|
Name |
Accession |
Description |
Interval |
E-value |
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-251 |
1.64e-166 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 459.96 E-value: 1.64e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQKLHIDP 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 81 TLPVTVERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLY 160
Cdd:PRK09544 81 TLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 161 DLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPEAVSQHPEFIAMFGPRGAEELAIYRHHHNHRHDLQG 240
Cdd:PRK09544 161 DLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPEVVSLHPEFISMFGPRGAEQLGIYRHHHNHRHDLQG 240
|
250
....*....|.
gi 768329558 241 RIVLRKGQGPS 251
Cdd:PRK09544 241 RIVLRRGNDRS 251
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-231 |
6.04e-84 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 250.39 E-value: 6.04e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ------RDPGLRIGYVPQ 74
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 75 KLHIDPTLPVTVE------------RFMRLTRGSKNAeILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLL 142
Cdd:COG1121 83 RAEVDWDFPITVRdvvlmgrygrrgLFRRPSRADREA-VDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 143 VLDEPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPEAVSQHPEFIAMFGprga 222
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLSRAYG---- 236
|
....*....
gi 768329558 223 EELAIYRHH 231
Cdd:COG1121 237 GPVALLAHG 245
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-202 |
9.21e-82 |
|
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: 243.98 E-value: 9.21e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 7 LDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV------QRDPGLRIGYVPQKLHIDP 80
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrvfgkpLEKERKRIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 81 TLPVTVERFMRLTRGSK-----------NAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQ 149
Cdd:cd03235 82 DFPISVRDVVLMGLYGHkglfrrlskadKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 768329558 150 GVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCLNHHICCSG 202
Cdd:cd03235 162 GVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-207 |
3.44e-55 |
|
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: 177.54 E-value: 3.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV-----------QRDPGLRIGYV 72
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaslsRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 73 PQklHIDPTLPVTVE------------RFMRLTRGSKNAeILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQ 140
Cdd:COG1120 81 PQ--EPPAPFGLTVRelvalgryphlgLFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 141 LLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEAV 207
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLkDGRIVAQGPPEEV 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-207 |
7.50e-54 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 173.71 E-value: 7.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ---RDPGL-------RIGYVPQ 74
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgEDVARdpaevrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 75 KLHIDPTLpvTVE-------RFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEP 147
Cdd:COG1131 81 EPALYPDL--TVRenlrffaRLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768329558 148 TQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAV 207
Cdd:COG1131 159 TSGLDPEARRELWELLRELA-AEGKTVLLSTHYLEEAERLCDRVAIIDKgRIVADGTPDEL 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-193 |
5.03e-53 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 170.11 E-value: 5.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 14 FNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQKLHIDPTLPVTVERFM--- 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRDLVamg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 91 ---------RLTRGSKnAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYD 161
Cdd:NF040873 82 rwarrglwrRLTRDDR-AAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180 190
....*....|....*....|....*....|..
gi 768329558 162 LINQLRVElNCGVLMVSHDLHLVMAKTDEVLC 193
Cdd:NF040873 161 LLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-196 |
2.14e-49 |
|
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: 160.29 E-value: 2.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 6 TLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ-----------RDPGLRIGYVPQ 74
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILldgkdlaslspKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 75 klhidptlpvtverfmrltrgsknaeilpALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVN 154
Cdd:cd03214 81 -----------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768329558 155 GQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03214 132 HQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKD 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-196 |
6.14e-45 |
|
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: 150.35 E-value: 6.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKF----NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------------QRDP 65
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllklsrrlRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 66 GLRIGYVPQKLH--IDPTLPV---TVERFMRLTRGSKNAEILPALKRVQAGHLLNA------PLQkLSGGETQRVLLARA 134
Cdd:cd03257 81 RKEIQMVFQDPMssLNPRMTIgeqIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEevlnryPHE-LSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768329558 135 LLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYA 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-196 |
8.88e-45 |
|
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: 148.31 E-value: 8.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ-------RDPGL---RIGYVPQ 74
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkdikKEPEEvkrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 75 KLHIDPTLpvTVErfmrltrgsknaEILpalkrvqaghllnaplqKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVN 154
Cdd:cd03230 81 EPSLYENL--TVR------------ENL-----------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768329558 155 GQVSLYDLINQLRVElNCGVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03230 130 SRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNN 170
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-215 |
5.10e-44 |
|
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: 148.25 E-value: 5.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKF-NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGL------------RIGY 71
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-GKditkknlrelrrKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQklhiDP----TLPvTVER---F----MRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQ 140
Cdd:COG1122 80 VFQ----NPddqlFAP-TVEEdvaFgpenLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 141 LLVLDEPTQGVDVNGQVSLYDLINQLRVElNCGVLMVSHDLHLVMAKTDEVLCLNHH-ICCSGTPEAVSQHPEFIA 215
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGrIVADGTPREVFSDYELLE 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-215 |
3.64e-42 |
|
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: 150.05 E-value: 3.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKF--NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPT---TGSV-----------QRD 64
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVlldgrdllelsEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 65 PGLRIGYVPQklhiDPTL---PVTVE-------RFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARA 134
Cdd:COG1123 81 RGRRIGMVFQ----DPMTqlnPVTVGdqiaealENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 135 LLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPEF 213
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDgRIVEDGPPEEILAAPQA 236
|
..
gi 768329558 214 IA 215
Cdd:COG1123 237 LA 238
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-212 |
9.69e-42 |
|
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: 142.63 E-value: 9.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRN----VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV---------QRDPGLR-- 68
Cdd:COG1124 1 MLEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpvtrRRRKAFRrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 IGYVPQklhiDPTLPV----TVERFMR-----LTRGSKNAEILPALKRV--QAGHLLNAPLQkLSGGETQRVLLARALLN 137
Cdd:COG1124 81 VQMVFQ----DPYASLhprhTVDRILAeplriHGLPDREERIAELLEQVglPPSFLDRYPHQ-LSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 138 QPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPE 212
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNgRIVEELTVADLLAGPK 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-211 |
1.37e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 148.51 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRN-----VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ--------------RD 64
Cdd:COG1123 260 LLEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgkdltklsrrslRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 65 PGLRIGYVPQ--KLHIDPTLPV--TVERFMR----LTRGSKNAEILPALKRVQ--AGHLLNAPLQkLSGGETQRVLLARA 134
Cdd:COG1123 340 LRRRVQMVFQdpYSSLNPRMTVgdIIAEPLRlhglLSRAERRERVAELLERVGlpPDLADRYPHE-LSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 135 LLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHP 211
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDgRIVEDGPTEEVFANP 496
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-223 |
2.66e-41 |
|
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: 141.53 E-value: 2.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ--------RDPGLR--IGYVP 73
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrkEPREARrqIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 74 QKLHIDPTLpvTVE-------RFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDE 146
Cdd:COG4555 81 DERGLYDRL--TVReniryfaELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 147 PTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQH-------PEFIAMFG 218
Cdd:COG4555 159 PTNGLDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKgKVVAQGSLDELREEigeenleDAFVALIG 237
|
....*
gi 768329558 219 PRGAE 223
Cdd:COG4555 238 SEEGE 242
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-197 |
4.39e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 137.25 E-value: 4.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 6 TLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD---------PGLR--IGYVPQ 74
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDgkplsamppPEWRrqVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 75 klhiDPTL-PVTVERFMRLTRGSKN-----AEILPALKRVQ-AGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEP 147
Cdd:COG4619 82 ----EPALwGGTVRDNLPFPFQLRErkfdrERALELLERLGlPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 768329558 148 TQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNHH 197
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-180 |
8.75e-40 |
|
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: 136.45 E-value: 8.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ----------RDPGLRIGYVP 73
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwngepirdarEDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 74 QKLHIDPTLpvTVERFMRLTRGSKN-----AEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPT 148
Cdd:COG4133 82 HADGLKPEL--TVRENLRFWAALYGlradrEAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|..
gi 768329558 149 QGVDVNGQVSLYDLINQLRvELNCGVLMVSHD 180
Cdd:COG4133 160 TALDAAGVALLAELIAAHL-ARGGAVLLTTHQ 190
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-215 |
1.50e-39 |
|
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: 137.48 E-value: 1.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ---RD------------- 64
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgRDitglpphriarlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 65 -----------PGL------RIGyvpQKLHIDPTLPVTVERFMRLTRGSK--NAEILPALKRVQAGHLLNAPLQKLSGGE 125
Cdd:COG0411 81 iartfqnprlfPELtvlenvLVA---AHARLGRGLLAALLRLPRARREEReaRERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 126 TQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTP 204
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFgRVIAEGTP 237
|
250
....*....|.
gi 768329558 205 EAVSQHPEFIA 215
Cdd:COG0411 238 AEVRADPRVIE 248
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-217 |
1.60e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 139.85 E-value: 1.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV---QRD-----PGLR-IGY 71
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIlldGRDvtglpPEKRnVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQKLHIDPTLpvTVE-------RFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVL 144
Cdd:COG3842 82 VFQDYALFPHL--TVAenvafglRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 145 DEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLH--LVMAktDEVLCLNH-HICCSGTPEAVSQHP--EFIAMF 217
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeaLALA--DRIAVMNDgRIEQVGTPEEIYERPatRFVADF 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-197 |
2.32e-39 |
|
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: 135.67 E-value: 2.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 7 LDNVSIKFNQRN--VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV-----------QRDPGLRIGYVP 73
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdltklsLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 74 QklhiDP---TLPVTVER---FMRLTRGSKNAEILP----ALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLV 143
Cdd:cd03225 82 Q----NPddqFFGPTVEEevaFGLENLGLPEEEIEErveeALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 768329558 144 LDEPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCLNHH 197
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-194 |
3.85e-39 |
|
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: 135.98 E-value: 3.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 2 TSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTG-SVQ---RDPGL--------RI 69
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlfgERRGGedvwelrkRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 70 GYVPQKLH--IDPTLPV----------TVERFMRLTRGSKN-AEILpaLKRVQAGHLLNAPLQKLSGGETQRVLLARALL 136
Cdd:COG1119 81 GLVSPALQlrFPRDETVldvvlsgffdSIGLYREPTDEQRErAREL--LELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 137 NQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCL 194
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-207 |
1.67e-38 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 134.86 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 8 DNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ-----------RDPGLRIGYVPQkl 76
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlngrplaawspWELARRRAVLPQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 77 HIDPTLPVTVERFMRL------TRGSKNAEILP-ALKRVQAGHLLNAPLQKLSGGETQRVLLARALL-------NQPQLL 142
Cdd:COG4559 83 HSSLAFPFTVEEVVALgraphgSSAAQDRQIVReALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 143 VLDEPTQGVDVNGQVSLYDLINQLRVElNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAV 207
Cdd:COG4559 163 FLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQgRLVAQGTPEEV 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-210 |
2.46e-38 |
|
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: 140.28 E-value: 2.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQ-RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGL------------RIGY 71
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-GVdlsdldpaswrrQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQKLHIdptLPVTVERFMRLtrGSKNA---EILPALKRVQAGHL-------LNAPL----QKLSGGETQRVLLARALLN 137
Cdd:COG4988 416 VPQNPYL---FAGTIRENLRL--GRPDAsdeELEAALEAAGLDEFvaalpdgLDTPLgeggRGLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768329558 138 QPQLLVLDEPTQGVDVNGQVSLYDLINQLRveLNCGVLMVSHDLHLvMAKTDEVLCLNH-HICCSGTPEAVSQH 210
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRLA--KGRTVILITHRLAL-LAQADRILVLDDgRIVEQGTHEELLAK 561
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-192 |
2.52e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 133.24 E-value: 2.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKF----NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV-------------QR 63
Cdd:COG1136 1 MSPLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlidgqdisslserEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 64 DpGLR---IGYVPQKLHIDPTLpvTVE-------RFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLAR 133
Cdd:COG1136 81 A-RLRrrhIGFVFQFFNLLPEL--TALenvalplLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 134 ALLNQPQLLVLDEPTQGVD-VNGQvSLYDLINQLRVELNCGVLMVSHDLHLvMAKTDEVL 192
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDsKTGE-EVLELLRELNRELGTTIVMVTHDPEL-AARADRVI 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-195 |
4.15e-38 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 132.40 E-value: 4.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD-------PGLRIGYVPQKLH 77
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDgkpldiaARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 78 IDPTLPVtVERFMRLT--RGSKNAEILPA----LKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGV 151
Cdd:cd03269 81 LYPKMKV-IDQLVYLAqlKGLKKEEARRRidewLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768329558 152 D-VNGQVsLYDLINQLRVElNCGVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:cd03269 160 DpVNVEL-LKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLN 202
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-222 |
5.12e-38 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 136.89 E-value: 5.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ-----------RDPGLRIGYVP 73
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddvealsaRAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 74 QK--LHIDPTLPVTVE--------RFMRLTRGSKNAeILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLV 143
Cdd:PRK09536 84 QDtsLSFEFDVRQVVEmgrtphrsRFDTWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 144 LDEPTQGVDVNGQVSLYDLINQLrVELNCGVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEAVSQHPEFIAMFGPRGA 222
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLaDGRVRAAGPPADVLTADTLRAAFDARTA 241
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-181 |
7.24e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 133.29 E-value: 7.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRN----VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD------PGLRIG 70
Cdd:COG1116 4 AAPALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDgkpvtgPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 71 YVPQklhiDPTL-P-VTVE-------RFMRLTRGSKNAEILPALKRVQAGHLLNA-PLQkLSGGETQRVLLARALLNQPQ 140
Cdd:COG1116 84 VVFQ----EPALlPwLTVLdnvalglELRGVPKAERRERARELLELVGLAGFEDAyPHQ-LSGGMRQRVAIARALANDPE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 768329558 141 LLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDL 181
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDV 199
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-196 |
7.51e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.08 E-value: 7.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV-------QRDPGLRIGYVPQKLH 77
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlwdgeplDPEDRRRIGYLPEERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 78 IDPTLPV--TVERFMRLtRGSKNAEILPA----LKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGV 151
Cdd:COG4152 82 LYPKMKVgeQLVYLARL-KGLSKAEAKRRadewLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768329558 152 D-VNGQVsLYDLINQLRVElncG--VLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG4152 161 DpVNVEL-LKDVIRELAAK---GttVIFSSHQMELVEELCDRIVIINK 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-195 |
1.84e-37 |
|
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: 128.90 E-value: 1.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 6 TLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDP-----------GLRIGYVPQ 74
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkdiaklpleelRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 75 klhidptlpvtverfmrltrgsknaeilpalkrvqaghllnaplqkLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVN 154
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 768329558 155 GQVSLYDLINQLRVElNCGVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:cd00267 115 SRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLK 154
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-212 |
2.67e-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: 2.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 7 LDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV----QRDPGLR--------IGYVPQ 74
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgEDITGLPpheiarlgIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 75 KLHIDPTLPV-----------TVERFMRLTRGSKNAEI----LPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQP 139
Cdd:cd03219 83 IPRLFPELTVlenvmvaaqarTGSGLLLARARREEREAreraEELLERVGLADLADRPAGELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768329558 140 QLLVLDEPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPE 212
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQgRVIAEGTPDEVRNNPR 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-196 |
5.40e-37 |
|
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: 128.46 E-value: 5.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ-------------RDPGLRIGY 71
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILidgedltdledelPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQklhiDPTLpvtverFMRLTrgsknaeilpALKRVQAGhllnaplqkLSGGETQRVLLARALLNQPQLLVLDEPTQGV 151
Cdd:cd03229 81 VFQ----DFAL------FPHLT----------VLENIALG---------LSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768329558 152 DVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03229 132 DPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-214 |
8.64e-37 |
|
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: 129.71 E-value: 8.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------------QRDPG 66
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlvdgqditglsekeLYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 67 LRIGYVPQK------LhidptlpvTVE--------RFMRLTRGSKNAEILPALKRV---QAGHLLnaPLQkLSGGETQRV 129
Cdd:COG1127 82 RRIGMLFQGgalfdsL--------TVFenvafplrEHTDLSEAEIRELVLEKLELVglpGAADKM--PSE-LSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 130 LLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEAV- 207
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLaDGKIIAEGTPEELl 230
|
250
....*....|.
gi 768329558 208 -SQHP---EFI 214
Cdd:COG1127 231 aSDDPwvrQFL 241
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-197 |
1.71e-36 |
|
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: 126.02 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQklhidptlpv 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 85 tverfmrltrgsknaeilpalkrvqaghllnaplqkLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLIN 164
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180 190
....*....|....*....|....*....|...
gi 768329558 165 qlrvELNCGVLMVSHDLHLVMAKTDEVLCLNHH 197
Cdd:cd03221 115 ----EYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-148 |
1.84e-36 |
|
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: 126.22 E-value: 1.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD-----------PGLRIGYVPQKLHIDPTLPV---- 84
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQDPQLFPRLTVrenl 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768329558 85 -TVERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQK----LSGGETQRVLLARALLNQPQLLVLDEPT 148
Cdd:pfam00005 81 rLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-180 |
6.53e-36 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 133.27 E-value: 6.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 7 LDNVSIKFNQRNVLSGVSLALQPG-RIlTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQKLHIDPTLPV- 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGdRI-GLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 85 ------------TVERFMRL-TRGSKNAEILPALKRVQA------------------------GHLLNAPLQKLSGGETQ 127
Cdd:COG0488 80 dtvldgdaelraLEAELEELeAKLAEPDEDLERLAELQEefealggweaearaeeilsglgfpEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 768329558 128 RVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRvelnCGVLMVSHD 180
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP----GTVLVVSHD 208
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-180 |
1.60e-35 |
|
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: 125.68 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRN----VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV-------------QRDPGL 67
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisklsekELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 68 R--IGYVPQKLHIDPTLPVT--VE---RFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQ 140
Cdd:cd03255 81 RrhIGFVFQSFNLLPDLTALenVElplLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 768329558 141 LLVLDEPTQGVD-VNGQVsLYDLINQLRVELNCGVLMVSHD 180
Cdd:cd03255 161 IILADEPTGNLDsETGKE-VMELLRELNKEAGTTIVVVTHD 200
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-207 |
1.72e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 126.81 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 8 DNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ-----------RDPGLRIGYVPQKL 76
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngrpladwspAELARRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 77 HIdpTLPVTVERFMRL-----TRGSKNAEILP--ALKRVQAGHLLNAPLQKLSGGETQRVLLARALL------NQPQLLV 143
Cdd:PRK13548 86 SL--SFPFTVEEVVAMgraphGLSRAEDDALVaaALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768329558 144 LDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAV 207
Cdd:PRK13548 164 LDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQgRLVADGTPAEV 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-196 |
2.22e-35 |
|
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: 125.32 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD--------PGLR-IGYVPQK 75
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvtgvpPERRnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 76 LHIDPTLpvTVE-------RFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPT 148
Cdd:cd03259 81 YALFPHL--TVAeniafglKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768329558 149 QGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNE 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-184 |
4.64e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 124.78 E-value: 4.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKF-NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ---RD---------PGLR--I 69
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngQDlsrlkrreiPYLRrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 70 GYVPQKLHIDPTLPVT--VERFMRLTrGSKNAEI----LPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLV 143
Cdd:COG2884 82 GVVFQDFRLLPDRTVYenVALPLRVT-GKSRKEIrrrvREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 768329558 144 LDEPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLV 184
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELV 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-192 |
5.76e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 130.57 E-value: 5.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQKLH-IDPTL 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEeLDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 83 PVtVERFMRLTRGSKNAEILPALKRVQ-AGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNgqvSLyD 161
Cdd:COG0488 395 TV-LDELRDGAPGGTEQEVRGYLGRFLfSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIE---TL-E 469
|
170 180 190
....*....|....*....|....*....|.
gi 768329558 162 LINQLRVELNCGVLMVSHDLHLVMAKTDEVL 192
Cdd:COG0488 470 ALEEALDDFPGTVLLVSHDRYFLDRVATRIL 500
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-205 |
5.93e-35 |
|
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: 124.40 E-value: 5.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 8 DNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTG-------SVQRDPG---LRIGYVPQKLH 77
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghDVVREPRevrRRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 78 IDPTLPVT--VERFMRLtRGSKNAE----ILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGV 151
Cdd:cd03265 84 VDDELTGWenLYIHARL-YGVPGAErrerIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768329558 152 DVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPE 205
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHgRIIAEGTPE 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-198 |
6.63e-35 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 124.12 E-value: 6.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKF----NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD------PGLRIGYVPQ 74
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgepvtgPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 75 KlhiDPTLP-VTVE-------RFMRLTRGSKNAEILPALKRVQAGHLLNA-PLQkLSGGETQRVLLARALLNQPQLLVLD 145
Cdd:cd03293 81 Q---DALLPwLTVLdnvalglELQGVPKAEARERAEELLELVGLSGFENAyPHQ-LSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 768329558 146 EPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLhlvmaktDEVLCLNHHI 198
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETGKTVLLVTHDI-------DEAVFLADRV 202
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-211 |
4.15e-34 |
|
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: 122.61 E-value: 4.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD----PGL----------RIG 70
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgediSGLseaelyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 71 YVPQK--LHIDPTLPVTVERFMRLTRGSKNAEI----LPALKRV---QAGHLLNAplqKLSGGETQRVLLARALLNQPQL 141
Cdd:cd03261 81 MLFQSgaLFDSLTVFENVAFPLREHTRLSEEEIreivLEKLEAVglrGAEDLYPA---ELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768329558 142 LVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEAV--SQHP 211
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLyDGKIVAEGTPEELraSDDP 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-217 |
2.43e-33 |
|
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: 120.52 E-value: 2.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 7 LDNVSIKFNQRnVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD--------PGLR-IGYVPQKLH 77
Cdd:cd03299 3 VENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlpPEKRdISYVPQNYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 78 IDPTLPV--TVERFMRLTRGSK---NAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVD 152
Cdd:cd03299 82 LFPHMTVykNIAYGLKKRKVDKkeiERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 153 VNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHP--EFIAMF 217
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNgKLIQVGKPEEVFKKPknEFVAEF 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-205 |
2.85e-33 |
|
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: 126.42 E-value: 2.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKF--NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ---------RDPGLR--IGY 71
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdlDEDDLRrrIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQKLHIDPTlpvTVERFMRLTR-GSKNAEILPALKRVQAGHL-------LNAPL----QKLSGGETQRVLLARALLNQP 139
Cdd:COG4987 414 VPQRPHLFDT---TLRENLRLARpDATDEELWAALERVGLGDWlaalpdgLDTWLgeggRRLSGGERRRLALARALLRDA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 140 QLLVLDEPTQGVD-VNGQVSLYDLINQLRvelNCGVLMVSHDLHLvMAKTDEVLCL-NHHICCSGTPE 205
Cdd:COG4987 491 PILLLDEPTEGLDaATEQALLADLLEALA---GRTVLLITHRLAG-LERMDRILVLeDGRIVEQGTHE 554
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-210 |
3.00e-33 |
|
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: 126.87 E-value: 3.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQR--NVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------QRDPG-LR--IGY 71
Cdd:COG2274 474 IELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrQIDPAsLRrqIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQklhiDPTL-PVTVERFMRLTRGSKN-AEILPALKRVQAGHLLNA-PL----------QKLSGGETQRVLLARALLNQ 138
Cdd:COG2274 554 VLQ----DVFLfSGTIRENITLGDPDATdEEIIEAARLAGLHDFIEAlPMgydtvvgeggSNLSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768329558 139 PQLLVLDEPTQGVDVNGQVSLYDLINQLRVelNCGVLMVSHDLHLVmAKTDEVLCLNH-HICCSGTPEAVSQH 210
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKgRIVEDGTHEELLAR 699
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-196 |
4.44e-33 |
|
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: 117.87 E-value: 4.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRN--VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ------RDPGL-----RIGY 71
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlRDLDLeslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQklhiDPtlpvtverfmrltrgsknaeilpalkrvqagHLLNAPLQK--LSGGETQRVLLARALLNQPQLLVLDEPTQ 149
Cdd:cd03228 81 VPQ----DP-------------------------------FLFSGTIREniLSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 768329558 150 GVDVNGQVSLYDLINQLRVelNCGVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03228 126 ALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDD 169
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-196 |
6.11e-33 |
|
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: 119.01 E-value: 6.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 19 VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGS-------VQRDP---GLRIGYVPQKLHIDPTLPV--TV 86
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFatvdgfdVVKEPaeaRRRLGFVSDSTGLYDRLTAreNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 87 ERFMRLtRGSKNAEILPALK----RVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDL 162
Cdd:cd03266 100 EYFAGL-YGLKGDELTARLEeladRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
|
170 180 190
....*....|....*....|....*....|....
gi 768329558 163 INQLRvELNCGVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03266 179 IRQLR-ALGKCILFSTHIMQEVERLCDRVVVLHR 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-217 |
2.00e-32 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 118.16 E-value: 2.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 2 TSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ---RD-PGLR--------I 69
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgEDiTGLPphriarlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 70 GYVPQKLHIDPTLpvTVE------RFMRLTRGSKNA------EILPALK---RVQAGHllnaplqkLSGGETQRVLLARA 134
Cdd:COG0410 81 GYVPEGRRIFPSL--TVEenlllgAYARRDRAEVRAdlervyELFPRLKerrRQRAGT--------LSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 135 LLNQPQLLVLDEPTQG-----VDvngqvSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVS 208
Cdd:COG0410 151 LMSRPKLLLLDEPSLGlapliVE-----EIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVLERgRIVLEGTAAELL 224
|
....*....
gi 768329558 209 QHPEFIAMF 217
Cdd:COG0410 225 ADPEVREAY 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-207 |
6.52e-32 |
|
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: 116.38 E-value: 6.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 19 VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD----PGLR--------IGYVPQKLHIDPTLpvTV 86
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrdiTGLPpheraragIGYVPEGRRIFPEL--TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 87 ERFMRLT----RGSKNAEIL-------PALKRvqaghLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQG----- 150
Cdd:cd03224 93 EENLLLGayarRRAKRKARLervyelfPRLKE-----RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGlapki 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 151 VDvngqvSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAV 207
Cdd:cd03224 168 VE-----EIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERgRVVLEGTAAEL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-204 |
1.19e-31 |
|
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: 115.68 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 13 KFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTG-------SVQRDPGL---RIGYVPQKLHIDPTL 82
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtayingySIRTDRKAarqSLGYCPQFDALFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 83 pvTVE---RFM-RLTRGSK---NAEILPALKRVQAGHLLNAPLQKLSGGeTQRVL-LARALLNQPQLLVLDEPTQGVDVN 154
Cdd:cd03263 91 --TVRehlRFYaRLKGLPKseiKEEVELLLRVLGLTDKANKRARTLSGG-MKRKLsLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 155 GQVSLYDLINQLRVelNCGVLMVSHDLHLVmaktdEVLCLNHHI------CCSGTP 204
Cdd:cd03263 168 SRRAIWDLILEVRK--GRSIILTTHSMDEA-----EALCDRIAImsdgklRCIGSP 216
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-209 |
1.33e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 116.31 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 3 SLVTLDNVSIKF-NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ---RDPGL----------- 67
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILvdgQDVTAlrgralrrlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 68 RIGYVPQKLHIDPTLPV-------------TVERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARA 134
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVltnvlagrlgrtsTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768329558 135 LLNQPQLLVLDEPTQGVD-VNGQVSLyDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQ 209
Cdd:COG3638 161 LVQEPKLILADEPVASLDpKTARQVM-DLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDgRVVFDGPPAELTD 236
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-195 |
2.03e-31 |
|
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: 113.85 E-value: 2.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 7 LDNVSIKF--NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------QRDP---GLRIGYVP 73
Cdd:cd03246 3 VENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisQWDPnelGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 74 QKLhidptlpvtverfmRLTRGSKNAEIlpalkrvqaghllnaplqkLSGGETQRVLLARALLNQPQLLVLDEPTQGVDV 153
Cdd:cd03246 83 QDD--------------ELFSGSIAENI-------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768329558 154 NGQVSLYDLINQLRVElNCGVLMVSHDLHLVmAKTDEVLCLN 195
Cdd:cd03246 130 EGERALNQAIAALKAA-GATRIVIAHRPETL-ASADRILVLE 169
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-166 |
2.25e-31 |
|
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: 114.98 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGrILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD--------PGLR--IGYVPQ 74
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDgqdvlkqpQKLRrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 75 KLHIDPTlpVTVERFM-------RLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEP 147
Cdd:cd03264 80 EFGVYPN--FTVREFLdyiawlkGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170
....*....|....*....
gi 768329558 148 TQGVDVNGQVSLYDLINQL 166
Cdd:cd03264 158 TAGLDPEERIRFRNLLSEL 176
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-217 |
3.07e-31 |
|
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: 115.03 E-value: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD--------PGLR-IGYVPQK 75
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkditnlpPHKRpVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 76 LHIDPTLPVT--VERFMRLTRGSKN---AEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQG 150
Cdd:cd03300 81 YALFPHLTVFenIAFGLRLKKLPKAeikERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 151 VDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPE--FIAMF 217
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKgKIQQIGTPEEIYEEPAnrFVADF 230
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
13-205 |
3.86e-31 |
|
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: 116.72 E-value: 3.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 13 KFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGS-------VQRDPGL---RIGYVPQKLHIDPTL 82
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTarvagydVVREPRKvrrSIGIVPQYASVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 83 P-----VTVERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQV 157
Cdd:TIGR01188 82 TgrenlEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768329558 158 SLYDLINQLrVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPE 205
Cdd:TIGR01188 162 AIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHgRIIAEGTPE 209
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-220 |
8.46e-31 |
|
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: 119.47 E-value: 8.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKF--NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV-----------QRDPGLRIGY 71
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQklhiDPTL-PVTVE----RFMRLTRgsknAEILPALKRVQAgH------------LLNAPLQKLSGGETQRVLLARA 134
Cdd:COG4618 411 LPQ----DVELfDGTIAeniaRFGDADP----EKVVAAAKLAGV-HemilrlpdgydtRIGEGGARLSGGQRQRIGLARA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 135 LLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLvMAKTDEVLCLNHhiccsGTpeavsqhpefI 214
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVITHRPSL-LAAVDKLLVLRD-----GR----------V 544
|
....*.
gi 768329558 215 AMFGPR 220
Cdd:COG4618 545 QAFGPR 550
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-191 |
9.42e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.58 E-value: 9.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ--------RDPG----LR 68
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILldgepvrfRSPRdaqaAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 IGYVPQKLHIDPTLPVT--------VERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQ 140
Cdd:COG1129 81 IAIIHQELNLVPNLSVAeniflgrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768329558 141 LLVLDEPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEV 191
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLK-AQGVAIIYISHRLDEVFEIADRV 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-184 |
9.48e-31 |
|
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: 115.92 E-value: 9.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRN----VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAP---TTGSVQRDP----------- 65
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGedllklsekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 66 ----GLRIGYVPQklhiDP--TL-PV-TVERFM--------RLTRGSKNAEILPALKRV---QAGHLLNA-PLQkLSGGE 125
Cdd:COG0444 81 rkirGREIQMIFQ----DPmtSLnPVmTVGDQIaeplrihgGLSKAEARERAIELLERVglpDPERRLDRyPHE-LSGGM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 768329558 126 TQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLV 184
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVV 214
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
8-179 |
1.00e-30 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 113.91 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 8 DNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD------------PGLRIGYVPQ- 74
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgqdithlpmherARLGIGYLPQe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 75 -----KLHIDPTLPVTVERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQ 149
Cdd:TIGR04406 85 asifrKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFA 164
|
170 180 190
....*....|....*....|....*....|
gi 768329558 150 GVDVNGQVSLYDLINQLRvELNCGVLMVSH 179
Cdd:TIGR04406 165 GVDPIAVGDIKKIIKHLK-ERGIGVLITDH 193
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-194 |
1.05e-30 |
|
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: 118.93 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKF-NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV-----------QRDPGLRIGYV 72
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladadADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 73 PQKLHIdptLPVTVERFMRL-TRGSKNAEILPALKRVQAGHLLNAPLQ-----------KLSGGETQRVLLARALLNQPQ 140
Cdd:TIGR02857 402 PQHPFL---FAGTIAENIRLaRPDASDAEIREALERAGLDEFVAALPQgldtpigeggaGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 768329558 141 LLVLDEPTQGVDVNGQVSLYDLINQLRVelNCGVLMVSHDLHLvMAKTDEVLCL 194
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLAL-AALADRIVVL 529
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-217 |
1.25e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 116.33 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSlVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------QRDPGLR-IGY 71
Cdd:COG3839 1 MAS-LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIliggrdvtDLPPKDRnIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQKLHIDPTLpvTVE-------RFMRLTRGSKNAEILPALKRVQAGHLLNA-PLQkLSGGETQRVLLARALLNQPQLLV 143
Cdd:COG3839 80 VFQSYALYPHM--TVYeniafplKLRKVPKAEIDRRVREAAELLGLEDLLDRkPKQ-LSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768329558 144 LDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHP--EFIAMF 217
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDgRIQQVGTPEELYDRPanLFVAGF 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-210 |
2.37e-30 |
|
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: 113.05 E-value: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 6 TLDNVSIKF-NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ--------------RDPGLRIG 70
Cdd:cd03256 2 EVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdinklkgkalRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 71 YVPQKLHIDPTLPV-------------TVERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLN 137
Cdd:cd03256 82 MIFQQFNLIERLSVlenvlsgrlgrrsTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768329558 138 QPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQH 210
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDgRIVFDGPPAELTDE 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-196 |
2.78e-30 |
|
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: 112.81 E-value: 2.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 13 KFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ--------RDPGL--RIGYV-PQKLHIDPT 81
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpwkRRKKFlrRIGVVfGQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 82 LPVtVE--RFMRLTRGSKNAEILPALKRV----QAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNG 155
Cdd:cd03267 110 LPV-IDsfYLLAAIYDLPPARFKKRLDELsellDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 768329558 156 QVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03267 189 QENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-195 |
4.55e-30 |
|
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: 111.19 E-value: 4.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 6 TLDNVSIKFN-QRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------QRDPGLRIGYVPQkl 76
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpikAKERRKSIGYVMQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 77 hiDPT---LPVTVERfmRLTRGSKNAeilpALKRVQAGHLL-----NAPLQK----LSGGETQRVLLARALLNQPQLLVL 144
Cdd:cd03226 79 --DVDyqlFTDSVRE--ELLLGLKEL----DAGNEQAETVLkdldlYALKERhplsLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768329558 145 DEPTQGVDVNGQVSLYDLINQLRVELNCgVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKA-VIVITHDYEFLAKVCDRVLLLA 200
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-218 |
7.35e-30 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 112.54 E-value: 7.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFN-----QRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ--------------RDP 65
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTidgrditakkkkklKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 66 GLRIGYVPQklhidptLP------VTVER---FmrltrGSKN-----AEilpALKRVQ-AGHLLNAPLQ-------KLSG 123
Cdd:TIGR04521 81 RKKVGLVFQ-------FPehqlfeETVYKdiaF-----GPKNlglseEE---AEERVKeALELVGLDEEylerspfELSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 124 GETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSG 202
Cdd:TIGR04521 146 GQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKgKIVLDG 225
|
250
....*....|....*.
gi 768329558 203 TPEAVSQHPEFIAMFG 218
Cdd:TIGR04521 226 TPREVFSDVDELEKIG 241
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-212 |
9.28e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 113.70 E-value: 9.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV---------QRDPGLR-IGYVPQ 74
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIvlngrdlftNLPPRERrVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 75 klHID--PTLpvTVE-------RFMRLTRGSKNAEILPALKRVQAGHLLNA-PLQkLSGGETQRVLLARALLNQPQLLVL 144
Cdd:COG1118 83 --HYAlfPHM--TVAeniafglRVRPPSKAEIRARVEELLELVQLEGLADRyPSQ-LSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768329558 145 DEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPE 212
Cdd:COG1118 158 DEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQgRIEQVGTPDEVYDRPA 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-214 |
1.42e-29 |
|
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: 111.75 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKF--NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGL-------------RI 69
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-GLdtldeenlweirkKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 70 GYVPQKlhidptlP------VTVER---FMRLTRGSKNAEILP----ALKRVQAGHLLNAPLQKLSGGETQRVLLARALL 136
Cdd:TIGR04520 80 GMVFQN-------PdnqfvgATVEDdvaFGLENLGVPREEMRKrvdeALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 137 NQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDL-HLVMAktDEVLCLNH-HICCSGTPEAVSQHPEFI 214
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMeEAVLA--DRVIVMNKgKIVAEGTPREIFSQVELL 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-236 |
1.65e-29 |
|
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: 113.27 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 23 VSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV-------------------QRdpglRIGYVPQKLHIDPTLp 83
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggevlqdsargiflpphRR----RIGYVFQEARLFPHL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 84 vTVER-----FMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVS 158
Cdd:COG4148 93 -SVRGnllygRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 159 LYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPEFIAMFGPRGAEEL--AIYRHHHNHR 235
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQgRVVASGPLAEVLSRPDLLPLAGGEEAGSVleATVAAHDPDY 251
|
.
gi 768329558 236 H 236
Cdd:COG4148 252 G 252
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-212 |
5.14e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 109.35 E-value: 5.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTlDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD-------P-------G 66
Cdd:COG1137 1 MMTLEA-ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDgedithlPmhkrarlG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 67 lrIGYVPQ------KLhidptlpvTVE-------RFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLAR 133
Cdd:COG1137 80 --IGYLPQeasifrKL--------TVEdnilavlELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 134 ALLNQPQLLVLDEPTQGVD---VNgqvSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQ 209
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDpiaVA---DIQKIIRHLK-ERGIGVLITDHNVRETLGICDRAYIISEgKVLAEGTPEEILN 225
|
...
gi 768329558 210 HPE 212
Cdd:COG1137 226 NPL 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-212 |
8.00e-29 |
|
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: 108.78 E-value: 8.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD------------PGLRIGYV 72
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqditklpmhkrARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 73 PQKLHIDPTLpvTVE-------RFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLD 145
Cdd:cd03218 81 PQEASIFRKL--TVEenilavlEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 146 EPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPE 212
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEgKVLAEGTPEEIAANEL 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-217 |
2.16e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 110.19 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 3 SLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV-------------QRDpglrI 69
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvthrsiqQRD----I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 70 GYVPQKLHIDPTLPV--TVE---RFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVL 144
Cdd:PRK11432 81 CMVFQSYALFPHMSLgeNVGyglKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 145 DEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHP--EFIAMF 217
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKgKIMQIGSPQELYRQPasRFMASF 236
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
9-192 |
4.92e-28 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 106.23 E-value: 4.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 9 NVSIKFNQRnvLSGVSLALQ---PGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGL---------------RIG 70
Cdd:cd03297 1 MLCVDIEKR--LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 71 YVPQKLHIDPTLPVtVERFMRLTRGSKNAEIL----PALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDE 146
Cdd:cd03297 79 LVFQQYALFPHLNV-RENLAFGLKRKRNREDRisvdELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 768329558 147 PTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVL 192
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIV 203
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-179 |
5.69e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 111.44 E-value: 5.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKF-NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQKLHIDP-TL 82
Cdd:COG4178 363 LALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLgTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 83 ------PVTVERFmrltrgsKNAEILPALKRVQAGHL---LNAPL---QKLSGGETQRVLLARALLNQPQLLVLDEPTQG 150
Cdd:COG4178 443 reallyPATAEAF-------SDAELREALEAVGLGHLaerLDEEAdwdQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180 190
....*....|....*....|....*....|
gi 768329558 151 VDVNGQVSLYDLINQlrvEL-NCGVLMVSH 179
Cdd:COG4178 516 LDEENEAALYQLLRE---ELpGTTVISVGH 542
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-207 |
8.30e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 106.64 E-value: 8.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ-----------RDPGLRIGYVP 73
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgdkpismlssRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 74 QKlHIDPTlPVTVERFM------------RLTrGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQL 141
Cdd:PRK11231 83 QH-HLTPE-GITVRELVaygrspwlslwgRLS-AEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 142 LVLDEPTQGVDVNGQVSLYDLINQLRVElncG--VLMVSHDL--------HLVMAKTDEVLclnhhicCSGTPEAV 207
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQ---GktVVTVLHDLnqasrycdHLVVLANGHVM-------AQGTPEEV 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-212 |
1.06e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.63 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ-----------RDPglRIGYVP 73
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgtdvsrlhaRDR--KVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 74 QKLHIDPTLPV--------TV-ERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVL 144
Cdd:PRK10851 81 QHYALFRHMTVfdniafglTVlPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768329558 145 DEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPE 212
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQgNIEQAGTPDQVWREPA 229
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-207 |
1.15e-27 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 106.08 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 6 TLDNVSIkfnqRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLaPTTGSVQRDpGLRI------------GYVP 73
Cdd:COG4138 2 QLNDVAV----AGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLN-GRPLsdwsaaelarhrAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 74 QklHIDPTLPVTVERFMRLTRGSK------NAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLN-------QPQ 140
Cdd:COG4138 76 Q--QQSPPFAMPVFQYLALHQPAGasseavEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 141 LLVLDEPTQGVDVNGQVSLYDLINQLrVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAV 207
Cdd:COG4138 154 LLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQgKLVASGETAEV 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-205 |
1.20e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 110.64 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSikF---NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV-----------QRDpgLR-- 68
Cdd:COG1132 340 IEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirdltLES--LRrq 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 IGYVPQklhiDPTLpvtverFMR-----LTRGSKNA---EILPALKRVQAGHL-------LNAPL----QKLSGGETQRV 129
Cdd:COG1132 416 IGVVPQ----DTFL------FSGtirenIRYGRPDAtdeEVEEAAKAAQAHEFiealpdgYDTVVgergVNLSGGQRQRI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768329558 130 LLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVelNCGVLMVSHDLHLVMaKTDEVLCLNH-HICCSGTPE 205
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIR-NADRILVLDDgRIVEQGTHE 559
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-217 |
1.40e-27 |
|
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: 105.88 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------QRDPGLR-IGYVPQK 75
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedatDVPVQERnVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 76 LHIDPTLPVT------VERFMRLTRGSKN---AEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDE 146
Cdd:cd03296 83 YALFRHMTVFdnvafgLRVKPRSERPPEAeirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768329558 147 PTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHP--EFIAMF 217
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKgRIEQVGTPDEVYDHPasPFVYSF 236
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-183 |
1.97e-27 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 105.21 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 2 TSLVTLDNVSIKFNQR----NVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ----------RDP-- 65
Cdd:COG4181 6 APIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRlagqdlfaldEDAra 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 66 GLR---IGYVPQKLHIDPTLPVtVERFM---RLtRGSKNAEILPA--LKRVQAGHLLNA-PLQkLSGGETQRVLLARALL 136
Cdd:COG4181 86 RLRarhVGFVFQSFQLLPTLTA-LENVMlplEL-AGRRDARARARalLERVGLGHRLDHyPAQ-LSGGEQQRVALARAFA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768329558 137 NQPQLLVLDEPTQGVD-VNGQVSLyDLINQLRVELNCGVLMVSHDLHL 183
Cdd:COG4181 163 TEPAILFADEPTGNLDaATGEQII-DLLFELNRERGTTLVLVTHDPAL 209
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-181 |
2.76e-27 |
|
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: 109.37 E-value: 2.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 19 VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV-----------QRDPGLRIGYVPQKLHIDPTlpvTVE 87
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvssldQDEVRRRVSVCAQDAHLFDT---TVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 88 RFMRLTRG-SKNAEILPALKRVQAGHLLNAPL-----------QKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNG 155
Cdd:TIGR02868 427 ENLRLARPdATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
|
170 180
....*....|....*....|....*.
gi 768329558 156 QVSLYDLINQLRVELncGVLMVSHDL 181
Cdd:TIGR02868 507 ADELLEDLLAALSGR--TVVLITHHL 530
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-182 |
3.17e-27 |
|
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: 104.57 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 7 LDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLL-----APTTGSVQRDPG-------------LR 68
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKdiydldvdvlelrRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 IGYVPQKlhidPTL-PVTVERFMRLT---RGSKNAEILP-----ALKRVQAGHLLNAPLQ--KLSGGETQRVLLARALLN 137
Cdd:cd03260 83 VGMVFQK----PNPfPGSIYDNVAYGlrlHGIKLKEELDerveeALRKAALWDEVKDRLHalGLSGGQQQRLCLARALAN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768329558 138 QPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELncGVLMVSHDLH 182
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQ 201
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-182 |
3.18e-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: 103.84 E-value: 3.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ---------RDPGLRIGYVpqk 75
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgksyqknIEALRRIGAL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 76 lhID-PTL--PVTVERFMRLT---RGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQ 149
Cdd:cd03268 78 --IEaPGFypNLTARENLRLLarlLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190
....*....|....*....|....*....|...
gi 768329558 150 GVDVNGQVSLYDLINQLRVElNCGVLMVSHDLH 182
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQ-GITVLISSHLLS 187
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-196 |
3.42e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 106.71 E-value: 3.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVqrdpglRI-GYVPQK------------------LHIDp 80
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV------RVlGYVPFKrrkefarrigvvfgqrsqLWWD- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 81 tLPVtVERFmRLtrgskNAEI--LPA---LKRV-------QAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPT 148
Cdd:COG4586 111 -LPA-IDSF-RL-----LKAIyrIPDaeyKKRLdelvellDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768329558 149 QGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH 230
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-152 |
4.22e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 106.04 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ----------RDPGLRIG 70
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsraRHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 71 YVPQKLHIDPTLPV-----TVERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLD 145
Cdd:PRK13537 84 VVPQFDNLDPDFTVrenllVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
....*..
gi 768329558 146 EPTQGVD 152
Cdd:PRK13537 164 EPTTGLD 170
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-217 |
4.65e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.96 E-value: 4.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 2 TSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIGYVP-QKLHID- 79
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-GQDITHVPaENRHVNt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 80 --------PTLPV--TVERFMRLtRGSKNAEILP----ALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLD 145
Cdd:PRK09452 91 vfqsyalfPHMTVfeNVAFGLRM-QKTPAAEITPrvmeALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768329558 146 EPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPE--FIAMF 217
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDgRIEQDGTPREIYEEPKnlFVARF 244
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-196 |
4.97e-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: 102.51 E-value: 4.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKfnqrNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ--------RDPG----LRIGY 71
Cdd:cd03215 4 VLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITldgkpvtrRSPRdairAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VP---QKLHIDPTLPVtverfmrltrgSKNAeILPALkrvqaghllnaplqkLSGGETQRVLLARALLNQPQLLVLDEPT 148
Cdd:cd03215 80 VPedrKREGLVLDLSV-----------AENI-ALSSL---------------LSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768329558 149 QGVDVNGQVSLYDLINQLRVElNCGVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYE 179
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-191 |
5.05e-27 |
|
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: 102.12 E-value: 5.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ--------RDPG----LRIGYV 72
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILvdgkevsfASPRdarrAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 73 PQklhidptlpvtverfmrltrgsknaeilpalkrvqaghllnaplqkLSGGETQRVLLARALLNQPQLLVLDEPTQGVD 152
Cdd:cd03216 81 YQ----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190
....*....|....*....|....*....|....*....
gi 768329558 153 VNGQVSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEV 191
Cdd:cd03216 115 PAEVERLFKVIRRLR-AQGVAVIFISHRLDEVFEIADRV 152
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-152 |
7.02e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 106.07 E-value: 7.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ----------RDPGLRIGYVPQ 74
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 75 KLHIDPTLPV-----TVERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQ 149
Cdd:PRK13536 122 FDNLDLEFTVrenllVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
...
gi 768329558 150 GVD 152
Cdd:PRK13536 202 GLD 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-217 |
8.17e-27 |
|
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: 103.92 E-value: 8.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFN-QRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------QRDP-GLR--IGYV 72
Cdd:cd03295 1 IEFENVTKRYGgGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedirEQDPvELRrkIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 73 PQKLHIDPTLPV--------TVERFMRLTRGSKNAEILpALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVL 144
Cdd:cd03295 81 IQQIGLFPHMTVeenialvpKLLKWPKEKIRERADELL-ALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 145 DEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLhlvmaktDEVLCLNHHICC--------SGTPEAV--SQHPEFI 214
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDI-------DEAFRLADRIAImkngeivqVGTPDEIlrSPANDFV 232
|
...
gi 768329558 215 AMF 217
Cdd:cd03295 233 AEF 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-196 |
1.07e-26 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 103.04 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRN----VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV---------QRDPGLR-- 68
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgtdltlLSGKELRka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 ---IGYVPQKLHI--DPTLPVTVERFMRLTRGSKN---AEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQ 140
Cdd:cd03258 81 rrrIGMIFQHFNLlsSRTVFENVALPLEIAGVPKAeieERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 141 LLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-195 |
2.06e-26 |
|
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: 102.69 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQ-RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD---------PGLR--IGYV 72
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdirevtlDSLRraIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 73 PQklhiDPTL-PVTVE---RFMRLTrgSKNAEILPALKRVQ-AGHLLNAPLQ----------KLSGGETQRVLLARALLN 137
Cdd:cd03253 81 PQ----DTVLfNDTIGyniRYGRPD--ATDEEVIEAAKAAQiHDKIMRFPDGydtivgerglKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 138 QPQLLVLDEPTQGVDVNGQVSLYDLINQLRVelNCGVLMVSHDLHLVMaKTDEVLCLN 195
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIV-NADKIIVLK 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-199 |
2.16e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.71 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 2 TSLVTLDNVSIKFNQ----RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLL-APTTGSVQRD------------ 64
Cdd:PRK15134 3 QPLLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpSPPVVYPSGDirfhgesllhas 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 65 -------PGLRIGYVPQK-------LH-IDPTLP--VTVERFMRltRGSKNAEILPALKRV---QAGHLLNAPLQKLSGG 124
Cdd:PRK15134 83 eqtlrgvRGNKIAMIFQEpmvslnpLHtLEKQLYevLSLHRGMR--REAARGEILNCLDRVgirQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768329558 125 ETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNHHIC 199
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-191 |
2.18e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.65 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ--------RDPG----LR 68
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILidgkpvriRSPRdaiaLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 IGYVPQKLHIDPTLPVTvERFMrLTRGSKNAEILP---ALKRVQAghL---------LNAPLQKLSGGETQRVLLARALL 136
Cdd:COG3845 82 IGMVHQHFMLVPNLTVA-ENIV-LGLEPTKGGRLDrkaARARIRE--LserygldvdPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 137 NQPQLLVLDEPT-----QGVDvngqvSLYDLINQLRVElNCGVLMVSHDLHLVMAKTDEV 191
Cdd:COG3845 158 RGARILILDEPTavltpQEAD-----ELFEILRRLAAE-GKSIIFITHKLREVMAIADRV 211
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
8-163 |
3.15e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 101.49 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 8 DNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV------QRDPGLR--IGYVPQKLHID 79
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkldggdIDDPDVAeaCHYLGHRNAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 80 PTLpvTVE---RFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQ 156
Cdd:PRK13539 86 PAL--TVAenlEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
....*..
gi 768329558 157 VSLYDLI 163
Cdd:PRK13539 164 ALFAELI 170
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-196 |
5.54e-26 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 100.79 E-value: 5.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------QRDPGLR-IGYVPQK 75
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtDLPPKDRdIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 76 LHIDPTLpvTVERFMRL---TRGSKNAEILPALKRV----QAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPT 148
Cdd:cd03301 81 YALYPHM--TVYDNIAFglkLRKVPKDEIDERVREVaellQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768329558 149 QGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-196 |
1.31e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.33 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 17 RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ--------RDPG----LRIGYVPQ--KLH-IDPT 81
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvriRSPRdairAGIAYVPEdrKGEgLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 82 LPVT----------VERFMRLTRGSKNAEILPALKR--VQAGHlLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQ 149
Cdd:COG1129 345 LSIRenitlasldrLSRGGLLDRRRERALAEEYIKRlrIKTPS-PEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 768329558 150 GVDVNGQVSLYDLINQLRVElNCGVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG1129 424 GIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMRE 469
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-196 |
1.65e-25 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 99.63 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQ-RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ------------RDPGLR-- 68
Cdd:TIGR02673 1 MIEFHNVSKAYPGgVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRiagedvnrlrgrQLPLLRrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 IGYVPQKLHIDPTLPV--TVERFMRLtRGSKNAEI----LPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLL 142
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVyeNVALPLEV-RGKKEREIqrrvGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 768329558 143 VLDEPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLN-KRGTTVIVATHDLSLVDRVAHRVIILDD 212
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-194 |
1.68e-25 |
|
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: 99.23 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 7 LDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV----QRDPGL-----------RIGY 71
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVylngQETPPLnskkaskfrreKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQK------LHIDPTLPVTVErFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLD 145
Cdd:TIGR03608 81 LFQNfalienETVEENLDLGLK-YKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768329558 146 EPTQGVDVNGQVSLYDLINQLRVElNCGVLMVSHDLhLVMAKTDEVLCL 194
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-180 |
2.42e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.09 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 6 TLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAP---TTGSV-------------QRdpglRI 69
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVllngrrltalpaeQR----RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 70 GYVPQKLHIDPTLPVtVERFM-----RLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVL 144
Cdd:COG4136 79 GILFQDDLLFPHLSV-GENLAfalppTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 768329558 145 DEPTQGVDVNGQVSLYDLI-NQLRvELNCGVLMVSHD 180
Cdd:COG4136 158 DEPFSKLDAALRAQFREFVfEQIR-QRGIPALLVTHD 193
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-212 |
2.56e-25 |
|
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: 103.61 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQ----RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAP----TTGSV----------- 61
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSIlfdgqdllgls 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 62 ----QRDPGLRIGYVPQklhiDP--TL-PV-TVERFM--------RLTRGSKNAEILPALKRVQ---AGHLLNA-PLQkL 121
Cdd:COG4172 83 erelRRIRGNRIAMIFQ----EPmtSLnPLhTIGKQIaevlrlhrGLSGAAARARALELLERVGipdPERRLDAyPHQ-L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 122 SGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLV--MAktDEVLCLNH-HI 198
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVrrFA--DRVAVMRQgEI 235
|
250
....*....|....
gi 768329558 199 CCSGTPEAVSQHPE 212
Cdd:COG4172 236 VEQGPTAELFAAPQ 249
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-179 |
2.67e-25 |
|
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: 99.20 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFN--QRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------QRDPG-LR--IGY 71
Cdd:cd03245 3 IEFRNVSFSYPnqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirQLDPAdLRrnIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQklhiDPTL--------------PVTVERFMRLtrgsknAEILPALKRVQaGHLLNAPLQ------KLSGGETQRVLL 131
Cdd:cd03245 83 VPQ----DVTLfygtlrdnitlgapLADDERILRA------AELAGVTDFVN-KHPNGLDLQigergrGLSGGQRQAVAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768329558 132 ARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNcgVLMVSH 179
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKT--LIIITH 197
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
20-184 |
1.24e-24 |
|
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: 102.17 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRI-----LTLLGPNGAGKSTLVRVVLGLLAPTTGSVqrDPGLRIGYVPQKLHIDptLPVTVERFMRLTR 94
Cdd:COG1245 351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPD--YDGTVEEFLRSAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 95 GSK------NAEILpalKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRV 168
Cdd:COG1245 427 TDDfgssyyKTEII---KPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAE 503
|
170
....*....|....*.
gi 768329558 169 ELNCGVLMVSHDLHLV 184
Cdd:COG1245 504 NRGKTAMVVDHDIYLI 519
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-179 |
1.37e-24 |
|
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: 96.47 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 16 QRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAP--TTGSV--------QRDPGLRIGYVPQKLHIDPTLpvT 85
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVlingrpldKRSFRKIIGYVPQDDILHPTL--T 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 86 VERFMRLTrgsknaeilpalkrvqaghllnAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQ 165
Cdd:cd03213 99 VRETLMFA----------------------AKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRR 156
|
170
....*....|....
gi 768329558 166 LRvELNCGVLMVSH 179
Cdd:cd03213 157 LA-DTGRTIICSIH 169
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
10-236 |
1.47e-24 |
|
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: 100.19 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 10 VSIKFNQRnvLSGVSLALQ---PGR-ILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGL---------------RIG 70
Cdd:TIGR02142 1 LSARFSKR--LGDFSLDADftlPGQgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 71 YVPQKLHIDPTLPV--TVERFMRLTRGSKNAEILPALKRVQA-GHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEP 147
Cdd:TIGR02142 79 YVFQEARLFPHLSVrgNLRYGMKRARPSERRISFERVIELLGiGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 148 TQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEAVSQHPEFIAM-FGPRGAEEL 225
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLeDGRVAAAGPIAEVWASPDLPWLaREDQGSLIE 238
|
250
....*....|.
gi 768329558 226 AIYRHHHNHRH 236
Cdd:TIGR02142 239 GVVAEHDQHYG 249
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-197 |
2.14e-24 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 97.12 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFN-------QRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ-RDPG------ 66
Cdd:COG4778 1 MTTLLEVENLSKTFTlhlqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvRHDGgwvdla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 67 ---------LR---IGYVPQKLHIDP---TLPVTVERFmrLTRGSKNAEilpALKRvqAGHLL---NAPlQKL------- 121
Cdd:COG4778 81 qaspreilaLRrrtIGYVSQFLRVIPrvsALDVVAEPL--LERGVDREE---ARAR--ARELLarlNLP-ERLwdlppat 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 122 -SGGETQRVLLARALLNQPQLLVLDEPTQGVD-VNGQVSLyDLINQLRVElNCGVLMVSHDLHLVMAKTDEVLCLNHH 197
Cdd:COG4778 153 fSGGEQQRVNIARGFIADPPLLLLDEPTASLDaANRAVVV-ELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
15-210 |
2.24e-24 |
|
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: 97.37 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 15 NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPG--------------LRIGYVPQKLHIDP 80
Cdd:TIGR02315 13 NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTditklrgkklrklrRRIGMIFQHYNLIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 81 TLPV-------------TVERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEP 147
Cdd:TIGR02315 93 RLTVlenvlhgrlgykpTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768329558 148 TQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQH 210
Cdd:TIGR02315 173 IASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAgEIVFDGAPSELDDE 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-214 |
3.13e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 97.37 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD-------PGLRI---G 70
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRgqhieglPGHQIarmG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 71 YVPQKLHIDPTLPVTV-ERFMRLTRGSKNAEIL------PA---------------LKRVQAGHLLNAPLQKLSGGETQR 128
Cdd:PRK11300 82 VVRTFQHVRLFREMTViENLLVAQHQQLKTGLFsgllktPAfrraesealdraatwLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 129 VLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNHHI-CCSGTPEAV 207
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTpLANGTPEEI 241
|
....*..
gi 768329558 208 SQHPEFI 214
Cdd:PRK11300 242 RNNPDVI 248
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-180 |
3.29e-24 |
|
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: 100.78 E-value: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 6 TLDNVSIKFN-QRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQKLHIDPTLPV 84
Cdd:TIGR03719 6 TMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 85 --TVERFMrltrgsknAEILPALKR----------------------------VQA--GHLLN----------------A 116
Cdd:TIGR03719 86 reNVEEGV--------AEIKDALDRfneisakyaepdadfdklaaeqaelqeiIDAadAWDLDsqleiamdalrcppwdA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768329558 117 PLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNgqvSLYDLINQLRvELNCGVLMVSHD 180
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQ-EYPGTVVAVTHD 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-181 |
3.47e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 96.36 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 6 TLDNVSIKFNQRNVlsGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------QRDPGLR--------- 68
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqdltALPPAERpvsmlfqen 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 -----------IGyvpqkLHIDPTLpvtverfmRLTRGSKnAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLN 137
Cdd:COG3840 81 nlfphltvaqnIG-----LGLRPGL--------KLTAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 768329558 138 QPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDL 181
Cdd:COG3840 147 KRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDP 190
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-210 |
4.30e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 97.39 E-value: 4.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKF--NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGL----------- 67
Cdd:PRK13635 2 KEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG-GMvlseetvwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 68 -RIGYVPQklhiDPT---LPVTVE---RFMRLTRGSKNAEILP----ALKRVQAGHLLNAPLQKLSGGETQRVLLARALL 136
Cdd:PRK13635 81 rQVGMVFQ----NPDnqfVGATVQddvAFGLENIGVPREEMVErvdqALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768329558 137 NQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVmAKTDEVLCLNH-HICCSGTPEAVSQH 210
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKgEILEEGTPEEIFKS 230
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-184 |
4.32e-24 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 100.27 E-value: 4.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 30 GRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVqrDPGLRIGYVPQKLHIDPtlPVTVERFMRLTR---GSK--NAEILpa 104
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQYIKPDY--DGTVEDLLRSITddlGSSyyKSEII-- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 105 lKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLV 184
Cdd:PRK13409 439 -KPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMI 517
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3-207 |
4.70e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 96.50 E-value: 4.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 3 SLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDP-----------GLR-IG 70
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplharARRgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 71 YVPQKLHIDPTLPV------TVERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVL 144
Cdd:PRK10895 82 YLPQEASIFRRLSVydnlmaVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768329558 145 DEPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAV 207
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQgHLIAHGTPTEI 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-207 |
5.08e-24 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 96.54 E-value: 5.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLaPTTGSV-----------QRDPGLRIGYVPQklHIDPTLPVTVER 88
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIqfagqpleawsAAELARHRAYLSQ--QQTPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 89 FMRLTRGSKNAEILPAL------KRVQAGHLLNAPLQKLSGGETQRVLLARALL-----NQP--QLLVLDEPTQGVDVNG 155
Cdd:PRK03695 89 YLTLHQPDKTRTEAVASalnevaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 768329558 156 QVSLYDLINQLrVELNCGVLMVSHDLHLVMAKTDEVLCLNHHIC-CSGTPEAV 207
Cdd:PRK03695 169 QAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLlASGRRDEV 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-205 |
5.86e-24 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 96.88 E-value: 5.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKF-NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ-----RDPGLR---IGY 71
Cdd:PRK15056 3 QQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqpTRQALQknlVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQKLHIDPTLPVTVER-----------FMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQ 140
Cdd:PRK15056 83 VPQSEEVDWSFPVLVEDvvmmgryghmgWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768329558 141 LLVLDEPTQGVDVNGQVSLYDLINQLRVElNCGVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPE 205
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-195 |
1.38e-23 |
|
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: 95.64 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 19 VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------QRDPGLR--------------IGYVPQKL 76
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsfrgqdlyQLDRKQRrafrrdvqlvfqdsPSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 77 HIDPTLPVTVERFMRLTRGSKNAEILPALKRV--QAGHLLNAPlQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVN 154
Cdd:TIGR02769 106 TVRQIIGEPLRHLTSLDESEQKARIAELLDMVglRSEDADKLP-RQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 768329558 155 GQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMD 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-214 |
3.32e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.83 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIGYVP------- 73
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD-GVDLSHVPpyqrpin 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 74 ---QKLHIDPTLpvTVERFM-------RLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLV 143
Cdd:PRK11607 95 mmfQSYALFPHM--TVEQNIafglkqdKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 144 LDEPTQGVDVN----GQVSLYDLINqlRVELNCgvLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHP------E 212
Cdd:PRK11607 173 LDEPMGALDKKlrdrMQLEVVDILE--RVGVTC--VMVTHDQEEAMTMAGRIAIMNRgKFVQIGEPEEIYEHPttrysaE 248
|
..
gi 768329558 213 FI 214
Cdd:PRK11607 249 FI 250
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-192 |
4.12e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.54 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLvTLDNVSIKF----NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD------PGLRIG 70
Cdd:COG4525 1 MSML-TVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDgvpvtgPGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 71 YVPQKLHIDPTLPV--TVE---RFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLD 145
Cdd:COG4525 80 VVFQKDALLPWLNVldNVAfglRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768329558 146 EPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLH--LVMAkTDEVL 192
Cdd:COG4525 160 EPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEeaLFLA-TRLVV 207
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-179 |
9.97e-23 |
|
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: 91.06 E-value: 9.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKF-NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQKlhidPTLP 83
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQR----PYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 84 vtverfmrltRGSknaeilpaLKRVqaghlLNAPLQK-LSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDL 162
Cdd:cd03223 77 ----------LGT--------LREQ-----LIYPWDDvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170
....*....|....*..
gi 768329558 163 INQLRvelnCGVLMVSH 179
Cdd:cd03223 134 LKELG----ITVISVGH 146
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-207 |
1.04e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.22 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIGYVP----------- 73
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD-GLDVATTPsrelakrlail 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 74 -QKLHIdpTLPVTVE------RFM----RLTRGSKnAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLL 142
Cdd:COG4604 81 rQENHI--NSRLTVRelvafgRFPyskgRLTAEDR-EIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 143 VLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEAV 207
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMkDGRVVAQGTPEEI 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-214 |
1.26e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.22 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 19 VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIGY-------VPQKLHI------DPTLPVT 85
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIK-GEPIKYdkkslleVRKTVGIvfqnpdDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 86 VER---FMRLTRGSKNAEI----LPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVS 158
Cdd:PRK13639 96 VEEdvaFGPLNLGLSKEEVekrvKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 768329558 159 LYDLINQLRVElNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPEFI 214
Cdd:PRK13639 176 IMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDgKIIKEGTPKEVFSDIETI 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-183 |
1.44e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 92.19 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 2 TSLVTLDNVSIKFNQRN----VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV------------QRDP 65
Cdd:PRK11629 3 KILLQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsklssAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 66 GLR---IGYVPQKLHIDPTLPVTVERFMRLTRGSKN-AEI----LPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLN 137
Cdd:PRK11629 83 ELRnqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKpAEInsraLEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 768329558 138 QPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHL 183
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-184 |
4.22e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 91.67 E-value: 4.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 17 RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV------------------QRDPGL----RIGYVPQ 74
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplaklnraqrkafRRDIQMvfqdSISAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 75 KLHIDPTLPVTVERFMRLTRGSKNAEILPALKRVQ--AGHLLNAPlQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVD 152
Cdd:PRK10419 105 RKTVREIIREPLRHLLSLDKAERLARASEMLRAVDldDSVLDKRP-PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190
....*....|....*....|....*....|..
gi 768329558 153 VNGQVSLYDLINQLRVELNCGVLMVSHDLHLV 184
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQFGTACLFITHDLRLV 215
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-214 |
4.33e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 91.98 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 2 TSLVTLDNVSIKFN--QRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIG-----YVPQ 74
Cdd:PRK13632 5 SVMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKID-GITISkenlkEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 75 KLHI---DPT---LPVTVE---RF----MRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQL 141
Cdd:PRK13632 84 KIGIifqNPDnqfIGATVEddiAFglenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768329558 142 LVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMaKTDEVLCLNH-HICCSGTPEAVSQHPEFI 214
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEgKLIAQGKPKEILNNKEIL 236
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-148 |
4.67e-22 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 94.42 E-value: 4.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 16 QRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQKLHIDPTLPV--TVERFMrlt 93
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVreNVEEGV--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 94 rgsknAEILPALKR------------------------VQA------GHLLN----------------APLQKLSGGETQ 127
Cdd:PRK11819 96 -----AEVKAALDRfneiyaayaepdadfdalaaeqgeLQEiidaadAWDLDsqleiamdalrcppwdAKVTKLSGGERR 170
|
170 180
....*....|....*....|.
gi 768329558 128 RVLLARALLNQPQLLVLDEPT 148
Cdd:PRK11819 171 RVALCRLLLEKPDMLLLDEPT 191
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
11-166 |
7.09e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.84 E-value: 7.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 11 SIKFNQRN-------VLSGVSLALQPGRILTLLGPNGAGKSTLVRVvLGLL-APTTGSVQ---------RDPG------L 67
Cdd:COG4161 2 SIQLKNINcfygshqALFDINLECPSGETLVLLGPSGAGKSSLLRV-LNLLeTPDSGQLNiaghqfdfsQKPSekairlL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 68 R--IGYVPQKLHIDPTLPVT---VERFMRLTRGSKNAEILPA---LKRVQAGHLLNA-PLQkLSGGETQRVLLARALLNQ 138
Cdd:COG4161 81 RqkVGMVFQQYNLWPHLTVMenlIEAPCKVLGLSKEQAREKAmklLARLRLTDKADRfPLH-LSGGQQQRVAIARALMME 159
|
170 180 190
....*....|....*....|....*....|
gi 768329558 139 PQLLVLDEPTQGVD--VNGQVSlyDLINQL 166
Cdd:COG4161 160 PQVLLFDEPTAALDpeITAQVV--EIIREL 187
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-215 |
8.24e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.40 E-value: 8.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 17 RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ-----------RDPGLRIGYVPQKLHiDPTLPVT 85
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgepitkeniREVRKFVGLVFQNPD-DQIFSPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 86 VER-------FMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVS 158
Cdd:PRK13652 96 VEQdiafgpiNLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 159 LYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPEFIA 215
Cdd:PRK13652 176 LIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKgRIVAYGTVEEIFLQPDLLA 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-179 |
9.09e-22 |
|
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: 90.02 E-value: 9.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 3 SLVTLDNVSIKFNQRN----VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLL---APTTGSV-----QRDPGL--- 67
Cdd:cd03234 2 RVLPWWDVGLKAKNWNkyarILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQIlfngqPRKPDQfqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 68 RIGYVPQKLHIDPTLpvTVERF------MRLTRGSKNAEILP-----ALKRVQAGHLLNAPLQKLSGGETQRVLLARALL 136
Cdd:cd03234 82 CVAYVRQDDILLPGL--TVRETltytaiLRLPRKSSDAIRKKrvedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768329558 137 NQPQLLVLDEPTQGVDvngQVSLYDLINQLR--VELNCGVLMVSH 179
Cdd:cd03234 160 WDPKVLILDEPTSGLD---SFTALNLVSTLSqlARRNRIVILTIH 201
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-194 |
1.71e-21 |
|
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: 88.14 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKF--NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQrdpglrigyvpqklhIDPTL 82
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT---------------LDGVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 83 PVTVERFMRLTRGSKNaeilpalkrvQAGHLLNAPL-----QKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQV 157
Cdd:cd03247 66 VSDLEKALSSLISVLN----------QRPYLFDTTLrnnlgRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 768329558 158 SLYDLInqLRVELNCGVLMVSHdlHLV-MAKTDEVLCL 194
Cdd:cd03247 136 QLLSLI--FEVLKDKTLIWITH--HLTgIEHMDKILFL 169
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-192 |
1.94e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.76 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD------PGLRIGYVPQKLH 77
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 78 IDPTLPV--TVERFMRLT---RGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVD 152
Cdd:PRK11248 81 LLPWRNVqdNVAFGLQLAgveKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 768329558 153 VNGQVSLYDLINQLRVELNCGVLMVSHDL-HLVMAKTDEVL 192
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETGKQVLLITHDIeEAVFMATELVL 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-155 |
1.98e-21 |
|
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: 88.70 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 17 RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV---------QRDPGLR-IGYVPQKLHIDPTLPVtV 86
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllnggpldfQRDSIARgLLYLGHAPGIKTTLSV-L 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768329558 87 ERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNG 155
Cdd:cd03231 92 ENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-181 |
2.02e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 89.60 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV---QRDPGLRI-------- 69
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrMRDGQLRDlyalseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 70 ---------GYVPQklhiDPT--LPVTV-------ERFMRLtrGSKN-----AEILPALKRVQ--AGHLLNAPLQkLSGG 124
Cdd:PRK11701 83 rrrllrtewGFVHQ----HPRdgLRMQVsaggnigERLMAV--GARHygdirATAGDWLERVEidAARIDDLPTT-FSGG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 768329558 125 ETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDL 181
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDL 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-210 |
2.16e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.37 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRN----------------------VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTT 58
Cdd:COG1134 1 MSSMIEVENVSKSYRLYHepsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 59 GSVQRDpglriGYVPQKLHI----DPTLpvTVE-------RFMRLTRgsknAEILPALKRVQA----GHLLNAPLQKLSG 123
Cdd:COG1134 81 GRVEVN-----GRVSALLELgagfHPEL--TGReniylngRLLGLSR----KEIDEKFDEIVEfaelGDFIDQPVKTYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 124 GETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSG 202
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELR-ESGRTVIFVSHSMGAVRRLCDRAIWLEKgRLVMDG 228
|
....*...
gi 768329558 203 TPEAVSQH 210
Cdd:COG1134 229 DPEEVIAA 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-192 |
2.67e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.35 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSvqrdpgLRIGYVPQKLHIDPTlpv 84
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE------LLAGTAPLAEAREDT--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 85 tveRFM----RLT-------------RGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEP 147
Cdd:PRK11247 84 ---RLMfqdaRLLpwkkvidnvglglKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768329558 148 TQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVL 205
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
11-166 |
3.01e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 88.92 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 11 SIKFNQRNVLSGVSLAL-------QPGRILTLLGPNGAGKSTLVRVvLGLL-APTTGSVQ---------RDPG------L 67
Cdd:PRK11124 2 SIQLNGINCFYGAHQALfditldcPQGETLVLLGPSGAGKSSLLRV-LNLLeMPRSGTLNiagnhfdfsKTPSdkaireL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 68 R--IGYVPQKLHIDPTLPVT---VERFMR---LTRGSKNAEILPALKRVQAGHLLNA-PLQkLSGGETQRVLLARALLNQ 138
Cdd:PRK11124 81 RrnVGMVFQQYNLWPHLTVQqnlIEAPCRvlgLSKDQALARAEKLLERLRLKPYADRfPLH-LSGGQQQRVAIARALMME 159
|
170 180 190
....*....|....*....|....*....|
gi 768329558 139 PQLLVLDEPTQGVD--VNGQVslYDLINQL 166
Cdd:PRK11124 160 PQVLLFDEPTAALDpeITAQI--VSIIREL 187
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-243 |
3.79e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 88.29 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD------PGLRIGYVPQKLHIDPTLPV------TVE 87
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEgkqitePGPDRMVVFQNYSLLPWLTVrenialAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 88 RFMR-LTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQL 166
Cdd:TIGR01184 81 RVLPdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 167 RVELNCGVLMVSHDLhlvmaktDEVLCLNHHIC-CSGTPEAvsQHPEFIAMFGPRGAEELAIYrhHHNHRHDLQGRIV 243
Cdd:TIGR01184 161 WEEHRVTVLMVTHDV-------DEALLLSDRVVmLTNGPAA--NIGQILEVPFPRPRDRLEVV--EDPSYYDLRNEAL 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-197 |
3.85e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 88.23 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 2 TSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIGYVP-----QKL 76
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFE-GEDISTLKpeiyrQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 77 HIDPTLPV----TVE---RFMRLTRGSKnaeilPALKRVQAG--------HLLNAPLQKLSGGETQRVLLARALLNQPQL 141
Cdd:PRK10247 84 SYCAQTPTlfgdTVYdnlIFPWQIRNQQ-----PDPAIFLDDlerfalpdTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 142 LVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVmAKTDEVLCLNHH 197
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEI-NHADKVITLQPH 213
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-196 |
4.50e-21 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 91.77 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQK-------- 75
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHqleflrad 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 76 ----LHIDPTLPVTVERFMRLTRGSKNAEilpalkrvqaGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGV 151
Cdd:PRK10636 392 esplQHLARLAPQELEQKLRDYLGGFGFQ----------GDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768329558 152 DVNGQVSLYDLInqlrVELNCGVLMVSHDLHLVMAKTDEvLCLNH 196
Cdd:PRK10636 462 DLDMRQALTEAL----IDFEGALVVVSHDRHLLRSTTDD-LYLVH 501
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-218 |
7.36e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.53 E-value: 7.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 13 KFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ------------------------RDPGLR 68
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwqgkpldyskrgllalrqqvatvfQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 IGYVpqklHIDPTLPVTVERFmrltrGSKNAEIL----PALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVL 144
Cdd:PRK13638 90 IFYT----DIDSDIAFSLRNL-----GVPEAEITrrvdEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768329558 145 DEPTQGVDVNGQVSLYDLINQLRVELNcGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPEFIAMFG 218
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQgQILTHGAPGEVFACTEAMEQAG 234
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-192 |
7.50e-21 |
|
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: 87.85 E-value: 7.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 30 GRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIGYVPQKlhIDPTLPVTVERFMR------LTRGSKNAEILP 103
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQY--IKADYEGTVRDLLSsitkdfYTHPYFKTEIAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 104 ALKRVQaghLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHL 183
Cdd:cd03237 102 PLQIEQ---ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIM 178
|
....*....
gi 768329558 184 VMAKTDEVL 192
Cdd:cd03237 179 IDYLADRLI 187
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-205 |
8.88e-21 |
|
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: 87.28 E-value: 8.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 9 NVSIKFN-QRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD---------PGLR--IGYVPQkl 76
Cdd:cd03254 7 NVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDgidirdisrKSLRsmIGVVLQ-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 77 hiDPTL-PVTVERFMRLTR-GSKNAEILPALKRVQAGHLLNApLQK------------LSGGETQRVLLARALLNQPQLL 142
Cdd:cd03254 85 --DTFLfSGTIMENIRLGRpNATDEEVIEAAKEAGAHDFIMK-LPNgydtvlgenggnLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768329558 143 VLDEPTQGVDVNGQVSLYDLINQLRVelNCGVLMVSHDLHLVMaKTDEVLCLNH-HICCSGTPE 205
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIK-NADKILVLDDgKIIEEGTHD 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-192 |
9.56e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.50 E-value: 9.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 23 VSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------QRDPGLRIG----YVPQK-----LHIDPTL--- 82
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRImlngkeinALSTAQRLArglvYLPEDrqssgLYLDAPLawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 83 --PVTVERFMRLTRGSKNAEILPALKR---VQAGHLlNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQV 157
Cdd:PRK15439 362 vcALTHNRRGFWIKPARENAVLERYRRalnIKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170 180 190
....*....|....*....|....*....|....*
gi 768329558 158 SLYDLINQLrVELNCGVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK15439 441 DIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVL 474
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-195 |
1.09e-20 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 90.69 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 33 LTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQKlHID-------PTL------PVTVERFMRLTRGSKNA 99
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQH-HVDgldlssnPLLymmrcfPGVPEQKLRAHLGSFGV 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 100 eilpalkrvqAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNgqvSLYDLINQLrVELNCGVLMVSH 179
Cdd:PLN03073 617 ----------TGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD---AVEALIQGL-VLFQGGVLMVSH 682
|
170
....*....|....*.
gi 768329558 180 DLHLVMAKTDEVLCLN 195
Cdd:PLN03073 683 DEHLISGSVDELWVVS 698
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-207 |
1.12e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 88.30 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQ-----RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIGYVPQKLHID 79
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 80 PT---------LPV------TVERFMRLtrGSKNAEIlpALKRVQ--AGHLL-----------NAPLQkLSGGETQRVLL 131
Cdd:PRK13646 82 PVrkrigmvfqFPEsqlfedTVEREIIF--GPKNFKM--NLDEVKnyAHRLLmdlgfsrdvmsQSPFQ-MSGGQMRKIAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768329558 132 ARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAV 207
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEgSIVSQTSPKEL 233
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-156 |
2.10e-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: 85.87 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 6 TLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV---------QRD-PGLRIGYVPQK 75
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrwngtplaeQRDePHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 76 LHIDPTLPVTVE-RFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVN 154
Cdd:TIGR01189 82 PGLKPELSALENlHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
..
gi 768329558 155 GQ 156
Cdd:TIGR01189 162 GV 163
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-196 |
2.66e-20 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 85.92 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV------------QRDPGLR--IGYVPQKLHIDPTLPV- 84
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqdvsdlrgRAIPYLRrkIGVVFQDFRLLPDRNVy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 85 -TVERFMRLTRGSK---NAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVD---VNGQV 157
Cdd:cd03292 97 eNVAFALEVTGVPPreiRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDpdtTWEIM 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 768329558 158 SLYDLINQLRVElncgVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03292 177 NLLKKINKAGTT----VVVATHAKELVDTTRHRVIALER 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-217 |
3.24e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 88.16 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSlVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV----QR----DPGLR-IGY 71
Cdd:PRK11000 1 MAS-VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigeKRmndvPPAERgVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQKLHIDPTLPV--TVERFMRLTrGSKNAEILpalKRV-------QAGHLLNAPLQKLSGGETQRVLLARALLNQPQLL 142
Cdd:PRK11000 80 VFQSYALYPHLSVaeNMSFGLKLA-GAKKEEIN---QRVnqvaevlQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 143 VLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPE--FIAMF 217
Cdd:PRK11000 156 LLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAgRVAQVGKPLELYHYPAnrFVAGF 233
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-180 |
3.48e-20 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 89.18 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQKLHIDPTLPV 84
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 85 TVERFMRLTRGSKNAEilpALKRVQAGHLL------NAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVS 158
Cdd:PRK15064 400 TLFDWMSQWRQEGDDE---QAVRGTLGRLLfsqddiKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIES 476
|
170 180
....*....|....*....|...
gi 768329558 159 LydlinQLRVELNCGVLM-VSHD 180
Cdd:PRK15064 477 L-----NMALEKYEGTLIfVSHD 494
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-218 |
3.68e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.78 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 3 SLVTLDNVSIKF--NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQR--------------DPG 66
Cdd:PRK13640 4 NIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKitvdgitltaktvwDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 67 LRIGYV---PQKLHIDPTLPVTVErFMRLTRGSKNAEILPALKRV--QAGHL--LNAPLQKLSGGETQRVLLARALLNQP 139
Cdd:PRK13640 84 EKVGIVfqnPDNQFVGATVGDDVA-FGLENRAVPRPEMIKIVRDVlaDVGMLdyIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 140 QLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDL-HLVMAktDEVLCLNH-HICCSGTPEAVSQHPEFIAMF 217
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIdEANMA--DQVLVLDDgKLLAQGSPVEIFSKVEMLKEI 240
|
.
gi 768329558 218 G 218
Cdd:PRK13640 241 G 241
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
27-192 |
5.04e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 87.09 E-value: 5.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 27 LQPGRILTLLGPNGAGKSTLVRVVLGLLAP---TTGSVQRDpGLRIGYVPQK------------LHIDPTlpVTVERFMR 91
Cdd:PRK09473 39 LRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFN-GREILNLPEKelnklraeqismIFQDPM--TSLNPYMR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 92 ----------LTRGSKNAE-------ILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVN 154
Cdd:PRK09473 116 vgeqlmevlmLHKGMSKAEafeesvrMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVT 195
|
170 180 190
....*....|....*....|....*....|....*...
gi 768329558 155 GQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK09473 196 VQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVL 233
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-180 |
5.51e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 88.47 E-value: 5.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 7 LDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQ-KLHIDPTlpVT 85
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQhRAELDPE--KT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 86 VERfmRLTRGSKNAEIlPALKRVQAGHLLN---------APLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNgq 156
Cdd:PRK11147 400 VMD--NLAEGKQEVMV-NGRPRHVLGYLQDflfhpkramTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE-- 474
|
170 180
....*....|....*....|....
gi 768329558 157 vSLyDLINQLRVELNCGVLMVSHD 180
Cdd:PRK11147 475 -TL-ELLEELLDSYQGTVLLVSHD 496
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-169 |
6.00e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 88.64 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLvrvvLGLLA----PTTGSVQ------------RDPGLR 68
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSL----LSLIAgarkIQQGRVEvlggdmadarhrRAVCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 IGYVPQKL--HIDPTLPVT--VERFMRLtRGSKNAEilpalKRVQAGHLLNA---------PLQKLSGGETQRVLLARAL 135
Cdd:NF033858 78 IAYMPQGLgkNLYPTLSVFenLDFFGRL-FGQDAAE-----RRRRIDELLRAtglapfadrPAGKLSGGMKQKLGLCCAL 151
|
170 180 190
....*....|....*....|....*....|....
gi 768329558 136 LNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVE 169
Cdd:NF033858 152 IHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAE 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-198 |
8.99e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.80 E-value: 8.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD--------PG----LR 68
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgnpcarltPAkahqLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 IGYVPQKLHIDPTLPVTVERFMRLTRGSKNAEILPALKRVQAGHL-LNAPLQKLSGGETQRVLLARALLNQPQLLVLDEP 147
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLdLDSSAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768329558 148 TQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHlvmaktdEVLCLNHHI 198
Cdd:PRK15439 168 TASLTPAETERLFSRIRELL-AQGVGIVFISHKLP-------EIRQLADRI 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-179 |
9.17e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.35 E-value: 9.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 3 SLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLL-----APTTGSVQRDPG----------- 66
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQdifkmdvielr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 67 LRIGYVPQKLHIDPTLPV--TVERFMRLTRGSKN-----AEILPALKRVQ----AGHLLNAPLQKLSGGETQRVLLARAL 135
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIfeNVALGLKLNRLVKSkkelqERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 768329558 136 LNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNcgVLMVSH 179
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMT--IVLVTH 203
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-184 |
9.44e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 86.67 E-value: 9.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRN----VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ---------RDPGLR--- 68
Cdd:COG1135 2 IELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLvdgvdltalSERELRaar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 --IGYVPQklH------------IDptLPvtverfMRLTRGSKnAEIlpaLKRVqaGHLL---------NAPLQKLSGGE 125
Cdd:COG1135 82 rkIGMIFQ--HfnllssrtvaenVA--LP------LEIAGVPK-AEI---RKRV--AELLelvglsdkaDAYPSQLSGGQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 768329558 126 TQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLV 184
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVV 204
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-212 |
1.11e-19 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 84.66 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV----------------QRdpgL 67
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTItvdgedltdskkdinkLR---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 68 RIGYVPQKLHIDP--------TL-PVTVERfMRLTRGSKNAEILpaLKRVQAGHLLNA-PLQkLSGGETQRVLLARALLN 137
Cdd:COG1126 78 KVGMVFQQFNLFPhltvlenvTLaPIKVKK-MSKAEAEERAMEL--LERVGLADKADAyPAQ-LSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 138 QPQLLVLDEPTQGVD---VnGQVsLyDLINQLRVElncG--VLMVSHDLHLvmAKT--DEVLCLNH-HICCSGTPEAVSQ 209
Cdd:COG1126 154 EPKVMLFDEPTSALDpelV-GEV-L-DVMRDLAKE---GmtMVVVTHEMGF--AREvaDRVVFMDGgRIVEEGPPEEFFE 225
|
...
gi 768329558 210 HPE 212
Cdd:COG1126 226 NPQ 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-217 |
1.12e-19 |
|
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: 85.39 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 23 VSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ---------RDPGLR------IGYVPQKLHIDP------- 80
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLidgqdiaamSRKELRelrrkkISMVFQSFALLPhrtvlen 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 81 -TLPVTVERFMRLTRGSKNAEilpALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSL 159
Cdd:cd03294 123 vAFGLEVQGVPRAEREERAAE---ALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 160 YDLINQLRVELNCGVLMVSHDLhlvmaktDEVLCLNHHICC--------SGTPEAVSQHP--EFIAMF 217
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDL-------DEALRLGDRIAImkdgrlvqVGTPEEILTNPanDYVREF 260
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-209 |
1.21e-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: 83.73 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 9 NVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLA--PTTGSVQRDpglrigyvpqklHIDPT-LPVT 85
Cdd:cd03217 5 DLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFK------------GEDITdLPPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 86 vERF-MRLTRGSKNAEILPALKrvqAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLIN 164
Cdd:cd03217 73 -ERArLGIFLAFQYPPEIPGVK---NADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVIN 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 768329558 165 QLRvELNCGVLMVSHDLHLV-MAKTDEV-LCLNHHICCSGTPEAVSQ 209
Cdd:cd03217 149 KLR-EEGKSVLIITHYQRLLdYIKPDRVhVLYDGRIVKSGDKELALE 194
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-212 |
1.46e-19 |
|
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: 87.05 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 22 GVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLaPTTGSVQRDpGLRIGYVPQK--------LHI---------DPTLpv 84
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFD-GQDLDGLSRRalrplrrrMQVvfqdpfgslSPRM-- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 85 TVER---------FMRLTRGSKNAEILPALKRVqagHLLNAPLQK----LSGGETQRVLLARALLNQPQLLVLDEPTQGV 151
Cdd:COG4172 380 TVGQiiaeglrvhGPGLSAAERRARVAEALEEV---GLDPAARHRypheFSGGQRQRIAIARALILEPKLLVLDEPTSAL 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768329558 152 DVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPE 212
Cdd:COG4172 457 DVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDgKVVEQGPTEQVFDAPQ 518
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-192 |
1.49e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.29 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 17 RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLL-APTTGSVQ--------RDP--GLR--IGYVPQ--KLH-IDP 80
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYpGRWEGEIFidgkpvkiRNPqqAIAqgIAMVPEdrKRDgIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 81 TLPV-------TVERFMRLTRGSKNAE---ILPALKR--VQAGHLLnAPLQKLSGGETQRVLLARALLNQPQLLVLDEPT 148
Cdd:PRK13549 355 VMGVgknitlaALDRFTGGSRIDDAAElktILESIQRlkVKTASPE-LAIARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 768329558 149 QGVDVNGQVSLYDLINQLrVELNCGVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVL 476
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-194 |
1.57e-19 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 84.50 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ---RDPGLRI----------- 69
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATyimRSGAELElyqlseaerrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 70 ------GYVPQklHIDPTLPVTV-------ERFMRLTR---GSKNAEILPALKRVQ--AGHLLNAPLQkLSGGETQRVLL 131
Cdd:TIGR02323 83 lmrtewGFVHQ--NPRDGLRMRVsaganigERLMAIGArhyGNIRATAQDWLEEVEidPTRIDDLPRA-FSGGMQQRLQI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768329558 132 ARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCL 194
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-196 |
1.94e-19 |
|
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: 83.82 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFN--QRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD---------PGLR--IGY 71
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghdvrdytlASLRrqIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQKLHI-DPTLpvtVERFMRLTRGSKNAEILPALKRVQAGHLL-NAPLQ----------KLSGGETQRVLLARALLNQP 139
Cdd:cd03251 81 VSQDVFLfNDTV---AENIAYGRPGATREEVEEAARAANAHEFImELPEGydtvigergvKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 768329558 140 QLLVLDEPTQGVDVNGQVSLYDLINQLRVelNCGVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIE-NADRIVVLED 211
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-196 |
3.37e-19 |
|
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: 82.93 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKF--NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDP------GL-----RIGY 71
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiGLhdlrsRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQklhiDPTLpvtverFmrltRGS--KN---------AEILPALKRVQAGHLLNAPLQKL-----------SGGETQRV 129
Cdd:cd03244 83 IPQ----DPVL------F----SGTirSNldpfgeysdEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768329558 130 LLARALLNQPQLLVLDEPTQGVDvngqVSLYDLINQ-LRVEL-NCGVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVD----PETDALIQKtIREAFkDCTVLTIAHRLDTII-DSDRILVLDK 212
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-203 |
4.06e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.17 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKF-NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD---------PGLR--IGY 71
Cdd:PRK13657 334 AVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDgtdirtvtrASLRrnIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQklhiDPTL-PVTVERFMRLTR-GSKNAEILPALKRVQAGHLLNAPLQK-----------LSGGETQRVLLARALLNQ 138
Cdd:PRK13657 414 VFQ----DAGLfNRSIEDNIRVGRpDATDEEMRAAAERAQAHDFIERKPDGydtvvgergrqLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 139 PQLLVLDEPTQGVDVNGQVSLYDLINQLRVelNCGVLMVSHDLHLVmAKTDEVLCLNH-HICCSGT 203
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTV-RNADRILVFDNgRVVESGS 552
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-214 |
7.06e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 83.36 E-value: 7.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD--------PGL-----RIGYVPQklhiDPTLPV-T 85
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkpidysrKGLmklreSVGMVFQ----DPDNQLfS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 86 VERFMRLTRGSKNAEiLP----------ALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNG 155
Cdd:PRK13636 98 ASVYQDVSFGAVNLK-LPedevrkrvdnALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 156 QVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPEFI 214
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEgRVILQGNPKEVFAEKEML 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-181 |
7.81e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 82.45 E-value: 7.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVR-------------VVLGLLAPTTGSVQRDPGLRIG 70
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdlIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 71 YVPQKLHIDPTLpVTVERFM---RLTRGSKNAEI----LPALKRV----QAGHLLNaplqKLSGGETQRVLLARALLNQP 139
Cdd:PRK09493 81 MVFQQFYLFPHL-TALENVMfgpLRVRGASKEEAekqaRELLAKVglaeRAHHYPS----ELSGGQQQRVAIARALAVKP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768329558 140 QLLVLDEPTQGVDvngqvslydliNQLRVElncgVLMVSHDL 181
Cdd:PRK09493 156 KLMLFDEPTSALD-----------PELRHE----VLKVMQDL 182
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-181 |
8.04e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 8.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ--------------RDPG 66
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILylgkevtfngpkssQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 67 lrIGYVPQKLHIDPTLPVT---------VERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLN 137
Cdd:PRK10762 81 --IGIIHQELNLIPQLTIAeniflgrefVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 768329558 138 QPQLLVLDEPTQGVDVNGQVSLYDLINQLRVElNCGVLMVSHDL 181
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRL 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-192 |
8.12e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 8.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSG-----VSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ--------RDP--GLR--IGYVPQKLHIDP-T 81
Cdd:PRK10762 263 LSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTldghevvtRSPqdGLAngIVYISEDRKRDGlV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 82 LPVTVERFMRLT---RGSKNAEILPALKRVQA-GH---LLN-------APLQKLSGGETQRVLLARALLNQPQLLVLDEP 147
Cdd:PRK10762 343 LGMSVKENMSLTalrYFSRAGGSLKHADEQQAvSDfirLFNiktpsmeQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768329558 148 TQGVDVNGQVSLYDLINQLRVElNCGVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK10762 423 TRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRIL 466
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-181 |
9.59e-19 |
|
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: 81.42 E-value: 9.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------QRDPGL-----RIGY 71
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglkltDDKKNInelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQKLHIDPTL---------PVTVErfmRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLL 142
Cdd:cd03262 81 VFQQFNLFPHLtvlenitlaPIKVK---GMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 768329558 143 VLDEPTQGVD--VNGQVslYDLINQLRVElNCGVLMVSHDL 181
Cdd:cd03262 158 LFDEPTSALDpeLVGEV--LDVMKDLAEE-GMTMVVVTHEM 195
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
5-218 |
1.02e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.15 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFN-----QRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ----------RDPGLRI 69
Cdd:PRK13634 3 ITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigervitagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 70 gyVPQKLHIDPTLP------VTVER---FMRLTRGSKNAEIL----PALKRVQAGH--LLNAPLQkLSGGETQRVLLARA 134
Cdd:PRK13634 83 --LRKKVGIVFQFPehqlfeETVEKdicFGPMNFGVSEEDAKqkarEMIELVGLPEelLARSPFE-LSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 135 LLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEAVSQHPEF 213
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMhKGTVFLQGTPREIFADPDE 239
|
....*
gi 768329558 214 IAMFG 218
Cdd:PRK13634 240 LEAIG 244
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-184 |
1.31e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 83.24 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIGYVP--------QKLHI---------DPTL 82
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD-GQDITGLSgrelrplrRRMQMvfqdpyaslNPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 83 PV--TVERFMR----LTRGSKNAEILPALKRV--QAGHLLNAPLQkLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVN 154
Cdd:COG4608 113 TVgdIIAEPLRihglASKAERRERVAELLELVglRPEHADRYPHE-FSGGQRQRIGIARALALNPKLIVCDEPVSALDVS 191
|
170 180 190
....*....|....*....|....*....|
gi 768329558 155 GQVSLYDLINQLRVELNCGVLMVSHDLHLV 184
Cdd:COG4608 192 IQAQVLNLLEDLQDELGLTYLFISHDLSVV 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-195 |
1.74e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.07 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 17 RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV------------QRDPGLR--IGYVPQKLHIDPTL 82
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditrlknREVPFLRrqIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 83 PVTVERFMRLTRGSKNAEILPalKRVQAG----HLL----NAPLQkLSGGETQRVLLARALLNQPQLLVLDEPTQGVD-- 152
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDDIR--RRVSAAldkvGLLdkakNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDda 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 768329558 153 -VNGQVSLYDLINQLRVElncgVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:PRK10908 172 lSEGILRLFEEFNRVGVT----VLMATHDIGLISRRSYRMLTLS 211
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-169 |
2.46e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.08 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD-------PGLRI---- 69
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkditdwQTAKImrea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 70 -GYVPQKLHIDPTLPVT---------VERFMRLTRGSKNAEILPAL--KRVQ-AGhllnaplqKLSGGETQRVLLARALL 136
Cdd:PRK11614 82 vAIVPEGRRVFSRMTVEenlamggffAERDQFQERIKWVYELFPRLheRRIQrAG--------TMSGGEQQMLAIGRALM 153
|
170 180 190
....*....|....*....|....*....|...
gi 768329558 137 NQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVE 169
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ 186
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-181 |
2.66e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.68 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------QRDPGLR---- 68
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinninynKLDHKLAaqlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 IGYVPQKLH-ID-------------PT-----LPVTVERFMRltrgsKNAEILpaLKRVQAGHLLNAPLQKLSGGETQRV 129
Cdd:PRK09700 82 IGIIYQELSvIDeltvlenlyigrhLTkkvcgVNIIDWREMR-----VRAAMM--LLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 768329558 130 LLARALLNQPQLLVLDEPTQGVdVNGQVS-LYDLINQLRVElNCGVLMVSHDL 181
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSL-TNKEVDyLFLIMNQLRKE-GTAIVYISHKL 205
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-182 |
3.26e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.19 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 8 DNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV-----------QRDPGLRIGYVPQkl 76
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaSKEVARRIGLLAQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 77 hiDPTLP--VTVERFMR---------LTRGSKNAE--ILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLV 143
Cdd:PRK10253 89 --NATTPgdITVQELVArgryphqplFTRWRKEDEeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 768329558 144 LDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLH 182
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLN 205
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-215 |
3.91e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 81.03 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLL--------APTTGSVQRD-------PGLR 68
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNgeplaaiDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 IG----YVPQKLHidPTLPVTVERFMRLTR----------GSKNAEIL-PALKRVQAGHLLNAPLQKLSGGETQRVLLAR 133
Cdd:PRK13547 81 LArlraVLPQAAQ--PAFAFSAREIVLLGRypharragalTHRDGEIAwQALALAGATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 134 AL---------LNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCL-NHHICCSGT 203
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLaDGAIVAHGA 238
|
250
....*....|..
gi 768329558 204 PEAVSQhPEFIA 215
Cdd:PRK13547 239 PADVLT-PAHIA 249
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-207 |
4.37e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 81.32 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQ---RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGL---------- 67
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 68 -RIGYVPQklhiDPT---LPVTVE---RFMRLTRGSKNAEILP----ALKRVQAGHLLNAPLQKLSGGETQRVLLARALL 136
Cdd:PRK13650 81 hKIGMVFQ----NPDnqfVGATVEddvAFGLENKGIPHEEMKErvneALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768329558 137 NQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVmAKTDEVLCL-NHHICCSGTPEAV 207
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMkNGQVESTSTPREL 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-191 |
4.94e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.65 E-value: 4.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD--------------PG 66
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqemrfasttaalaAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 67 LRIGYvpQKLHIDPTLPVtVERFM--RL--TRGSKNAEILPALKRVQAGHL-----LNAPLQKLSGGETQRVLLARALLN 137
Cdd:PRK11288 81 VAIIY--QELHLVPEMTV-AENLYlgQLphKGGIVNRRLLNYEAREQLEHLgvdidPDTPLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 768329558 138 QPQLLVLDEPTQGVDVNGQVSLYDLINQLRVElNCGVLMVSHDLHLVMAKTDEV 191
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAI 210
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-196 |
5.48e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.85 E-value: 5.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQR---NVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIG-----YV 72
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD-GVPLVqydhhYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 73 PQKLHIDPTLPVtverfmrLTRGSKNAEILPALKRVQAGHLLNAPLQ-----------------------KLSGGETQRV 129
Cdd:TIGR00958 554 HRQVALVGQEPV-------LFSGSVRENIAYGLTDTPDEEIMAAAKAanahdfimefpngydtevgekgsQLSGGQKQRI 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768329558 130 LLARALLNQPQLLVLDEPTQGVDVNGQVSLYdlinQLRVELNCGVLMVSHDLHLVmAKTDEVLCLNH 196
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDAECEQLLQ----ESRSRASRTVLLIAHRLSTV-ERADQILVLKK 688
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-213 |
5.53e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.57 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQR--NVLSGVSLALQPGRILTLLGPNGAGKSTLvrvvLGLLA----PTTGSVQ---------RDPGLR 68
Cdd:PRK11160 338 SLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTL----LQLLTrawdPQQGEILlngqpiadySEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 --IGYVPQKLHI-DPTLpvtverfmR--LTRGSKNA---EILPALKRVQAGHLL--NAPL--------QKLSGGETQRVL 130
Cdd:PRK11160 414 qaISVVSQRVHLfSATL--------RdnLLLAAPNAsdeALIEVLQQVGLEKLLedDKGLnawlgeggRQLSGGEQRRLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 131 LARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQlrVELNCGVLMVSHDLHLvMAKTDEVLCLNH-HICCSGT-PEAVS 208
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAE--HAQNKTVLMITHRLTG-LEQFDRICVMDNgQIIEQGThQELLA 562
|
....*
gi 768329558 209 QHPEF 213
Cdd:PRK11160 563 QQGRY 567
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-211 |
7.30e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 81.29 E-value: 7.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 22 GVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV---------QRDPGLR-----IGYVPQklhiDPTLPVTVe 87
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVawlgkdllgMKDDEWRavrsdIQMIFQ----DPLASLNP- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 88 rfmRLTRGSKNAEIL----PALK------RVQA--------GHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQ 149
Cdd:PRK15079 114 ---RMTIGEIIAEPLrtyhPKLSrqevkdRVKAmmlkvgllPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768329558 150 GVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLC--LNHHICCsGTPEAVSQHP 211
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVmyLGHAVEL-GTYDEVYHNP 253
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-180 |
7.61e-18 |
|
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: 82.29 E-value: 7.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 8 DNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQ-KLHIDPTLPVTV 86
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQsRDALDPNKTVWE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 87 E-----RFMRLtrgsKNAEIlPALKRVQAGHLLNAPLQK----LSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQV 157
Cdd:TIGR03719 406 EisgglDIIKL----GKREI-PSRAYVGRFNFKGSDQQKkvgqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLR 480
|
170 180
....*....|....*....|....*.
gi 768329558 158 SLYDLInqlrveLN---CgVLMVSHD 180
Cdd:TIGR03719 481 ALEEAL------LNfagC-AVVISHD 499
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-196 |
7.71e-18 |
|
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: 79.50 E-value: 7.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 19 VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD----PGLRIGYvpqklHIDPTLpvTVE---RFMR 91
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRgrvsSLLGLGG-----GFNPEL--TGReniYLNG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 92 LTRGSKNAEILPALKRVQA----GHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLR 167
Cdd:cd03220 110 RLLGLSRKEIDEKIDEIIEfselGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL 189
|
170 180
....*....|....*....|....*....
gi 768329558 168 vELNCGVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03220 190 -KQGKTVILVSHDPSSIKRLCDRALVLEK 217
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-192 |
8.32e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 80.27 E-value: 8.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKF---------NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV---------- 61
Cdd:COG4167 1 MSALLEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEIlinghkleyg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 62 ---QR---------------DPGLRIGYV---PQKLHIDptlpvtverfmrLTRGSKNAEILPALKRVqaGHL---LNAP 117
Cdd:COG4167 81 dykYRckhirmifqdpntslNPRLNIGQIleePLRLNTD------------LTAEEREERIFATLRLV--GLLpehANFY 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768329558 118 LQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVL 192
Cdd:COG4167 147 PHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVL 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-194 |
1.48e-17 |
|
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: 78.67 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQR---NVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQKLHIDP 80
Cdd:cd03248 11 IVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 81 TL----PVTVER--------------FMRLTRGSKNAEILPALKRVQAGHLLNAPLQ--KLSGGETQRVLLARALLNQPQ 140
Cdd:cd03248 91 SLvgqePVLFARslqdniayglqscsFECVKEAAQKAHAHSFISELASGYDTEVGEKgsQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 768329558 141 LLVLDEPTQGVDVNGQVSLYDLINQLRVelNCGVLMVSHDLHLVmAKTDEVLCL 194
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTV-ERADQILVL 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-194 |
1.49e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.23 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIK-FNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ--------RDPG----LRIG 70
Cdd:COG3845 257 VLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRldgeditgLSPRerrrLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 71 YVPQ-------------------KLHIDPtlPVTVERFMRLTRGSKNAEILPALKRVQAGHLlNAPLQKLSGGETQRVLL 131
Cdd:COG3845 337 YIPEdrlgrglvpdmsvaenlilGRYRRP--PFSRGGFLDRKAIRAFAEELIEEFDVRTPGP-DTPARSLSGGNQQKVIL 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768329558 132 ARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLhlvmaktDEVLCL 194
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELR-DAGAAVLLISEDL-------DEILAL 468
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-207 |
1.71e-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: 81.39 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 22 GVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV------------QRDPGLR------IGYVPQKLHIDP--- 80
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtKPGPDGRgrakryIGILHQEYDLYPhrt 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 81 -----TLPVTVERFMRLTRgsKNAEIlpALKRV-----QAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQG 150
Cdd:TIGR03269 382 vldnlTEAIGLELPDELAR--MKAVI--TLKMVgfdeeKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 151 VDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEV-LCLNHHICCSGTPEAV 207
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAaLMRDGKIVKIGDPEEI 515
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-182 |
1.73e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 78.93 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGL--LAP---TTGSVQ------RDPGL-- 67
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILldgediYDPDVdv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 68 -----RIGYVPQKlhidPT-LPVTVER---F-MRLtRGSKNAEILP-----ALKRVqagHL-------LNAPLQKLSGGE 125
Cdd:COG1117 88 velrrRVGMVFQK----PNpFPKSIYDnvaYgLRL-HGIKSKSELDeiveeSLRKA---ALwdevkdrLKKSALGLSGGQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 126 TQRVLLARALLNQPQLLVLDEPTQGVDvngQVS---LYDLINQLRVELncGVLMVSHDLH 182
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALD---PIStakIEELILELKKDY--TIVIVTHNMQ 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-152 |
1.97e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.29 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLA--PTTGS--------VQRDPGL--- 67
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGShiellgrtVQREGRLard 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 68 ------RIGYVPQKLHIDPTLPVtVERFMRLTRGS--------------KNAEILPALKRVQAGHLLNAPLQKLSGGETQ 127
Cdd:PRK09984 81 irksraNTGYIFQQFNLVNRLSV-LENVLIGALGStpfwrtcfswftreQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180
....*....|....*....|....*
gi 768329558 128 RVLLARALLNQPQLLVLDEPTQGVD 152
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLD 184
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-182 |
2.82e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.59 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFN-----QRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV-------------QRdpG 66
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvtklpeyKR--A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 67 LRIGYVPQklhiDP---TLP-VTVE----------RFMRLTRGSKNAEI---LPALKRVQAG--HLLNAPLQKLSGGETQ 127
Cdd:COG1101 80 KYIGRVFQ----DPmmgTAPsMTIEenlalayrrgKRRGLRRGLTKKRRelfRELLATLGLGleNRLDTKVGLLSGGQRQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768329558 128 RVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLH 182
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNME 210
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-212 |
3.09e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 78.64 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 2 TSLVTLDNVSIKFNQRN--VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV---------QRDPGLR-- 68
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitdDNFEKLRkh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 IGYV---PQKLHIDPTLPVTV----ERFMRLTRgsKNAEILP-ALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQ 140
Cdd:PRK13648 85 IGIVfqnPDNQFVGSIVKYDVafglENHAVPYD--EMHRRVSeALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768329558 141 LLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMaKTDEVLCLNH-HICCSGTPEAVSQHPE 212
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAM-EADHVIVMNKgTVYKEGTPTEIFDHAE 234
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
5-148 |
3.55e-17 |
|
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: 80.25 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFN-QRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpG----------LR--IGY 71
Cdd:COG5265 358 VRFENVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILID-GqdirdvtqasLRaaIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQklhiDPTL-PVTVE---RFMRLtrGSKNAEILPALKRVQAGHLLNA-PLQ----------KLSGGETQRVLLARALL 136
Cdd:COG5265 437 VPQ----DTVLfNDTIAyniAYGRP--DASEEEVEAAARAAQIHDFIESlPDGydtrvgerglKLSGGEKQRVAIARTLL 510
|
170
....*....|..
gi 768329558 137 NQPQLLVLDEPT 148
Cdd:COG5265 511 KNPPILIFDEAT 522
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
15-183 |
3.86e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.51 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 15 NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV------------QRDPGLR---IGYVPQKLHID 79
Cdd:PRK10584 21 HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVslvgqplhqmdeEARAKLRakhVGFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 80 PTLPvTVE--RFMRLTRGSKNAEilpalKRVQAGHLL----------NAPLQkLSGGETQRVLLARALLNQPQLLVLDEP 147
Cdd:PRK10584 101 PTLN-ALEnvELPALLRGESSRQ-----SRNGAKALLeqlglgkrldHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 768329558 148 TQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHL 183
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQL 209
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-192 |
4.15e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.87 E-value: 4.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 23 VSLALQPGRILTLLGPNGAGKSTLVRVVLGLL-APTTGSV---QRDPGLR---------IGYVPQ--KLH-IDPTLPV-- 84
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVfinGKPVDIRnpaqairagIAMVPEdrKRHgIVPILGVgk 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 85 -----TVERFMRLTRGSKNAEILPALKRVQAGHLLNA----PLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNG 155
Cdd:TIGR02633 359 nitlsVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTAspflPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
170 180 190
....*....|....*....|....*....|....*..
gi 768329558 156 QVSLYDLINQLRVElNCGVLMVSHDLHLVMAKTDEVL 192
Cdd:TIGR02633 439 KYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVL 474
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-179 |
4.29e-17 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 80.06 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 2 TSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLG-----------LLAPTTGSVQR--DPGLR 68
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGSGETiwDIKKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 IGYVPQKLHIDPTLPVTV-------------------ERFMRLTRgsknaEILPALKrvQAGHLLNAPLQKLSGGETQRV 129
Cdd:PRK10938 338 IGYVSSSLHLDYRVSTSVrnvilsgffdsigiyqavsDRQQKLAQ-----QWLDILG--IDKRTADAPFHSLSWGQQRLA 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768329558 130 LLARALLNQPQLLVLDEPTQGVD-VNGQVSLyDLINQLRVELNCGVLMVSH 179
Cdd:PRK10938 411 LIVRALVKHPTLLILDEPLQGLDpLNRQLVR-RFVDVLISEGETQLLFVSH 460
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-215 |
7.20e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.35 E-value: 7.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRN-----VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ-RDpgLRIG-YVPQKL 76
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvGD--IYIGdKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 77 HIDPTLPVTVERFMRLTRG-----------------SKNAEILP-ALK------RVQAGHLLN-----------APLQkL 121
Cdd:PRK13631 99 LITNPYSKKIKNFKELRRRvsmvfqfpeyqlfkdtiEKDIMFGPvALGvkkseaKKLAKFYLNkmglddsylerSPFG-L 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 122 SGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVElNCGVLMVSHDLHLVMAKTDEVLCLNH-HICC 200
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKgKILK 256
|
250
....*....|....*
gi 768329558 201 SGTPEAVSQHPEFIA 215
Cdd:PRK13631 257 TGTPYEIFTDQHIIN 271
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-205 |
8.89e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.03 E-value: 8.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 7 LDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLA--PTTGSVQRDpGLRIgyvpqkLHIDPT--- 81
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLD-GEDI------LELSPDera 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 82 -------------LP-VTVERFMRLtrgSKNAEILPALKRVQAGHLLNAPLQKL---------------SGGETQRVLLA 132
Cdd:COG0396 76 ragiflafqypveIPgVSVSNFLRT---ALNARRGEELSAREFLKLLKEKMKELgldedfldryvnegfSGGEKKRNEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768329558 133 RALLNQPQLLVLDEPTQGVDVNG--QVSlyDLINQLRVElNCGVLMVSHD---LHLVmaKTDEVLCL-NHHICCSGTPE 205
Cdd:COG0396 153 QMLLLEPKLAILDETDSGLDIDAlrIVA--EGVNKLRSP-DRGILIITHYqriLDYI--KPDFVHVLvDGRIVKSGGKE 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-152 |
9.02e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 77.10 E-value: 9.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 3 SLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ-------------------R 63
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtarslsqqkgliR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 64 DPGLRIGYVPQKLHIDPTL---------PVTVErfmRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARA 134
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRtvleniiegPVIVK---GEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170
....*....|....*...
gi 768329558 135 LLNQPQLLVLDEPTQGVD 152
Cdd:PRK11264 159 LAMRPEVILFDEPTSALD 176
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
3-179 |
9.51e-17 |
|
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: 79.02 E-value: 9.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 3 SLVTLDNVSIKFNQRNVL-SGVSLALQPGRILTLLGPNGAGKSTLVRVvLGLLAPTTGSV-QRDPGLRIGYVPQKLHID- 79
Cdd:TIGR00954 450 NGIKFENIPLVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRI-LGELWPVYGGRlTKPAKGKLFYVPQRPYMTl 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 80 PTL------PVTVERFMRltRGSKNAEILPALKRVQAGHLLNAP---------LQKLSGGETQRVLLARALLNQPQLLVL 144
Cdd:TIGR00954 529 GTLrdqiiyPDSSEDMKR--RGLSDKDLEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*
gi 768329558 145 DEPTQGVDVNGQVSLYDLINQLRVELncgvLMVSH 179
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYRLCREFGITL----FSVSH 637
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-207 |
9.99e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 77.40 E-value: 9.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGS-----------------VQRDPGLRIGYVPQKLHIDptl 82
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKiiidgvditdkkvklsdIRKKVGLVFQYPEYQLFEE--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 83 pvTVER---FMRLTRGSKNAEILPALKRVQA-------GHLLNAPLQkLSGGETQRVLLARALLNQPQLLVLDEPTQGVD 152
Cdd:PRK13637 100 --TIEKdiaFGPINLGLSEEEIENRVKRAMNivgldyeDYKDKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 153 VNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNHHIC-CSGTPEAV 207
Cdd:PRK13637 177 PKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCeLQGTPREV 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-192 |
1.32e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 77.70 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD-------------------------------PGLR 68
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQgqdllkadpeaqkllrqkiqivfqnpygslnPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 IGYV---PQKLHIDptlpvtverfmrLTRGSKNAEILPALKRV--QAGHLLNAPlQKLSGGETQRVLLARALLNQPQLLV 143
Cdd:PRK11308 111 VGQIleePLLINTS------------LSAAERREKALAMMAKVglRPEHYDRYP-HMFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768329558 144 LDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK11308 178 ADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVM 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
17-155 |
1.57e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.23 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 17 RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV---------QRDPGLR----IGYVPQklhIDPTLp 83
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgepirrQRDEYHQdllyLGHQPG---IKTEL- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 84 vTVE---RF-MRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNG 155
Cdd:PRK13538 90 -TALenlRFyQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-221 |
1.89e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.36 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 6 TLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDP-----------GLRIGYVPQ 74
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpleswsskafARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 75 KLhiDPTLPVTVERFMRLTR----------GSKNAE-ILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLV 143
Cdd:PRK10575 93 QL--PAAEGMTVRELVAIGRypwhgalgrfGAADREkVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 144 LDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPEFIAMFG-PRG 221
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGgEMIAQGTPAELMRGETLEQIYGiPMG 250
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-179 |
2.02e-16 |
|
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: 75.22 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 24 SLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------QRDPGLR-IGYVPQKLHIDPTLpvTVERFMRLTR 94
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlingvdvtAAPPADRpVSMLFQENNLFAHL--TVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 95 GSK---NAE----ILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLR 167
Cdd:cd03298 96 SPGlklTAEdrqaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170
....*....|..
gi 768329558 168 VELNCGVLMVSH 179
Cdd:cd03298 176 AETKMTVLMVTH 187
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-181 |
2.38e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 77.90 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 26 ALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPG------------------------LRIGYVPQklHIDpT 81
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSwdevlkrfrgtelqdyfkklangeIKVAHKPQ--YVD-L 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 82 LPV----TVERFMRLT--RGSKNaEILpalKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNG 155
Cdd:COG1245 172 IPKvfkgTVRELLEKVdeRGKLD-ELA---EKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180
....*....|....*....|....*.
gi 768329558 156 QVSLYDLINQLrVELNCGVLMVSHDL 181
Cdd:COG1245 248 RLNVARLIREL-AEEGKYVLVVEHDL 272
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-215 |
2.65e-16 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 75.65 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQR---NVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD---------PGLR--IG 70
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDgvdirdlnlRWLRsqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 71 YVPQklhiDPTL--------------PVTVERFMRltrGSKNAEI------LPALKRVQAGhllnaplQK---LSGGETQ 127
Cdd:cd03249 81 LVSQ----EPVLfdgtiaenirygkpDATDEEVEE---AAKKANIhdfimsLPDGYDTLVG-------ERgsqLSGGQKQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 128 RVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCgvLMVSHDLHLVMaKTDEVLCLNH-HICCSGTpea 206
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTT--IVIAHRLSTIR-NADLIAVLQNgQVVEQGT--- 220
|
....*....
gi 768329558 207 vsqHPEFIA 215
Cdd:cd03249 221 ---HDELMA 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-196 |
2.69e-16 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 77.86 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLdNVSIKFNQ--------RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDP------- 65
Cdd:TIGR01193 464 RTELNNL-NGDIVINDvsysygygSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdid 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 66 --GLR--IGYVPQK-----------LHIDPTLPVTVERFMRLTRgskNAEILPALKRVQAGH--LLNAPLQKLSGGETQR 128
Cdd:TIGR01193 543 rhTLRqfINYLPQEpyifsgsilenLLLGAKENVSQDEIWAACE---IAEIKDDIENMPLGYqtELSEEGSSISGGQKQR 619
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 129 VLLARALLNQPQLLVLDEPTQGVDVngqVSLYDLINQLRVELNCGVLMVSHDLHlVMAKTDEVLCLNH 196
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDT---ITEKKIVNNLLNLQDKTIIFVAHRLS-VAKQSDKIIVLDH 683
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-195 |
3.32e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.93 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV-----------QRDPGLRIGYVPQklhiDPTLPV---T 85
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrevnaenEKWVRSKVGLVFQ----DPDDQVfssT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 86 VE-------RFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVS 158
Cdd:PRK13647 97 VWddvafgpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 768329558 159 LYDLINQLRVElNCGVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:PRK13647 177 LMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLK 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-191 |
3.83e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 76.38 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQR----NVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD---------PGLR--- 68
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDgqdltalseKELRkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 --IGYVPQklHIDPTLPVTVerF------MRLTRGSK---NAEILPALKRVQAGHLLNA-PLQkLSGGETQRVLLARALL 136
Cdd:PRK11153 82 rqIGMIFQ--HFNLLSSRTV--FdnvalpLELAGTPKaeiKARVTELLELVGLSDKADRyPAQ-LSGGQKQRVAIARALA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768329558 137 NQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEV 191
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRV 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-195 |
5.69e-16 |
|
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: 73.99 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKF--NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIGYVP-----QKLH 77
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEID-GIDISTIPledlrSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 78 I---DPTL-----PVTVERFMRLTrgskNAEILPALKRVQAGhlLNaplqkLSGGETQRVLLARALLNQPQLLVLDEPTQ 149
Cdd:cd03369 86 IipqDPTLfsgtiRSNLDPFDEYS----DEEIYGALRVSEGG--LN-----LSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 768329558 150 GVDVNGQVSLYDLInqlRVEL-NCGVLMVSHDLHLVmAKTDEVLCLN 195
Cdd:cd03369 155 SIDYATDALIQKTI---REEFtNSTILTIAHRLRTI-IDYDKILVMD 197
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-152 |
7.03e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.46 E-value: 7.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 6 TLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPT--TGSV---QRDPG----LRIGYVPQKL 76
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTIlanNRKPTkqilKRTGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 77 HIDPTLPV----TVERFMRLTRG-SKNAEILPA--------LKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLV 143
Cdd:PLN03211 150 ILYPHLTVretlVFCSLLRLPKSlTKQEKILVAesviselgLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLI 229
|
....*....
gi 768329558 144 LDEPTQGVD 152
Cdd:PLN03211 230 LDEPTSGLD 238
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-152 |
7.26e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.43 E-value: 7.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTS-LVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVV--LGLLAP---TTGSV------------- 61
Cdd:PRK14239 1 MTEpILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIvynghniysprtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 62 -------------QRDP-----------GLRIGYVPQKLHIDPtlpvTVERFMrltrgsKNAEILPALKrvqaGHLLNAP 117
Cdd:PRK14239 81 tvdlrkeigmvfqQPNPfpmsiyenvvyGLRLKGIKDKQVLDE----AVEKSL------KGASIWDEVK----DRLHDSA 146
|
170 180 190
....*....|....*....|....*....|....*
gi 768329558 118 LqKLSGGETQRVLLARALLNQPQLLVLDEPTQGVD 152
Cdd:PRK14239 147 L-GLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-196 |
8.11e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 74.35 E-value: 8.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKfNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAP----TTGSVQRD---------PGL 67
Cdd:PRK10418 1 MPQQIELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDgkpvapcalRGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 68 RIGYVPQ--KLHIDPTLPVT---VERFMRLTRGSKNAEILPALKRV---QAGHLLNAPLQKLSGGETQRVLLARALLNQP 139
Cdd:PRK10418 80 KIATIMQnpRSAFNPLHTMHthaRETCLALGKPADDATLTAALEAVgleNAARVLKLYPFEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 768329558 140 QLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSH 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-215 |
8.83e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.04 E-value: 8.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRN-----VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGS------------------- 60
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaipanlkkikevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 61 -VQRDPGLRIGYVPQKLHIDptlpvTVER---FMRLTRGSKNAEI---LPAL-KRVQ--AGHLLNAPLQkLSGGETQRVL 130
Cdd:PRK13645 87 rLRKEIGLVFQFPEYQLFQE-----TIEKdiaFGPVNLGENKQEAykkVPELlKLVQlpEDYVKRSPFE-LSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 131 LARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQ 209
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEgKVISIGSPFEIFS 240
|
....*.
gi 768329558 210 HPEFIA 215
Cdd:PRK13645 241 NQELLT 246
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-181 |
1.05e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.00 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 26 ALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPG------------------------LRIGYVPQklHIDpT 81
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSwdevlkrfrgtelqnyfkklyngeIKVVHKPQ--YVD-L 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 82 LPV----TVERFMRLT--RGSKNaEILpalKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNG 155
Cdd:PRK13409 172 IPKvfkgKVRELLKKVdeRGKLD-EVV---ERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170 180
....*....|....*....|....*.
gi 768329558 156 QVSLYDLINQLRVELNcgVLMVSHDL 181
Cdd:PRK13409 248 RLNVARLIRELAEGKY--VLVVEHDL 271
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-191 |
1.06e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.74 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTT--------GSVQRDPGLR---- 68
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyegeiifeGEELQASNIRdter 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 --IGYVPQKLHIDPTLPVTVERFM--RLTRGSK---NAEILPA---LKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQ 138
Cdd:PRK13549 82 agIAIIHQELALVKELSVLENIFLgnEITPGGImdyDAMYLRAqklLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768329558 139 PQLLVLDEPTQGVDVNGQVSLYDLINQLRvelNCGVLMV--SHDLHLVMAKTDEV 191
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLK---AHGIACIyiSHKLNEVKAISDTI 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-180 |
1.07e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.92 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKF----NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVvLGLLAPTTGSVQRDPG---------- 66
Cdd:PRK10535 1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNI-LGCLDKPTSGTYRVAGqdvatldada 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 67 ---LR---IGYVPQKLHIDPTLPVT-----------VERFMRLTRgsknAEILpaLKRVQAGHLLNAPLQKLSGGETQRV 129
Cdd:PRK10535 80 laqLRrehFGFIFQRYHLLSHLTAAqnvevpavyagLERKQRLLR----AQEL--LQRLGLEDRVEYQPSQLSGGQQQRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768329558 130 LLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHD 180
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHD 203
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
9-190 |
1.20e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.06 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 9 NVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ-------RDPGL---RIGYVPQKLHI 78
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILferqsikKDLCTyqkQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 79 DPTLPVTVERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDvngQVS 158
Cdd:PRK13540 86 NPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELS 162
|
170 180 190
....*....|....*....|....*....|....*
gi 768329558 159 LYDLINQLRVELNCG--VLMVSH-DLHLVMAKTDE 190
Cdd:PRK13540 163 LLTIITKIQEHRAKGgaVLLTSHqDLPLNKADYEE 197
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-212 |
1.46e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.03 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD----PGL---RIGYVP 73
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDgeniPAMsrsRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 74 QKLHI----------------------------DPTLPVTVerFMRLT----RGSknAEILPAlkrvqaghllnaplqKL 121
Cdd:PRK11831 84 KRMSMlfqsgalftdmnvfdnvayplrehtqlpAPLLHSTV--MMKLEavglRGA--AKLMPS---------------EL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 122 SGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCL-NHHICC 200
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVaDKKIVA 224
|
250
....*....|..
gi 768329558 201 SGTPEAVSQHPE 212
Cdd:PRK11831 225 HGSAQALQANPD 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-189 |
1.52e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.92 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLV-----------------------------RVVLGLLA 55
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnrmnelesevrvegrveffnqniyerRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 56 PTTGSVQRDPGL--------------RIGYVPqKLHIDPTLPVTVerfmrltrgsKNAEILPALKrvqagHLLNAPLQKL 121
Cdd:PRK14258 88 RQVSMVHPKPNLfpmsvydnvaygvkIVGWRP-KLEIDDIVESAL----------KDADLWDEIK-----HKIHKSALDL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 122 SGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTD 189
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-250 |
1.75e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.07 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 24 SLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ---------RDPGLR------IGYVPQKLHIDPTLPVTVE- 87
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLidgvdiakiSDAELRevrrkkIAMVFQSFALMPHMTVLDNt 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 88 ----RFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLI 163
Cdd:PRK10070 128 afgmELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 164 NQLRVELNCGVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEAVSQHP--EFIAMFGpRGAEELAIYRHHHNHRHDLQG 240
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVGTPDEILNNPanDYVRTFF-RGVDISQVFSAKDIARRTPNG 286
|
250
....*....|
gi 768329558 241 RIVLRKGQGP 250
Cdd:PRK10070 287 LIRKTPGFGP 296
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-196 |
1.97e-15 |
|
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: 73.29 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKF--NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD---------PGLR--IGY 71
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDghdlaladpAWLRrqVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQKlhiDPTLPVTVERFMRLTRGSKNAEILPALKRVQAGH--LLNAPL----------QKLSGGETQRVLLARALLNQP 139
Cdd:cd03252 81 VLQE---NVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHdfISELPEgydtivgeqgAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 768329558 140 QLLVLDEPTQGVDVNGQVSLydLINQLRVELNCGVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03252 158 RILIFDEATSALDYESEHAI--MRNMHDICAGRTVIIIAHRLSTVK-NADRIIVMEK 211
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-182 |
2.05e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 74.93 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 9 NVSIKFNQRNvlsgvslalQPGriltLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQ-------------- 74
Cdd:PRK15064 19 NISVKFGGGN---------RYG----LIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQdqfafeeftvldtv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 75 ----------KLHIDP--TLP-VTVERFMRLTR-GSKNAEILPALKRVQAGHLL----------NAPLQKLSGGETQRVL 130
Cdd:PRK15064 86 imghtelwevKQERDRiyALPeMSEEDGMKVADlEVKFAEMDGYTAEARAGELLlgvgipeeqhYGLMSEVAPGWKLRVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768329558 131 LARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQlrveLNCGVLMVSHDLH 182
Cdd:PRK15064 166 LAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE----RNSTMIIISHDRH 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-194 |
2.11e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.59 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKFNQR---NVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDP---------GLR 68
Cdd:PRK13642 1 MNKILEVENLVFKYEKEsdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 --IGYV---PQKLHIDPTLPVTVERFMRlTRGSKNAEILpalKRVQAGHLLNAPLQ-------KLSGGETQRVLLARALL 136
Cdd:PRK13642 81 rkIGMVfqnPDNQFVGATVEDDVAFGME-NQGIPREEMI---KRVDEALLAVNMLDfktrepaRLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 137 NQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVmAKTDEVLCL 194
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVM 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-194 |
2.45e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.89 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRN----VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDP-------------- 65
Cdd:PRK10261 12 VLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqviels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 66 -----------GLRIGYVPQK--LHIDPTLPV--TVERFMRLTRGSKNAEILPALKRV-------QAGHLLNAPLQKLSG 123
Cdd:PRK10261 92 eqsaaqmrhvrGADMAMIFQEpmTSLNPVFTVgeQIAESIRLHQGASREEAMVEAKRMldqvripEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768329558 124 GETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCL 194
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-166 |
2.78e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 74.67 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLvTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD--PGLRIGYVPQKLHI 78
Cdd:PRK10938 1 MSSL-QISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfsHITRLSFEQLQKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 79 DPT--------LPVTVERFMRLTR-----GSKNAEILPAL-KRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVL 144
Cdd:PRK10938 80 SDEwqrnntdmLSPGEDDTGRTTAeiiqdEVKDPARCEQLaQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLIL 159
|
170 180
....*....|....*....|..
gi 768329558 145 DEPTQGVDVNGQVSLYDLINQL 166
Cdd:PRK10938 160 DEPFDGLDVASRQQLAELLASL 181
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-206 |
2.84e-15 |
|
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: 72.78 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 28 QPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDP------------------------GLRIGYVPQKL-HIDPTL 82
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdeildefrgselqnyftkllegDVKVIVKPQYVdLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 83 PVTVERFMRLTRGSKNAEILpaLKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDL 162
Cdd:cd03236 104 KGKVGELLKKKDERGKLDEL--VDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768329558 163 INQLRVELNcGVLMVSHDLHLVMAKTDevlclnhHICCS-GTPEA 206
Cdd:cd03236 182 IRELAEDDN-YVLVVEHDLAVLDYLSD-------YIHCLyGEPGA 218
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-187 |
4.90e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.11 E-value: 4.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 19 VLSG-VSLALQPGRILTLLGPNGAGKSTLVRVVLGLLaPTTGSV--------QRDPGL---RIGYVPQklhiDPTLP-VT 85
Cdd:PRK11174 364 TLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLkingielrELDPESwrkHLSWVGQ----NPQLPhGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 86 VERFMRLTRGSKN-AEILPALKRVQAG-------HLLNAPLQK----LSGGETQRVLLARALLNQPQLLVLDEPTQGVDV 153
Cdd:PRK11174 439 LRDNVLLGNPDASdEQLQQALENAWVSeflpllpQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768329558 154 NGQVSLYDLINQLRVELNCgvLMVSH---DLH-----LVMAK 187
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTT--LMVTHqleDLAqwdqiWVMQD 558
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-230 |
7.90e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.32 E-value: 7.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLL-------------APTTGSVQRDPGLR-I 69
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgtwdgeiywsgSPLKASNIRDTERAgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 70 GYVPQKLHIDPTLPVTVERFM--RLT----RGSKNAEILPA---LKRVQAGHLLNA-PLQKLSGGETQRVLLARALLNQP 139
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLgnEITlpggRMAYNAMYLRAknlLRELQLDADNVTrPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 140 QLLVLDEPTQGVDVNGQVSLYDLINQLRVElNCGVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPEAVSQHPEFIAMFgp 219
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMM-- 237
|
250
....*....|.
gi 768329558 220 RGAEELAIYRH 230
Cdd:TIGR02633 238 VGREITSLYPH 248
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-214 |
8.40e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 72.08 E-value: 8.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFN-----QRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGL------------ 67
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 68 ---RIGYVPQKlhidPTLPVTVERFMR-LTRGSKN-------AEILPALKRVQAG---HLLNAPLQKLSGGETQRVLLAR 133
Cdd:PRK13649 83 irkKVGLVFQF----PESQLFEETVLKdVAFGPQNfgvsqeeAEALAREKLALVGiseSLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 134 ALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPE 212
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKgKLVLSGKPKDIFQDVD 237
|
..
gi 768329558 213 FI 214
Cdd:PRK13649 238 FL 239
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-232 |
8.74e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.07 E-value: 8.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ-------------------RDPGLRIGYVPQKLHIDP 80
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdivvsstskqkeikpvrKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 81 TLPVTVERFMRLTRGSKNAEILPALKRVQAG----HLLNAPLQkLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQ 156
Cdd:PRK13643 102 VLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGladeFWEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768329558 157 VSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPEFIAmfgprgAEELAIYRHHH 232
Cdd:PRK13643 181 IEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKgHIISCGTPSDVFQEVDFLK------AHELGVPKATH 250
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-207 |
9.55e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.04 E-value: 9.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 1 MTSLVTLDNVSIKF------NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGL------- 67
Cdd:PRK13633 1 MNEMIKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVD-GLdtsdeen 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 68 ------RIGYVPQklHIDPTLPVT-VERfmRLTRGSKNAEILP---------ALKRV-------QAGHLLnaplqklSGG 124
Cdd:PRK13633 80 lwdirnKAGMVFQ--NPDNQIVATiVEE--DVAFGPENLGIPPeeirervdeSLKKVgmyeyrrHAPHLL-------SGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 125 ETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVmAKTDEVLCLNH-HICCSGT 203
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSgKVVMEGT 227
|
....
gi 768329558 204 PEAV 207
Cdd:PRK13633 228 PKEI 231
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-195 |
1.22e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.04 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQR-----NVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ--------RDPGLRIGY 71
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQKLHIDPT--------------------------LPVTVER---FMRLTRGSKNAEILP-ALKRVQAGHLLNAPLQK- 120
Cdd:PRK13651 83 VLEKLVIQKTrfkkikkikeirrrvgvvfqfaeyqlFEQTIEKdiiFGPVSMGVSKEEAKKrAAKYIELVGLDESYLQRs 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 121 ---LSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:PRK13651 163 pfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-214 |
1.55e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.40 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ---------------RDPGLRIGYV---PQKLHIDPT 81
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagyhitpetgnknlKKLRKKVSLVfqfPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 82 LPVTVErFMRLTRGSKNAEI----LPALKRVQ-AGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQ 156
Cdd:PRK13641 103 VLKDVE-FGPKNFGFSEDEAkekaLKWLKKVGlSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 768329558 157 VSLYDLINQLRVELNCgVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPEFI 214
Cdd:PRK13641 182 KEMMQLFKDYQKAGHT-VILVTHNMDDVAEYADDVLVLEHgKLIKHASPKEIFSDKEWL 239
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-180 |
2.78e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 71.69 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 8 DNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQ-KLHIDPTLPVTV 86
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQsRDALDPNKTVWE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 87 E-----RFMRLtrgsKNAEIlPALKRVQAGHLLNAPLQK----LSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQV 157
Cdd:PRK11819 408 EisgglDIIKV----GNREI-PSRAYVGRFNFKGGDQQKkvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLR 482
|
170 180
....*....|....*....|....*.
gi 768329558 158 SLYDLInqlrveLN---CgVLMVSHD 180
Cdd:PRK11819 483 ALEEAL------LEfpgC-AVVISHD 501
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-152 |
3.59e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 9 NVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLL--APTTGSVQrdpglrigyVPQkLHIDPTLPVtV 86
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVD---------VPD-NQFGREASL-I 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 87 ERFMRltRGSKNA--EILPALKRVQAgHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVD 152
Cdd:COG2401 104 DAIGR--KGDFKDavELLNAVGLSDA-VLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-204 |
4.60e-14 |
|
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: 71.58 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 17 RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV---QRDPGLRIGYVPQKLHIDPTLPV-----TVER 88
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvgGKDIETNLDAVRQSLGMCPQHNIlfhhlTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 89 FMRL-------TRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYD 161
Cdd:TIGR01257 1023 HILFyaqlkgrSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 768329558 162 LInqLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTP 204
Cdd:TIGR01257 1103 LL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQgRLYCSGTP 1144
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-192 |
4.95e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.10 E-value: 4.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 23 VSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ--------RDPG--LRIGYV--PQKLHIDPTLPV-TVE-- 87
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYldgkpidiRSPRdaIRAGIMlcPEDRKAEGIIPVhSVAdn 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 88 ----------RFMRLTRGSKNAEIlpALKRVQAghlLN-------APLQKLSGGETQRVLLARALLNQPQLLVLDEPTQG 150
Cdd:PRK11288 352 inisarrhhlRAGCLINNRWEAEN--ADRFIRS---LNiktpsreQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768329558 151 VDVNGQVSLYDLINQLrVELNCGVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK11288 427 IDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIV 467
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-181 |
6.29e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.84 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 24 SLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQK-----------------------LHIDP 80
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRrpvsmlfqennlfshltvaqnigLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 81 TLPVTVERFMRLTRGSKNAEILPALKRVqaghllnaPLQkLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLY 160
Cdd:PRK10771 99 GLKLNAAQREKLHAIARQMGIEDLLARL--------PGQ-LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180
....*....|....*....|.
gi 768329558 161 DLINQLRVELNCGVLMVSHDL 181
Cdd:PRK10771 170 TLVSQVCQERQLTLLMVSHSL 190
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-208 |
7.31e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.60 E-value: 7.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGL--LAPTTGSVQRDPGL--RIGYV--PQKL-- 76
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALceKCGYVerPSKVge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 77 ---------------HIDPTLPVTvERFMR-----LTR---------------------GSKNAE----ILPALKRVQAG 111
Cdd:TIGR03269 81 pcpvcggtlepeevdFWNLSDKLR-RRIRKriaimLQRtfalygddtvldnvlealeeiGYEGKEavgrAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 112 HLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEV 191
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*...
gi 768329558 192 LCL-NHHICCSGTPEAVS 208
Cdd:TIGR03269 240 IWLeNGEIKEEGTPDEVV 257
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
30-181 |
8.88e-14 |
|
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: 67.21 E-value: 8.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 30 GRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIGYVPQKLhidptlpvtverfmrltrgsknaeilpalkrvq 109
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD-GITPVYKPQYI--------------------------------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768329558 110 aghllnaplqKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDL 181
Cdd:cd03222 71 ----------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDL 132
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
6-179 |
1.13e-13 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 68.44 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 6 TLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGllapttgsvqrDPGLRI--------GYVPQKLH 77
Cdd:TIGR01978 2 KIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG-----------HPSYEVtsgtilfkGQDLLELE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 78 ID--------------PTLP-VTVERFMrltRGSKNA----EILPALKRVQAGHLLNAPLQKL---------------SG 123
Cdd:TIGR01978 71 PDeraraglflafqypEEIPgVSNLEFL---RSALNArrsaRGEEPLDLLDFEKLLKEKLALLdmdeeflnrsvnegfSG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 124 GETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVElNCGVLMVSH 179
Cdd:TIGR01978 148 GEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREP-DRSFLIITH 202
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-196 |
1.50e-13 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 69.75 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 2 TSLVTLDNVSIKF--NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD---------PGLR-- 68
Cdd:TIGR02203 328 RGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghdladytlASLRrq 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 69 IGYVPQKLHI-DPTLPVTVeRFMRlTRGSKNAEILPALKRVQAGHLLNA-PL----------QKLSGGETQRVLLARALL 136
Cdd:TIGR02203 408 VALVSQDVVLfNDTIANNI-AYGR-TEQADRAEIERALAAAYAQDFVDKlPLgldtpigengVLLSGGQRQRLAIARALL 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 137 NQPQLLVLDEPTQGVDVNGQVSLYDLINqlRVELNCGVLMVSHDLHLVmAKTDEVLCLNH 196
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALE--RLMQGRTTLVIAHRLSTI-EKADRIVVMDD 542
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-196 |
1.56e-13 |
|
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: 67.11 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRN-----VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRdPGlRIGYVPQKLHId 79
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-PG-SIAYVSQEPWI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 80 ptLPVTV------------ERFMRLTRG---SKNAEILPALKRVQAGhllnaplQK---LSGGETQRVLLARALLNQPQL 141
Cdd:cd03250 78 --QNGTIrenilfgkpfdeERYEKVIKAcalEPDLEILPDGDLTEIG-------EKginLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 768329558 142 LVLDEPTQGVDVNGQVSLYDliNQLRVELNCG--VLMVSHDLHLVmAKTDEVLCLNH 196
Cdd:cd03250 149 YLLDDPLSAVDAHVGRHIFE--NCILGLLLNNktRILVTHQLQLL-PHADQIVVLDN 202
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-191 |
1.64e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.15 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 15 NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGL-----------------RIGYVPQKLH 77
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkdifqidaiklrkEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 78 IDPTLPVTVERFMRL-TRGSKNAE-----ILPALKRV----QAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEP 147
Cdd:PRK14246 101 PFPHLSIYDNIAYPLkSHGIKEKReikkiVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 768329558 148 TQGVDVNGQVSLYDLINQLRVELncGVLMVSHDLHLVMAKTDEV 191
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYV 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-218 |
4.29e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.15 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 15 NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPttgSVQRDP-----GLRI---------GYVPQKLHIDP 80
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPK---GVKGSGsvllnGMPIdakemraisAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 81 TLpvTVER---FM-------RLTRGSKNA---EILPALKRVQAGHLL-NAPLQK--LSGGETQRVLLARALLNQPQLLVL 144
Cdd:TIGR00955 113 TL--TVREhlmFQahlrmprRVTKKEKRErvdEVLQALGLRKCANTRiGVPGRVkgLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 145 DEPTQGVDvngQVSLYDLINQLRVELNCG--VLMVSHDlhlvmaKTDEVLCLNHHICC--------SGTPeavSQHPEFI 214
Cdd:TIGR00955 191 DEPTSGLD---SFMAYSVVQVLKGLAQKGktIICTIHQ------PSSELFELFDKIILmaegrvayLGSP---DQAVPFF 258
|
....
gi 768329558 215 AMFG 218
Cdd:TIGR00955 259 SDLG 262
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-196 |
4.46e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.19 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 16 QRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLApTTGSV----------QRDPGL----RIGYVPQKLH--ID 79
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIwfdgqplhnlNRRQLLpvrhRIQVVFQDPNssLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 80 PTLPV--TVERFMR-----LTRGSKNAEILPALKRVQaghlLNAPLQ-----KLSGGETQRVLLARALLNQPQLLVLDEP 147
Cdd:PRK15134 377 PRLNVlqIIEEGLRvhqptLSAAQREQQVIAVMEEVG----LDPETRhrypaEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768329558 148 TQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQ 501
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
19-217 |
7.00e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.18 E-value: 7.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 19 VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--------QRDPGLR-IGYVPQKLHIDPTLpvTVERF 89
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIwiggrvvnELEPADRdIAMVFQNYALYPHM--SVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 90 MRL---TRGSKNAEIlpaLKRVQA-------GHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSL 159
Cdd:PRK11650 97 MAYglkIRGMPKAEI---EERVAEaarilelEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQM 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768329558 160 YDLINQLRVELNCGVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHPE--FIAMF 217
Cdd:PRK11650 174 RLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGgVAEQIGTPVEVYEKPAstFVASF 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
121-192 |
9.02e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 9.02e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768329558 121 LSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVElNCGVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRIL 462
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-191 |
9.36e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 9.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 6 TLDNVSIK--FNQRNVLS-------GVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ--------RDP--G 66
Cdd:PRK09700 256 NVSNLAHEtvFEVRNVTSrdrkkvrDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRlngkdispRSPldA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 67 LR--IGYVPQKLHIDPTLP-------VTVERFMRLTR--GS----------KNAEILPALKRVQAgHLLNAPLQKLSGGE 125
Cdd:PRK09700 336 VKkgMAYITESRRDNGFFPnfsiaqnMAISRSLKDGGykGAmglfhevdeqRTAENQRELLALKC-HSVNQNITELSGGN 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 126 TQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLrVELNCGVLMVSHDLHLVMAKTDEV 191
Cdd:PRK09700 415 QQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRI 479
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-179 |
2.24e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.86 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 9 NVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLL-----APTTGSVQ----------RDP---GLRIG 70
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRlfgrniyspdVDPievRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 71 YVPQKLHIDPTLPV--TVERFMRLTRGSKNAEILP-----ALKRV----QAGHLLNAPLQKLSGGETQRVLLARALLNQP 139
Cdd:PRK14267 89 MVFQYPNPFPHLTIydNVAIGVKLNGLVKSKKELDervewALKKAalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 768329558 140 QLLVLDEPTQGVDVNGQVSLYDLINQLRVELNcgVLMVSH 179
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKEYT--IVLVTH 206
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-198 |
3.32e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 65.28 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 23 VSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV-------------------QRdpglRIGYVPQKLHIDPTLp 83
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvlfdaekgiclppeKR----RIGYVFQDARLFPHY- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 84 vTVERFMRL-TRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDL 162
Cdd:PRK11144 92 -KVRGNLRYgMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 768329558 163 INQLRVELNCGVLMVSHDLhlvmaktDEVLCLNHHI 198
Cdd:PRK11144 171 LERLAREINIPILYVSHSL-------DEILRLADRV 199
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
23-196 |
5.19e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.04 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 23 VSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV----------------QR------------DPGLRIGY--- 71
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhplhfgdysyrsQRirmifqdpstslNPRQRISQild 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQKLHIDPTLPvtvERFMRLTRGSKNAEILPalkrvqaGHLLNAPlQKLSGGETQRVLLARALLNQPQLLVLDEPTQGV 151
Cdd:PRK15112 112 FPLRLNTDLEPE---QREKQIIETLRQVGLLP-------DHASYYP-HMLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 768329558 152 DVNGQVSLYDLINQLRVELNCGVLMVSHdlHLVMAK--TDEVLCLNH 196
Cdd:PRK15112 181 DMSMRSQLINLMLELQEKQGISYIYVTQ--HLGMMKhiSDQVLVMHQ 225
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
7-192 |
1.09e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 63.39 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 7 LD--NVSIKFNQRN----VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLG-------------------LLAPTTGSV 61
Cdd:COG4170 4 LDirNLTIEIDTPQgrvkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGitkdnwhvtadrfrwngidLLKLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 62 QRDPGLRIGYVPQ--KLHIDPTLPV-----------TVE-RFMRLTRGSKNAEIlPALKRV---QAGHLLNAPLQKLSGG 124
Cdd:COG4170 84 RKIIGREIAMIFQepSSCLDPSAKIgdqlieaipswTFKgKWWQRFKWRKKRAI-ELLHRVgikDHKDIMNSYPHELTEG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 125 ETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLV--MAKTDEVL 192
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESIsqWADTITVL 232
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
120-181 |
1.39e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.66 E-value: 1.39e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768329558 120 KLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLrVELNCGVLMVSHDL 181
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINEL-AAEGKGVIVISSEL 464
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-153 |
1.68e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 3 SLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQklhiDPTL 82
Cdd:PRK11147 2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQ----DPPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 83 PVT-----------------VERFMRLTR---GSKNAEILPALKRVQA--GHL-----------------LNA--PLQKL 121
Cdd:PRK11147 78 NVEgtvydfvaegieeqaeyLKRYHDISHlveTDPSEKNLNELAKLQEqlDHHnlwqlenrinevlaqlgLDPdaALSSL 157
|
170 180 190
....*....|....*....|....*....|..
gi 768329558 122 SGGETQRVLLARALLNQPQLLVLDEPTQGVDV 153
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDI 189
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-152 |
2.17e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.22 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 23 VSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQR-----DPG-----LRIGYVPQ--------------KLHi 78
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGdiatrRRVGYMSQafslygeltvrqnlELH- 363
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768329558 79 dptlpvtvERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVD 152
Cdd:NF033858 364 --------ARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-199 |
2.36e-11 |
|
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: 63.39 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 19 VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVqRDPGlRIGYVPQKLHIdptLPVTVE----------- 87
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-KHSG-RISFSPQTSWI---MPGTIKdniifglsyde 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 88 -RFMRLTRGSKNAEILPALKRVQAGHLLNAPLqKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYD----- 161
Cdd:TIGR01271 516 yRYTSVIKACQLEEDIALFPEKDKTVLGEGGI-TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEsclck 594
|
170 180 190
....*....|....*....|....*....|....*....
gi 768329558 162 -LINQLRvelncgVLMVSHDLHLvmAKTDEVLCLNHHIC 199
Cdd:TIGR01271 595 lMSNKTR------ILVTSKLEHL--KKADKILLLHEGVC 625
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-168 |
3.76e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 60.74 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 2 TSLVTLDNVSIKF----NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLaPTTGSVQRD---PGL------- 67
Cdd:cd03233 1 ASTLSWRNISFTTgkgrSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT-EGNVSVEGDihyNGIpykefae 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 68 ----RIGYVPQKLHIDPTLpvTVERFMRLTRGSKNaeilpalkrvqaghllNAPLQKLSGGETQRVLLARALLNQPQLLV 143
Cdd:cd03233 80 kypgEIIYVSEEDVHFPTL--TVRETLDFALRCKG----------------NEFVRGISGGERKRVSIAEALVSRASVLC 141
|
170 180
....*....|....*....|....*
gi 768329558 144 LDEPTQGVDvngQVSLYDLINQLRV 168
Cdd:cd03233 142 WDNSTRGLD---SSTALEILKCIRT 163
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-211 |
4.25e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.42 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 15 NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV----QRDPGLRIGYVPQKLHIDPTLPV----TV 86
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdIPLTKLQLDSWRSRLAVVSQTPFlfsdTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 87 ERFMRLTRGSKNAEILPALKRVQAGH--LLNAPLQ----------KLSGGETQRVLLARALLNQPQLLVLDEPTQGVDvn 154
Cdd:PRK10789 406 ANNIALGRPDATQQEIEHVARLASVHddILRLPQGydtevgergvMLSGGQKQRISIARALLLNAEILILDDALSAVD-- 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 155 GQVSLYDLINQLRVELNCGVLMVSHDLHlVMAKTDEVLCLNH-HICCSGTPEAVSQHP 211
Cdd:PRK10789 484 GRTEHQILHNLRQWGEGRTVIISAHRLS-ALTEASEILVMQHgHIAQRGNHDQLAQQS 540
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-212 |
4.33e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.14 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 13 KFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIGYVPQKlhiDPTLPVTVERFMRL 92
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVN-GQTINLVRDK---DGQLKVADKNQLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 93 TRGSKNA--------EILPALKRVqaghlLNAPLQ--------------------------------KLSGGETQRVLLA 132
Cdd:PRK10619 90 LRTRLTMvfqhfnlwSHMTVLENV-----MEAPIQvlglskqeareravkylakvgideraqgkypvHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 133 RALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLmVSHDLHLVMAKTDEVLCLNH-HICCSGTPEAVSQHP 211
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQgKIEEEGAPEQLFGNP 243
|
.
gi 768329558 212 E 212
Cdd:PRK10619 244 Q 244
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
10-152 |
6.14e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 59.95 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 10 VSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVvlglLAP--TTGSV---------QRDPGLR--IGYVPQK- 75
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDV----LAGrkTAGVItgeilingrPLDKNFQrsTGYVEQQd 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768329558 76 LHIdPTLpvTVERFMRLTrgsknaeilpalkrvqaghllnAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVD 152
Cdd:cd03232 89 VHS-PNL--TVREALRFS----------------------ALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-211 |
1.03e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.39 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKF-NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV----------QRDPGLR--IG 70
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfSKLQGIRklVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 71 YVPQKLHIDpTLPVTVERfmRLTRGSKNAEILP---------ALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQL 141
Cdd:PRK13644 81 IVFQNPETQ-FVGRTVEE--DLAFGPENLCLPPieirkrvdrALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768329558 142 LVLDEPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLVMAkTDEVLCLNH-HICCSGTPEAVSQHP 211
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEELHD-ADRIIVMDRgKIVLEGEPENVLSDV 226
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
120-184 |
1.32e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.53 E-value: 1.32e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768329558 120 KLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLV 184
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALV 217
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-213 |
1.70e-10 |
|
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: 59.87 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 19 VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPglRIGYVPQKLHIdptLPVTVE----------- 87
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--RISFSSQFSWI---MPGTIKeniifgvsyde 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 88 -RFMRLTRGSKNAEILPALKRVQaghllNAPLQK----LSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYD- 161
Cdd:cd03291 127 yRYKSVVKACQLEEDITKFPEKD-----NTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEs 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 768329558 162 -----LINQLRvelncgVLMVSHDLHLvmAKTDEVLCLNHHIC-CSGT-PEAVSQHPEF 213
Cdd:cd03291 202 cvcklMANKTR------ILVTSKMEHL--KKADKILILHEGSSyFYGTfSELQSLRPDF 252
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-179 |
1.93e-10 |
|
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: 60.69 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQ--RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLApTTGSVQRDpGLR------------IG 70
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQID-GVSwnsvtlqtwrkaFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 71 YVPQKLHI---------DPTLPVTVERFMRLTR--GSKNA-EILPA---LKRVQAGHLlnaplqkLSGGETQRVLLARAL 135
Cdd:TIGR01271 1296 VIPQKVFIfsgtfrknlDPYEQWSDEEIWKVAEevGLKSViEQFPDkldFVLVDGGYV-------LSNGHKQLMCLARSI 1368
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768329558 136 LNQPQLLVLDEPTQGVDvngQVSLYDLINQLRVEL-NCGVLMVSH 179
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLD---PVTLQIIRKTLKQSFsNCTVILSEH 1410
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
120-184 |
2.04e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.82 E-value: 2.04e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768329558 120 KLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLV 184
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQML 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-184 |
2.50e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.25 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 23 VSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIGYVP----QKLH-------------IDPTLPVT 85
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFN-GQRIDTLSpgklQALRrdiqfifqdpyasLDPRQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 86 VE-----RFMRLTRGSKNAE-ILPALKRV--QAGHLLNAPlQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQV 157
Cdd:PRK10261 422 DSimeplRVHGLLPGKAAAArVAWLLERVglLPEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
|
170 180
....*....|....*....|....*..
gi 768329558 158 SLYDLINQLRVELNCGVLMVSHDLHLV 184
Cdd:PRK10261 501 QIINLLLDLQRDFGIAYLFISHDMAVV 527
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-179 |
3.90e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.50 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 2 TSLVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLA--PTTGSV--------QRDPGLRigy 71
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDIlfkgesilDLEPEER--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 vpQKLHI-----DP-TLP-VTVERFMRLTRGSKN-AEILPALKRVQAGHLLNAPLQKL---------------SGGETQR 128
Cdd:CHL00131 82 --AHLGIflafqYPiEIPgVSNADFLRLAYNSKRkFQGLPELDPLEFLEIINEKLKLVgmdpsflsrnvnegfSGGEKKR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768329558 129 -VLLARALLNqPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCgVLMVSH 179
Cdd:CHL00131 160 nEILQMALLD-SELAILDETDSGLDIDALKIIAEGINKLMTSENS-IILITH 209
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4-179 |
4.25e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 57.57 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRNVLSgVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV-------QRDPGLRIGYVPQKL 76
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyykncniNNIAKPYCTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 77 HIdpTLPVTVERFMRL-TRGSKNAEILP-ALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEptqgVDVN 154
Cdd:PRK13541 80 GL--KLEMTVFENLKFwSEIYNSAETLYaAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE----VETN 153
|
170 180
....*....|....*....|....*...
gi 768329558 155 GQVSLYDLINQLRV-ELNCG--VLMVSH 179
Cdd:PRK13541 154 LSKENRDLLNNLIVmKANSGgiVLLSSH 181
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-152 |
1.33e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.81 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKF-NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD---------PGLR--IGYV 72
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDgrplsslshSVLRqgVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 73 PQklhiDPTlpVTVERF---MRLTRGSKNAEILPALKRVQAGHL-------LNAPL----QKLSGGETQRVLLARALLNQ 138
Cdd:PRK10790 421 QQ----DPV--VLADTFlanVTLGRDISEEQVWQALETVQLAELarslpdgLYTPLgeqgNNLSVGQKQLLALARVLVQT 494
|
170
....*....|....
gi 768329558 139 PQLLVLDEPTQGVD 152
Cdd:PRK10790 495 PQILILDEATANID 508
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-195 |
2.25e-09 |
|
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: 57.65 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 19 VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIGYV-----PQKLHIDPTLPVTVERFMRLT 93
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID-GLNIAKIglhdlRFKITIIPQDPVLFSGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 94 ----RGSKNAEILPALkrvQAGHL------LNAPL--------QKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNG 155
Cdd:TIGR00957 1380 ldpfSQYSDEEVWWAL---ELAHLktfvsaLPDKLdhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1456
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768329558 156 QvslyDLINQ-LRVEL-NCGVLMVSHDLHLVMAKTdEVLCLN 195
Cdd:TIGR00957 1457 D----NLIQStIRTQFeDCTVLTIAHRLNTIMDYT-RVIVLD 1493
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-152 |
2.29e-09 |
|
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: 57.65 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGlrIGYVPQKLHI-DPTLPVTV-------ERFMR 91
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQAWIqNDSLRENIlfgkalnEKYYQ 731
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 92 LTRGS----KNAEILPALKRVQAGHL-LNaplqkLSGGETQRVLLARALLNQPQLLVLDEPTQGVD 152
Cdd:TIGR00957 732 QVLEAcallPDLEILPSGDRTEIGEKgVN-----LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-195 |
3.06e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 19 VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDP------GLR-----IGYVPQKlhidPTLPVTVE 87
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfGLMdlrkvLGIIPQA----PVLFSGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 88 RFMRLTRGSKN-AEILPALKRvqaGHL----------LNAPL----QKLSGGETQRVLLARALLNQPQLLVLDEPTQGVD 152
Cdd:PLN03130 1330 RFNLDPFNEHNdADLWESLER---AHLkdvirrnslgLDAEVseagENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768329558 153 VNGQVslydLINQ-LRVEL-NCGVLMVSHDLHLVMaKTDEVLCLN 195
Cdd:PLN03130 1407 VRTDA----LIQKtIREEFkSCTMLIIAHRLNTII-DCDRILVLD 1446
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
8-192 |
3.65e-09 |
|
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: 54.64 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 8 DNVSIKFNQRNVLSGVSlalqpgriltllgpnGAGKSTLVrvvlgllapttgsvqrdpgLRIGYVPQKLHIDPTLPvtve 87
Cdd:cd03238 14 LDVSIPLNVLVVVTGVS---------------GSGKSTLV-------------------NEGLYASGKARLISFLP---- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 88 rfmrltRGSKNAEI----LPALKRVQAGHL-LNAPLQKLSGGETQRVLLARALLNQPQ--LLVLDEPTQGVDvngQVSLY 160
Cdd:cd03238 56 ------KFSRNKLIfidqLQFLIDVGLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH---QQDIN 126
|
170 180 190
....*....|....*....|....*....|....
gi 768329558 161 DLINQLRVELNCG--VLMVSHDLHlVMAKTDEVL 192
Cdd:cd03238 127 QLLEVIKGLIDLGntVILIEHNLD-VLSSADWII 159
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-203 |
3.69e-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: 56.95 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 25 LALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQ----------RDPGLRIGYVPQKLHIDPTLPVTVERFM--RL 92
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATvagksiltniSDVHQNMGYCPQFDAIDDLLTGREHLYLyaRL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 93 tRGSKNAEIlpalKRVQaghllNAPLQKL-------------SGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSL 159
Cdd:TIGR01257 2040 -RGVPAEEI----EKVA-----NWSIQSLglslyadrlagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 768329558 160 YDLINQLRVElNCGVLMVSHDLhlvmaKTDEVLCLNHHICCSGT 203
Cdd:TIGR01257 2110 WNTIVSIIRE-GRAVVLTSHSM-----EECEALCTRLAIMVKGA 2147
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-195 |
3.85e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 19 VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD----PGLRIGYVPQKLHIDPTLPVTVERFMRLT- 93
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDdcdvAKFGLTDLRRVLSIIPQSPVLFSGTVRFNi 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 94 ---RGSKNAEILPALKRVQAGHLL-NAPL----QKLSGGET----QRVLL--ARALLNQPQLLVLDEPTQGVDVNGQvsl 159
Cdd:PLN03232 1331 dpfSEHNDADLWEALERAHIKDVIdRNPFgldaEVSEGGENfsvgQRQLLslARALLRRSKILVLDEATASVDVRTD--- 1407
|
170 180 190
....*....|....*....|....*....|....*...
gi 768329558 160 yDLINQ-LRVEL-NCGVLMVSHDLHLVMaKTDEVLCLN 195
Cdd:PLN03232 1408 -SLIQRtIREEFkSCTMLVIAHRLNTII-DCDKILVLS 1443
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-180 |
4.17e-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: 53.92 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 29 PGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRdpglrigyvpqklhIDPTlpvtverfmrltrgsknaEILPALKRV 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------IDGE------------------DILEEVLDQ 48
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768329558 109 QAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLIN-----QLRVELNCGVLMVSHD 180
Cdd:smart00382 49 LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEKNLTVILTTND 125
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-218 |
4.86e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.18 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQRNV--LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD---------PGLR--IGY 71
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDghdlrdytlASLRnqVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 72 VPQKLHI--DptlpvTVERFMRLTRGSK--NAEILPALKRVQAGHLLNaPLQK------------LSGGETQRVLLARAL 135
Cdd:PRK11176 422 VSQNVHLfnD-----TIANNIAYARTEQysREQIEEAARMAYAMDFIN-KMDNgldtvigengvlLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 136 LNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVelNCGVLMVSHDLHLVmAKTDEVLCLNH-HICCSGTpeavsqHPEFI 214
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI-EKADEILVVEDgEIVERGT------HAELL 566
|
....
gi 768329558 215 AMFG 218
Cdd:PRK11176 567 AQNG 570
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-181 |
6.19e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.17 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 8 DNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVV--LGLLAPT---TGSV----------QRDPG---LRI 69
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVtfhgknlyapDVDPVevrRRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 70 GYVPQKLHIDPT------------------LPVTVERFMRltRGSKNAEILPALKrvQAGhllnaplQKLSGGETQRVLL 131
Cdd:PRK14243 94 GMVFQKPNPFPKsiydniaygaringykgdMDELVERSLR--QAALWDEVKDKLK--QSG-------LSLSGGQQQRLCI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 768329558 132 ARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNcgVLMVSHDL 181
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYT--IIIVTHNM 210
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
102-208 |
1.53e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 55.02 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 102 LPALKRVQAGHL-LNAPLQKLSGGETQRVLLARALL---NQPQLLVLDEPTQGV---DVNgqvSLYDLINQLrVELNCGV 174
Cdd:TIGR00630 810 LQTLCDVGLGYIrLGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLhfdDIK---KLLEVLQRL-VDKGNTV 885
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 768329558 175 LMVSHDLHlVMAKTDEVLCL-------NHHICCSGTPEAVS 208
Cdd:TIGR00630 886 VVIEHNLD-VIKTADYIIDLgpeggdgGGTVVASGTPEEVA 925
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-157 |
1.60e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 15 NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGS--VQRDpglRIGYVPQKLHI------------DP 80
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDAsvVIRG---TVAYVPQVSWIfnatvrdnilfgSP 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 81 TLPVTVERFMRLTRGSKNAEILPALKRVQAGHL-LNaplqkLSGGETQRVLLARALLNQPQLLVLDEPTQGVD--VNGQV 157
Cdd:PLN03130 705 FDPERYERAIDVTALQHDLDLLPGGDLTEIGERgVN-----ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDahVGRQV 779
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-181 |
2.10e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.56 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 9 NVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTG---------------------SVQRDPGL 67
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggrsifnyrdvlEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 68 ---RIGYVPQKLHIDPTLPVTVERFM--RLTRGSKNAEILP-ALKRVQAGHLLNAPLqKLSGGETQRVLLARALLNQPQL 141
Cdd:PRK14271 106 lfqRPNPFPMSIMDNVLAGVRAHKLVprKEFRGVAQARLTEvGLWDAVKDRLSDSPF-RLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 768329558 142 LVLDEPTQGVDVNGQVSLYDLINQLRVELNcgVLMVSHDL 181
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLT--VIIVTHNL 222
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-184 |
2.34e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.28 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQKLHIDPTLPVTVErFMRLTRGSKNA 99
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGIENIE-FKMLCMGFKRK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 100 EILPALKRV----QAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEP-TQGVDVNGQVSLyDLINQLRvELNCGV 174
Cdd:PRK13546 119 EIKAMTPKIiefsELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCL-DKIYEFK-EQNKTI 196
|
170
....*....|
gi 768329558 175 LMVSHDLHLV 184
Cdd:PRK13546 197 FFVSHNLGQV 206
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-194 |
3.32e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 9 NVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIGY-------------VPQK 75
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQ-GKEIDFksskealengismVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 76 LHIdpTLPVTVERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQ----------KLSGGETQRVLLARALLNQPQLLVLD 145
Cdd:PRK10982 82 LNL--VLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDididprakvaTLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768329558 146 EPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDLHLVMAKTDEVLCL 194
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-152 |
3.34e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 10 VSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLapTTGSVQRD------PGL------RIGYVPQK-L 76
Cdd:TIGR00956 769 VKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGdrlvngRPLdssfqrSIGYVQQQdL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 77 HIdPTlpVTVER------FMR----LTRGSKNAEILPALKRVQ----AGHLLNAPLQKLSGGETQRVLLARALLNQPQLL 142
Cdd:TIGR00956 847 HL-PT--STVREslrfsaYLRqpksVSKSEKMEYVEEVIKLLEmesyADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLL 923
|
170
....*....|.
gi 768329558 143 V-LDEPTQGVD 152
Cdd:TIGR00956 924 LfLDEPTSGLD 934
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-191 |
8.66e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 8.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTT--------GSVQRDPGLR------IGYVPQKLHIDPTLPVT 85
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyegeilfdGEVCRFKDIRdsealgIVIIHQELALIPYLSIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 86 VERFM---RLTRG-------SKNAEILpaLKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNG 155
Cdd:NF040905 97 ENIFLgneRAKRGvidwnetNRRAREL--LAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEED 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 768329558 156 QVSLYDLINQLRVElncGV--LMVSHDLHLVMAKTDEV 191
Cdd:NF040905 175 SAALLDLLLELKAQ---GItsIIISHKLNEIRRVADSI 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
113-181 |
1.01e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 1.01e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768329558 113 LLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDL 181
Cdd:PTZ00265 572 LVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
99-184 |
1.02e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 51.46 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 99 AEILPALKRVQAGHL-LNAPLQKLSGGETQRVLLARALLNQ---PQLLVLDEPTQGV---DVNgqvSLYDLINQLrVELN 171
Cdd:cd03271 147 ARKLQTLCDVGLGYIkLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLhfhDVK---KLLEVLQRL-VDKG 222
|
90
....*....|...
gi 768329558 172 CGVLMVSHDLHLV 184
Cdd:cd03271 223 NTVVVIEHNLDVI 235
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
119-196 |
1.37e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.37e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768329558 119 QKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELNCGVLMVSHDLHLVmAKTDEVLCLNH 196
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI-KRSDKIVVFNN 1433
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-155 |
1.44e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.62 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 15 NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD-----PGLRIGYVPQKLHIdPTLPV---TV 86
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDgktatRGDRSRFMAYLGHL-PGLKAdlsTL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768329558 87 E--RFMRLTRGsKNAEILP--ALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNG 155
Cdd:PRK13543 101 EnlHFLCGLHG-RRAKQMPgsALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
33-184 |
2.11e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.91 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 33 LTLL-GPNGAGKSTL---VRVVL-GLLAPTTGSVQRDP-----GLRIGYVPQKLHIDPTLPVTVERFMRLTRGS---KNA 99
Cdd:cd03240 24 LTLIvGQNGAGKTTIieaLKYALtGELPPNSKGGAHDPklireGEVRAQVKLAFENANGKKYTITRSLAILENVifcHQG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 100 EILPALKRvqaghllnaPLQKLSGGetQRVL--------LARALLNQPQLLVLDEPTQGVDV-NGQVSLYDLINQLRVEL 170
Cdd:cd03240 104 ESNWPLLD---------MRGRCSGG--EKVLasliirlaLAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQK 172
|
170
....*....|....
gi 768329558 171 NCGVLMVSHDLHLV 184
Cdd:cd03240 173 NFQLIVITHDEELV 186
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-161 |
3.10e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAP--TTGSVQRDpglRIGYVPQKLHI-DPTLPVTV--------ER 88
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaeTSSVVIRG---SVAYVPQVSWIfNATVRENIlfgsdfesER 709
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768329558 89 FMR---LTRGSKNAEILPALKRVQAGHL-LNaplqkLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYD 161
Cdd:PLN03232 710 YWRaidVTALQHDLDLLPGRDLTEIGERgVN-----ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD 781
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-218 |
3.23e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 19 VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSV--QRDpglrIGYVPQKLHI------DPTLPVTVERFM 90
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaERS----IAYVPQQAWImnatvrGNILFFDEEDAA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 91 RLTRGSKNAEILPALKRVQAGhLLNAPLQK---LSGGETQRVLLARALLNQPQLLVLDEPTQGVDVN-GQVSLYDLInql 166
Cdd:PTZ00243 751 RLADAVRVSQLEADLAQLGGG-LETEIGEKgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECF--- 826
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 768329558 167 rvelnCGVL------MVSHDLHLVmAKTDEVLCLNH-HICCSGTPEAVSQHPEFIAMFG 218
Cdd:PTZ00243 827 -----LGALagktrvLATHQVHVV-PRADYVVALGDgRVEFSGSSADFMRTSLYATLAA 879
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-152 |
4.16e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.85 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKFNQ--RNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLApTTGSVQRDpGLR------------IG 70
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQID-GVSwnsvplqkwrkaFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 71 YVPQKLHI---------DPTLPVTVERFMRLTRgsknaEIlpALKRV--QAGHLLNAPLQK----LSGGETQRVLLARAL 135
Cdd:cd03289 81 VIPQKVFIfsgtfrknlDPYGKWSDEEIWKVAE-----EV--GLKSVieQFPGQLDFVLVDggcvLSHGHKQLMCLARSV 153
|
170
....*....|....*..
gi 768329558 136 LNQPQLLVLDEPTQGVD 152
Cdd:cd03289 154 LSKAKILLLDEPSAHLD 170
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
15-181 |
5.29e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.12 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 15 NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVR-VVLGLLAPTTGSVQRDPGLRIGYVPQklhidptlpvtverfmrlt 93
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaIGLALGGAQSATRRRSGVKAGCIVAA------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 94 rgsknAEILPALKRVQaghllnaplqkLSGGETQRV----LLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVE 169
Cdd:cd03227 67 -----VSAELIFTRLQ-----------LSGGEKELSalalILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK 130
|
170
....*....|..
gi 768329558 170 lNCGVLMVSHDL 181
Cdd:cd03227 131 -GAQVIVITHLP 141
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
114-184 |
7.64e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 7.64e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768329558 114 LNAPLQKLSGGETQRVLLARALLN---QPQLLVLDEPTQGVDVNGQVSLYDLINQLrVELNCGVLMVSHDLHLV 184
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSL-THQGHTVVIIEHNMHVV 875
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-242 |
9.39e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 9.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQKlhiDPTLP 83
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQE---TPALP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 84 VTV--------ERFMRLTRGSKNAEI-------------LPALK----RVQAGHLLNA----------PLQKLSGGETQR 128
Cdd:PRK10636 78 QPAleyvidgdREYRQLEAQLHDANErndghaiatihgkLDAIDawtiRSRAASLLHGlgfsneqlerPVSDFSGGWRMR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 129 VLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRVELncgvLMVSHDLHLVMAKTDEVLclnhHICCSGTPEAVS 208
Cdd:PRK10636 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTL----ILISHDRDFLDPIVDKII----HIEQQSLFEYTG 229
|
250 260 270
....*....|....*....|....*....|....
gi 768329558 209 QHPEFIAMFGPRGAEELAIYRHHHNHRHDLQGRI 242
Cdd:PRK10636 230 NYSSFEVQRATRLAQQQAMYESQQERVAHLQSYI 263
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-182 |
3.48e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 7 LDNVSIKFNQRNVLSG-VSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpglrigyvpqklhidpTLPVT 85
Cdd:PRK10522 325 LRNVTFAYQDNGFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLD----------------GKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 86 VER-----------------FMRLTrGSKNAEILPA-----LKRVQAGHLLNapLQ-------KLSGGETQRVLLARALL 136
Cdd:PRK10522 389 AEQpedyrklfsavftdfhlFDQLL-GPEGKPANPAlvekwLERLKMAHKLE--LEdgrisnlKLSKGQKKRLALLLALA 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 768329558 137 NQPQLLVLDEPTQGVDVNGQVSLY-DLINQLRvELNCGVLMVSHDLH 182
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFYqVLLPLLQ-EMGKTIFAISHDDH 511
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
14-166 |
5.52e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.65 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 14 FNQRNVLSGVSLALQPGRILTLLGPNGAG--KSTLVRVVLGllaPTTGsvqRDPGLRIGYVPQKLHIDPTL----PV--- 84
Cdd:NF000106 23 FGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAG---RRPWRF*TWCANRRALRRTIg*hrPVr*g 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 85 ------------TVERFMRLTRGSKNAEILPALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVD 152
Cdd:NF000106 97 rresfsgrenlyMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
170
....*....|....
gi 768329558 153 VNGQVSLYDLINQL 166
Cdd:NF000106 177 PRTRNEVWDEVRSM 190
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
121-212 |
8.42e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.60 E-value: 8.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 121 LSGGETQRVLLARALLNQP---QLLVLDEPTQGV---DVNgqvSLYDLINQLrVELNCGVLMVSHDLhlvmaktDEVLCL 194
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDIR---KLLEVLHRL-VDKGNTVVVIEHNL-------DVIKTA 899
|
90 100 110
....*....|....*....|....*....|.
gi 768329558 195 NH-------------HICCSGTPEAVSQHPE 212
Cdd:PRK00349 900 DWiidlgpeggdgggEIVATGTPEEVAKVEA 930
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-229 |
2.32e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.88 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 20 LSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRIGYVPQKLHIDPTLPVTVE---RFMRLTRgS 96
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIElkgLMMGLTK-E 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 97 KNAEILP-ALKRVQAGHLLNAPLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGVDVNGQVSLYDLINQLRvELNCGVL 175
Cdd:PRK13545 119 KIKEIIPeIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFK-EQGKTIF 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 176 MVSHDLHLVMAKTDEVLCLNH-HICCSG-TPEAVSQHPEFIAMFGPRGAEELAIYR 229
Cdd:PRK13545 198 FISHSLSQVKSFCTKALWLHYgQVKEYGdIKEVVDHYDEFLKKYNQMSVEERKDFR 253
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-167 |
3.26e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.01 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 4 LVTLDNVSIKFNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGL--LAPTTGSV--------QRDPGLRIGY-V 72
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVefkgkdllELSPEDRAGEgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 73 PQKLHIDPTLPVTVERFMRLTrgSKNA----EILPALKRV-------QAGHLLNAPLQKL--------SGGETQRV-LLA 132
Cdd:PRK09580 81 FMAFQYPVEIPGVSNQFFLQT--ALNAvrsyRGQEPLDRFdfqdlmeEKIALLKMPEDLLtrsvnvgfSGGEKKRNdILQ 158
|
170 180 190
....*....|....*....|....*....|....*
gi 768329558 133 RALLnQPQLLVLDEPTQGVDVNGQVSLYDLINQLR 167
Cdd:PRK09580 159 MAVL-EPELCILDESDSGLDIDALKIVADGVNSLR 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-152 |
3.44e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 19 VLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGllAPTTGSVQRDpgLRIGYVPQKLHI-----------DPTLP-VTV 86
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGD--IRISGFPKKQETfarisgyceqnDIHSPqVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 87 ER------FMRLTRGSKNAEIL----PALKRVQAGHLLNA-----PLQKLSGGETQRVLLARALLNQPQLLVLDEPTQGV 151
Cdd:PLN03140 971 REsliysaFLRLPKEVSKEEKMmfvdEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
.
gi 768329558 152 D 152
Cdd:PLN03140 1051 D 1051
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
121-212 |
4.59e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 121 LSGGETQRVLLARALL---NQPQLLVLDEPTQGV---DVNgqvSLYDLINQLrVELNCGVLMVSHDLhlvmaktDEVLCL 194
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLhfhDIR---KLLEVLHRL-VDKGNTVVVIEHNL-------DVIKTA 895
|
90 100 110
....*....|....*....|....*....|.
gi 768329558 195 NH-------------HICCSGTPEAVSQHPE 212
Cdd:COG0178 896 DWiidlgpeggdgggEIVAEGTPEEVAKVKA 926
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
122-154 |
3.35e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 3.35e-04
10 20 30
....*....|....*....|....*....|...
gi 768329558 122 SGGETQRVLLARALLNQPQLLVLDEPTQGVDVN 154
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLH 378
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
7-69 |
1.19e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.21 E-value: 1.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768329558 7 LDNVSIKFNQrnvlsgvslalqPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLRI 69
Cdd:COG3950 14 FEDLEIDFDN------------PPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKL 64
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
7-122 |
1.23e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.60 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 7 LDNVSIKfNQRNvLSGVSLALQPGrILTLLGPNGAGKSTLVRvVLGLLAPTTGSVQ---RDPGLRIGYVPQKLHIDPTLP 83
Cdd:COG3593 3 LEKIKIK-NFRS-IKDLSIELSDD-LTVLVGENNSGKSSILE-ALRLLLGPSSSRKfdeEDFYLGDDPDLPEIEIELTFG 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 768329558 84 VTVERFMR-LTRGSKNAEILPALKRVQAghLLNAPLQKLS 122
Cdd:COG3593 79 SLLSRLLRlLLKEEDKEELEEALEELNE--ELKEALKALN 116
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
27-64 |
1.28e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.53 E-value: 1.28e-03
10 20 30
....*....|....*....|....*....|....*...
gi 768329558 27 LQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRD 64
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVRED 229
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
121-212 |
1.49e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 121 LSGGETQRVLLARALLNQpqlL-----VLDEPTQGV---DvNGQvslydLINQLRvEL----NCgVLMVSHDlHLVMAKT 188
Cdd:COG0178 486 LSGGEAQRIRLATQIGSG---LvgvlyVLDEPSIGLhqrD-NDR-----LIETLK-RLrdlgNT-VIVVEHD-EDTIRAA 553
|
90 100 110
....*....|....*....|....*....|.
gi 768329558 189 DEVLCL-----NH--HICCSGTPEAVSQHPE 212
Cdd:COG0178 554 DYIIDIgpgagEHggEVVAQGTPEEILKNPD 584
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
105-186 |
2.37e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.01 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 105 LKRVQAGHL-LNAPLQKLSGGETQRVLLARALLNQPQ--LLVLDEPTQGVDVNGQVSLYDLINQLRvELNCGVLMVSHDL 181
Cdd:cd03270 121 LVDVGLGYLtLSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLR-DLGNTVLVVEHDE 199
|
....*
gi 768329558 182 HLVMA 186
Cdd:cd03270 200 DTIRA 204
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
5-153 |
3.56e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 37.97 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 5 VTLDNVSIKF--NQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDpGLRIGYVP-----QKLH 77
Cdd:cd03288 20 IKIHDLCVRYenNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVID-GIDISKLPlhtlrSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 78 I---DPTLPVTVERFM----------RLTRGSKNAEILPALKRVQAGhlLNAPL----QKLSGGETQRVLLARALLNQPQ 140
Cdd:cd03288 99 IilqDPILFSGSIRFNldpeckctddRLWEALEIAQLKNMVKSLPGG--LDAVVteggENFSVGQRQLFCLARAFVRKSS 176
|
170
....*....|...
gi 768329558 141 LLVLDEPTQGVDV 153
Cdd:cd03288 177 ILIMDEATASIDM 189
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
7-68 |
4.24e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 37.72 E-value: 4.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768329558 7 LDNVSIK----FNQRNVLSGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTTGSVQRDPGLR 68
Cdd:COG1106 2 LISFSIEnfrsFKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKLV 67
|
|
| PrkA |
COG2766 |
Predicted Ser/Thr protein kinase [Signal transduction mechanisms]; |
31-48 |
4.36e-03 |
|
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
Pssm-ID: 442049 [Multi-domain] Cd Length: 675 Bit Score: 37.89 E-value: 4.36e-03
|
| TsaE |
pfam02367 |
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in ... |
26-48 |
6.48e-03 |
|
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in the synthesis of threonylcarbamoyl adenosine (t(6)A).
Pssm-ID: 460540 Cd Length: 127 Bit Score: 35.87 E-value: 6.48e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
99-183 |
6.76e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 99 AEILPALKRVQA----------GHL-LNAPLQKLSGGETQRVLLARALL---NQPQLLVLDEPTQGVDVNGQVSLYDLIN 164
Cdd:PRK00635 1667 AETFPFLKKIQKplqalidnglGYLpLGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLR 1746
|
90
....*....|....*....
gi 768329558 165 QLrVELNCGVLMVSHDLHL 183
Cdd:PRK00635 1747 TL-VSLGHSVIYIDHDPAL 1764
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
21-58 |
8.21e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.11 E-value: 8.21e-03
10 20 30
....*....|....*....|....*....|....*...
gi 768329558 21 SGVSLALQPGRILTLLGPNGAGKSTLVRVVLGLLAPTT 58
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
121-227 |
9.24e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.30 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329558 121 LSGGETQRVLLARALLNQPQ--LLVLDEPTQGVDvngQVSLYDLINQLRVELNCG--VLMVSHDLHlVMAKTDEVLCL-- 194
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLH---QRDNRRLINTLKRLRDLGntLIVVEHDED-TIRAADYVIDIgp 564
|
90 100 110
....*....|....*....|....*....|....*...
gi 768329558 195 ---NH--HICCSGTPEAVSQHPEFIAMFGPRGAEELAI 227
Cdd:TIGR00630 565 gagEHggEVVASGTPEEILANPDSLTGQYLSGRKKIEV 602
|
|
| |
