQPTRQALQKNLVAYVPQSEEvdwSF-------PVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 111 EEPLKLNTRLDNQA--RIAK------VEQTLKLVGLLpEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDP 182
Cdd:PRK15056 97 VEDVVMMGRYGHMGwlRRAKkrdrqiVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495265151 183 SVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDkILVMKQGKVVESGKTDVIF 238
Cdd:PRK15056 176 KTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTF 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-232 |
2.77e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRV-LNIRMVFQN---SNE-SLNPG 103
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAqLGIGIIYQElsvIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 ITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHmLSDGQRQRVALARAIILNPQVIVADEPFAALDPS 183
Cdd:PRK09700 101 LYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN-LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495265151 184 VRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:PRK09700 180 EVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-226 |
3.85e-20 |
|
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: 85.95 E-value: 3.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENL--RFD--NCHGKRWQnkgskfTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNerk 76
Cdd:COG4778 1 MTTLLEVENLskTFTlhLQGGKRLP------VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 77 leHYDNK--------HRVLNIR-----MVFQnsneSLN--PGITLGSILEEPLKLNTRLDNQARiAKVEQTLKLVGLlPE 141
Cdd:COG4778 72 --HDGGWvdlaqaspREILALRrrtigYVSQ----FLRviPRVSALDVVAEPLLERGVDREEAR-ARARELLARLNL-PE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 142 HRF-FYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKI 220
Cdd:COG4778 144 RLWdLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRV 222
|
....*.
gi 495265151 221 LVMKQG 226
Cdd:COG4778 223 VDVTPF 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
24-229 |
3.89e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 85.70 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVL---NIRMVFQNSNESL 100
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFlrrQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 101 NPgiTLGSILEEPLKLNTRLDNQARiAKVEQTLKLVGLLPEHRFFYRHmLSDGQRQRVALARAIILNPQVIVADEPFAAL 180
Cdd:PRK10908 93 DR--TVYDNVAIPLIIAGASGDDIR-RRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495265151 181 DPSVRSQTVNLLMELQReLGLGFIFISHNLGIVRHISDKILVMKQGKVV 229
Cdd:PRK10908 169 DDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
32-237 |
4.62e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.95 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRvLNIRMVF-----QNSneslnpgitl 106
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQR-LARGLVYlpedrQSS---------- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 GSILEEPLKLNTR----------LDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEP 176
Cdd:PRK15439 351 GLYLDAPLAWNVCalthnrrgfwIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495265151 177 FAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVI 237
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
32-239 |
4.73e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.10 E-value: 4.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIR----MVFQNSNESLNPGITLG 107
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRkkvgVVFQFPESQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 SILEEPLKLNTRLDNQARIAKveQTLKLVGLLPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQ 187
Cdd:PRK13643 105 DVAFGPQNFGIPKEKAEKIAA--EKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495265151 188 TVNLLMELQrELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFH 239
Cdd:PRK13643 183 MMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-231 |
5.48e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.81 E-value: 5.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 10 LRFDNChGKRWqnKGSKfTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKlehydnkhrvlni 89
Cdd:PRK11288 5 LSFDGI-GKTF--PGVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 90 rMVFQNSNESLNPGItlgSILEEPLKL--------NTRL----------DNQARIAKVEQTLKLVGLL--PEHRFFYrhm 149
Cdd:PRK11288 68 -MRFASTTAALAAGV---AIIYQELHLvpemtvaeNLYLgqlphkggivNRRLLNYEAREQLEHLGVDidPDTPLKY--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 150 LSDGQRQRVALARAIILNPQVIVADEPFAALdpSVRSQTVnlLMELQREL---GLGFIFISHNLGIVRHISDKILVMKQG 226
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSL--SAREIEQ--LFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDG 216
|
....*
gi 495265151 227 KVVES 231
Cdd:PRK11288 217 RYVAT 221
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
32-232 |
5.97e-20 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 86.68 E-value: 5.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGS-------IYLNERKLEHydnkhrvlNIRMVFQNSneSLNPGI 104
Cdd:TIGR01188 12 VNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTarvagydVVREPRKVRR--------SIGIVPQYA--SVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 105 TLgsilEEPLKLNTRL---DNQARIAKVEQTLKLVGLLpEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALD 181
Cdd:TIGR01188 82 TG----RENLEMMGRLyglPKDEAEERAEELLELFELG-EAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495265151 182 PSVRSQTVNLLMELqRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:TIGR01188 157 PRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEG 206
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-235 |
6.50e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 85.75 E-value: 6.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLeQPDSGSIYLNERKLEHYDnkHRVLNIRMVF--QNSNESLNPGITL 106
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWS--AAELARHRAYlsQQQTPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 GSILEEPLKLNTRlDNQARIAKVEQTLKLVGLLPEHrffyRHMLSDGQRQRVALARAII-----LNP--QVIVADEPFAA 179
Cdd:PRK03695 89 YLTLHQPDKTRTE-AVASALNEVAEALGLDDKLGRS----VNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 180 LDpsVRSQtvNLLMELQREL---GLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTD 235
Cdd:PRK03695 164 LD--VAQQ--AALDRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRD 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-230 |
7.17e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.20 E-value: 7.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 2 NDLLSVENLrfdnchGKRWqnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNER-KLEHY 80
Cdd:COG0488 313 KKVLELEGL------SKSY---GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETvKIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 81 DnkhrvlnirmvfQNsNESLNPGITLgsileeplklntrLDNQARIAKVEQTLKLVGLLpeHRF-FYRHM-------LSD 152
Cdd:COG0488 384 D------------QH-QEELDPDKTV-------------LDELRDGAPGGTEQEVRGYL--GRFlFSGDDafkpvgvLSG 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 153 GQRQRVALARAIILNPQVIVADEPFAALDPsvrsQTVNLLMELqreLgLGF----IFISHNLGIVRHISDKILVMKQGKV 228
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLDI----ETLEALEEA---L-DDFpgtvLLVSHDRYFLDRVATRILEFEDGGV 507
|
..
gi 495265151 229 VE 230
Cdd:COG0488 508 RE 509
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
29-198 |
7.97e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 84.33 E-value: 7.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKL-EHYDNKHRVlnirMVFQNSNESLNPGITlg 107
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaEQRDEPHEN----ILYLGHLPGLKPELS-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 siLEEPLKLNTRLDNQARIAkVEQTLKLVGLLP-EHRFFyrHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPsvrs 186
Cdd:TIGR01189 90 --ALENLHFWAAIHGGAQRT-IEDALAAVGLTGfEDLPA--AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK---- 160
|
170
....*....|..
gi 495265151 187 QTVNLLMELQRE 198
Cdd:TIGR01189 161 AGVALLAGLLRA 172
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-250 |
1.02e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 85.28 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKL---LVGLEQPD--SGSIYLNERKLehYDNKHRVLNIR----MVFQ 94
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEVRLFGRNI--YSPDVDPIEVRrevgMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 95 NSNESlnPGITLGSILEEPLKLNTRLDNQARIAK-VEQTLKLVGLLPE--HRFF-YRHMLSDGQRQRVALARAIILNPQV 170
Cdd:PRK14267 93 YPNPF--PHLTIYDNVAIGVKLNGLVKSKKELDErVEWALKKAALWDEvkDRLNdYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 171 IVADEPFAALDPSVRSQTVNLLMELQRELGLgfIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLV 250
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
32-232 |
1.19e-19 |
|
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: 84.69 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLN-----ERKLEHydnkhrVLNIRMVFQNSNE---SLNPG 103
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAglvpwKRRKKF------LRRIGVVFGQKTQlwwDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 itlgsileEPLKLNTRLDN------QARIAKVEQTLKLVGLL--PEHRffyrhmLSDGQRQRVALARAIILNPQVIVADE 175
Cdd:cd03267 114 --------DSFYLLAAIYDlpparfKKRLDELSELLDLEELLdtPVRQ------LSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495265151 176 PFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
36-209 |
1.29e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.45 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 36 IQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVL----NIRMVFQNSneSLNPGITLGSILE 111
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlrakHVGFVFQSF--MLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 112 EPLKLNTRLDNQARIAKVEqTLKLVGLlpEHRFfyRHM---LSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQT 188
Cdd:PRK10584 111 LPALLRGESSRQSRNGAKA-LLEQLGL--GKRL--DHLpaqLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180
....*....|....*....|.
gi 495265151 189 VNLLMELQRELGLGFIFISHN 209
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTHD 206
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
32-234 |
1.55e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.91 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSI---YLNERKLEHYDNKHRVL-----------------NIR- 90
Cdd:PRK13651 26 VSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEKVLeklviqktrfkkikkikEIRr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 91 ---MVFQNSNESLNPGITLGSILEEPLKLNTRLDNQARIAKveQTLKLVGL----LPEHRFfyrhMLSDGQRQRVALARA 163
Cdd:PRK13651 106 rvgVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAA--KYIELVGLdesyLQRSPF----ELSGGQKRRVALAGI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495265151 164 IILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKT 234
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDT 249
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
32-232 |
1.76e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.38 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQNS---NESLNPGITLGS 108
Cdd:PRK11176 362 INFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVhlfNDTIANNIAYAR 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 I-------LEEPLKLNTRLDnqaRIAKVEQTLKLV----GLlpehrffyrhMLSDGQRQRVALARAIILNPQVIVADEPF 177
Cdd:PRK11176 442 TeqysreqIEEAARMAYAMD---FINKMDNGLDTVigenGV----------LLSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 178 AALDPSVRSQTVNLLMELQRELGLgfIFISHNLGIVRHiSDKILVMKQGKVVESG 232
Cdd:PRK11176 509 SALDTESERAIQAALDELQKNRTS--LVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
32-232 |
2.08e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 83.35 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLE--QPDSGSIYLNERKLEHYDNKHRV-LNIRMVFQNSNESlnPGITLGS 108
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERArLGIFLAFQYPPEI--PGVKNAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ILEEplkLNtrldnqariakveqtlklVGLlpehrffyrhmlSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQT 188
Cdd:cd03217 97 FLRY---VN------------------EGF------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495265151 189 VNLLMELqRELGLGFIFISHNLGIVRHI-SDKILVMKQGKVVESG 232
Cdd:cd03217 144 AEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-230 |
2.19e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 86.95 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRFdnchgkRWQNKGskFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYD-NK 83
Cdd:PRK10522 323 LELRNVTF------AYQDNG--FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQpED 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 HRVLnIRMVFQNsneslnpgitlgsileepLKLNTRLDN----QARIAKVEQTLKLVGL-----LPEHRFFYRHmLSDGQ 154
Cdd:PRK10522 395 YRKL-FSAVFTD------------------FHLFDQLLGpegkPANPALVEKWLERLKMahkleLEDGRISNLK-LSKGQ 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495265151 155 RQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHiSDKILVMKQGKVVE 230
Cdd:PRK10522 455 KKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
24-210 |
1.30e-18 |
|
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: 84.72 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQNsneslnPG 103
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQD------AH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 ITLGSILEeplklNTRLDN-QARIAKVEQTLKLVGL------LP--------EHRFFyrhmLSDGQRQRVALARAIILNP 168
Cdd:TIGR02868 420 LFDTTVRE-----NLRLARpDATDEELWAALERVGLadwlraLPdgldtvlgEGGAR----LSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495265151 169 QVIVADEPFAALDPSVRSQTVNLLmeLQRELGLGFIFISHNL 210
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
29-232 |
1.57e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.53 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQNSNESlnPGIT--- 105
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAA--EGMTvre 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 106 LGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLP-EHRFFyrHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSV 184
Cdd:PRK10575 105 LVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPlAHRLV--DSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495265151 185 RSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:PRK10575 183 QVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-232 |
3.24e-18 |
|
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: 79.90 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRFDNchgKRWQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGL--EQPDSGSIYLNERKLehYDN 82
Cdd:cd03213 4 LSFRNLTVTV---KSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPL--DKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 83 KHRVLnIRMVFQNsnESLNPGITlgsileeplklntrldnqariakVEQTLKLVGLLpehrffyrHMLSDGQRQRVALAR 162
Cdd:cd03213 79 SFRKI-IGYVPQD--DILHPTLT-----------------------VRETLMFAAKL--------RGLSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495265151 163 AIILNPQVIVADEPFAALDPSvrsqTVNLLMELQREL---GLGFIFISHNL-GIVRHISDKILVMKQGKVVESG 232
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSS----SALQVMSLLRRLadtGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
24-246 |
4.51e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 80.98 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLL--VGLEQPD---SGSIYLNERKLehYDNKHRVLNIR----MVFQ 94
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNI--YSPRTDTVDLRkeigMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 95 NSNE---SLNPGITLGsileepLKLNTRLDNQARIAKVEQTLKLVGLLPE--HRFFYRHM-LSDGQRQRVALARAIILNP 168
Cdd:PRK14239 94 QPNPfpmSIYENVVYG------LRLKGIKDKQVLDEAVEKSLKGASIWDEvkDRLHDSALgLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 169 QVIVADEPFAALDPSVRSQTVNLLMELQRELGLgfIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYT 246
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKET 243
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-198 |
6.89e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 6.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRfdnCHgkrwqnKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEhyDNKH 84
Cdd:PRK13539 3 LEGEDLA---CV------RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID--DPDV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 85 RVlniRMVFQNSNESLNPGITlgsiLEEPLKLNTRLDNQARiAKVEQTLKLVGLLP-EHRFFyrHMLSDGQRQRVALARA 163
Cdd:PRK13539 72 AE---ACHYLGHRNAMKPALT----VAENLEFWAAFLGGEE-LDIAAALEAVGLAPlAHLPF--GYLSAGQKRRVALARL 141
|
170 180 190
....*....|....*....|....*....|....*
gi 495265151 164 IILNPQVIVADEPFAALDPSvrsqTVNLLMELQRE 198
Cdd:PRK13539 142 LVSNRPIWILDEPTAALDAA----AVALFAELIRA 172
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
32-197 |
7.37e-18 |
|
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: 79.07 E-value: 7.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKL-EHYDNKHRVLnIRMVFQnsneslnPGITLGSIL 110
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdFQRDSIARGL-LYLGHA-------PGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 111 EEPLKLNTRLDNQariAKVEQTLKLVGLLP-EHRFFyrHMLSDGQRQRVALARAIILNPQVIVADEPFAALDpsvrSQTV 189
Cdd:cd03231 91 LENLRFWHADHSD---EQVEEALARVGLNGfEDRPV--AQLSAGQQRRVALARLLLSGRPLWILDEPTTALD----KAGV 161
|
....*...
gi 495265151 190 NLLMELQR 197
Cdd:cd03231 162 ARFAEAMA 169
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
32-176 |
7.74e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERK----LE---HYDNKHRVL-NIRMVFQNSNESLNPG 103
Cdd:COG0488 17 VSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrigyLPqepPLDDDLTVLdTVLDGDAELRALEAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 ITLGSILEEPLKLNTRLDN-QARI---------AKVEQTLKLVGLLPEHrfFYRHM--LSDGQRQRVALARAIILNPQVI 171
Cdd:COG0488 97 EELEAKLAEPDEDLERLAElQEEFealggweaeARAEEILSGLGFPEED--LDRPVseLSGGWRRRVALARALLSEPDLL 174
|
....*
gi 495265151 172 VADEP 176
Cdd:COG0488 175 LLDEP 179
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-235 |
1.05e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.16 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQ--PDSGSIYLNE---RKLEHYDNKHRV-----------L 87
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHValcEKCGYVERPSKVgepcpvcggtlE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 88 NIRMVFQNSNESLNPGIT--LGSILEEPLKL---NTRLDNQAR------------IAKVEQTLKLVGLlpEHRFFyrHM- 149
Cdd:TIGR03269 91 PEEVDFWNLSDKLRRRIRkrIAIMLQRTFALygdDTVLDNVLEaleeigyegkeaVGRAVDLIEMVQL--SHRIT--HIa 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 150 --LSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGK 227
Cdd:TIGR03269 167 rdLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGE 246
|
....*...
gi 495265151 228 VVESGKTD 235
Cdd:TIGR03269 247 IKEEGTPD 254
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
32-238 |
1.05e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.05 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLN----------------IRMVFQN 95
Cdd:PRK13631 45 ISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITnpyskkiknfkelrrrVSMVFQF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 96 SNESLNPGITLGSILEEPLKLNTRLDNQARIAKveqtLKLVGLLPEHRFFYRH--MLSDGQRQRVALARAIILNPQVIVA 173
Cdd:PRK13631 125 PEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAK----FYLNKMGLDDSYLERSpfGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 174 DEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIF 238
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
24-227 |
1.18e-17 |
|
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: 77.10 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIylnerklehydnkhrvlnirmvfqnsneslnpg 103
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 itlgsileeplklntRLDNQARIAKVEQtlklvgllpehrffyrhmLSDGQRQRVALARAIILNPQVIVADEPFAALDPs 183
Cdd:cd03221 58 ---------------TWGSTVKIGYFEQ------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL- 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495265151 184 vrsQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGK 227
Cdd:cd03221 104 ---ESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
24-238 |
1.19e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 79.67 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQnsnESLNP- 102
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ---HHLTPe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 103 GITLGSILE---EP-LKLNTRLDNQARiAKVEQTLKLVGL--LPEHRFfyrHMLSDGQRQRVALARAIILNPQVIVADEP 176
Cdd:PRK11231 90 GITVRELVAygrSPwLSLWGRLSAEDN-ARVNQAMEQTRInhLADRRL---TDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495265151 177 FAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIF 238
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
32-233 |
1.24e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.79 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYdnkhrvlnirmvfqnSNESLNPGITLGS--- 108
Cdd:PRK11160 359 LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY---------------SEAALRQAISVVSqrv 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 -ILEEPLKLNTRL-DNQARIAKVEQTLKLVGL--LPEH------------RffyrhMLSDGQRQRVALARAIILNPQVIV 172
Cdd:PRK11160 424 hLFSATLRDNLLLaAPNASDEALIEVLQQVGLekLLEDdkglnawlgeggR-----QLSGGEQRRLGIARALLHDAPLLL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495265151 173 ADEPFAALDPSVRSQTVNLLMELQRELGLgfIFISHNLGIVRHIsDKILVMKQGKVVESGK 233
Cdd:PRK11160 499 LDEPTEGLDAETERQILELLAEHAQNKTV--LMITHRLTGLEQF-DRICVMDNGQIIEQGT 556
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
29-234 |
1.34e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.67 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDS---------GSIYLNERKLEHYDNKHRVlNIRMVFQNSNE- 98
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIRKSRA-NTGYIFQQFNLv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 99 ---SLNPGITLGSILEEPL-KLNTRLDNQARIAKVEQTLKLVGLLpehRFFYRHM--LSDGQRQRVALARAIILNPQVIV 172
Cdd:PRK09984 99 nrlSVLENVLIGALGSTPFwRTCFSWFTREQKQRALQALTRVGMV---HFAHQRVstLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495265151 173 ADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKT 234
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-235 |
1.45e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 80.52 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLN-----ERKLEHydnkhrVLNIRMVF-QNSN-------- 97
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgyvpfKRRKEF------ARRIGVVFgQRSQlwwdlpai 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 98 ESLNpgiTLGSILEEPlklntrlDNQARiakveQTLK-LVGLLPEHRFFYR--HMLSDGQRQRVALARAIILNPQVIVAD 174
Cdd:COG4586 115 DSFR---LLKAIYRIP-------DAEYK-----KRLDeLVELLDLGELLDTpvRQLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495265151 175 EPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTD 235
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLE 240
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-225 |
2.75e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.62 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 1 MNDLLSVENLRFdnchgkrwqNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERklehy 80
Cdd:PRK09544 1 MTSLVSLENVSV---------SFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 81 dnkhrvLNIRMVFQNsneslnpgITLGSILEEPLKLNTRLDNQARIAKVEQTLKLV--GLLPEHRFfyrHMLSDGQRQRV 158
Cdd:PRK09544 67 ------LRIGYVPQK--------LYLDTTLPLTVNRFLRLRPGTKKEDILPALKRVqaGHLIDAPM---QKLSGGETQRV 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495265151 159 ALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQ 225
Cdd:PRK09544 130 LLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
32-232 |
7.73e-17 |
|
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: 76.68 E-value: 7.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQNsneslnPGITLGSIle 111
Cdd:cd03369 27 VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQD------PTLFSGTI-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 112 eplKLNTRLDNQARIAKVEQTLKLV--GLlpehrffyrhMLSDGQRQRVALARAIILNPQVIVADEPFAALDpsvrSQTV 189
Cdd:cd03369 99 ---RSNLDPFDEYSDEEIYGALRVSegGL----------NLSQGQRQLLCLARALLKRPRVLVLDEATASID----YATD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495265151 190 NLLMELQREL--GLGFIFISHNLGIVRHIsDKILVMKQGKVVESG 232
Cdd:cd03369 162 ALIQKTIREEftNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-229 |
1.32e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLRFDNCHGKRwqnkgskfTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYD-- 81
Cdd:COG3845 257 VLEVENLSVRDDRGVP--------ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSpr 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 82 --NKHRVLNI---RM---------VFQNsneslnpgITLGSILEEPLKLNTRLDNQARIAKVEQTLKlvgllpehRFFYR 147
Cdd:COG3845 329 erRRLGVAYIpedRLgrglvpdmsVAEN--------LILGRYRRPPFSRGGFLDRKAIRAFAEELIE--------EFDVR 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 148 --------HMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELqRELGLGFIFISHNLGIVRHISDK 219
Cdd:COG3845 393 tpgpdtpaRSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDR 471
|
250
....*....|
gi 495265151 220 ILVMKQGKVV 229
Cdd:COG3845 472 IAVMYEGRIV 481
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
32-232 |
2.05e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 76.22 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGleQPD----SGSIYLNERKLEHYDNKHRV-LNIRMVFQNSNESlnPGITL 106
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERAhLGIFLAFQYPIEI--PGVSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 GSILEepLKLNTR--------LDNQARIAKVEQTLKLVGLLPehRFFYRHM---LSDGQRQRVALARAIILNPQVIVADE 175
Cdd:CHL00131 102 ADFLR--LAYNSKrkfqglpeLDPLEFLEIINEKLKLVGMDP--SFLSRNVnegFSGGEKKRNEILQMALLDSELAILDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495265151 176 PFAALDPS---VRSQTVNLLMELQRelglGFIFISHNLGIVRHIS-DKILVMKQGKVVESG 232
Cdd:CHL00131 178 TDSGLDIDalkIIAEGINKLMTSEN----SIILITHYQRLLDYIKpDYVHVMQNGKIIKTG 234
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
32-235 |
2.39e-16 |
|
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: 75.51 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKhrvlnirmvfqnsneslnpgiTLGSILE 111
Cdd:TIGR03740 19 ISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLH---------------------KIGSLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 112 EP-----------LKLNTRLDNQARiAKVEQTLKLVGLlpEHRFFYR-HMLSDGQRQRVALARAIILNPQVIVADEPFAA 179
Cdd:TIGR03740 78 SPplyenltarenLKVHTTLLGLPD-SRIDEVLNIVDL--TNTGKKKaKQFSLGMKQRLGIAIALLNHPKLLILDEPTNG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495265151 180 LDPsVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTD 235
Cdd:TIGR03740 155 LDP-IGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKIN 209
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-250 |
3.23e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 76.29 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 26 KFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIY-----LNERKLEHYDNkhrVLNIR----MVFQNS 96
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIFNYRD---VLEFRrrvgMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 97 NESlnPGITLGSILE--EPLKLNTRLD----NQARIAKVEQTLKLVGLLPEHRFfyrhMLSDGQRQRVALARAIILNPQV 170
Cdd:PRK14271 111 NPF--PMSIMDNVLAgvRAHKLVPRKEfrgvAQARLTEVGLWDAVKDRLSDSPF----RLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 171 IVADEPFAALDPSVRSQTVNLLMELQRELGLgfIFISHNLGIVRHISDKILVMKQGKVVESGKTDVIFHWPKDEYTKKLV 250
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTV--IIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-233 |
3.27e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.38 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 3 DLLSVENLRFDNCHgKRWqnkGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDN 82
Cdd:PRK13537 1 GPMSVAPIDFRNVE-KRY---GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 83 KHRvLNIRMVFQNSNesLNPGITLgsilEEPLKLNTR---LDNQARIAKVEQTLKLVGLlpEHRFFYR-HMLSDGQRQRV 158
Cdd:PRK13537 77 HAR-QRVGVVPQFDN--LDPDFTV----RENLLVFGRyfgLSAAAARALVPPLLEFAKL--ENKADAKvGELSGGMKRRL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 159 ALARAIILNPQVIVADEPFAALDPSVRsqtvNLLMELQREL---GLGFIFISHNLGIVRHISDKILVMKQGKVVESGK 233
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQAR----HLMWERLRSLlarGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGA 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-228 |
3.97e-16 |
|
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: 77.56 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENL---RFDNCHGKRWQNkgskftlgpINFSIQAGETLAIVGANGSGKSLLAKLLVGL-EQPDSGSIYLNERKLEH 79
Cdd:TIGR02633 257 ILEARNLtcwDVINPHRKRVDD---------VSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 80 YD----------------NKHRVLNIRMVFQNsneslnpgITLgSILEEPLKLnTRLDNQARIAKVEQTLKLVGLLPEHR 143
Cdd:TIGR02633 328 RNpaqairagiamvpedrKRHGIVPILGVGKN--------ITL-SVLKSFCFK-MRIDAAAELQIIGSAIQRLKVKTASP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 144 FFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVM 223
Cdd:TIGR02633 398 FLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVI 476
|
....*
gi 495265151 224 KQGKV 228
Cdd:TIGR02633 477 GEGKL 481
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-252 |
5.05e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.46 E-value: 5.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDS-----GSI-YLNERKLEHYDNKHRVL-NIRMVFQNSN---ESLN 101
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVeFFNQNIYERRVNLNRLRrQVSMVHPKPNlfpMSVY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 102 PGITLG-SILEEPLKLntRLDNqariaKVEQTLKLVGLLPE--HRFFYRHM-LSDGQRQRVALARAIILNPQVIVADEPF 177
Cdd:PRK14258 106 DNVAYGvKIVGWRPKL--EIDD-----IVESALKDADLWDEikHKIHKSALdLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 178 AALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQ-----GKVVESGKTDVIFHWPKDEYTKKLVHA 252
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTREYVLS 258
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
34-232 |
7.81e-16 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 74.12 E-value: 7.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 34 FSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSI---------------YLNERKLEHYDN----KHRVLNIRMvfq 94
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVkvagaspgkgwrhigYVPQRHEFAWDFpisvAHTVMSGRT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 95 nsneslnpgitlGSIleEPLKLNTRLDNQAriakVEQTLKLVGLlpehrffyRHM-------LSDGQRQRVALARAIILN 167
Cdd:TIGR03771 78 ------------GHI--GWLRRPCVADFAA----VRDALRRVGL--------TELadrpvgeLSGGQRQRVLVARALATR 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 168 PQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMkQGKVVESG 232
Cdd:TIGR03771 132 PSVLLLDEPFTGLDMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRVVLL-NGRVIADG 194
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-208 |
8.02e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 76.38 E-value: 8.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 2 NDLLSVENLRFDNCHGKRwqnkgskfTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKlehyd 81
Cdd:COG4178 360 DGALALEDLTLRTPDGRP--------LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA----- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 82 nkhrvlniRMVF--QNsneslnPGITLGSiLEEPL---KLNTRLDNqariAKVEQTLKLVGLlpeHRFFYR--------H 148
Cdd:COG4178 427 --------RVLFlpQR------PYLPLGT-LREALlypATAEAFSD----AELREALEAVGL---GHLAERldeeadwdQ 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495265151 149 MLSDGQRQRVALARAIILNPQVIVADEPFAALDPsvrsQTVNLLME-LQREL-GLGFIFISH 208
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE----ENEAALYQlLREELpGTTVISVGH 542
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
24-250 |
8.21e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.82 E-value: 8.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAK-------LLVGLEQpdSGSIYLNERKLehYDNKHRVLNIR----MV 92
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNL--YAPDVDPVEVRrrigMV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 93 FQNSN---ESLNPGITLGSileeplKLNTRLDNQARIakVEQTLKLVGLLPEHRFFYRH---MLSDGQRQRVALARAIIL 166
Cdd:PRK14243 97 FQKPNpfpKSIYDNIAYGA------RINGYKGDMDEL--VERSLRQAALWDEVKDKLKQsglSLSGGQQQRLCIARAIAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 167 NPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLgfIFISHNLGIVRHISDKILVM---------KQGKVVESGKTDVI 237
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKI 246
|
250
....*....|...
gi 495265151 238 FHWPKDEYTKKLV 250
Cdd:PRK14243 247 FNSPQQQATRDYV 259
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
23-249 |
9.66e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.16 E-value: 9.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 23 KGSKfTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNE--------------------------RK 76
Cdd:PRK10895 14 KGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplhararrgigylpqeasifRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 77 LEHYDNKHRVLNIRmvfqnsnESLNPgitlgsilEEPLKLNTRLDNQARIAKVEQTLKlvgllpehrffyrHMLSDGQRQ 156
Cdd:PRK10895 93 LSVYDNLMAVLQIR-------DDLSA--------EQREDRANELMEEFHIEHLRDSMG-------------QSLSGGERR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 157 RVALARAIILNPQVIVADEPFAALDPsVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDV 236
Cdd:PRK10895 145 RVEIARALAANPKFILLDEPFAGVDP-ISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTE 223
|
250
....*....|...
gi 495265151 237 IFhwpKDEYTKKL 249
Cdd:PRK10895 224 IL---QDEHVKRV 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-237 |
1.63e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.87 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIY-----------LNERKL---EHYDNKHRVLNI 89
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvpararLARARIgvvPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 90 R---MVF-------QNSNESLNPgitlgSILEeplklNTRLDNQARiAKVEQtlklvgllpehrffyrhmLSDGQRQRVA 159
Cdd:PRK13536 132 RenlLVFgryfgmsTREIEAVIP-----SLLE-----FARLESKAD-ARVSD------------------LSGGMKRRLT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 160 LARAIILNPQVIVADEPFAALDPSVRsqtvNLLMELQREL---GLGFIFISHNLGIVRHISDKILVMKQG-KVVESGKTD 235
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHAR----HLIWERLRSLlarGKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGRPHA 258
|
..
gi 495265151 236 VI 237
Cdd:PRK13536 259 LI 260
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
29-208 |
2.33e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.42 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYlnerklehydnKHRVLNIRMVFQNsneslnPGITLGs 108
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-----------MPEGEDLLFLPQR------PYLPLG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ileeplklntrldnqariakveqTLKLVGLLPehrffYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPsvrsQT 188
Cdd:cd03223 79 -----------------------TLREQLIYP-----WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ES 126
|
170 180
....*....|....*....|
gi 495265151 189 VNLLMELQRELGLGFIFISH 208
Cdd:cd03223 127 EDRLYQLLKELGITVISVGH 146
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
24-232 |
2.81e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.49 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQNSNESLNpg 103
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFE-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 ITLGSILE---EPLKlnTRLD--NQARIAKVEQTLKLVGLlpeHRFFYRHM--LSDGQRQRVALARAIILNPQVIVADEP 176
Cdd:PRK09536 92 FDVRQVVEmgrTPHR--SRFDtwTETDRAAVERAMERTGV---AQFADRPVtsLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495265151 177 FAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-232 |
7.05e-15 |
|
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: 71.53 E-value: 7.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 19 RWQNKGSKFT--------LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPD---SGSIYLNERKLEHYDNKHRVL 87
Cdd:cd03234 5 PWWDVGLKAKnwnkyariLNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 88 NIRmvfqnSNESLNPGITLgsilEE------PLKLNTRLDNQARIAKVEQT-LKLVGLLPehrffYRHM----LSDGQRQ 156
Cdd:cd03234 85 YVR-----QDDILLPGLTV----REtltytaILRLPRKSSDAIRKKRVEDVlLRDLALTR-----IGGNlvkgISGGERR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495265151 157 RVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGI-VRHISDKILVMKQGKVVESG 232
Cdd:cd03234 151 RVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQPRSdLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
34-256 |
2.67e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.29 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 34 FSIQAGETLAIVGANGSGKSLLAKLLVG-------------------LEQ--P--DSGSIY------LNE--RKLEHYdn 82
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGevllddgriiyeqdlivarLQQdpPrnVEGTVYdfvaegIEEqaEYLKRY-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 83 kHRVLniRMVFQNSNESLnpgitlgsiLEEPLKLNTRLDNQ------ARIAkveQTLKLVGLLPEHRFfyrHMLSDGQRQ 156
Cdd:PRK11147 102 -HDIS--HLVETDPSEKN---------LNELAKLQEQLDHHnlwqleNRIN---EVLAQLGLDPDAAL---SSLSGGWLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 157 RVALARAIILNPQVIVADEPFAALDpsvrSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVEsgktdv 236
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVS------ 233
|
250 260
....*....|....*....|
gi 495265151 237 ifhWPKDeYTKKLVHAHQAL 256
Cdd:PRK11147 234 ---YPGN-YDQYLLEKEEAL 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
32-227 |
4.01e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.50 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLeQPD---SGSIYLNERKLEHY---DNKHRvlNIRMVFQN----SNESLN 101
Cdd:PRK13549 24 VSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASnirDTERA--GIAIIHQElalvKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 102 PGITLGSileEPLKlNTRLDNQARIAKVEQTLKLVGLL--PEHRFFYrhmLSDGQRQRVALARAIILNPQVIVADEPFAA 179
Cdd:PRK13549 101 ENIFLGN---EITP-GGIMDYDAMYLRAQKLLAQLKLDinPATPVGN---LGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495265151 180 LDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGK 227
Cdd:PRK13549 174 LTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-232 |
5.78e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.55 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLRFDnchgkrWQNKGSKFTLGPINFSIQAGETLAIVGANGSGK-SLLAKLLVGLEQPDSGSIYLneRKLEHYdnk 83
Cdd:PLN03232 615 ISIKNGYFS------WDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGELSHAETSSVVI--RGSVAY--- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 hrVLNIRMVFqnsNESLNPGITLGSILEeplklNTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHM-LSDGQRQRVALAR 162
Cdd:PLN03232 684 --VPQVSWIF---NATVRENILFGSDFE-----SERYWRAIDVTALQHDLDLLPGRDLTEIGERGVnISGGQKQRVSMAR 753
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495265151 163 AIILNPQVIVADEPFAALDPSVRSQTVNLLM--ELQrelGLGFIFISHNLGIVRHIsDKILVMKQGKVVESG 232
Cdd:PLN03232 754 AVYSNSDIYIFDDPLSALDAHVAHQVFDSCMkdELK---GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEG 821
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
35-227 |
6.28e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.80 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 35 SIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIylnerkleHYDNKHRVLN---------IRMVFQNSNesLNPGIT 105
Cdd:PRK10762 26 NVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSI--------LYLGKEVTFNgpkssqeagIGIIHQELN--LIPQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 106 ------LGsilEEPLKLNTRLDNQARIAKVEQTLKLVGLlpehRFFYRHMLSD---GQRQRVALARAIILNPQVIVADEP 176
Cdd:PRK10762 96 iaenifLG---REFVNRFGRIDWKKMYAEADKLLARLNL----RFSSDKLVGElsiGEQQMVEIAKVLSFESKVIIMDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495265151 177 FAALDPSVRSQTVNLLMELqRELGLGFIFISHNLGIVRHISDKILVMKQGK 227
Cdd:PRK10762 169 TDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
33-237 |
6.51e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.81 E-value: 6.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 33 NFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGsiylnerklEHYDNKHRVlnIRMVFQ------------NSNESL 100
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG---------ERQSQFSHI--TRLSFEqlqklvsdewqrNNTDML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 101 NP-----GITLGSILEEPLKlntrldNQARIAKVEQTLKLVGLLpEHRFFYrhmLSDGQRQRVALARAIILNPQVIVADE 175
Cdd:PRK10938 92 SPgeddtGRTTAEIIQDEVK------DPARCEQLAQQFGITALL-DRRFKY---LSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495265151 176 PFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTDVI 237
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
32-230 |
7.73e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.45 E-value: 7.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLE--QPDSGSIYLnerklehydnkhrvlnirmvfqnsneslnPGITLGSi 109
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV-----------------------------PDNQFGR- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 110 lEEPLklntrLDNQARIAKVEQTLKL---VGLlpEHRFFYR---HMLSDGQRQRVALARAIILNPQVIVADEPFAALDPS 183
Cdd:COG2401 99 -EASL-----IDAIGRKGDFKDAVELlnaVGL--SDAVLWLrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495265151 184 VRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMK-QGKVVE 230
Cdd:COG2401 171 TAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVgYGGVPE 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-229 |
9.83e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 9.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 31 PINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERklehydnkhrvlniRMVFQNSNESLNPGITL---- 106
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK--------------PIDIRSPRDAIRAGIMLcped 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 --------GSILEEPLKLNTR---------LDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQRQRVALARAIILNPQ 169
Cdd:PRK11288 337 rkaegiipVHSVADNINISARrhhlragclINNRWEAENADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 170 VIVADEPFAALDPSVRSQTVNLLMELQrELGLGFIFISHNLGIVRHISDKILVMKQGKVV 229
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-228 |
1.84e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENL---RFDNCHGKRWQNkgskftlgpINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDS-GSIYLNERKLEhy 80
Cdd:PRK13549 260 LEVRNLtawDPVNPHIKRVDD---------VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVK-- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 81 dnkhrvlnIRmvfqNSNESLNPGITL--------GSILEEPLKLN------------TRLDNQARIAKVEQTLKLVGLLP 140
Cdd:PRK13549 329 --------IR----NPQQAIAQGIAMvpedrkrdGIVPVMGVGKNitlaaldrftggSRIDDAAELKTILESIQRLKVKT 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 141 EHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKI 220
Cdd:PRK13549 397 ASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRV 475
|
....*...
gi 495265151 221 LVMKQGKV 228
Cdd:PRK13549 476 LVMHEGKL 483
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-232 |
2.59e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.38 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 20 WQNKGSKFTLGPINFSIQAGETLAIVGANGSGK-SLLAKLLVGLEQPDSGSIYLneRKLEHYdnkhrVLNIRMVFqnsNE 98
Cdd:PLN03130 624 WDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVI--RGTVAY-----VPQVSWIF---NA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 99 SLNPGITLGSILEEPlklntRLDNQARIAKVEQTLKLvglLPEH---RFFYRHM-LSDGQRQRVALARAIILNPQVIVAD 174
Cdd:PLN03130 694 TVRDNILFGSPFDPE-----RYERAIDVTALQHDLDL---LPGGdltEIGERGVnISGGQKQRVSMARAVYSNSDVYIFD 765
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 175 EPFAALDPSVRSQTVNLLmeLQREL-GLGFIFISHNLGIVRHIsDKILVMKQGKVVESG 232
Cdd:PLN03130 766 DPLSALDAHVGRQVFDKC--IKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
29-229 |
2.67e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.60 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKhRVLNI--------RMVFqnSNESL 100
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA-KIMREavaivpegRRVF--SRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 101 NPGITLGSILEEplklntRLDNQARIAKVEQtlkLVGLLPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAAL 180
Cdd:PRK11614 98 EENLAMGGFFAE------RDQFQERIKWVYE---LFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495265151 181 DPSVRSQTVNLLMELqRELGLGFIFISHNLGIVRHISDKILVMKQGKVV 229
Cdd:PRK11614 169 APIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
25-245 |
3.30e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.97 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 25 SKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIY-----LNERKLEHYDNKHRVLNiRMVFQNSNES 99
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfhdipLTKLQLDSWRSRLAVVS-QTPFLFSDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 100 LNpGITLGsileEPLKLNTRLDNQARIAKV-EQTLKlvglLPEHrffYRH-------MLSDGQRQRVALARAIILNPQVI 171
Cdd:PRK10789 406 AN-NIALG----RPDATQQEIEHVARLASVhDDILR----LPQG---YDTevgergvMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 172 VADEPFAALDpsvrSQTVNLLMELQRELGLG--FIFISHNLGIVRHiSDKILVMKQGKVVESGKTDVIFH---WPKDEY 245
Cdd:PRK10789 474 ILDDALSAVD----GRTEHQILHNLRQWGEGrtVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQqsgWYRDMY 547
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
28-226 |
3.37e-13 |
|
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: 66.97 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 28 TLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLN-----ERKLEHYDNKHRvLNIRMVFQNS---NES 99
Cdd:cd03290 16 TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknesEPSFEATRSRNR-YSVAYAAQKPwllNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 100 LNPGITLGSileePLklntrldNQARIAKVEQTLKL---VGLLP---EHRFFYRHM-LSDGQRQRVALARAIILNPQVIV 172
Cdd:cd03290 95 VEENITFGS----PF-------NKQRYKAVTDACSLqpdIDLLPfgdQTEIGERGInLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 173 ADEPFAALDPSVRSQTVNL-LMELQRELGLGFIFISHNLGIVRHiSDKILVMKQG 226
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
29-182 |
4.50e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.41 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERkleHYDNKHRVLNirMVFQNSNESLNPGItlgS 108
Cdd:PRK13543 27 FGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRSRF--MAYLGHLPGLKADL---S 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 109 ILEEPLKLNTRLDNQARiAKVEQTLKLVGLLPEHRFFYRHmLSDGQRQRVALARaIILNPQVI-VADEPFAALDP 182
Cdd:PRK13543 99 TLENLHFLCGLHGRRAK-QMPGSALAIVGLAGYEDTLVRQ-LSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDL 170
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-228 |
5.80e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNerklehydnkHRVLNIRmvfqNSNESLNPGITL----- 106
Cdd:PRK10762 271 VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLD----------GHEVVTR----SPQDGLANGIVYisedr 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 ---GSILEEPLKLNT-------------RLDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQRQRVALARAIILNPQV 170
Cdd:PRK10762 337 krdGLVLGMSVKENMsltalryfsraggSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 171 IVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKV 228
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
32-232 |
1.42e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.07 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDnkhrvLNIRM----------------VFQN 95
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD-----IATRRrvgymsqafslygeltVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 96 sneslnpgitlgsileepLKLNTRL------DNQARIAKVEQTLKLVGllpehrffYRHMLSD----GQRQRVALARAII 165
Cdd:NF033858 360 ------------------LELHARLfhlpaaEIAARVAEMLERFDLAD--------VADALPDslplGIRQRLSLAVAVI 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495265151 166 LNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGfIFIShnlgivRHI------SDKILVMKQGKVVESG 232
Cdd:NF033858 414 HKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIS------THFmneaerCDRISLMHAGRVLASD 479
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-222 |
1.47e-12 |
|
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: 66.73 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 35 SIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNER------KLEHyDNKHRVlniRMVFqnsnESLNPGITLGS 108
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisykpqYISP-DYDGTV---EEFL----RSANTDDFGSS 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ILE----EPLKLNTRLDNQariakveqtlklvglLPEhrffyrhmLSDGQRQRVALARAIILNPQVIVADEPFAALDPSV 184
Cdd:COG1245 434 YYKteiiKPLGLEKLLDKN---------------VKD--------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180 190
....*....|....*....|....*....|....*...
gi 495265151 185 RSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILV 222
Cdd:COG1245 491 RLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-229 |
1.55e-12 |
|
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: 66.77 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDS--GSIYLNERKLE--HYDNKHRVlNIRMVFQN---- 95
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKasNIRDTERA-GIVIIHQEltlv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 96 SNESLNPGITLGSILEEPlklNTRLDNQARIAKVEQTLKLVGL--LPEHRFFYRhmLSDGQRQRVALARAiiLNPQV--I 171
Cdd:TIGR02633 91 PELSVAENIFLGNEITLP---GGRMAYNAMYLRAKNLLRELQLdaDNVTRPVGD--YGGGQQQLVEIAKA--LNKQArlL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 172 VADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVV 229
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
32-231 |
2.85e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.97 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDS--GSIylnerkleHYDNKHRVlnirmvFQNSNESLNPGIT---- 105
Cdd:NF040905 20 VNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEI--------LFDGEVCR------FKDIRDSEALGIViihq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 106 ------LGSILE------EPLKlNTRLDNQARIAKVEQTLKLVGL--LPEHRffyrhmLSD---GQRQRVALARAIILNP 168
Cdd:NF040905 86 elalipYLSIAEniflgnERAK-RGVIDWNETNRRARELLAKVGLdeSPDTL------VTDigvGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495265151 169 QVIVADEPFAALDPSVRSQTVNLLMELqRELGLGFIFISHNLGIVRHISDKILVMKQGKVVES 231
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-222 |
3.15e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.99 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 36 IQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNER------KLEHyDNKHRV-LNIRMVFQNSNES-LNPGITlg 107
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykpqYIKP-DYDGTVeDLLRSITDDLGSSyYKSEII-- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 sileEPLKLNTRLDNQariakveqtlklvglLPEhrffyrhmLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQ 187
Cdd:PRK13409 439 ----KPLQLERLLDKN---------------VKD--------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180 190
....*....|....*....|....*....|....*
gi 495265151 188 TVNLLMELQRELGLGFIFISHNLGIVRHISDKILV 222
Cdd:PRK13409 492 VAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-229 |
5.20e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.14 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEhydnkhrvlnirmvFQNSNESLNPGItlgS 108
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID--------------FKSSKEALENGI---S 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ILEEPLklntrldNQARIAKVEQTLKLvGLLPEHRFFYRH-------------------------MLSDGQRQRVALARA 163
Cdd:PRK10982 77 MVHQEL-------NLVLQRSVMDNMWL-GRYPTKGMFVDQdkmyrdtkaifdeldididprakvaTLSVSQMQMIEIAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 164 IILNPQVIVADEPFAALDpsvrSQTVNLLMELQREL---GLGFIFISHNLGIVRHISDKILVMKQGKVV 229
Cdd:PRK10982 149 FSYNAKIVIMDEPTSSLT----EKEVNHLFTIIRKLkerGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-232 |
7.10e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 65.35 E-value: 7.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 28 TLGPINFSIQAGETLAIVGANGSGKS-LLAKLLVGLEqpdsgsiylnerKLE-HYDNKHRVLNIRMVFQNSNESLNPGIT 105
Cdd:TIGR00957 653 TLNGITFSIPEGALVAVVGQVGCGKSsLLSALLAEMD------------KVEgHVHMKGSVAYVPQQAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 106 LGSILEEPlklntrldnqariaKVEQTLKLVGLLPEHRFFYRH----------MLSDGQRQRVALARAIILNPQVIVADE 175
Cdd:TIGR00957 721 FGKALNEK--------------YYQQVLEACALLPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 176 PFAALDPSVRSQTVNLLMELQREL-GLGFIFISHNLGIVRHIsDKILVMKQGKVVESG 232
Cdd:TIGR00957 787 PLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-235 |
8.75e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 64.68 E-value: 8.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 17 GKRWQNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPD---SGSIYLNERKLEHydnkhRVLNIRMVF 93
Cdd:TIGR00955 29 GCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDA-----KEMRAISAY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 94 QNSNESLNPGITLGSIL--EEPLKLNTRLDNQARIAKVEQTLKLVGLLP----------EHRffyrhMLSDGQRQRVALA 161
Cdd:TIGR00955 104 VQQDDLFIPTLTVREHLmfQAHLRMPRRVTKKEKRERVDEVLQALGLRKcantrigvpgRVK-----GLSGGERKRLAFA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 162 RAIILNPQVIVADEPFAALDPSVRSQTVNLLMEL-QRelglGFIFIshnlgIVRH--------ISDKILVMKQGKVVESG 232
Cdd:TIGR00955 179 SELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQK----GKTII-----CTIHqpsselfeLFDKIILMAEGRVAYLG 249
|
...
gi 495265151 233 KTD 235
Cdd:TIGR00955 250 SPD 252
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-208 |
8.99e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.66 E-value: 8.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 4 LLSVENLRFDnchgkrWQNKgskFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLehyDNK 83
Cdd:PRK13540 1 MLDVIELDFD------YHDQ---PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI---KKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 84 HRVLNIRMVFQNSNESLNPGITLGSILEEPLKL---NTRLDNQARIAKVEQTLKlvgllpehrfFYRHMLSDGQRQRVAL 160
Cdd:PRK13540 69 LCTYQKQLCFVGHRSGINPYLTLRENCLYDIHFspgAVGITELCRLFSLEHLID----------YPCGLLSSGQKRQVAL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495265151 161 ARAIILNPQVIVADEPFAALDpSVRSQTVNLLMELQRELGLGFIFISH 208
Cdd:PRK13540 139 LRLWMSKAKLWLLDEPLVALD-ELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-208 |
1.51e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.80 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNER-KLEHYDNKHRVLN-IRMVFQNSNESLN 101
Cdd:TIGR03719 333 GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvKLAYVDQSRDALDpNKTVWEEISGGLD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 102 PgITLGSIleeplKLNTRL----------DNQariakveqtlKLVGllpehrffyrhMLSDGQRQRVALARAIILNPQVI 171
Cdd:TIGR03719 413 I-IKLGKR-----EIPSRAyvgrfnfkgsDQQ----------KKVG-----------QLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495265151 172 VADEPFAALDpsvrsqtVNLLMELQRELgLGF----IFISH 208
Cdd:TIGR03719 466 LLDEPTNDLD-------VETLRALEEAL-LNFagcaVVISH 498
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
24-226 |
4.19e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.88 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQNSneslnpg 103
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTP------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 itlgSILEEPLKLNTRLDNQARIAKVEQTLKLVGL----LPEHRFFYR-HMLSDGQRQRVALARAIILNPQVIVADEPFA 178
Cdd:PRK10247 91 ----TLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLerfaLPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495265151 179 ALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQG 226
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
39-233 |
7.73e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.82 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 39 GETLAIVGANGSGKSLLAKLLVGLEQPDS--GSIYLNERKLEHYDNKhrvlniRMVFQNSNESLNPGITLGSILE--EPL 114
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILK------RTGFVTQDDILYPHLTVRETLVfcSLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 115 KLNTRLDNQARIAKVEQTLKLVGLLP-EHRF----FYRHmLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTV 189
Cdd:PLN03211 168 RLPKSLTKQEKILVAESVISELGLTKcENTIignsFIRG-ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495265151 190 NLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGK 233
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGK 290
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-249 |
2.29e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.64 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYlnerklehydnkhRVLNIRM-VFQNSNESlnpGITLGSil 110
Cdd:PLN03073 528 LNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-------------RSAKVRMaVFSQHHVD---GLDLSS-- 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 111 eEPLKLNTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVN 190
Cdd:PLN03073 590 -NPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQ 668
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 191 LLMELQRelglGFIFISHNLGIVRHISDKILVMKQGKVVEsgktdviFHWPKDEYTKKL 249
Cdd:PLN03073 669 GLVLFQG----GVLMVSHDEHLISGSVDELWVVSEGKVTP-------FHGTFHDYKKTL 716
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
32-235 |
2.85e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDnkhrvlnirmvfqnSNESLNPGITLgsILE 111
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHN--------------ANEAINHGFAL--VTE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 112 EP----LKLNTRLDNQARIAKVEQTLKLVGLL--------------------PEHRffyRHM--LSDGQRQRVALARAII 165
Cdd:PRK10982 331 ERrstgIYAYLDIGFNSLISNIRNYKNKVGLLdnsrmksdtqwvidsmrvktPGHR---TQIgsLSGGNQQKVIIGRWLL 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495265151 166 LNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKV---VESGKTD 235
Cdd:PRK10982 408 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVagiVDTKTTT 479
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
32-234 |
2.97e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLE--QPDSGSIYLNER-------KLEHYDNKHRVL--NIR---------- 90
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlKNDHHIVFKNEHtndmtneQDYQGDEEQNVGmkNVNefsltkeggs 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 91 ----MVFQNSNESLNPGI-----------TLGSIL-EEPL-------------KLNTRLDNQARIAKVEQTLKLVGLLPE 141
Cdd:PTZ00265 1267 gedsTVFKNSGKILLDGVdicdynlkdlrNLFSIVsQEPMlfnmsiyenikfgKEDATREDVKRACKFAAIDEFIESLPN 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 142 HRFF----YRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHiS 217
Cdd:PTZ00265 1347 KYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-S 1425
|
250 260
....*....|....*....|.
gi 495265151 218 DKILVM----KQGKVVESGKT 234
Cdd:PTZ00265 1426 DKIVVFnnpdRTGSFVQAHGT 1446
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-222 |
4.05e-10 |
|
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: 58.57 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 25 SKFTLGPINFSIQAG-----ETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKhrvlnIRMVFQNSNES 99
Cdd:cd03237 6 MKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY-----IKADYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 100 LNPGITLGSI--------LEEPLKLNTRLDNQariakveqtlklvglLPEhrffyrhmLSDGQRQRVALARAIILNPQVI 171
Cdd:cd03237 81 LLSSITKDFYthpyfkteIAKPLQIEQILDRE---------------VPE--------LSGGELQRVAIAACLSKDADIY 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495265151 172 VADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILV 222
Cdd:cd03237 138 LLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-195 |
4.87e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 33 NFS--IQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNErKLE-HYDNKHRvlnirmvfqnsnESLNPGITLgsi 109
Cdd:PRK11147 337 DFSaqVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGT-KLEvAYFDQHR------------AELDPEKTV--- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 110 leeplklntrLDNqarIAKVEQTLkLVGLLPEHRFFY---------RHM-----LSDGQRQRVALARaIILNP-QVIVAD 174
Cdd:PRK11147 401 ----------MDN---LAEGKQEV-MVNGRPRHVLGYlqdflfhpkRAMtpvkaLSGGERNRLLLAR-LFLKPsNLLILD 465
|
170 180
....*....|....*....|.
gi 495265151 175 EPFAALDpsvrSQTVNLLMEL 195
Cdd:PRK11147 466 EPTNDLD----VETLELLEEL 482
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
32-261 |
7.12e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 7.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNER------KLEHYDNKHRVLNIR-MVFQNSNESlNPGI 104
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdiNLKWWRSKIGVVSQDpLLFSNSIKN-NIKY 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 105 TLGSI-----LEEPLK---------LNTRLDNQARIA-------------------KVEQTLK---------------LV 136
Cdd:PTZ00265 483 SLYSLkdleaLSNYYNedgndsqenKNKRNSCRAKCAgdlndmsnttdsneliemrKNYQTIKdsevvdvskkvlihdFV 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 137 GLLPEHrffYRHM-------LSDGQRQRVALARAIILNPQVIVADEPFAALDPS---VRSQTVNLLMELQRELGlgfIFI 206
Cdd:PTZ00265 563 SALPDK---YETLvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQKTINNLKGNENRIT---III 636
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 495265151 207 SHNLGIVRHiSDKILVMKQGKVVESGKTDVIFHWP-KDEYTKKLVHAHQALINGQS 261
Cdd:PTZ00265 637 AHRLSTIRY-ANTIFVLSNRERGSTVDVDIIGEDPtKDNKENNNKNNKDDNNNNNN 691
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-223 |
7.14e-10 |
|
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: 57.76 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 39 GETLAIVGANGSGKSLLAKLLVGLEQPDSGSI-----------YLNERKLEHYDNKHRVLNIRMVFQNSNESLNPGITLG 107
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNYFTKLLEGDVKVIVKPQYVDLIPKAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 108 SILEeplkLNTRLDNQARIAKVEQTLKLVGLLPehrffyRHM--LSDGQRQRVALARAIILNPQVIVADEPFAALDPSVR 185
Cdd:cd03236 106 KVGE----LLKKKDERGKLDELVDQLELRHVLD------RNIdqLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 495265151 186 SQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVM 223
Cdd:cd03236 176 LNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-232 |
1.19e-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: 58.49 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEhydnkhrvLNIRMVFQN-----SNESLNPGITL 106
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE--------TNLDAVRQSlgmcpQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 GSILEEPLKLNTRLDNQARIaKVEQTLKLVGLlPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRS 186
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQL-EMEAMLEDTGL-HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495265151 187 QTVNLLMELQRelGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:TIGR01257 1099 SIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
39-226 |
3.51e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.30 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 39 GETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLnerklehydnkhrvlnirmvfqnsnesLNPGITLGSILEEplklnt 118
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------IDGEDILEEVLDQ------ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 119 rldnqariakveqtlklvgLLPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPS-----VRSQTVNLLM 193
Cdd:smart00382 49 -------------------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqeallLLLEELRLLL 109
|
170 180 190
....*....|....*....|....*....|....*...
gi 495265151 194 ELQRELGLGFIFISHNL-----GIVRHISDKILVMKQG 226
Cdd:smart00382 110 LLKSEKNLTVILTTNDEkdlgpALLRRRFDRRIVLLLI 147
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-232 |
3.67e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 25 SKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLnERKLEHYDNKHRVLN--IRmvfqnsneslnp 102
Cdd:PTZ00243 672 PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-ERSIAYVPQQAWIMNatVR------------ 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 103 gitlGSIL---EEPlklNTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHM-LSDGQRQRVALARAIILNPQVIVADEPFA 178
Cdd:PTZ00243 739 ----GNILffdEED---AARLADAVRVSQLEADLAQLGGGLETEIGEKGVnLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495265151 179 ALDPSVRSQTVNLLMeLQRELGLGFIFISHNLGIVRHiSDKILVMKQGKVVESG 232
Cdd:PTZ00243 812 ALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSG 863
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
32-230 |
3.69e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.72 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLE------------HYDNKHRVLNirMVFQN---- 95
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavkkgmAYITESRRDN--GFFPNfsia 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 96 SNESLNPGITLG----------SILEEPLKLNTRLDNQARIAKVEQTLKlvgllpehrffyrhMLSDGQRQRVALARAII 165
Cdd:PRK09700 360 QNMAISRSLKDGgykgamglfhEVDEQRTAENQRELLALKCHSVNQNIT--------------ELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495265151 166 LNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVE 230
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
32-232 |
3.70e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.57 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLE--QPDSGSIYLNERKLEHYDNKHRV-LNIRMVFQNSNESlnPGITLGS 108
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAgEGIFMAFQYPVEI--PGVSNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ILEEPLKLNTRLDNQARIAK------VEQTLKLVGLLPEhrFFYRHM---LSDGQRQRVALARAIILNPQVIVADEPFAA 179
Cdd:PRK09580 98 FLQTALNAVRSYRGQEPLDRfdfqdlMEEKIALLKMPED--LLTRSVnvgFSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495265151 180 LDP---SVRSQTVNLLMELQRelglGFIFISHNLGIVRHIS-DKILVMKQGKVVESG 232
Cdd:PRK09580 176 LDIdalKIVADGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-248 |
3.71e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.82 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 27 FTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNerklehydNKHRVLNIRMVFQNSNESLN----P 102
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK--------GSAALIAISSGLNGQLTGIEnielK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 103 GITLGSILEEPLKLNTRLDNQARIAK-VEQTLKlvgllpehrffyrhMLSDGQRQRVALARAIILNPQVIVADEPFAALD 181
Cdd:PRK13545 110 GLMMGLTKEKIKEIIPEIIEFADIGKfIYQPVK--------------TYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495265151 182 PSVRSQTVNLLMELqRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGK-TDVIFHWpkDEYTKK 248
Cdd:PRK13545 176 QTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDiKEVVDHY--DEFLKK 240
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-208 |
3.79e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 33 NFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNER-KLEHYDnkhrvlnirmvfQnSNESLNPG-------- 103
Cdd:PRK11819 344 SFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETvKLAYVD------------Q-SRDALDPNktvweeis 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 -----ITLGSIleeplKLNTRldnqARIAK-----VEQTlKLVGllpehrffyrhMLSDGQRQRVALARAIILNPQVIVA 173
Cdd:PRK11819 411 ggldiIKVGNR-----EIPSR----AYVGRfnfkgGDQQ-KKVG-----------VLSGGERNRLHLAKTLKQGGNVLLL 469
|
170 180 190
....*....|....*....|....*....|....*....
gi 495265151 174 DEPFAALDpsvrsqtVNLLMELQRELgLGF----IFISH 208
Cdd:PRK11819 470 DEPTNDLD-------VETLRALEEAL-LEFpgcaVVISH 500
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
27-235 |
5.71e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.21 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 27 FTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIylnerklehydNKHRVLNIRMVfqnsNESLNPGITL 106
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAI----SAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 GSILEepLKLNTRLDNQARIAKVeqTLKLVGLLPEHRFFYRHM--LSDGQRQRVALARAIILNPQVIVADEPFAALDPSV 184
Cdd:PRK13546 103 IENIE--FKMLCMGFKRKEIKAM--TPKIIEFSELGEFIYQPVkkYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495265151 185 RSQTVNLLMELqRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTD 235
Cdd:PRK13546 179 AQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELD 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-239 |
7.03e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.33 E-value: 7.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 23 KGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKHRVLNIRMVFQnsneslNP 102
Cdd:PTZ00243 1320 EGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQ------DP 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 103 GITLGSIleeplKLNTRLDNQARIAKVEQTLKLVGL----LPEHRFFYRHML------SDGQRQRVALARAII-LNPQVI 171
Cdd:PTZ00243 1394 VLFDGTV-----RQNVDPFLEASSAEVWAALELVGLrervASESEGIDSRVLeggsnySVGQRQLMCMARALLkKGSGFI 1468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 172 VADEPFAALDPSVRSQTVNLLMElqrelglGF-----IFISHNLGIVRHIsDKILVMKQGKVVESG-------KTDVIFH 239
Cdd:PTZ00243 1469 LMDEATANIDPALDRQIQATVMS-------AFsaytvITIAHRLHTVAQY-DKIIVMDHGAVAEMGsprelvmNRQSIFH 1540
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
29-232 |
1.10e-08 |
|
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: 53.81 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLeQPDSGSIylnERKLeHYDNK-----HRVLNIRMVFQNSNESLNPG 103
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-TEGNVSV---EGDI-HYNGIpykefAEKYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 ITlgsileeplklntrldnqariakVEQTLKLVGLLPEHRFFyrHMLSDGQRQRVALARAIILNPQVIVADEPFAALDPS 183
Cdd:cd03233 98 LT-----------------------VRETLDFALRCKGNEFV--RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495265151 184 VRSQTVNLLMELQRELGL-GFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:cd03233 153 TALEILKCIRTMADVLKTtTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
29-232 |
6.47e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGlEQPDS---------GSIYLNERKLEHYDNKhRVLNIRMVFQNSNE- 98
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAP-RLARLRAVLPQAAQp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 99 ----SLNPGITLGSIleePLKLNTRLDNQARIAKVEQTLKLVGLLPEHRffyRHM--LSDGQRQRVALARAI-------- 164
Cdd:PRK13547 95 afafSAREIVLLGRY---PHARRAGALTHRDGEIAWQALALAGATALVG---RDVttLSGGELARVQFARVLaqlwpphd 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495265151 165 -ILNPQVIVADEPFAALDPSVRSQTVNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQGKVVESG 232
Cdd:PRK13547 169 aAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
29-226 |
7.46e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.17 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIylnerklehydnKHrvlNIRMVFQNSNESLNPGITLGS 108
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------------KH---SGRISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 109 ILEEPLKLNTRLDNQARIAKVEQTLKlvgLLPEHRFFYRH----MLSDGQRQRVALARAIILNPQVIVADEPFAALDPSV 184
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKACQLEEDIT---KFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495265151 185 RSQT----VNLLMELQRElglgfIFISHNLGIVRhISDKILVMKQG 226
Cdd:cd03291 195 EKEIfescVCKLMANKTR-----ILVTSKMEHLK-KADKILILHEG 234
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
32-70 |
1.08e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 1.08e-07
10 20 30
....*....|....*....|....*....|....*....
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSI 70
Cdd:PRK15064 338 LNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
32-229 |
2.04e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLE--QPDSGSIYLNERKLehydnkhRVLNIRmvfqnsnESLNPGI----- 104
Cdd:NF040905 279 VSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEV-------DVSTVS-------DAIDAGLayvte 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 105 ---TLGSILEEPLKLNTRLDNQARIAKVeqtlklvGLLPEHRFF-----YRH-M-------------LSDGQRQRVALAR 162
Cdd:NF040905 345 drkGYGLNLIDDIKRNITLANLGKVSRR-------GVIDENEEIkvaeeYRKkMniktpsvfqkvgnLSGGNQQKVVLSK 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495265151 163 AIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVV 229
Cdd:NF040905 418 WLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
29-181 |
3.89e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.06 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 29 LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIylnerklehydnKHrvlNIRMVFQNSNESLNPGITLGS 108
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI------------KH---SGRISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495265151 109 ILEEPLKLNTRLDNQARIAKVEQTLklvGLLPEHRFFYRH----MLSDGQRQRVALARAIILNPQVIVADEPFAALD 181
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQLEEDI---ALFPEKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-228 |
6.24e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 24 GSKFTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIylnerklehydnkhrvlnirmvfqnsneSLNPG 103
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI----------------------------GLAKG 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 ITLGSILEEPLKL----NTRLDNQARIAKVEQTLKLVGLL------------PEHRFfyrhmlSDGQRQRVALARAIILN 167
Cdd:PRK10636 375 IKLGYFAQHQLEFlradESPLQHLARLAPQELEQKLRDYLggfgfqgdkvteETRRF------SGGEKARLVLALIVWQR 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495265151 168 PQVIVADEPFAALDPSVRSQTVNLLMELQRELglgfIFISHNLGIVRHISDKILVMKQGKV 228
Cdd:PRK10636 449 PNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-232 |
7.64e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.94 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 27 FTLGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIY---LNERKLEHYDNKHRVLNIRMvfqnsneslNPG 103
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIidgLNIAKIGLHDLRFKITIIPQ---------DPV 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 104 ITLGSileepLKLNTRLDNQARIAKVEQTLKL------VGLLPEHRFFY----RHMLSDGQRQRVALARAIILNPQVIVA 173
Cdd:TIGR00957 1371 LFSGS-----LRMNLDPFSQYSDEEVWWALELahlktfVSALPDKLDHEcaegGENLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495265151 174 DEPFAALDpsvrSQTVNLLMELQREL--GLGFIFISHNLGIVRHISdKILVMKQGKVVESG 232
Cdd:TIGR00957 1446 DEATAAVD----LETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
32-208 |
2.54e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.21 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKlehydnkhrvlNIRMVFQNsneslnPGITLGSILE 111
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG-----------KLFYVPQR------PYMTLGTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 112 EPLKLNTRLDNQAR---IAKVEQTLKLVGLlpeHRFFYRHM-----------LSDGQRQRVALARAIILNPQVIVADEPF 177
Cdd:TIGR00954 534 QIIYPDSSEDMKRRglsDKDLEQILDNVQL---THILEREGgwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|.
gi 495265151 178 AALDPSVRSQtvnlLMELQRELGLGFIFISH 208
Cdd:TIGR00954 611 SAVSVDVEGY----MYRLCREFGITLFSVSH 637
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
151-235 |
3.07e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.42 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 151 SDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQGKVVE 230
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
|
....*
gi 495265151 231 SGKTD 235
Cdd:NF000106 225 DGKVD 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
36-226 |
3.09e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 48.09 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 36 IQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLehydnkhrVLNIRMVFQNSN-----ESLNPGITLgsil 110
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--------LTNISDVHQNMGycpqfDAIDDLLTG---- 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 111 EEPLKLNTRLDN--QARIAKVEQ-TLKLVGLLpehrfFYRHML----SDGQRQRVALARAIILNPQVIVADEPFAALDPS 183
Cdd:TIGR01257 2030 REHLYLYARLRGvpAEEIEKVANwSIQSLGLS-----LYADRLagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495265151 184 VRSQTVNLLMELQRElGLGFIFISHNLGIVRHISDKILVMKQG 226
Cdd:TIGR01257 2105 ARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
43-226 |
7.66e-06 |
|
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: 45.68 E-value: 7.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 43 AIVGANGSGKS-LLAKLLVGLeqpdSGSIYLNERKLEHYDN----KHRVLNIRMVFQNSNEslnpgitlgsileEPLKLN 117
Cdd:cd03240 26 LIVGQNGAGKTtIIEALKYAL----TGELPPNSKGGAHDPKlireGEVRAQVKLAFENANG-------------KKYTIT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 118 TRLD--NQARIAKVEQTLKLvglLPEHRFFyrhmLSDGQRQ------RVALARAIILNPQVIVADEPFAALDP-SVRSQT 188
Cdd:cd03240 89 RSLAilENVIFCHQGESNWP---LLDMRGR----CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESL 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 495265151 189 VNLLMELQRELGLGFIFISHNLGIVRHISDKILVMKQG 226
Cdd:cd03240 162 AEIIEERKSQKNFQLIVITHDEELVDAADHIYRVEKDG 199
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-230 |
7.83e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNErklehYD-NKHRVLNIRMVfqnsneslnpgitLGSIL 110
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG-----CDiSKFGLMDLRKV-------------LGIIP 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 111 EEP------LKLNTRLDNQARIAKVEQTLKLVGLLPEHRffyRHML-------------SDGQRQRVALARAIILNPQVI 171
Cdd:PLN03130 1320 QAPvlfsgtVRFNLDPFNEHNDADLWESLERAHLKDVIR---RNSLgldaevseagenfSVGQRQLLSLARALLRRSKIL 1396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495265151 172 VADEPFAALDpsVRsqTVNLLMELQRE--LGLGFIFISHNLGIVrhI-SDKILVMKQGKVVE 230
Cdd:PLN03130 1397 VLDEATAAVD--VR--TDALIQKTIREefKSCTMLIIAHRLNTI--IdCDRILVLDAGRVVE 1452
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-182 |
2.06e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 45.67 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 10 LRFDNCHGKR-WQNKG--------SKFT------LGPINFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDsGSIYL-- 72
Cdd:TIGR01271 1201 LVIENPHAQKcWPSGGqmdvqgltAKYTeagravLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIdg 1279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 73 ---NERKLEHYDNKHRVL-------------NIRMVFQNSNESL---NPGITLGSILEE-PLKLNTRLDNQARIakveqt 132
Cdd:TIGR01271 1280 vswNSVTLQTWRKAFGVIpqkvfifsgtfrkNLDPYEQWSDEEIwkvAEEVGLKSVIEQfPDKLDFVLVDGGYV------ 1353
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495265151 133 lklvgllpehrffyrhmLSDGQRQRVALARAIILNPQVIVADEPFAALDP 182
Cdd:TIGR01271 1354 -----------------LSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
36-222 |
4.25e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.94 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 36 IQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLnerklehydnkhrvlnirmvfqnsneslnPGITlgsILEEPLK 115
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-----------------------------DGIT---PVYKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 116 LNtrldnqariakveqtlklvgllpehrffyrhmLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLLMEL 195
Cdd:cd03222 70 ID--------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*..
gi 495265151 196 QRELGLGFIFISHNLGIVRHISDKILV 222
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
21-224 |
4.55e-05 |
|
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: 42.73 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 21 QNKGSKFTLGPINFSIQAGETLAIVGANGSGKSLLAK---LLVGLEQPdsgsiylnerklehydnkhrvlnirmvfqnsn 97
Cdd:cd03227 3 VLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaigLALGGAQS-------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 98 eslnpgitlgsileeplKLNTRLDNQARIAKVEQTLKLVgllpehrfFYRHMLSDGQRQRVALARAIIL---NP-QVIVA 173
Cdd:cd03227 51 -----------------ATRRRSGVKAGCIVAAVSAELI--------FTRLQLSGGEKELSALALILALaslKPrPLYIL 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495265151 174 DEPFAALDPSVRSQTVNLLMElQRELGLGFIFISHNLGIVRhISDKILVMK 224
Cdd:cd03227 106 DEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLPELAE-LADKLIHIK 154
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
44-192 |
5.70e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 44 IVGANGSGKSLLAKLLVGLEQPDSGSIYlnerklehYDNKHrVLNIRMVFQnSNESLNPGITLGSILEEPLKLNTRLDNQ 123
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIY--------YKNCN-INNIAKPYC-TYIGHNLGLKLEMTVFENLKFWSEIYNS 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 124 AR-IAKVEQTLKLVGLLPEHRFfyrhMLSDGQRQRVALARAIILNPQVIVADEPFAALDPSVRSQTVNLL 192
Cdd:PRK13541 101 AEtLYAAIHYFKLHDLLDEKCY----SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-230 |
7.64e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDSGSIYLNErklehYD-NKHRVLNIRMVFQNSNESlnPGITLGSIl 110
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD-----CDvAKFGLTDLRRVLSIIPQS--PVLFSGTV- 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 111 eeplKLNtrLD-----NQARIAKVEQTLKLVGLLPEHRFFYRHMLSDG-------QRQRVALARAIILNPQVIVADEPFA 178
Cdd:PLN03232 1327 ----RFN--IDpfsehNDADLWEALERAHIKDVIDRNPFGLDAEVSEGgenfsvgQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495265151 179 ALDpsVRSQTVnllmeLQRELGLGF-----IFISHNLGIVRHiSDKILVMKQGKVVE 230
Cdd:PLN03232 1401 SVD--VRTDSL-----IQRTIREEFksctmLVIAHRLNTIID-CDKILVLSSGQVLE 1449
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
150-232 |
1.54e-04 |
|
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: 41.15 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 150 LSDGQRQRVALARAIILNPQ--VIVADEPFAALDPSVRSQTVNLLMELqRELGLGFIFISHNLGIVRHiSDKILVMKQ-- 225
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSS-ADWIIDFGPgs 165
|
90
....*....|.
gi 495265151 226 ----GKVVESG 232
Cdd:cd03238 166 gksgGKVVFSG 176
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-235 |
3.81e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.63 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 22 NKGSKFT-LGPINFSIQAGETLAIVGANGSGKSLLAKLL----VGLEQPDSGSIYLNERKLEHYDNKHRVlniRMVFQNS 96
Cdd:TIGR00956 69 RDTKTFDiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRG---DVVYNAE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 97 NESLNPGITLGSILEEPLKL---NTRLDNQARIAKVEQ----TLKLVGLlpEHRF-------FYRHmLSDGQRQRVALAR 162
Cdd:TIGR00956 146 TDVHFPHLTVGETLDFAARCktpQNRPDGVSREEYAKHiadvYMATYGL--SHTRntkvgndFVRG-VSGGERKRVSIAE 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495265151 163 AIILNPQVIVADEPFAALDPSVRSQTVNLLMELQREL-GLGFIFISHNLGIVRHISDKILVMKQGKVVESGKTD 235
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILdTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPAD 296
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
128-208 |
1.38e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 128 KVEQTLKLVGL---LPEHRFfyrHMLSDGQrQRVAL-ARAIILNPQVIVADEPFAALDPsvrsqtvnllmeLQRELGLGF 203
Cdd:PRK10938 380 LAQQWLDILGIdkrTADAPF---HSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDP------------LNRQLVRRF 443
|
90
....*....|....*..
gi 495265151 204 I------------FISH 208
Cdd:PRK10938 444 VdvlisegetqllFVSH 460
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
83-255 |
1.61e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 83 KHRVLNIRMVFQNSNESLNPGITLGSI---LEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHMLSDGQRQRVA 159
Cdd:PLN03073 275 QQRELEFETETGKGKGANKDGVDKDAVsqrLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 160 LARAIILNPQVIVADEPFAALDPSVRSQTVNLLMELQRElglgFIFISHNLGIVRHISDKILVMkQGKVVESGKTDV-IF 238
Cdd:PLN03073 355 LARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKT----FIVVSHAREFLNTVVTDILHL-HGQKLVTYKGDYdTF 429
|
170
....*....|....*..
gi 495265151 239 HWPKDEYTKKLVHAHQA 255
Cdd:PLN03073 430 ERTREEQLKNQQKAFES 446
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
19-133 |
2.74e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 38.95 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 19 RWQNKGSKFTLGPINFsiqagetlaIVGANGSGKSLLAKLLVGLEQPDSGSIYLNERKLEHYDNKH----RVLNIRMVFQ 94
Cdd:COG4694 13 AFKDFGWLAFFKKLNL---------IYGENGSGKSTLSRILRSLELGDTSSEVIAEFEIEAGGSAPnpsvRVFNRDFVEE 83
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 495265151 95 N--SNESLNPGITLGsilEEPLKLNTRLD-NQARIAKVEQTL 133
Cdd:COG4694 84 NlrSGEEIKGIFTLG---EENIELEEEIEeLEKEIEDLKKEL 122
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
27-240 |
2.84e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 38.41 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 27 FTLGPINFsiqagetlaIVGANGSGKSLLAKLLVGLEQpdSGSIYLN-ERKLEHYDNKHRVLNIRMVFQNSNESLNPGIT 105
Cdd:COG4938 17 LELKPLTL---------LIGPNGSGKSTLIQALLLLLQ--SNFIYLPaERSGPARLYPSLVRELSDLGSRGEYTADFLAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 106 LGSILEEPLKLNTRLDN-QARIAKVEQT-LKLVGLLPEHRFFYR----------HMLSDGQRQR----VALARAIIlNPQ 169
Cdd:COG4938 86 LENLEILDDKSKELLEQvEEWLEKIFPGkVEVDASSDLVRLVFRpsgngkriplSNVGSGVSELlpilLALLSAAK-PGS 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495265151 170 VIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVRHISdkiLVMKQGKVVESgkTDVIFHW 240
Cdd:COG4938 165 LLIIEEPEAHLHPKAQSALAELLAELANS-GVQVIIETHSDYILNGLR---NLIKEGKLLDP--DDVAVYF 229
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
32-182 |
2.91e-03 |
|
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: 38.30 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 32 INFSIQAGETLAIVGANGSGKSLLAKLLVGLEQPDsGSIYL-----NERKLEHYDNKHRVLNiRMVFqnsneslnpgitl 106
Cdd:cd03289 23 ISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIdgvswNSVPLQKWRKAFGVIP-QKVF------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 107 gsILEEPLKLNtrLD-----NQARIAKV--EQTLKLV-----GLLPEHRFFYRHMLSDGQRQRVALARAIILNPQVIVAD 174
Cdd:cd03289 88 --IFSGTFRKN--LDpygkwSDEEIWKVaeEVGLKSVieqfpGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 163
|
....*...
gi 495265151 175 EPFAALDP 182
Cdd:cd03289 164 EPSAHLDP 171
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
70-214 |
4.33e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.75 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 70 IYLNERKLEHYDNKHRVLNIRMVFQNSNESLNPGITLGSILEEPLKLNTRLDNQARIAKVEQTLKLVGLLPEHRFFYRHM 149
Cdd:pfam13304 145 LSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 150 ------------LSDGQRQRVALARAIILNPQ---VIVADEPFAALDPSVRSQTVNLLMELQRElGLGFIFISHNLGIVR 214
Cdd:pfam13304 225 enggggelpafeLSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRN-GAQLILTTHSPLLLD 303
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
5-208 |
7.59e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 36.90 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 5 LSVENLR-FDNCHgkrwqnkgskftlgpINFSIQAGETLaIVGANGSGKS----LLAKLLVGLEQPDSGSIYLN-ERKLE 78
Cdd:COG3950 6 LTIENFRgFEDLE---------------IDFDNPPRLTV-LVGENGSGKTtlleAIALALSGLLSRLDDVKFRKlLIRNG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 79 HYDNKHRVL----------------------NIRMVFQNSNESLNPGITLGSILE------EPLKLNTRLDNQARIAKVE 130
Cdd:COG3950 70 EFGDSAKLIlyygtsrllldgplkklerlkeEYFSRLDGYDSLLDEDSNLREFLEwlreylEDLENKLSDELDEKLEAVR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495265151 131 QTLKlvGLLPE----------HRFFYRHM---------LSDGQRQRVALA-----RAIILNPQ---------VIVADEPF 177
Cdd:COG3950 150 EALN--KLLPDfkdiridrdpGRLVILDKngeelplnqLSDGERSLLALVgdlarRLAELNPAlenplegegIVLIDEID 227
|
250 260 270
....*....|....*....|....*....|....*
gi 495265151 178 AALDPSVRSQTVNLLME----LQrelglgFIFISH 208
Cdd:COG3950 228 LHLHPKWQRRILPDLRKifpnIQ------FIVTTH 256
|
|
| |
