|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-309 |
8.25e-139 |
|
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: 395.19 E-value: 8.25e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARKNWlgkvterVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQP---SQG---------- 71
Cdd:COG0444 1 LLEVRNLKVYFPTRRGV-------VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGeilfdgedll 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 72 NYSRRDGKQHNG--MQMVFQDPLSSLDPRLPVWRIITEPVWIQKRSSERERRILAEDLAQQVGIRP--EYLDRLPHAFSG 147
Cdd:COG0444 74 KLSEKELRKIRGreIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 148 GQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELG 227
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 228 ETQQVLTHPAHPYTRLLLDSVPKTGAPlAEDLVLRKTELPGNRTLPEGCFFRDRCPLAIRGCENKQ-ILLSSESGCEVRC 306
Cdd:COG0444 234 PVEELFENPRHPYTRALLSSIPRLDPD-GRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEpPLREVGPGHRVAC 312
|
...
gi 740855357 307 WRA 309
Cdd:COG0444 313 HLY 315
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-309 |
5.39e-138 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 393.33 E-value: 5.39e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEFLLALQDVHVSFPARKNWLGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG--------- 71
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGeilfdgqdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 72 -NYSRRDGKQHN-GMQMVFQDPLSSLDPRLPVWRIITEPVWIQKRSSERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQ 149
Cdd:COG4608 83 tGLSGRELRPLRrRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 150 RQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGET 229
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 230 QQVLTHPAHPYTRLLLDSVPKTG-APLAEDLVLrKTELPGNRTLPEGCFFRDRCPLAIRGCENKQILLSS-ESGCEVRCW 307
Cdd:COG4608 243 DELYARPLHPYTQALLSAVPVPDpERRRERIVL-EGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREvGPGHQVACH 321
|
..
gi 740855357 308 RA 309
Cdd:COG4608 322 LA 323
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-250 |
1.98e-122 |
|
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: 360.37 E-value: 1.98e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEFLLALQDVHVSFPARKnwlgkvTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG--------- 71
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRG------KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGsilfdgkdl 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 72 -NYSRRDGKQHNG-MQMVFQDPLSSLDPRLPVWRIITEPVWIQKRSSERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQ 149
Cdd:COG1123 330 tKLSRRSLRELRRrVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 150 RQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGET 229
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
250 260
....*....|....*....|.
gi 740855357 230 QQVLTHPAHPYTRLLLDSVPK 250
Cdd:COG1123 490 EEVFANPQHPYTRALLAAVPS 510
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-250 |
2.70e-120 |
|
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: 355.53 E-value: 2.70e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARKNWLGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGmLQPSQG-------NYSRRD 77
Cdd:COG4172 275 LLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGeirfdgqDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 78 GKQ----HNGMQMVFQDPLSSLDPRLPVWRIITEPVWIQKRS-SERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQRQR 152
Cdd:COG4172 354 RRAlrplRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGlSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 153 IAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQV 232
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
250
....*....|....*...
gi 740855357 233 LTHPAHPYTRLLLDSVPK 250
Cdd:COG4172 514 FDAPQHPYTRALLAAAPL 531
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-249 |
6.58e-108 |
|
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: 314.05 E-value: 6.58e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARKnwlgkvtERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN--------YSRR 76
Cdd:COG1124 1 MLEVRNLSVSYGQGG-------RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEvtfdgrpvTRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 77 DGKQHNGMQMVFQDPLSSLDPRLPVWRIITEPVWIQKRSsERERRIlaEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIA 156
Cdd:COG1124 74 RKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLP-DREERI--AELLEQVGLPPSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 157 RALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHP 236
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
250
....*....|...
gi 740855357 237 AHPYTRLLLDSVP 249
Cdd:COG1124 231 KHPYTRELLAASL 243
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-227 |
6.29e-105 |
|
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: 305.58 E-value: 6.29e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARKNWlgkvterVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG-------NYSRRD 77
Cdd:cd03257 1 LLEVKNLSVSFPTGGGS-------VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGsiifdgkDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 78 GKQ----HNGMQMVFQDPLSSLDPRLPVWRIITEPVWIQKR-SSERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQRQR 152
Cdd:cd03257 74 RRLrkirRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKlSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740855357 153 IAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELG 227
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-309 |
7.04e-105 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 309.20 E-value: 7.04e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEFLLALQDVHVSFPARKNwLGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG--------- 71
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRG-LFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGelyyqgqdl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 72 -NYSRRDGKQ-HNGMQMVFQDPLSSLDPRLPVWRIITEPVWIQKRSSERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQ 149
Cdd:PRK11308 80 lKADPEAQKLlRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 150 RQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGET 229
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 230 QQVLTHPAHPYTRLLLDSVPKTGAPLAEDLVLRKTELPGNRTLPEGCFFRDRCPLAIRGCENKQILLSSESGCEVRCWRA 309
Cdd:PRK11308 240 EQIFNNPRHPYTQALLSATPRLNPDDRRERIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYDGRLVACFAV 319
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-309 |
8.63e-95 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 283.91 E-value: 8.63e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPAR--KNWLGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYS-------R 75
Cdd:PRK15079 8 LLEVADLKVHFDIKdgKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 76 RDGKQ----HNGMQMVFQDPLSSLDPRLPVWRIITEPVWI-QKRSSERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQR 150
Cdd:PRK15079 88 MKDDEwravRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 151 QRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQ 230
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 231 QVLTHPAHPYTRLLLDSVPKTGAPLAEDLV--LRKTELPGNRTLPEGCFFRDRCPLAIRGCENKQILLSSESGCEVRCWR 308
Cdd:PRK15079 248 EVYHNPLHPYTKALMSAVPIPDPDLERNKTiqLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLEGSFRHAVSCLK 327
|
.
gi 740855357 309 A 309
Cdd:PRK15079 328 V 328
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-258 |
1.34e-84 |
|
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: 264.24 E-value: 1.34e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEFLLALQDVHVSFparknwlGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRR---D 77
Cdd:COG4172 2 MSMPLLSVEDLSVAF-------GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSilfD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 78 GKQ-------------HNGMQMVFQDPLSSLDPRLPVWRIITEPVWIQKRSSERERRILAEDLAQQVGIR-PEY-LDRLP 142
Cdd:COG4172 75 GQDllglserelrrirGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPdPERrLDAYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 143 HAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQ 222
Cdd:COG4172 155 HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGE 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 740855357 223 IVELGETQQVLTHPAHPYTRLLLDSVPK-TGAPLAED 258
Cdd:COG4172 235 IVEQGPTAELFAAPQHPYTRKLLAAEPRgDPRPVPPD 271
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-247 |
2.11e-82 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 249.75 E-value: 2.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARKNWLGKvtERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG------------N 72
Cdd:COG4167 4 LLEVRNLSKTFKYRTGLFRR--QQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGeilinghkleygD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 73 YSRRdgKQHngMQMVFQDPLSSLDPRLPVWRIITEPVWIQKRSSERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQRQR 152
Cdd:COG4167 82 YKYR--CKH--IRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 153 IAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQV 232
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEV 237
|
250
....*....|....*
gi 740855357 233 LTHPAHPYTRLLLDS 247
Cdd:COG4167 238 FANPQHEVTKRLIES 252
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-310 |
6.23e-72 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 225.37 E-value: 6.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEFLLALQDVHVSFPARKnwlGKVTervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQ--GNYSRRDG 78
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPD---GDVT----AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGriGGSATFNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 79 --------KQHNGMQ-----MVFQDPLSSLDPRLPVWRIITEPVWIQKRSSERErrilaedlAQQVGIR-------PEYL 138
Cdd:PRK09473 81 reilnlpeKELNKLRaeqisMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAE--------AFEESVRmldavkmPEAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 139 DRL---PHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRV 215
Cdd:PRK09473 153 KRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 216 AVMYLGQIVELGETQQVLTHPAHPYTRLLLDSVPKTGaplAEDLVLrkTELPGNR----TLPEGCFFRDRCPLAIRGCEN 291
Cdd:PRK09473 233 LVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPRLD---AEGESL--LTIPGNPpnllRLPKGCPFQPRCPHAMEICSS 307
|
330
....*....|....*....
gi 740855357 292 KQILLSSESGCEVRCWRAV 310
Cdd:PRK09473 308 APPLEEFGPGRLRACFKPV 326
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-245 |
3.64e-70 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 226.51 E-value: 3.64e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARKNWLGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLqPSQGNYSRRDGKQHN-- 82
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNln 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 83 ---------GMQMVFQDPLSSLDPRLPVWRIITEPVWIQKRS---SERERRILAedLAQQVGIRPEYLDRLPHAFSGGQR 150
Cdd:PRK15134 354 rrqllpvrhRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTlsaAQREQQVIA--VMEEVGLDPETRHRYPAEFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 151 QRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQ 230
Cdd:PRK15134 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCE 511
|
250
....*....|....*
gi 740855357 231 QVLTHPAHPYTRLLL 245
Cdd:PRK15134 512 RVFAAPQQEYTRQLL 526
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-258 |
1.11e-68 |
|
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: 222.47 E-value: 1.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARknwlgkvteRVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLqPSQGNYS---RRDGKQH 81
Cdd:COG1123 4 LLEVRDLSVRYPGG---------DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRISgevLLDGRDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 82 NGMQ---------MVFQDPLSSLDPrLPVWRIITEPVWIQKRSSErERRILAEDLAQQVGIrPEYLDRLPHAFSGGQRQR 152
Cdd:COG1123 74 LELSealrgrrigMVFQDPMTQLNP-VTVGDQIAEALENLGLSRA-EARARVLELLEAVGL-ERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 153 IAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQV 232
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260
....*....|....*....|....*.
gi 740855357 233 LTHPAHPYTRLLLDSVPKTGAPLAED 258
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAA 256
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-269 |
9.03e-66 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 217.42 E-value: 9.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 2 SEFLLALQDVHVSFPARKNWLGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYS------- 74
Cdd:PRK10261 310 GEPILQVRNLVTRFPLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqrid 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 75 ----------RRDgkqhngMQMVFQDPLSSLDPRLPVWRIITEPVWIQKRSSERERRILAEDLAQQVGIRPEYLDRLPHA 144
Cdd:PRK10261 390 tlspgklqalRRD------IQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 145 FSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIV 224
Cdd:PRK10261 464 FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 740855357 225 ELGETQQVLTHPAHPYTRLLLDSVP--KTGAPLAEDlVLRKTELPGN 269
Cdd:PRK10261 544 EIGPRRAVFENPQHPYTRKLMAAVPvaDPSRQRPQR-VLLSDDLPSN 589
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-248 |
3.19e-63 |
|
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: 200.80 E-value: 3.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 12 HVSFPARKNWLGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRR-------DGKQHNG- 83
Cdd:TIGR02769 7 DVTHTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqdlyqlDRKQRRAf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 84 ---MQMVFQDPLSSLDPRLPVWRIITEPV--WIQKRSSERERRILAedLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARA 158
Cdd:TIGR02769 87 rrdVQLVFQDSPSAVNPRMTVRQIIGEPLrhLTSLDESEQKARIAE--LLDMVGLRSEDADKLPRQLSGGQLQRINIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 159 LSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHpAH 238
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KH 243
|
250
....*....|
gi 740855357 239 PYTRLLLDSV 248
Cdd:TIGR02769 244 PAGRNLQSAV 253
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
32-248 |
8.97e-62 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 197.22 E-value: 8.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRR-------DGKQHNG----MQMVFQDPLSSLDPRLP 100
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRgeplaklNRAQRKAfrrdIQMVFQDSISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 101 VWRIITEPVWIQKRSSERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQ 180
Cdd:PRK10419 108 VREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 181 AQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVelgETQQV--LTHPAHPYTRLLLDSV 248
Cdd:PRK10419 188 AGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV---ETQPVgdKLTFSSPAGRVLQNAV 254
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
28-289 |
1.55e-59 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 193.58 E-value: 1.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 28 RVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPS----------QGN-------YSRRD--GKQhngMQMVF 88
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwNGIdllklspRERRKiiGRE---IAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 89 QDPLSSLDPRLPVWRIITE-------PVWIQKRSSERERRILAedLAQQVGIR--PEYLDRLPHAFSGGQRQRIAIARAL 159
Cdd:COG4170 96 QEPSSCLDPSAKIGDQLIEaipswtfKGKWWQRFKWRKKRAIE--LLHRVGIKdhKDIMNSYPHELTEGECQKVMIAMAI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 160 SSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHP 239
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHP 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 740855357 240 YTRLLLDSVPKTGAPLAEDLVLrkTELPGN----RTLPEGCFFRDRCPLAIRGC 289
Cdd:COG4170 254 YTKALLRSMPDFRQPLPHKSRL--NTLPGSipplQHLPIGCRLGPRCPYAQKKC 305
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
31-306 |
6.14e-59 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 191.88 E-value: 6.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGM-----------LQPSQGNYSRRDGKQHNG-----MQMVFQDPLSS 94
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypgrvmaekLEFNGQDLQRISEKERRNlvgaeVAMIFQDPMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 95 LDPRLPVWRIITEPVWIQKRSSERERRILAEDLAQQVGI-RPEY-LDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPT 172
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpDPASrLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 173 SALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYTRLLLDSVPKtg 252
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALPE-- 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 253 apLAED---LVLRKTELPGNRTLPEGCFFRDRCPLAIRGCENKQILLSSESGCEVRC 306
Cdd:PRK11022 260 --FAQDkarLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLAGRQSKC 314
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-247 |
1.99e-57 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 186.15 E-value: 1.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 3 EFLLALQDVHVSFPARKNWLGKvtERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHN 82
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGWFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 83 G--------MQMVFQDPLSSLDPRLPVWRIITEPVWIQKR--SSERERRILAEdlAQQVGIRPEYLDRLPHAFSGGQRQR 152
Cdd:PRK15112 80 GdysyrsqrIRMIFQDPSTSLNPRQRISQILDFPLRLNTDlePEQREKQIIET--LRQVGLLPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 153 IAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQV 232
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
250
....*....|....*
gi 740855357 233 LTHPAHPYTRLLLDS 247
Cdd:PRK15112 238 LASPLHELTKRLIAG 252
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-272 |
5.04e-57 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 187.21 E-value: 5.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 8 LQDVHVSFPARKNwlgkvteRVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG-------NYSRRDGKQ 80
Cdd:COG1135 4 LENLSKTFPTKGG-------PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGsvlvdgvDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 81 HNGMQ----MVFQDP--LSSLDprlpVWRIITEPVWIQKRS-SERERRIlaEDLAQQVGIRpEYLDRLPHAFSGGQRQRI 153
Cdd:COG1135 77 LRAARrkigMIFQHFnlLSSRT----VAENVALPLEIAGVPkAEIRKRV--AELLELVGLS-DKADAYPSQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 154 AIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVL 233
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVF 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 740855357 234 THPAHPYTRLLLDSVpkTGAPLAEDLVLRKTELPGNRTL 272
Cdd:COG1135 230 ANPQSELTRRFLPTV--LNDELPEELLARLREAAGGGRL 266
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-236 |
1.69e-54 |
|
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: 177.39 E-value: 1.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 8 LQDVHVSFPARKNwlgkvteRVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG-------------NYS 74
Cdd:cd03258 4 LKNVSKVFGDTGG-------KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGsvlvdgtdltllsGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 75 RRDGKQHNGMqmVFQ--DPLSSLDprlpVWRIITEPVWIQKRS-SERERRIlaEDLAQQVGIRpEYLDRLPHAFSGGQRQ 151
Cdd:cd03258 77 LRKARRRIGM--IFQhfNLLSSRT----VFENVALPLEIAGVPkAEIEERV--LELLELVGLE-DKADAYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 152 RIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQ 231
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
....*
gi 740855357 232 VLTHP 236
Cdd:cd03258 228 VFANP 232
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-236 |
4.26e-54 |
|
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: 175.98 E-value: 4.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFParknwlgkvtERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG----------NYSR 75
Cdd:COG1122 1 IELENLSFSYP----------GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGevlvdgkditKKNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 76 RDGKQHNGMqmVFQDPLSSLdprlpvwriITEPVW-------IQKRSSERERRILAEDLAQQVGIRpEYLDRLPHAFSGG 148
Cdd:COG1122 71 RELRRKVGL--VFQNPDDQL---------FAPTVEedvafgpENLGLPREEIRERVEEALELVGLE-HLADRPPHELSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 149 QRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQaRRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGE 228
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
....*...
gi 740855357 229 TQQVLTHP 236
Cdd:COG1122 218 PREVFSDY 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-262 |
4.05e-52 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 180.82 E-value: 4.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 27 ERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYS------RRDGKQ----------------HNGM 84
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllRRRSRQvielseqsaaqmrhvrGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 85 QMVFQDPLSSLDPRLPVWRIITEPVWIQKRSSERERRILAEDLAQQVGIrPE---YLDRLPHAFSGGQRQRIAIARALSS 161
Cdd:PRK10261 107 AMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRI-PEaqtILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 162 EPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYT 241
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYT 265
|
250 260
....*....|....*....|.
gi 740855357 242 RLLLDSVPKTGAPLAEDLVLR 262
Cdd:PRK10261 266 RALLAAVPQLGAMKGLDYPRR 286
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-248 |
5.40e-52 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 171.65 E-value: 5.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 22 LGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN--YSRRDGKQHNGMQM------------- 86
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEvhYRMRDGQLRDLYALseaerrrllrtew 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 87 --VFQDPLSSLDPRLPVWRIITEPVWIQKRSSERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPD 164
Cdd:PRK11701 92 gfVHQHPRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 165 VIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYTRLL 244
Cdd:PRK11701 172 LVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLL 251
|
....
gi 740855357 245 LDSV 248
Cdd:PRK11701 252 VSSV 255
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-242 |
1.20e-51 |
|
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: 170.16 E-value: 1.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEFLLALQDVHVSFparknwlgkvtERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG-------NY 73
Cdd:COG1127 1 MSEPMIEVRNLTKSF-----------GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGeilvdgqDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 74 SRRDGKQHNGMQ----MVFQDP--LSSldprLPVWRIITEPVWIQKRSSERERRILAEDLAQQVGIrPEYLDRLPHAFSG 147
Cdd:COG1127 70 TGLSEKELYELRrrigMLFQGGalFDS----LTVFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMPSELSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 148 GQRQRIAIARALSSEPDVIVLDEPTSALD-ISVqAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVEL 226
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
250
....*....|....*.
gi 740855357 227 GETQQVLTHPaHPYTR 242
Cdd:COG1127 224 GTPEELLASD-DPWVR 238
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-225 |
1.41e-51 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 169.45 E-value: 1.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARKNwlgkvteRVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYS---------- 74
Cdd:COG1136 4 LLELRNLTKSYGTGEG-------EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdissls 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 75 -------RRdgkQHNGMqmVFQDPlsSLDPRLPVWRIITEPVWIQKRSSeRERRILAEDLAQQVGIrPEYLDRLPHAFSG 147
Cdd:COG1136 77 erelarlRR---RHIGF--VFQFF--NLLPELTALENVALPLLLAGVSR-KERRERARELLERVGL-GDRLDHRPSQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740855357 148 GQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMsDRVAVMYLGQIVE 225
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARA-DRVIRLRDGRIVS 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
5-218 |
2.58e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 169.89 E-value: 2.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARKNwlgkvteRVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQHNGM 84
Cdd:COG1116 7 ALELRGVSKRFPTGGG-------GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEV-LVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 85 Q----MVFQDPlsSLdprLPvWRIITEPVWI---QKRSSERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIAR 157
Cdd:COG1116 79 GpdrgVVFQEP--AL---LP-WLTVLDNVALgleLRGVPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740855357 158 ALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVS-VVRhMSDRVAVM 218
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVF-LADRVVVL 212
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-248 |
2.93e-51 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 169.02 E-value: 2.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFparknwlGKVtervHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG---------NYSR 75
Cdd:COG1126 1 MIEIENLHKSF-------GDL----EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtitvdgedlTDSK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 76 RD-GKQHNGMQMVFQDPlsSLDPRLPVWRIITE-PVWIQKRSSErERRILAEDLAQQVGIrPEYLDRLPHAFSGGQRQRI 153
Cdd:COG1126 70 KDiNKLRRKVGMVFQQF--NLFPHLTVLENVTLaPIKVKKMSKA-EAEERAMELLERVGL-ADKADAYPAQLSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 154 AIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVL 233
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFF 224
|
250
....*....|....*
gi 740855357 234 THPAHPYTRLLLDSV 248
Cdd:COG1126 225 ENPQHERTRAFLSKV 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-255 |
3.58e-51 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 176.82 E-value: 3.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEFLLALQDVHVSFpaRKnwlGKVTERVhaLNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRD--- 77
Cdd:PRK15134 1 MTQPLLAIENLSVAF--RQ---QQTVRTV--VNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDirf 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 78 --------------GKQHNGMQMVFQDPLSSLDPRLPVWRIITEpVWIQKRSSERE-RRILAEDLAQQVGIR--PEYLDR 140
Cdd:PRK15134 74 hgesllhaseqtlrGVRGNKIAMIFQEPMVSLNPLHTLEKQLYE-VLSLHRGMRREaARGEILNCLDRVGIRqaAKRLTD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 141 LPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYL 220
Cdd:PRK15134 153 YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQN 232
|
250 260 270
....*....|....*....|....*....|....*
gi 740855357 221 GQIVELGETQQVLTHPAHPYTRLLLDSVPkTGAPL 255
Cdd:PRK15134 233 GRCVEQNRAATLFSAPTHPYTQKLLNSEP-SGDPV 266
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-240 |
1.83e-50 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 170.66 E-value: 1.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEFLLALQDVHVSFparknwlGKVTervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnysrR---D 77
Cdd:COG3842 1 MAMPALELENVSKRY-------GDVT----ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSG----RillD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 78 GKQHNGMQ-------MVFQDPlsSLDPRLPVWRIITEPVWIQKRS-SERERRilAEDLAQQVGIrPEYLDRLPHAFSGGQ 149
Cdd:COG3842 66 GRDVTGLPpekrnvgMVFQDY--ALFPHLTVAENVAFGLRMRGVPkAEIRAR--VAELLELVGL-EGLADRYPHQLSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 150 RQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHN----VSvvrhMSDRVAVMYLGQIVE 225
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRIEQ 216
|
250
....*....|....*
gi 740855357 226 LGETQQVLTHPAHPY 240
Cdd:COG3842 217 VGTPEEIYERPATRF 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-218 |
1.02e-49 |
|
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: 164.57 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPARKnwlgkvtERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQHNG-- 83
Cdd:cd03293 1 LEVRNVSKTYGGGG-------GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV-LVDGEPVTGpg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 84 --MQMVFQDPlsSLdprLPvWRIITEPVWI---QKRSSERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARA 158
Cdd:cd03293 73 pdRGYVFQQD--AL---LP-WLTVLDNVALgleLQGVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 159 LSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVM 218
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
22-227 |
2.37e-49 |
|
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: 163.46 E-value: 2.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 22 LGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrDGKQHNGMQ-------MVFQDPlsS 94
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI-DGRDVTGVPperrnigMVFQDY--A 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 95 LDPRLPVWRIITEPVWIQKRSsERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSA 174
Cdd:cd03259 83 LFPHLTVAENIAFGLKLRGVP-KAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 740855357 175 LDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELG 227
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-273 |
4.52e-48 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 164.20 E-value: 4.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 8 LQDVHVSFPARKNWlgkvterVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN----------YSR-- 75
Cdd:PRK11153 4 LKNISKVFPQGGRT-------IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRvlvdgqdltaLSEke 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 76 -RDGKQHNGMqmVFQ--DPLSSldprlpvwRIITE----PVWIQKRS-SERERRIlaEDLAQQVGIRpEYLDRLPHAFSG 147
Cdd:PRK11153 77 lRKARRQIGM--IFQhfNLLSS--------RTVFDnvalPLELAGTPkAEIKARV--TELLELVGLS-DKADRYPAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 148 GQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELG 227
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQG 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 740855357 228 ETQQVLTHPAHPYTRLLLDSVpkTGAPLAEDLVLRKTELPGNRTLP 273
Cdd:PRK11153 224 TVSEVFSHPKHPLTREFIQST--LHLDLPEDYLARLQAEPTTGSGP 267
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-242 |
2.51e-47 |
|
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: 158.82 E-value: 2.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 8 LQDVHVSFPARknwlgkvtervHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYS---------RRDG 78
Cdd:cd03261 3 LRGLTKSFGGR-----------TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedisglSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 79 KQH--NGMQMVFQDP--LSSLDprlpVWRIITEPVWIQKRSSERERRILAEDLAQQVGIRPeYLDRLPHAFSGGQRQRIA 154
Cdd:cd03261 72 LYRlrRRMGMLFQSGalFDSLT----VFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRG-AEDLYPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 155 IARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLT 234
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
....*...
gi 740855357 235 HPaHPYTR 242
Cdd:cd03261 227 SD-DPLVR 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-223 |
3.46e-47 |
|
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: 158.04 E-value: 3.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPARKNwlgkvteRVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG------------NY 73
Cdd:cd03255 1 IELKNLSKTYGGGGE-------KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGevrvdgtdisklSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 74 SRRDGKQHNGMQMVFQDPlsSLDPRLPVWRIITEP-VWIQKRSSERERRilAEDLAQQVGIrPEYLDRLPHAFSGGQRQR 152
Cdd:cd03255 74 KELAAFRRRHIGFVFQSF--NLLPDLTALENVELPlLLAGVPKKERRER--AEELLERVGL-GDRLNHYPSELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740855357 153 IAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHmSDRVAVMYLGQI 223
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
28-233 |
7.83e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.53 E-value: 7.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 28 RVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYS---------RRDGKQHNGMqmVFQDPlsSLDPR 98
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvardPAEVRRRIGY--VPQEP--ALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 99 LPVWRIITepvwIQKR-----SSERERRIlaEDLAQQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTS 173
Cdd:COG1131 88 LTVRENLR----FFARlyglpRKEARERI--DELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 174 ALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVL 233
Cdd:COG1131 161 GLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-222 |
1.04e-46 |
|
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: 156.47 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 8 LQDVHVSFPARKNWlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN----------YSRRD 77
Cdd:cd03225 2 LKNLSFSYPDGARP---------ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvlvdgkdltkLSLKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 78 GKQHNGMqmVFQDPLSSLdprlpvwriITEPVW-------IQKRSSERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQR 150
Cdd:cd03225 73 LRRKVGL--VFQNPDDQF---------FGPTVEeevafglENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740855357 151 QRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQaRRNLTYVLISHNVSVVRHMSDRVAVMYLGQ 222
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
30-232 |
5.53e-46 |
|
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: 155.03 E-value: 5.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 30 HALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGML-----QPSQGNYsRRDGKQHNGMQ-----------MVFQDPls 93
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEV-LLDGKDIYDLDvdvlelrrrvgMVFQKP-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 94 slDP-RLPVWRIITEPVWIQKRSSERERRILAEDLAQQVGIRPEYLDRL-PHAFSGGQRQRIAIARALSSEPDVIVLDEP 171
Cdd:cd03260 91 --NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLhALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740855357 172 TSALDISVQAQILNLLVSLqaRRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQV 232
Cdd:cd03260 169 TSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
29-289 |
1.71e-45 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 156.89 E-value: 1.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 29 VHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGM---------------------LQPSQgnysRRDGKQHNgMQMV 87
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrvtadrmrfddidllrLSPRE----RRKLVGHN-VSMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 88 FQDPLSSLDPRLPVWRIITE--PVWIQK-----RSSERERRilAEDLAQQVGIRPEY--LDRLPHAFSGGQRQRIAIARA 158
Cdd:PRK15093 95 FQEPQSCLDPSERVGRQLMQniPGWTYKgrwwqRFGWRKRR--AIELLHRVGIKDHKdaMRSFPYELTEGECQKVMIAIA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 159 LSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAH 238
Cdd:PRK15093 173 LANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHH 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 740855357 239 PYTRLLLDSVPKTGAPLAEDlvLRKTELPGN----RTLPEGCFFRDRCPLAIRGC 289
Cdd:PRK15093 253 PYTQALIRAIPDFGSAMPHK--SRLNTLPGAipllEHLPIGCRLGPRCPYAQREC 305
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
30-236 |
8.46e-45 |
|
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: 153.76 E-value: 8.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 30 HALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG-------------NYSRRDGKQHNGMqmVFQDPLSSL- 95
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGtvtidgrditakkKKKLKDLRKKVGL--VFQFPEHQLf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 96 ------DprlpvwrIITEPVWIQKRSSERERRilAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLD 169
Cdd:TIGR04521 97 eetvykD-------IAFGPKNLGLSEEEAEER--VKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 170 EPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHP 236
Cdd:TIGR04521 168 EPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-237 |
5.58e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 150.62 E-value: 5.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEFLLALQDVHVSFparknwlgkvtERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG-------NY 73
Cdd:COG1121 2 MMMPAIELENLTVSY-----------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGtvrlfgkPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 74 SRRDGK-----QHNGMQMVFqdPLS-------SLDPRLPVWRIITepvwiqkrsseRERRILAEDLAQQVGIRpEYLDRL 141
Cdd:COG1121 71 RRARRRigyvpQRAEVDWDF--PITvrdvvlmGRYGRRGLFRRPS-----------RADREAVDEALERVGLE-DLADRP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 142 PHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMyLG 221
Cdd:COG1121 137 IGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLL-NR 214
|
250
....*....|....*.
gi 740855357 222 QIVELGETQQVLTHPA 237
Cdd:COG1121 215 GLVAHGPPEEVLTPEN 230
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-234 |
1.46e-43 |
|
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: 149.81 E-value: 1.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARknwlgkvtervHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG----------NYS 74
Cdd:COG1120 1 MLEAENLSVGYGGR-----------PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGevlldgrdlaSLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 75 RRD-GKQhngMQMVFQDPLSSLD------------PRLPVWRiitepvwiqkRSSERERRIlAEDLAQQVGIRpEYLDRL 141
Cdd:COG1120 70 RRElARR---IAYVPQEPPAPFGltvrelvalgryPHLGLFG----------RPSAEDREA-VEEALERTGLE-HLADRP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 142 PHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLG 221
Cdd:COG1120 135 VDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDG 214
|
250
....*....|...
gi 740855357 222 QIVELGETQQVLT 234
Cdd:COG1120 215 RIVAQGPPEEVLT 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-241 |
1.05e-42 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 150.30 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSeflLALQDVHVSFPARknwlgkvtervHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnysrR---D 77
Cdd:COG1118 1 MS---IEVRNISKRFGSF-----------TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSG----RivlN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 78 GK--------QHNGMQMVFQDPLssLDPRLPVW-------RIitepvwiqKRSSERERRILAEDLAQQVGIrPEYLDRLP 142
Cdd:COG1118 63 GRdlftnlppRERRVGFVFQHYA--LFPHMTVAeniafglRV--------RPPSKAEIRARVEELLELVQL-EGLADRYP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 143 HAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQ 222
Cdd:COG1118 132 SQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
250
....*....|....*....
gi 740855357 223 IVELGETQQVLTHPAHPYT 241
Cdd:COG1118 212 IEQVGTPDEVYDRPATPFV 230
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-222 |
1.19e-42 |
|
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: 144.83 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPARKNWlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKqhngmq 85
Cdd:cd03228 1 IEFKNVSFSYPGRPKP---------VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI-LIDGV------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 mvfqdPLSSLDPrlpvwriitepvwiqkrssererrilaEDLAQQVGirpeYLDRLPHAF---------SGGQRQRIAIA 156
Cdd:cd03228 65 -----DLRDLDL---------------------------ESLRKNIA----YVPQDPFLFsgtirenilSGGQRQRIAIA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740855357 157 RALSSEPDVIVLDEPTSALDISVQAQILNLLvsLQARRNLTYVLISHNVSVVRHMsDRVAVMYLGQ 222
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEAL--RALAKGKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
30-237 |
1.19e-42 |
|
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: 146.61 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 30 HALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHN------GMQMVFQDplSSLDPRLPVWR 103
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpphkrPVNTVFQN--YALFPHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 104 IITEPVWIQKRS-SERERRIlaEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQ 182
Cdd:cd03300 92 NIAFGLRLKKLPkAEIKERV--AEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 740855357 183 ILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPA 237
Cdd:cd03300 169 MQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-238 |
1.30e-42 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 149.84 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEflLALQDVHVSFparknwlGKVTervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGK- 79
Cdd:COG3839 1 MAS--LELENVSKSY-------GGVE----ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI-LIGGRd 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 80 ------QHNGMQMVFQDPlsSLDPRLPVWRIITEPVWIQKRS-SERERRIlaEDLAQQVGIRPeYLDRLPHAFSGGQRQR 152
Cdd:COG3839 67 vtdlppKDRNIAMVFQSY--ALYPHMTVYENIAFPLKLRKVPkAEIDRRV--REAAELLGLED-LLDRKPKQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 153 IAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLishnvsvVRH-------MSDRVAVMYLGQIVE 225
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIY-------VTHdqveamtLADRIAVMNDGRIQQ 214
|
250
....*....|...
gi 740855357 226 LGETQQVLTHPAH 238
Cdd:COG3839 215 VGTPEELYDRPAN 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
30-223 |
2.55e-42 |
|
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: 145.37 E-value: 2.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 30 HALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQHNG-----------MQMVFQDplSSLDPR 98
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI-IIDGLKLTDdkkninelrqkVGMVFQQ--FNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 99 LPVWRIITE-PVWIQKRSsERERRILAEDLAQQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDI 177
Cdd:cd03262 91 LTVLENITLaPIKVKGMS-KAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 740855357 178 SVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQI 223
Cdd:cd03262 169 ELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
29-222 |
4.86e-42 |
|
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: 143.48 E-value: 4.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 29 VHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN----------YSRRDGKQHNGMQMVFQDPlsSLDPR 98
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSilidgedltdLEDELPPLRRRIGMVFQDF--ALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 99 LPVWRIITEPVwiqkrssererrilaedlaqqvgirpeyldrlphafSGGQRQRIAIARALSSEPDVIVLDEPTSALDIS 178
Cdd:cd03229 91 LTVLENIALGL------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 740855357 179 VQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQ 222
Cdd:cd03229 135 TRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-251 |
1.18e-41 |
|
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: 145.09 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 17 ARKNWLGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG----------NYSRRDGKQ--HNGM 84
Cdd:cd03294 25 KSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGkvlidgqdiaAMSRKELRElrRKKI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 85 QMVFQDplSSLDPRLPVWRIITEPVWIQKRSS-ERERRilAEDLAQQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSEP 163
Cdd:cd03294 105 SMVFQS--FALLPHRTVLENVAFGLEVQGVPRaEREER--AAEALELVGLEG-WEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 164 DVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYTRL 243
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
....*...
gi 740855357 244 LLDSVPKT 251
Cdd:cd03294 260 FFRGVDRA 267
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-224 |
1.69e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 144.04 E-value: 1.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARKnwlgkvtervHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG-------NYSRRD 77
Cdd:COG3638 2 MLELRNLSKRYPGGT----------PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGeilvdgqDVTALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 78 GKQHNGMQ----MVFQDP-----LSSLD-------PRLPVWRIITEPVWiqkrsseRERRILAEDLAQQVGIrPEYLDRL 141
Cdd:COG3638 72 GRALRRLRrrigMIFQQFnlvprLSVLTnvlagrlGRTSTWRSLLGLFP-------PEDRERALEALERVGL-ADKAYQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 142 PHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLG 221
Cdd:COG3638 144 ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDG 223
|
...
gi 740855357 222 QIV 224
Cdd:COG3638 224 RVV 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
31-247 |
4.37e-41 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 142.82 E-value: 4.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGK---QHNGMQM------VFQDplSSLDPRLPV 101
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEI-FIDGEdirEQDPVELrrkigyVIQQ--IGLFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 102 WRIITEPVWIQKRSSERERRILAEdLAQQVGIRP-EYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQ 180
Cdd:cd03295 93 EENIALVPKLLKWPKEKIRERADE-LLALVGLDPaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITR 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 181 AQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYTRLLLDS 247
Cdd:cd03295 172 DQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
36-245 |
1.22e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 141.43 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 36 DLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQHNG-------MQMVFQDP-----LS-------SLD 96
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRI-LWNGQDLTAlppaerpVSMLFQENnlfphLTvaqniglGLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 97 PRLpvwriitepvwiqKRSSERERRIlaEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALD 176
Cdd:COG3840 98 PGL-------------KLTAEQRAQV--EQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 177 ISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYTRLLL 245
Cdd:COG3840 162 PALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-235 |
1.32e-40 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 148.75 E-value: 1.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPARKNwlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsrrdgkqhngmq 85
Cdd:COG4988 337 IELEDVSFSYPGGRP----------ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI------------ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 MVFQDPLSSLDPRLpvWR-----IITEPVWIQ-----------KRSSERErrilAEDLAQQVGIRpEYLDRLPH------ 143
Cdd:COG4988 395 LINGVDLSDLDPAS--WRrqiawVPQNPYLFAgtirenlrlgrPDASDEE----LEAALEAAGLD-EFVAALPDgldtpl 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 144 -----AFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLvsLQARRNLTYVLISHNVSVVRHMsDRVAVM 218
Cdd:COG4988 468 geggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL--RRLAKGRTVILITHRLALLAQA-DRILVL 544
|
250
....*....|....*..
gi 740855357 219 YLGQIVELGETQQVLTH 235
Cdd:COG4988 545 DDGRIVEQGTHEELLAK 561
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
32-223 |
1.79e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 140.34 E-value: 1.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnysrrdgkqhngmQMVFQD-PLSSLDPrlPVWR-----II 105
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSG-------------EIYLDGkPLSAMPP--PEWRrqvayVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 106 TEPVW--------------IQKRSSERERrilAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEP 171
Cdd:COG4619 81 QEPALwggtvrdnlpfpfqLRERKFDRER---ALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 740855357 172 TSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQI 223
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
28-223 |
2.12e-40 |
|
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: 139.07 E-value: 2.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 28 RVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG-------NYSRRDGKQHNGMQMVFQDPlsSLDPRLP 100
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGeikvlgkDIKKEPEEVKRRIGYLPEEP--SLYENLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 101 VWriitepvwiqkrssererrilaedlaqqvgirpEYLDrlphaFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQ 180
Cdd:cd03230 90 VR---------------------------------ENLK-----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESR 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 740855357 181 AQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQI 223
Cdd:cd03230 132 REFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
32-246 |
3.78e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 140.66 E-value: 3.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG---------NYSR---------RDGKQHNGMqmVFQDplS 93
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgditiDTARslsqqkgliRQLRQHVGF--VFQN--F 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 94 SLDP-RLPVWRIITEPVwIQKRSSERERRILAEDLAQQVGIRPEYlDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPT 172
Cdd:PRK11264 95 NLFPhRTVLENIIEGPV-IVKGEPKEEATARARELLAKVGLAGKE-TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740855357 173 SALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYTRLLLD 246
Cdd:PRK11264 173 SALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-237 |
5.93e-40 |
|
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: 139.88 E-value: 5.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFparknwlGKVtervHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG--NYSRRDGKQHN- 82
Cdd:cd03219 1 LEVRGLTKRF-------GGL----VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGsvLFDGEDITGLPp 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 83 ------GMQMVFQDPlsSLDPRLPVW-------RIITEPVWIQKRSSERERRIL--AEDLAQQVGIRpEYLDRLPHAFSG 147
Cdd:cd03219 70 heiarlGIGRTFQIP--RLFPELTVLenvmvaaQARTGSGLLLARARREEREARerAEELLERVGLA-DLADRPAGELSY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 148 GQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELG 227
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
250
....*....|
gi 740855357 228 ETQQVLTHPA 237
Cdd:cd03219 226 TPDEVRNNPR 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
24-227 |
1.45e-39 |
|
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: 138.16 E-value: 1.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 24 KVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGK-------QHNGMQMVFQDplSSLD 96
Cdd:cd03301 8 KRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI-YIGGRdvtdlppKDRDIAMVFQN--YALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 97 PRLPVWRIITEPVWIQKRS-SERERRIlaEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSAL 175
Cdd:cd03301 85 PHMTVYDNIAFGLKLRKVPkDEIDERV--REVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 740855357 176 DISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELG 227
Cdd:cd03301 162 DAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-243 |
1.52e-39 |
|
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: 147.29 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPARKNWlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN----------YSR 75
Cdd:COG2274 474 IELENVSFRYPGDSPP---------VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRilidgidlrqIDP 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 76 RDGKQHNGMqmVFQDP----------LSSLDPRLPVWRIItepvwiqkrssererrilaeDLAQQVGIRpEYLDRLPH-- 143
Cdd:COG2274 545 ASLRRQIGV--VLQDVflfsgtirenITLGDPDATDEEII--------------------EAARLAGLH-DFIEALPMgy 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 144 ---------AFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLvsLQARRNLTYVLISHNVSVVRHmSDR 214
Cdd:COG2274 602 dtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL--RRLLKGRTVIIIAHRLSTIRL-ADR 678
|
250 260
....*....|....*....|....*....
gi 740855357 215 VAVMYLGQIVELGETQQVLTHPAHpYTRL 243
Cdd:COG2274 679 IIVLDKGRIVEDGTHEELLARKGL-YAEL 706
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
32-173 |
1.53e-39 |
|
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: 135.85 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnYSRRDGKQHN---------GMQMVFQDPlsSLDPRLPVW 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEG-TILLDGQDLTdderkslrkEIGYVFQDP--QLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740855357 103 RIITEPVWIQKRSSERERRILAEDLAQ--QVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTS 173
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKlgLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
29-233 |
1.76e-39 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 138.84 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 29 VHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN------YSRRDGKQHNG-MQMVFQDPlsSLDPRLPV 101
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSilidgeDVRKEPREARRqIGVLPDER--GLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 102 WRIITEPVWIQKRSSErERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQA 181
Cdd:COG4555 92 RENIRYFAELYGLFDE-ELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 740855357 182 QILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVL 233
Cdd:COG4555 170 LLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-244 |
2.49e-39 |
|
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: 145.29 E-value: 2.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPARKNWlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKqhngmq 85
Cdd:COG4987 334 LELEDVSFRYPGAGRP---------VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI-TLGGV------ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 mvfqdPLSSLDPRLpVWRIITepvWIQKR-----SSERERRILA------EDLAQ---QVGIRPeYLDRLPH-------- 143
Cdd:COG4987 398 -----DLRDLDEDD-LRRRIA---VVPQRphlfdTTLRENLRLArpdatdEELWAaleRVGLGD-WLAALPDgldtwlge 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 144 ---AFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLvsLQARRNLTYVLISHNVSVVRHMsDRVAVMYL 220
Cdd:COG4987 468 ggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL--LEALAGRTVLLITHRLAGLERM-DRILVLED 544
|
250 260
....*....|....*....|....
gi 740855357 221 GQIVELGETQQVLTHPAHpYTRLL 244
Cdd:COG4987 545 GRIVEQGTHEELLAQNGR-YRQLY 567
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
30-242 |
3.56e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 138.25 E-value: 3.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 30 HALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGM--LQPSQ---GN--------YS---------RRDGkqhngmqMV 87
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEilldgediYDpdvdvvelrRRVG-------MV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 88 FQDPlsslDPrLP--VWRIITEPVWIQKRSSERERRILAEDLAQQVGIRPEYLDRL---PHAFSGGQRQRIAIARALSSE 162
Cdd:COG1117 98 FQKP----NP-FPksIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLkksALGLSGGQQQRLCIARALAVE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 163 PDVIVLDEPTSALD-ISVqAQILNLLVSLqaRRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYT 241
Cdd:COG1117 173 PEVLLMDEPTSALDpIST-AKIEELILEL--KKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRT 249
|
.
gi 740855357 242 R 242
Cdd:COG1117 250 E 250
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-237 |
8.81e-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: 8.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 2 SEFLLALQDVHVSFparknwlGKVTervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnysrR---DG 78
Cdd:COG0411 1 SDPLLEVRGLTKRF-------GGLV----AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSG----RilfDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 79 KQHNGM---QMV-------FQDP-----LSSLD-------PRLPVWRIITEPVWIQKRSSERERRILAEDLAQQVGIRpE 136
Cdd:COG0411 66 RDITGLpphRIArlgiartFQNPrlfpeLTVLEnvlvaahARLGRGLLAALLRLPRARREEREARERAEELLERVGLA-D 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 137 YLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVA 216
Cdd:COG0411 145 RADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIV 224
|
250 260
....*....|....*....|.
gi 740855357 217 VMYLGQIVELGETQQVLTHPA 237
Cdd:COG0411 225 VLDFGRVIAEGTPAEVRADPR 245
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-224 |
2.07e-38 |
|
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: 133.32 E-value: 2.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPArknwlgkvterVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnysrrdgkqhngmQ 85
Cdd:cd03216 1 LELRGITKRFGG-----------VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSG-------------E 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 MVFQD-PLSSLDPRLpvwriitepvwiqkrssererrilaedlAQQVGIRpeyldrLPHAFSGGQRQRIAIARALSSEPD 164
Cdd:cd03216 57 ILVDGkEVSFASPRD----------------------------ARRAGIA------MVYQLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 165 VIVLDEPTSALDISVQAQILNLLVSLQArRNLTYVLISHNVSVVRHMSDRVAVMYLGQIV 224
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRA-QGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
22-222 |
3.55e-38 |
|
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: 132.75 E-value: 3.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 22 LGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnysrrdgkqhngmqmvfqdplssldprlpv 101
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSG------------------------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 102 wRIITEPVWIQKRSSERERRilaedlaqQVGIRPEyldrlphaFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQA 181
Cdd:cd00267 55 -EILIDGKDIAKLPLEELRR--------RIGYVPQ--------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 740855357 182 QILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQ 222
Cdd:cd00267 118 RLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-227 |
5.13e-38 |
|
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: 132.94 E-value: 5.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 7 ALQDVHVSFPARKnwlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsrrdgkqhngmqM 86
Cdd:cd03214 1 EVENLSVGYGGRT-----------VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI------------L 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 87 VFQDPLSSLDPRlpvwriitepvwiqkrssERERRI-LAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDV 165
Cdd:cd03214 58 LDGKDLASLSPK------------------ELARKIaYVPQALELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740855357 166 IVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELG 227
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
31-240 |
1.04e-37 |
|
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: 134.00 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNY-------SRRDGKQHNgMQMVFQDplSSLDPRLPVWR 103
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedaTDVPVQERN-VGFVFQH--YALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 104 IITEPVWIQKRS---SERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQ 180
Cdd:cd03296 94 NVAFGLRVKPRSerpPEAEIRAKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 181 AQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPY 240
Cdd:cd03296 173 KELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
36-234 |
1.04e-37 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 133.94 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 36 DLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQHNGM-------QMVFQDplSSLDPRLPVWRIITEP 108
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL-TLNGQDHTTTppsrrpvSMLFQE--NNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 109 VWIQKRSSERERRILaEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLV 188
Cdd:PRK10771 96 LNPGLKLNAAQREKL-HAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 740855357 189 SLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLT 234
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
32-236 |
1.11e-36 |
|
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: 131.30 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGK-------QHNGMQMVFQDplSSLDPRLPVWRI 104
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI-LLNGKditnlppEKRDISYVPQN--YALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 105 ITEPVWIQKRS-SERERRILaeDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQI 183
Cdd:cd03299 92 IAYGLKKRKVDkKEIERKVL--EIAEMLGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 740855357 184 LNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHP 236
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-228 |
3.09e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.79 E-value: 3.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 8 LQDVHVSFParknwlgkvtERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG-------NYSRRDGKQ 80
Cdd:COG2884 4 FENVSKRYP----------GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGqvlvngqDLSRLKRRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 81 ------HNGMqmVFQDplSSLDPRLPVWRIITEPVWIQ-KRSSERERRIlaEDLAQQVGIRpEYLDRLPHAFSGGQRQRI 153
Cdd:COG2884 74 ipylrrRIGV--VFQD--FRLLPDRTVYENVALPLRVTgKSRKEIRRRV--REVLDLVGLS-DKAKALPHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740855357 154 AIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRnlTYVLI-SHNVSVVRHMSDRVAVMYLGQIVELGE 228
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRG--TTVLIaTHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
31-251 |
5.14e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 130.91 E-value: 5.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG--------------NYSRRDGKQHNGMqmVFQDPLSSLD 96
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtvtigervitagkkNKKLKPLRKKVGI--VFQFPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 97 PRLPVWRIITEPvwIQKRSSERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALD 176
Cdd:PRK13634 100 EETVEKDICFGP--MNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740855357 177 ISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHpYTRLLLDsVPKT 251
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE-LEAIGLD-LPET 250
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-235 |
7.12e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 135.68 E-value: 7.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPARKNwlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG----------NYSR 75
Cdd:COG1132 340 IEFENVSFSYPGDRP----------VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGrilidgvdirDLTL 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 76 RDGKQHNGMqmVFQDP------------LSSLDprlpvwriITEpvwiqkrssererrilaEDL---AQQVGIRpEYLDR 140
Cdd:COG1132 410 ESLRRQIGV--VPQDTflfsgtirenirYGRPD--------ATD-----------------EEVeeaAKAAQAH-EFIEA 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 141 LPH-----------AFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqaRRNLTYVLISHNVSVVR 209
Cdd:COG1132 462 LPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLSTIR 539
|
250 260
....*....|....*....|....*.
gi 740855357 210 HMsDRVAVMYLGQIVELGetqqvlTH 235
Cdd:COG1132 540 NA-DRILVLDDGRIVEQG------TH 558
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
28-218 |
6.71e-35 |
|
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: 125.72 E-value: 6.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 28 RVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHNGMQMVFQDP-LSSLDPRLP--VWRI 104
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPqRRSIDRDFPisVRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 105 I----TEPVWIQKRSSERERRILAEDLaQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQ 180
Cdd:cd03235 91 VlmglYGHKGLFRRLSKADKAKVDEAL-ERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 740855357 181 AQILNLLVSLQaRRNLTYVLISHNVSVVRHMSDRVAVM 218
Cdd:cd03235 169 EDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-237 |
7.43e-35 |
|
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: 129.45 E-value: 7.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 30 HALNGLDLQIR-----QGETlGIVGESGCGKSTLAQLLMGMLQPSQGN-------------------YSRRDGkqhngmq 85
Cdd:COG4148 9 LRRGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAIAGLERPDSGRirlggevlqdsargiflppHRRRIG------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 MVFQDPlsSLDPRLPVWRIITepvWIQKRSSERERRILAEDLAQQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSEPDV 165
Cdd:COG4148 81 YVFQEA--RLFPHLSVRGNLL---YGRKRAPRAERRISFDEVVELLGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740855357 166 IVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPA 237
Cdd:COG4148 155 LLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-225 |
1.14e-34 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 126.90 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEflLALQDVHVSFPARKnwlgkvtERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnYSRRDGKQ 80
Cdd:COG4525 1 MSM--LTVRHVSVRYPGGG-------QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSG-EITLDGVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 81 HNG----MQMVFQDplsslDPRLPvWRIITEPVWIQ---KRSSERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRI 153
Cdd:COG4525 71 VTGpgadRGVVFQK-----DALLP-WLNVLDNVAFGlrlRGVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740855357 154 AIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVM--YLGQIVE 225
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
31-227 |
1.69e-34 |
|
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: 125.17 E-value: 1.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG-------NYSRRDGKQHNGMQMVFQDPlsSLDPRLPVWr 103
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghDVVREPREVRRRIGIVFQDL--SVDDELTGW- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 104 iitEPVWIQKR-----SSERERRIlaEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDIS 178
Cdd:cd03265 92 ---ENLYIHARlygvpGAERRERI--DELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 740855357 179 VQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELG 227
Cdd:cd03265 166 TRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-232 |
2.16e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.91 E-value: 2.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 2 SEFLLALQDVHVSFPArknwlgkvterVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGK-- 79
Cdd:COG1129 1 AEPLLEMRGISKSFGG-----------VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEI-LLDGEpv 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 80 --------QHNGMQMVFQDPlsSLDPRLPVW------RIITEPVWIQKRSSERErrilAEDLAQQVG--IRPeylDRLPH 143
Cdd:COG1129 69 rfrsprdaQAAGIAIIHQEL--NLVPNLSVAeniflgREPRRGGLIDWRAMRRR----ARELLARLGldIDP---DTPVG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 144 AFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQArRNLTYVLISHNVSVVRHMSDRVAVMYLGQI 223
Cdd:COG1129 140 DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKA-QGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
....*....
gi 740855357 224 VELGETQQV 232
Cdd:COG1129 219 VGTGPVAEL 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
28-231 |
3.23e-34 |
|
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: 124.15 E-value: 3.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 28 RVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN---------YSRRDGKQHNGmqMVFQDplSSLDPR 98
Cdd:cd03263 14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTayingysirTDRKAARQSLG--YCPQF--DALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 99 LPVWriitEPVWIQ---KRSSERERRILAEDLAQQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSAL 175
Cdd:cd03263 90 LTVR----EHLRFYarlKGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 740855357 176 DISVQAQILNLLvsLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQ 231
Cdd:cd03263 165 DPASRRAIWDLI--LEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
31-236 |
3.74e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 124.74 E-value: 3.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN-------YSRRDGKQHNGMQ-------MVFQDplSSLD 96
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQlniaghqFDFSQKPSEKAIRllrqkvgMVFQQ--YNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 97 PRLPVWRIITE-PVWIQKRSSErERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSAL 175
Cdd:COG4161 95 PHLTVMENLIEaPCKVLGLSKE-QAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740855357 176 DISVQAQILNLLVSLQArRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGeTQQVLTHP 236
Cdd:COG4161 173 DPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQP 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-224 |
4.06e-34 |
|
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: 124.60 E-value: 4.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPARKnwlgkvtervHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG----------NYSR 75
Cdd:cd03256 1 IEVENLSKTYPNGK----------KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGsvlidgtdinKLKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 76 RDGKQHNG-MQMVFQDP------------LSSLDPRLPVWRIITEPVwiqkrsSERERRILAEDLaQQVGIRPEYLDRLp 142
Cdd:cd03256 71 KALRQLRRqIGMIFQQFnlierlsvlenvLSGRLGRRSTWRSLFGLF------PKEEKQRALAAL-ERVGLLDKAYQRA- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 143 HAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTyVLIS-HNVSVVRHMSDRVAVMYLG 221
Cdd:cd03256 143 DQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGIT-VIVSlHQVDLAREYADRIVGLKDG 221
|
...
gi 740855357 222 QIV 224
Cdd:cd03256 222 RIV 224
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
23-225 |
8.83e-34 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 123.23 E-value: 8.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 23 GKVTERVhaLNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNY-----------SRRDGKQHN-GMQMVFQd 90
Cdd:TIGR02211 14 GKLDTRV--LKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVlfngqslsklsSNERAKLRNkKLGFIYQ- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 91 pLSSLDPRLPVWRIITEPVWIQKRSSErERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDE 170
Cdd:TIGR02211 91 -FHHLLPDFTALENVAMPLLIGKKSVK-EAKERAYEMLEKVGLE-HRINHRPSELSGGERQRVAIARALVNQPSLVLADE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 740855357 171 PTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMsDRVAVMYLGQIVE 225
Cdd:TIGR02211 168 PTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-227 |
9.76e-34 |
|
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: 122.79 E-value: 9.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 30 HALNgLDLQIrQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnYSRRDGK-------------QHNGMQMVFQDplSSLD 96
Cdd:cd03297 13 FTLK-IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGG-TIVLNGTvlfdsrkkinlppQQRKIGLVFQQ--YALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 97 PRLPVWRIITepvWIQKRSSERERRILAEDLAQQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALD 176
Cdd:cd03297 88 PHLNVRENLA---FGLKRKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 740855357 177 ISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELG 227
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
8-234 |
1.12e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 124.33 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 8 LQDVHVSFPARKNWlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN-------YSRRDGKQ 80
Cdd:PRK13632 10 VENVSFSYPNSENN---------ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEikidgitISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 81 -HNGMQMVFQDPLS-------------SLD----PRLPVWRIItepvwiqkrssererrilaEDLAQQVGIRpEYLDRLP 142
Cdd:PRK13632 81 iRKKIGIIFQNPDNqfigatveddiafGLEnkkvPPKKMKDII-------------------DDLAKKVGME-DYLDKEP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 143 HAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRhMSDRVAVMYLGQ 222
Cdd:PRK13632 141 QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGK 219
|
250
....*....|..
gi 740855357 223 IVELGETQQVLT 234
Cdd:PRK13632 220 LIAQGKPKEILN 231
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
47-240 |
2.41e-33 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 124.91 E-value: 2.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 47 IVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQ------HN-GMQMVFQDplSSLDPRLPVWRIITEPVWIQKR-SSER 118
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSI-MLDGEDvtnvppHLrHINMVFQS--YALFPHMTVEENVAFGLKMRKVpRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 119 ERRILAEDLAQQVGirpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTY 198
Cdd:TIGR01187 78 KPRVLEALRLVQLE---EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 740855357 199 VLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPY 240
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
31-241 |
2.64e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 125.83 E-value: 2.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQHNGM-------QMVFQDplSSLDPRLPVWR 103
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI-MLDGQDITHVpaenrhvNTVFQS--YALFPHMTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 104 IITEPVWIQKRSSERERRILAEDLAQqvgIRPEYL-DRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQ 182
Cdd:PRK09452 106 NVAFGLRMQKTPAAEITPRVMEALRM---VQLEEFaQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQ 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 183 ILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYT 241
Cdd:PRK09452 183 MQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFV 241
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
27-233 |
3.00e-33 |
|
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: 121.95 E-value: 3.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 27 ERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN--YSRRDGKQ------HNGMQMVFQDP-LSSldp 97
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQilIDGIDIRDisrkslRSMIGVVLQDTfLFS--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 98 rlpvwRIITEPVWIQKRSSERERRILAedlAQQVGIRpEYLDRLP-----------HAFSGGQRQRIAIARALSSEPDVI 166
Cdd:cd03254 91 -----GTIMENIRLGRPNATDEEVIEA---AKEAGAH-DFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 167 VLDEPTSALDISVQAQILNLLVSLQARRnlTYVLISHNVSVVRHmSDRVAVMYLGQIVELGETQQVL 233
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-225 |
3.00e-33 |
|
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: 122.16 E-value: 3.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEFLLALQDVHVSFPARknwlgkvTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQ 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTG-------AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTV-RLAGQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 81 HNGMQ-------------MVFQDplSSLDPRLPVWRIITEPVWIQKRSSERERrilAEDLAQQVGIRpEYLDRLPHAFSG 147
Cdd:COG4181 76 LFALDedararlrarhvgFVFQS--FQLLPTLTALENVMLPLELAGRRDARAR---ARALLERVGLG-HRLDHYPAQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740855357 148 GQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHmSDRVAVMYLGQIVE 225
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
8-233 |
3.51e-33 |
|
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: 122.26 E-value: 3.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 8 LQDVHVSFPARKNwlgkvterVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG----------NYSRRD 77
Cdd:cd03249 3 FKNVSFRYPSRPD--------VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGeilldgvdirDLNLRW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 78 GKQHNGMqmVFQDPL----SsldprlpvwriITEPVWIQKRSSERErriLAEDLAQQVGIRpEYLDRLPHAF-------- 145
Cdd:cd03249 75 LRSQIGL--VSQEPVlfdgT-----------IAENIRYGKPDATDE---EVEEAAKKANIH-DFIMSLPDGYdtlvgerg 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 146 ---SGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVslQARRNLTYVLISHNVSVVRHmSDRVAVMYLGQ 222
Cdd:cd03249 138 sqlSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALD--RAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQ 214
|
250
....*....|.
gi 740855357 223 IVELGETQQVL 233
Cdd:cd03249 215 VVEQGTHDELM 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
4.01e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 123.42 E-value: 4.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEFLLALQDVHVSFParknwlgkvtERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG--------- 71
Cdd:PRK13636 1 MEDYILKVEELNYNYS----------DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGrilfdgkpi 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 72 NYSRRD-GKQHNGMQMVFQDPLSSLDPRLPVWRIITEPVWIQKRSSERERRIlaEDLAQQVGIRPeYLDRLPHAFSGGQR 150
Cdd:PRK13636 71 DYSRKGlMKLRESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRV--DNALKRTGIEH-LKDKPTHCLSFGQK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 151 QRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQ 230
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
|
...
gi 740855357 231 QVL 233
Cdd:PRK13636 228 EVF 230
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
34-247 |
6.03e-33 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 122.12 E-value: 6.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 34 GLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRR---DGKQHNGMQM-------VFQDPLSSLDPRLPVWR 103
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRvllDGKPVAPCALrgrkiatIMQNPRSAFNPLHTMHT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 104 IITEPvwIQKRSSERERRILAEDLAQqVGI--RPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQA 181
Cdd:PRK10418 101 HARET--CLALGKPADDATLTAALEA-VGLenAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740855357 182 QILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYTRLLLDS 247
Cdd:PRK10418 178 RILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
29-233 |
7.57e-33 |
|
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: 126.84 E-value: 7.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 29 VHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHNGMQ---------------MVFQDplS 93
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTkpgpdgrgrakryigILHQE--Y 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 94 SLDPRLPVWRIITEPVWIQKRSSERERRilAEDLAQQVGIRPEY----LDRLPHAFSGGQRQRIAIARALSSEPDVIVLD 169
Cdd:TIGR03269 375 DLYPHRTVLDNLTEAIGLELPDELARMK--AVITLKMVGFDEEKaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740855357 170 EPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVL 233
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
32-248 |
9.11e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.97 E-value: 9.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTL------------AQLLMGMLQPSQGNYSRRDGKQHNGMqmVFQD----P-LSS 94
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLlrcinkleeitsGDLIVDGLKVNDPKVDERLIRQEAGM--VFQQfylfPhLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 95 LDprlpvwRIITEPVWIqKRSSERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSA 174
Cdd:PRK09493 95 LE------NVMFGPLRV-RGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740855357 175 LDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYTRLLLDSV 248
Cdd:PRK09493 167 LDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
36-229 |
1.13e-32 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 120.35 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 36 DLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQHNG-------MQMVFQDplSSLDPRLPVWRIIT-- 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSI-KVNDQSHTGlapyqrpVSMLFQE--NNLFAHLTVRQNIGlg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 107 -EPVWiqKRSSERERRIlaEDLAQQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILN 185
Cdd:TIGR01277 95 lHPGL--KLNAEQQEKV--VDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 740855357 186 LLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGET 229
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
32-238 |
1.45e-32 |
|
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: 120.26 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQHN----GMQMVFQDplSSLDPRLPVWRIITE 107
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV-ILEGKQITepgpDRMVVFQN--YSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 108 PV-WIQKRSSERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNL 186
Cdd:TIGR01184 78 AVdRVLPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740855357 187 LVSLQARRNLTYVLISHNVSVVRHMSDRVAVM------YLGQIVELG-----ETQQVLTHPAH 238
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILEVPfprprDRLEVVEDPSY 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-227 |
2.60e-32 |
|
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: 118.18 E-value: 2.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPARKNWlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHNgmq 85
Cdd:cd03247 1 LSINNVSFSYPEQEQQ---------VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 mvFQDPLSSLDPRLPvwriitepvwiqkrsseRERRILAEDLAQQVGIRpeyldrlphaFSGGQRQRIAIARALSSEPDV 165
Cdd:cd03247 69 --LEKALSSLISVLN-----------------QRPYLFDTTLRNNLGRR----------FSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740855357 166 IVLDEPTSALDISVQAQILNLLvsLQARRNLTYVLISHNVSVVRHMsDRVAVMYLGQIVELG 227
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-223 |
2.72e-32 |
|
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: 117.70 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPARKNWLgkvtervhaLNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKqhngmq 85
Cdd:cd03246 1 LEVENVSFRYPGAEPPV---------LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-RLDGA------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 mvfqdPLSSLDPrlpvwriitepvwiqkrssererrilaEDLAQQVGIRPEYLDRLP-----HAFSGGQRQRIAIARALS 160
Cdd:cd03246 65 -----DISQWDP---------------------------NELGDHVGYLPQDDELFSgsiaeNILSGGQRQRLGLARALY 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740855357 161 SEPDVIVLDEPTSALDISVQAQILNLLVSLQArRNLTYVLISHNVSVVRhMSDRVAVMYLGQI 223
Cdd:cd03246 113 GNPRILVLDEPNSHLDVEGERALNQAIAALKA-AGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
31-225 |
5.07e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 120.27 E-value: 5.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHNGMQ------------MVFQDPLSSLDPR 98
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirpvrkrigMVFQFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 99 LPVWRIITEPVWIQKRSSERERRilAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDIS 178
Cdd:PRK13646 102 TVEREIIFGPKNFKMNLDEVKNY--AHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 740855357 179 VQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVE 225
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-240 |
7.24e-32 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 121.37 E-value: 7.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 35 LDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHNGMQ------------MVFQDplSSLDPRLPVW 102
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKgiflppekrrigYVFQE--ARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 103 RIITEPVWiqkRSSERERRILAEDLAQQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQ 182
Cdd:TIGR02142 94 GNLRYGMK---RARPSERRISFERVIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 740855357 183 ILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPY 240
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
31-232 |
7.45e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 120.15 E-value: 7.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG------------NYSRRDGKQHNGMqmVFQDPLSSLDPR 98
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGkiiidgvditdkKVKLSDIRKKVGL--VFQYPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 99 LPVWRIITEPVWIQKRSSERERRILAEdlAQQVGIRPE-YLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDI 177
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRA--MNIVGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 740855357 178 SVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQV 232
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-233 |
1.07e-31 |
|
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: 118.10 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPARKNWlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN----------YSR 75
Cdd:cd03251 1 VEFKNVTFRYPGDGPP---------VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRilidghdvrdYTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 76 RDGKQHNGMqmVFQDPLSSLDPrlpvwriITEPVWIQKRSSERERrilAEDLAQQVGIRpEYLDRLPHAF---------- 145
Cdd:cd03251 72 ASLRRQIGL--VSQDVFLFNDT-------VAENIAYGRPGATREE---VEEAARAANAH-EFIMELPEGYdtvigergvk 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 146 -SGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRnlTYVLISHNVSVVRHmSDRVAVMYLGQIV 224
Cdd:cd03251 139 lSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGKIV 215
|
....*....
gi 740855357 225 ELGETQQVL 233
Cdd:cd03251 216 ERGTHEELL 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
29-235 |
1.23e-31 |
|
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: 118.17 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 29 VHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG----------NYSRRDGKQHNG-MQMVFQDplSSLDP 97
Cdd:TIGR02315 15 KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGsillegtditKLRGKKLRKLRRrIGMIFQH--YNLIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 98 RLPVW------RIITEPVW--IQKRSSERERRIlAEDLAQQVGIRPEYLDRLpHAFSGGQRQRIAIARALSSEPDVIVLD 169
Cdd:TIGR02315 93 RLTVLenvlhgRLGYKPTWrsLLGRFSEEDKER-ALSALERVGLADKAYQRA-DQLSGGQQQRVAIARALAQQPDLILAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740855357 170 EPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTH 235
Cdd:TIGR02315 171 EPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-227 |
1.33e-31 |
|
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: 117.21 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 22 LGKVTERVHALN-GLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrDGKQHNGMQ-------MVFQDplS 93
Cdd:cd03298 3 LDKIRFSYGEQPmHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLI-NGVDVTAAPpadrpvsMLFQE--N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 94 SLDPRLPVWRIITEPVWIQKRSSERERRILAEDLAQqVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTS 173
Cdd:cd03298 80 NLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALAR-VGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 740855357 174 ALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELG 227
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
22-248 |
1.46e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 121.10 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 22 LGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrDGKQ-------HNGMQMVFQDplSS 94
Cdd:PRK11607 25 LTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDlshvppyQRPINMMFQS--YA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 95 LDPRLPVWRIITEPVwIQKRSSERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSA 174
Cdd:PRK11607 102 LFPHMTVEQNIAFGL-KQDKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740855357 175 LDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYTRLLLDSV 248
Cdd:PRK11607 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
31-236 |
2.83e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 118.26 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG---------NYSRRD---GKQHNGMqmVFQDPlsslDPR 98
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGevlikgepiKYDKKSlleVRKTVGI--VFQNP----DDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 99 LPVWRIITE----PVWIQKRSSERERRIlaEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSA 174
Cdd:PRK13639 91 LFAPTVEEDvafgPLNLGLSKEEVEKRV--KEALKAVGME-GFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740855357 175 LDISVQAQILNLLVSLQaRRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHP 236
Cdd:PRK13639 168 LDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-267 |
4.27e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 117.81 E-value: 4.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEFLLALQDVHVSFPArknwlgkvTERvHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsrrdgkQ 80
Cdd:PRK13635 1 MKEEIIRVEHISFRYPD--------AAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI------T 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 81 HNGMQ--------------MVFQDPlsslDPRLpVWRIITEPV--WIQKRSSERE---RRIlaEDLAQQVGIRpEYLDRL 141
Cdd:PRK13635 66 VGGMVlseetvwdvrrqvgMVFQNP----DNQF-VGATVQDDVafGLENIGVPREemvERV--DQALRQVGME-DFLNRE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 142 PHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHmSDRVAVMYLG 221
Cdd:PRK13635 138 PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKG 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 740855357 222 QIVELGETQQVLTHpAHPYTRLLLDsvpktgAPLAEDL--VLRKTELP 267
Cdd:PRK13635 217 EILEEGTPEEIFKS-GHMLQEIGLD------VPFSVKLkeLLKRNGIL 257
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
31-235 |
5.42e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.16 E-value: 5.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG----------NYSRRDGKQHNGMqmVFQDPLSSLdprlp 100
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGeifynnqaitDDNFEKLRKHIGI--VFQNPDNQF----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 101 VWRIITEPVWI----QKRSSERERRILAEDLaQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALD 176
Cdd:PRK13648 97 VGSIVKYDVAFglenHAVPYDEMHRRVSEAL-KQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 177 ISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHmSDRVAVMYLGQIVELGETQQVLTH 235
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
31-242 |
6.00e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 116.27 E-value: 6.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYS----RRDGKQHNGMQ----------MVFQDplSSLD 96
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnHFDFSKTPSDKairelrrnvgMVFQQ--YNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 97 PRLPVWRIITE-PVWIQKRSSErERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSAL 175
Cdd:PRK11124 95 PHLTVQQNLIEaPCRVLGLSKD-QALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 176 DISVQAQILNLLVSLQArRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETqqvlTHPAHPYTR 242
Cdd:PRK11124 173 DPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA----SCFTQPQTE 234
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
26-232 |
1.61e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 116.34 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 26 TERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG-----NYSRRDGKQ----HNGMQMVFQDPLSSLd 96
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGkvyvdGLDTSDEENlwdiRNKAGMVFQNPDNQI- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 97 prlpVWRIITEPVWIQKRS---SERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTS 173
Cdd:PRK13633 99 ----VATIVEEDVAFGPENlgiPPEEIRERVDESLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 174 ALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHmSDRVAVMYLGQIVELGETQQV 232
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
32-203 |
4.20e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 112.96 E-value: 4.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHNGMQMVFQD-----PLSSLDPRLPVWRIIT 106
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRlaylgHADGLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 107 epvWIQKRSSERERRILAEDLAQQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNL 186
Cdd:COG4133 98 ---FWAALYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAEL 173
|
170
....*....|....*..
gi 740855357 187 LVSLQARRNLTyVLISH 203
Cdd:COG4133 174 IAAHLARGGAV-LLTTH 189
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
28-233 |
4.67e-30 |
|
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: 113.30 E-value: 4.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 28 RVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQ----------HNGMQMVFQDPlsSLDP 97
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSI-RFDGRDitglppheraRAGIGYVPEGR--RIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 98 RLPVWRIITEPVWIQKRSSERERR--------ILAEDLAQQVGirpeyldrlphAFSGGQRQRIAIARALSSEPDVIVLD 169
Cdd:cd03224 89 ELTVEENLLLGAYARRRAKRKARLervyelfpRLKERRKQLAG-----------TLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740855357 170 EPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVL 233
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
31-266 |
5.33e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 115.22 E-value: 5.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRD------GKQ------HNGMQMVFQDPLSSLDPR 98
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstSKQkeikpvRKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 99 LPVWRIITEP--VWIQKRSSERerrILAEDLaQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALD 176
Cdd:PRK13643 101 TVLKDVAFGPqnFGIPKEKAEK---IAAEKL-EMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 177 ISVQAQILNLLVSLQaRRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTH----PAH----PYTRLLLDSV 248
Cdd:PRK13643 177 PKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEvdflKAHelgvPKATHFADQL 255
|
250
....*....|....*...
gi 740855357 249 PKTGAPLAEDLVLRKTEL 266
Cdd:PRK13643 256 QKTGAVTFEKLPITRAEL 273
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
32-223 |
6.44e-30 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 114.00 E-value: 6.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG---------NYSRRDgkqhngMQMVFQDPlssldpRLPVW 102
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGellagtaplAEARED------TRLMFQDA------RLLPW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 103 RIITEPVWIQKRSSERERrilAEDLAQQVGIRPEYLDrLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQ 182
Cdd:PRK11247 96 KKVIDNVGLGLKGQWRDA---ALQALAAVGLADRANE-WPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 740855357 183 ILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQI 223
Cdd:PRK11247 172 MQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-241 |
8.41e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 113.72 E-value: 8.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEFLLALQDVHVSFPARKnwlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLL--MGMLQP---------- 68
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKK-----------ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtitgsivy 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 69 -SQGNYSRR----DGKQHNGMqmVFQDPlsslDPrLPVwRIITEPVWIQKRSSERERRIL---AEDLAQQVGIRPEYLDR 140
Cdd:PRK14239 70 nGHNIYSPRtdtvDLRKEIGM--VFQQP----NP-FPM-SIYENVVYGLRLKGIKDKQVLdeaVEKSLKGASIWDEVKDR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 141 LpH----AFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqaRRNLTYVLISHNVSVVRHMSDRVA 216
Cdd:PRK14239 142 L-HdsalGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTG 218
|
250 260
....*....|....*....|....*
gi 740855357 217 VMYLGQIVELGETQQVLTHPAHPYT 241
Cdd:PRK14239 219 FFLDGDLIEYNDTKQMFMNPKHKET 243
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
6-227 |
8.97e-30 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 118.65 E-value: 8.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPARKNWLgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG----------NYSR 75
Cdd:TIGR02204 338 IEFEQVNFAYPARPDQP--------ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGrilldgvdlrQLDP 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 76 RDGKQHngMQMVFQDP-LSSLDPRlpvwriitEPVWIQKRSSERERRILAEDLAQQvgirPEYLDRLPHAF--------- 145
Cdd:TIGR02204 410 AELRAR--MALVPQDPvLFAASVM--------ENIRYGRPDATDEEVEAAARAAHA----HEFISALPEGYdtylgergv 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 146 --SGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRnlTYVLISHNVSVVRHmSDRVAVMYLGQI 223
Cdd:TIGR02204 476 tlSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGR--TTLIIAHRLATVLK-ADRIVVMDQGRI 552
|
....
gi 740855357 224 VELG 227
Cdd:TIGR02204 553 VAQG 556
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
31-287 |
2.03e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 113.16 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRR-----DGKQHNGMQ----MVFQDPLSSLdprlpV 101
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgidtgDFSKLQGIRklvgIVFQNPETQF-----V 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 102 WRIITE------------PVWIQKRSSererRILAEdlaqqVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLD 169
Cdd:PRK13644 92 GRTVEEdlafgpenlclpPIEIRKRVD----RALAE-----IGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 170 EPTSALDISVQAQILNLLVSLQaRRNLTYVLISHNVSVVrHMSDRVAVMYLGQIVELGETQQVLTHPAHPYTRLLLDSVP 249
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPSLI 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 740855357 250 KtgapLAEDLVLRKTELPGNRTLPEGCFFRDRCPLAIR 287
Cdd:PRK13644 240 E----LAENLKMHGVVIPWENTSSPSSFAEEICRLFLK 273
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
31-233 |
2.14e-29 |
|
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: 112.19 E-value: 2.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrdgkqhNGMQMVFQDPLS-------SLDPRLPVWR 103
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV------DGHDLALADPAWlrrqvgvVLQENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 104 IITEPVWIQKRSSERERRILAEDLAQQvgirPEYLDRLPHAF-----------SGGQRQRIAIARALSSEPDVIVLDEPT 172
Cdd:cd03252 91 SIRDNIALADPGMSMERVIEAAKLAGA----HDFISELPEGYdtivgeqgaglSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740855357 173 SALDISVQAQILNLLVSLQARRnlTYVLISHNVSVVRHmSDRVAVMYLGQIVELGETQQVL 233
Cdd:cd03252 167 SALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-236 |
3.85e-29 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 111.82 E-value: 3.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPArknwlgkvterVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLlMGML-QPSQGNYS---------- 74
Cdd:COG4598 9 LEVRDLHKSFGD-----------LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRC-INLLeTPDSGEIRvggeeirlkp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 75 RRDGKQH--NGMQ---------MVFQDplSSLDPRLPVWRIITE-PVWIQKRSSE--RERrilAEDLAQQVGIrPEYLDR 140
Cdd:COG4598 77 DRDGELVpaDRRQlqrirtrlgMVFQS--FNLWSHMTVLENVIEaPVHVLGRPKAeaIER---AEALLAKVGL-ADKRDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 141 LPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYL 220
Cdd:COG4598 151 YPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDL-AEEGRTMLVVTHEMGFARDVSSHVVFLHQ 229
|
250
....*....|....*.
gi 740855357 221 GQIVELGETQQVLTHP 236
Cdd:COG4598 230 GRIEEQGPPAEVFGNP 245
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
37-262 |
3.89e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 115.13 E-value: 3.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 37 LQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG-------------NYSRRDGKQHNgMQMVFQDplSSLDPRLPVWR 103
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGqvlidgvdiakisDAELREVRRKK-IAMVFQS--FALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 104 IITEPVWIQKRSSErERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQI 183
Cdd:PRK10070 126 NTAFGMELAGINAE-ERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 184 LNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYTRLLLDSVPKTGAPLAEDLVLR 262
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARR 282
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-226 |
4.21e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 116.32 E-value: 4.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 8 LQDVHVSFPARKnwLgkvtervhaLNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRdgkqhNGMQMV 87
Cdd:COG0488 1 LENLSKSFGGRP--L---------LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-----KGLRIG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 88 F--QDPlsSLDPRLPV-----------WRIITE----------PVWIQKRSSERERRIL----------AEDLAQQVGIR 134
Cdd:COG0488 65 YlpQEP--PLDDDLTVldtvldgdaelRALEAEleeleaklaePDEDLERLAELQEEFEalggweaearAEEILSGLGFP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 135 PEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDI-SVQ--AQILnllvslqARRNLTYVLISHNvsvvRHM 211
Cdd:COG0488 143 EEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEwlEEFL-------KNYPGTVLVVSHD----RYF 211
|
250
....*....|....*
gi 740855357 212 SDRVAvmylGQIVEL 226
Cdd:COG0488 212 LDRVA----TRILEL 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
32-224 |
5.10e-29 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 110.42 E-value: 5.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHNGMQ-----MVFQDPLSSLdprlpvwriIT 106
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERrksigYVMQDVDYQL---------FT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 107 EPVWiqkrsseRERRILAEDLAQQVGIRPEYL---------DRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDI 177
Cdd:cd03226 87 DSVR-------EELLLGLKELDAGNEQAETVLkdldlyalkERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 740855357 178 SVQAQILNLLVSLQARRNlTYVLISHNVSVVRHMSDRVAVMYLGQIV 224
Cdd:cd03226 160 KNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
32-239 |
6.68e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 111.60 E-value: 6.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDG-----KQHNGMQMVF-QDPLSSLDPRLP----- 100
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvRDKDGQLKVAdKNQLRLLRTRLTmvfqh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 101 --VWRIIT-------EPVWIQ--KRSSERERRILAEDlaqQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLD 169
Cdd:PRK10619 101 fnLWSHMTvlenvmeAPIQVLglSKQEARERAVKYLA---KVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 170 EPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHP 239
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-224 |
1.65e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.35 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEFLLALQDVHVSFPArknwlgkvterVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQ 80
Cdd:COG3845 1 MMPPALELRGITKRFGG-----------VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEI-LIDGKP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 81 HN----------GMQMVFQDPlsSLDPRLPVWR-II--TEPVWIQKRSSERERRILAEdLAQQVG--IRPeylDRLPHAF 145
Cdd:COG3845 69 VRirsprdaialGIGMVHQHF--MLVPNLTVAEnIVlgLEPTKGGRLDRKAARARIRE-LSERYGldVDP---DAKVEDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 146 SGGQRQRIAIARALSSEPDVIVLDEPTSALdisVQAQILNLLVSLQ--ARRNLTYVLISHNVSVVRHMSDRVAVMYLGQI 223
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVL---TPQEADELFEILRrlAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
.
gi 740855357 224 V 224
Cdd:COG3845 220 V 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-241 |
2.03e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 110.14 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN--------YSRRDGKQHNGMQ------MVFQDPlsSLDP 97
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKikvdgkvlYFGKDIFQIDAIKlrkevgMVFQQP--NPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 98 RLPVWRIITEPVWIQKRSSERERRILAEDLAQQVGIRPEYLDRL---PHAFSGGQRQRIAIARALSSEPDVIVLDEPTSA 174
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 175 LDIsVQAQILNLLVSlQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYT 241
Cdd:PRK14246 184 IDI-VNSQAIEKLIT-ELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
32-233 |
3.77e-28 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 114.45 E-value: 3.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrdgkqhNGMQMVFQDPLS-------SLDPRLPVWRI 104
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLV------DGVDLAIADPAWlrrqmgvVLQENVLFSRS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 105 ITEPVWIQKRSSERERRILAEDLAQQVgirpEYLDRLPHAF-----------SGGQRQRIAIARALSSEPDVIVLDEPTS 173
Cdd:TIGR01846 547 IRDNIALCNPGAPFEHVIHAAKLAGAH----DFISELPQGYntevgekganlSGGQRQRIAIARALVGNPRILIFDEATS 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 174 ALDISVQAQILNLLVSLQARRnlTYVLISHNVSVVRHmSDRVAVMYLGQIVELGETQQVL 233
Cdd:TIGR01846 623 ALDYESEALIMRNMREICRGR--TVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELL 679
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-224 |
6.39e-28 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 107.68 E-value: 6.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPARKNwlgkvtervHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN----------YSR 75
Cdd:cd03245 3 IEFRNVSFSYPNQEI---------PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSvlldgtdirqLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 76 RDGKQHNG--MQmvfqdplsslDPRLpVWRIITEPVWIQKRSSERERRILAEDLAqqvGIRpEYLDRLPHAF-------- 145
Cdd:cd03245 74 ADLRRNIGyvPQ----------DVTL-FYGTLRDNITLGAPLADDERILRAAELA---GVT-DFVNKHPNGLdlqigerg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 146 ---SGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRnlTYVLISHNVSVVRhMSDRVAVMYLGQ 222
Cdd:cd03245 139 rglSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLD-LVDRIIVMDSGR 215
|
..
gi 740855357 223 IV 224
Cdd:cd03245 216 IV 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-234 |
9.06e-28 |
|
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: 108.25 E-value: 9.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARKnwlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNY-----SRRDG- 78
Cdd:COG1119 3 LLELRNVTVRRGGKT-----------ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgERRGGe 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 79 -----KQHNGMqmVFQDPLSSLDPRLPVWRII------TEPVWiqKRSSERERRiLAEDLAQQVGIRpEYLDRLPHAFSG 147
Cdd:COG1119 72 dvwelRKRIGL--VSPALQLRFPRDETVLDVVlsgffdSIGLY--REPTDEQRE-RARELLELLGLA-HLADRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 148 GQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELG 227
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
....*..
gi 740855357 228 ETQQVLT 234
Cdd:COG1119 226 PKEEVLT 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-241 |
1.13e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.01 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 30 HALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnySRRDGKQ-----------------HNGMQMVFQDPl 92
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEE--ARVEGEVrlfgrniyspdvdpievRREVGMVFQYP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 93 sSLDPRLPVWRIITEPVWIQKR-SSERERRILAEDLAQQVGIRPEYLDRL---PHAFSGGQRQRIAIARALSSEPDVIVL 168
Cdd:PRK14267 95 -NPFPHLTIYDNVAIGVKLNGLvKSKKELDERVEWALKKAALWDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740855357 169 DEPTSALDISVQAQILNLLVSLqaRRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYT 241
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
32-237 |
1.21e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 110.19 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrDGKQ--HNGMQ-----MVFQDplSSLDPRLPVWRI 104
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI-DGEDvtHRSIQqrdicMVFQS--YALFPHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 105 ITEPVWIQKRSSERERRILAE-----DLAqqvGIRPEYLDRLphafSGGQRQRIAIARALSSEPDVIVLDEPTSALDISV 179
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEalelvDLA---GFEDRYVDQI----SGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 740855357 180 QAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPA 237
Cdd:PRK11432 172 RRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
32-234 |
1.37e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.94 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSrrdgkqhngmqmVFQDPLSSLDP-----RLPVWR--- 103
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR------------LNGRPLADWSPaelarRRAVLPqhs 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 104 ------IITEPVW---IQKRSSERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARAL------SSEPDVIVL 168
Cdd:PRK13548 86 slsfpfTVEEVVAmgrAPHGLSRAEDDALVAAALAQVDLA-HLAGRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740855357 169 DEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLT 234
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-237 |
1.47e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 109.93 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVhvsfpaRKNWLGKVtervHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrDGKQHNGMQ 85
Cdd:PRK11650 4 LKLQAV------RKSYDGKT----QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWI-GGRVVNELE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 -------MVFQDplSSLDPRLPVWRIITEPVWIQKRS-SERERRIlaEDLAQQVGIRPeYLDRLPHAFSGGQRQRIAIAR 157
Cdd:PRK11650 73 padrdiaMVFQN--YALYPHMSVRENMAYGLKIRGMPkAEIEERV--AEAARILELEP-LLDRKPRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 158 ALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNvsVVRHMS--DRVAVMYLGQIVELGETQQVLTH 235
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHD--QVEAMTlaDRVVVMNGGVAEQIGTPVEVYEK 225
|
..
gi 740855357 236 PA 237
Cdd:PRK11650 226 PA 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
31-236 |
1.66e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 108.35 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSR--RDGKQHNGMQM---------VFQDPLSSLdprl 99
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKitVDGITLTAKTVwdirekvgiVFQNPDNQF---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 100 pVWRIITEPV--WIQKRSSERERRI-LAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALD 176
Cdd:PRK13640 98 -VGATVGDDVafGLENRAVPRPEMIkIVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 177 ISVQAQILNLLVSLQARRNLTYVLISHNVSVVrHMSDRVAVMYLGQIVELGETQQVLTHP 236
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
32-233 |
1.69e-27 |
|
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: 112.15 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG----------NYSRRDGKQHNGM--QMV------------ 87
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGsvrldgadlsQWDREELGRHIGYlpQDVelfdgtiaenia 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 88 -FQDPlsslDPrlpvwriitepvwiqkrsserERRILAedlAQQVGIRpEYLDRLP-----------HAFSGGQRQRIAI 155
Cdd:COG4618 428 rFGDA----DP---------------------EKVVAA---AKLAGVH-EMILRLPdgydtrigeggARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740855357 156 ARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQArRNLTYVLISHNVSVVRHMsDRVAVMYLGQIVELGETQQVL 233
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPSLLAAV-DKLLVLRDGRVQAFGPRDEVL 554
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-227 |
1.89e-27 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 106.12 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPARknwlgkvtervHALNGLDLQIRQGeTLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQHNGMQ 85
Cdd:cd03264 1 LQLENLTKRYGKK-----------RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTI-RIDGQDVLKQP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 MVFQDPLSSL------DPRLPVWRIITEPVWIQKRSSERERRILAEDLaQQVGIRpEYLDRLPHAFSGGQRQRIAIARAL 159
Cdd:cd03264 68 QKLRRRIGYLpqefgvYPNFTVREFLDYIAWLKGIPSKEVKARVDEVL-ELVNLG-DRAKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740855357 160 SSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRnlTYVLISHNVSVVRHMSDRVAVMYLGQIVELG 227
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
23-227 |
1.94e-27 |
|
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: 106.30 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 23 GKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN---------YSRRDGKQHNGmqmVFQDPlS 93
Cdd:cd03266 12 RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFatvdgfdvvKEPAEARRRLG---FVSDS-T 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 94 SLDPRLPVWRIIT--EPVWIQKRSsERERRIlaEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEP 171
Cdd:cd03266 88 GLYDRLTARENLEyfAGLYGLKGD-ELTARL--EELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 740855357 172 TSALDISVQAQILNLLVSLQARRNlTYVLISHNVSVVRHMSDRVAVMYLGQIVELG 227
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
32-231 |
2.44e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 106.03 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQP---SQGNYsRRDGKQHNGMQ-------MVFQDPLssLDPRLPV 101
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEV-LLNGRRLTALPaeqrrigILFQDDL--LFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 102 WRIItePVWIQKRSSERERRILAEDLAQQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQA 181
Cdd:COG4136 94 GENL--AFALPPTIGRAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 740855357 182 QILNLLVSLQARRNLTYVLISHNVsvvrhmSDRVAVmylGQIVELGETQQ 231
Cdd:COG4136 171 QFREFVFEQIRQRGIPALLVTHDE------EDAPAA---GRVLDLGNWQH 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
24-223 |
3.28e-27 |
|
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: 105.57 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 24 KVTER----VHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQHNG------------MQMV 87
Cdd:cd03292 5 NVTKTypngTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTI-RVNGQDVSDlrgraipylrrkIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 88 FQDplSSLDPRLPVWriitEPVWIQKRSSERERRILAE---DLAQQVGIRPEYlDRLPHAFSGGQRQRIAIARALSSEPD 164
Cdd:cd03292 84 FQD--FRLLPDRNVY----ENVAFALEVTGVPPREIRKrvpAALELVGLSHKH-RALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 165 VIVLDEPTSALDISVQAQILNLLVSLQArRNLTYVLISHNVSVVRHMSDRVAVMYLGQI 223
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
31-233 |
3.48e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 107.86 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG--NYSRRDGKQhNGMQMVFQDPLSSLDPRLPVWRIITEP 108
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiEWIFKDEKN-KKKTKEKEKVLEKLVIQKTRFKKIKKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 109 VWIQKR-----------------------------SSERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARAL 159
Cdd:PRK13651 101 KEIRRRvgvvfqfaeyqlfeqtiekdiifgpvsmgVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740855357 160 SSEPDVIVLDEPTSALDISVQAQILNLLVSLQaRRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVL 233
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
31-223 |
4.11e-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: 104.44 E-value: 4.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrdgkqhNGMQMVFQDPLSSLDPRLpvwRIITEpvw 110
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITL------DGKPVTRRSPRDAIRAGI---AYVPE--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 111 iqkrssERERR--ILAEDLAQQVGirpeyldrLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLV 188
Cdd:cd03215 83 ------DRKREglVLDLSVAENIA--------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIR 148
|
170 180 190
....*....|....*....|....*....|....*
gi 740855357 189 SLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQI 223
Cdd:cd03215 149 EL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
32-234 |
4.14e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 106.35 E-value: 4.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN--YSRRDGKQHNGMQM-----VF-QDplSSLDPRLPVWR 103
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEvrLNGRPLAAWSPWELarrraVLpQH--SSLAFPFTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 104 IIT---EPVwiqkRSSERERRILAEDLAQQVGIRPeYLDRLPHAFSGGQRQRIAIARAL-------SSEPDVIVLDEPTS 173
Cdd:COG4559 95 VVAlgrAPH----GSSAAQDRQIVREALALVGLAH-LAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740855357 174 ALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLT 234
Cdd:COG4559 170 ALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLT 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-204 |
5.11e-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: 110.53 E-value: 5.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPARKNwlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDgkqhngmq 85
Cdd:TIGR02868 335 LELRDLSAGYPGAPP----------VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG-------- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 mvfqDPLSSLDPRLPVWRIitepVWIQKR-----SSERERRILA---------EDLAQQVGIRpEYLDRLPH-------- 143
Cdd:TIGR02868 397 ----VPVSSLDQDEVRRRV----SVCAQDahlfdTTVRENLRLArpdatdeelWAALERVGLA-DWLRALPDgldtvlge 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740855357 144 ---AFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLvsLQARRNLTYVLISHN 204
Cdd:TIGR02868 468 ggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
30-229 |
5.46e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 105.68 E-value: 5.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 30 HALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQ----------HNGM------QMVFqdpls 93
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSI-RLDGEDitklppheraRAGIayvpqgREIF----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 94 sldPRLPVWRIITEPVWIQKRsseRERRILAEDLAqqvgIRP---EYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDE 170
Cdd:TIGR03410 88 ---PRLTVEENLLTGLAALPR---RSRKIPDEIYE----LFPvlkEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 171 PTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGET 229
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAG 216
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
31-243 |
7.18e-27 |
|
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: 110.19 E-value: 7.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN----------YSRRDGKQHngMQMVFQDPLSSLDprlp 100
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQilldghdladYTLASLRRQ--VALVSQDVVLFND---- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 101 vwrIITEPVWIQKR---SSERERRILAEDLAQqvgirpEYLDRLPHAF-----------SGGQRQRIAIARALSSEPDVI 166
Cdd:TIGR02203 421 ---TIANNIAYGRTeqaDRAEIERALAAAYAQ------DFVDKLPLGLdtpigengvllSGGQRQRLAIARALLKDAPIL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 167 VLDEPTSALDISVQAQILNLLVSLQarRNLTYVLISHNVSVVRHmSDRVAVMYLGQIVELGETQQVLTHPAHpYTRL 243
Cdd:TIGR02203 492 ILDEATSALDNESERLVQAALERLM--QGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLARNGL-YAQL 564
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-241 |
1.14e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.38 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 29 VHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQ----PSQGNYSRRDGKQHNGM---------QMVFQDPlsSL 95
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeARVSGEVYLDGQDIFKMdvielrrrvQMVFQIP--NP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 96 DPRLPVWRIIT------EPVWIQKRSSERERRILAE-DLAQQVGIRpeyLDRLPHAFSGGQRQRIAIARALSSEPDVIVL 168
Cdd:PRK14247 94 IPNLSIFENVAlglklnRLVKSKKELQERVRWALEKaQLWDEVKDR---LDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740855357 169 DEPTSALDISVQAQILNLLVSLqaRRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYT 241
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-237 |
1.65e-26 |
|
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: 104.29 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFParknwlgkvteRVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnysrrdgkqhngm 84
Cdd:COG0410 3 MLEVENLHAGYG-----------GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSG------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 85 QMVFQD-PLSSLDP----RLPVW------RIITE---------PVWIQKRSSERERRI---------LAEDLAQQVGirp 135
Cdd:COG0410 59 SIRFDGeDITGLPPhriaRLGIGyvpegrRIFPSltveenlllGAYARRDRAEVRADLervyelfprLKERRRQRAG--- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 136 eYLdrlphafSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRV 215
Cdd:COG0410 136 -TL-------SGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRA 206
|
250 260
....*....|....*....|..
gi 740855357 216 AVMYLGQIVELGETQQVLTHPA 237
Cdd:COG0410 207 YVLERGRIVLEGTAAELLADPE 228
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
32-244 |
2.98e-26 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 108.88 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN-----YSRRDGKQH---NGMQMVFQ----------DPLS 93
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEilfdgIPREEIPREvlaNSVAMVDQdiflfegtvrDNLT 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 94 SLDPRLPvwriitepvwiqkrssERERRILAEDLA--QQVGIRP-EYLDRLPHA---FSGGQRQRIAIARALSSEPDVIV 167
Cdd:TIGR03796 575 LWDPTIP----------------DADLVRACKDAAihDVITSRPgGYDAELAEGganLSGGQRQRLEIARALVRNPSILI 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740855357 168 LDEPTSALDISVQAQIL-NLlvslqARRNLTYVLISHNVSVVRHmSDRVAVMYLGQIVELGETQQVLTHPAhPYTRLL 244
Cdd:TIGR03796 639 LDEATSALDPETEKIIDdNL-----RRRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELWAVGG-AYARLI 709
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
31-235 |
3.21e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 104.83 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG--------------NYSRRDGKQHNGmqMVFQDPLSSLD 96
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGsvrvddtlitstskNKDIKQIRKKVG--LVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 97 PRLPVWRIITEPvwiQKRS-SERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSAL 175
Cdd:PRK13649 100 EETVLKDVAFGP---QNFGvSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 176 DISVQAQILNLLVSLQaRRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTH 235
Cdd:PRK13649 177 DPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
32-233 |
3.32e-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: 103.46 E-value: 3.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDG-----------KQHNGMqmVFQD-PLSSLDPRL 99
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSI-LIDGqdirevtldslRRAIGV--VPQDtVLFNDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 100 PV----WRIITEPVWIQKRSSERERRILA--EDLAQQVGIRPEYLdrlphafSGGQRQRIAIARALSSEPDVIVLDEPTS 173
Cdd:cd03253 94 NIrygrPDATDEEVIEAAKAAQIHDKIMRfpDGYDTIVGERGLKL-------SGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 174 ALDISVQAQILNLLVSLQARRnlTYVLISHNVSVVRHmSDRVAVMYLGQIVELGETQQVL 233
Cdd:cd03253 167 ALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
32-235 |
5.33e-26 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 107.82 E-value: 5.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQhngmqmvfqdpLSSLDPRLPVWRIITEPVWI 111
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV-RLDGAD-----------LKQWDRETFGKHIGYLPQDV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 112 Q-------------KRSSERERRILAEDLAQQvgirPEYLDRLPHAF-----------SGGQRQRIAIARALSSEPDVIV 167
Cdd:TIGR01842 402 ElfpgtvaeniarfGENADPEKIIEAAKLAGV----HELILRLPDGYdtvigpggatlSGGQRQRIALARALYGDPKLVV 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740855357 168 LDEPTSALDISVQAQILNLLVSLQARRnLTYVLISHNVSVVrHMSDRVAVMYLGQIVELGETQQVLTH 235
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKALKARG-ITVVVITHRPSLL-GCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-242 |
6.37e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 103.58 E-value: 6.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLL--MGMLQP-----------SQGNYSRRDG--KQHNGMQMVFQDPlsSLD 96
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESevrvegrveffNQNIYERRVNlnRLRRQVSMVHPKP--NLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 97 PrLPVWRIITEPV----WIQKRSSER--ERRILAEDLAQQVG--IRPEYLDrlphaFSGGQRQRIAIARALSSEPDVIVL 168
Cdd:PRK14258 101 P-MSVYDNVAYGVkivgWRPKLEIDDivESALKDADLWDEIKhkIHKSALD-----LSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 169 DEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMY-----LGQIVELGETQQVLTHPAHPYTR 242
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNSPHDSRTR 253
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
29-250 |
1.05e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 103.34 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 29 VHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRdGKQ---------HNGMQMVFQDPLSSLDPRL 99
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR-GEPitkenirevRKFVGLVFQNPDDQIFSPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 100 PVWRIITEPVWIQKRSSERERRIlaEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISV 179
Cdd:PRK13652 96 VEQDIAFGPINLGLDEETVAHRV--SSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740855357 180 QAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHP-AHPYTRLLLDSVPK 250
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPdLLARVHLDLPSLPK 244
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
30-234 |
1.37e-25 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 106.87 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 30 HALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYS--------------RRDgkqhngMQMVFQDPlssl 95
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLldgvdirqidpadlRRN------IGYVPQDP---- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 96 dpRLpVWRIITEPVWIQKRSSERERRILAedlAQQVGIRpEYLDRLPHAF-----------SGGQRQRIAIARALSSEPD 164
Cdd:TIGR03375 549 --RL-FYGTLRDNIALGAPYADDEEILRA---AELAGVT-EFVRRHPDGLdmqigergrslSGGQRQAVALARALLRDPP 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 165 VIVLDEPTSALDISVQAQILNLLVSLQARRnlTYVLISHNVSVVRhMSDRVAVMYLGQIVELGETQQVLT 234
Cdd:TIGR03375 622 ILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQVLE 688
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-235 |
1.49e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 102.08 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEfLLALQDVHVSFPAR-------KNWLGKV----TERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPS 69
Cdd:COG1134 1 MSS-MIEVENVSKSYRLYhepsrslKELLLRRrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 70 QGNYsRRDGKqhngmqmvfqdpLSSL-------DPRLPVWriitEPVWI--------QKRSSERERRIlaEDLAqQVGir 134
Cdd:COG1134 80 SGRV-EVNGR------------VSALlelgagfHPELTGR----ENIYLngrllglsRKEIDEKFDEI--VEFA-ELG-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 135 pEYLDrLP-HAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNlTYVLISHNVSVVRHMSD 213
Cdd:COG1134 138 -DFID-QPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCD 214
|
250 260
....*....|....*....|..
gi 740855357 214 RVAVMYLGQIVELGETQQVLTH 235
Cdd:COG1134 215 RAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-218 |
1.80e-25 |
|
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: 100.62 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 21 WLGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrdgkqHNGMQMVFQDPlssldprlp 100
Cdd:cd03250 10 WDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-----PGSIAYVSQEP--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 101 vwriitepvWIQKRS------------SERERRI-----LAEDLAQ-------QVGIRPEYLdrlphafSGGQRQRIAIA 156
Cdd:cd03250 76 ---------WIQNGTirenilfgkpfdEERYEKVikacaLEPDLEIlpdgdltEIGEKGINL-------SGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740855357 157 RALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHmSDRVAVM 218
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVL 200
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
31-233 |
3.36e-25 |
|
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: 105.59 E-value: 3.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG----------NYSRRDGKQHngMQMVFQDPL----SSLD 96
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGeillngfslkDIDRHTLRQF--INYLPQEPYifsgSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 97 PRLpvwriitepvwIQ-KRSSERERRILAEDLAQqvgIRPEyLDRLPHAF-----------SGGQRQRIAIARALSSEPD 164
Cdd:TIGR01193 567 NLL-----------LGaKENVSQDEIWAACEIAE---IKDD-IENMPLGYqtelseegssiSGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 165 VIVLDEPTSALDISVQAQILNLLVSLQARrnlTYVLISHNVSVVRhMSDRVAVMYLGQIVELGETQQVL 233
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELL 696
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
31-209 |
5.06e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.23 E-value: 5.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKqhnGMQMVFQdpLSSLDPRLP--VWRIITEP 108
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA---RVAYVPQ--RSEVPDSLPltVRDLVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 109 VWIQK---RSSERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILN 185
Cdd:NF040873 82 RWARRglwRRLTRDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180
....*....|....*....|....
gi 740855357 186 LLVSLqARRNLTYVLISHNVSVVR 209
Cdd:NF040873 161 LLAEE-HARGATVVVVTHDLELVR 183
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
24-237 |
5.09e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 102.24 E-value: 5.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 24 KVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRD--GKQHNGMQ---------------- 85
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyIGDKKNNHelitnpyskkiknfke 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 ------MVFQDPLSSLDPRLPVWRIITEPVWI-QKRSSERERrilAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARA 158
Cdd:PRK13631 114 lrrrvsMVFQFPEYQLFKDTIEKDIMFGPVALgVKKSEAKKL---AKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 159 LSSEPDVIVLDEPTSALDISVQAQILNLLVSLQArRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPA 237
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKA-NNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
29-224 |
5.11e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.34 E-value: 5.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 29 VHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG----------NYSRRDGKQHnGMQMVFQDPLSS-LDP 97
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGsirldgeditGLSPRERRRL-GVAYIPEDRLGRgLVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 98 RLPVW------RIITEPVWiqKRSSERERRI--LAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLD 169
Cdd:COG3845 350 DMSVAenlilgRYRRPPFS--RGGFLDRKAIraFAEELIEEFDVRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 740855357 170 EPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIV 224
Cdd:COG3845 428 QPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
12-231 |
5.25e-25 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 105.04 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 12 HVSFPARKNwlGKVTervhaLNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrDGKqhngmqmvfqdP 91
Cdd:TIGR03797 456 RVTFRYRPD--GPLI-----LDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFY-DGQ-----------D 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 92 LSSLDPR---------LPVWRIITEPVWIQKRSSERERRILAEDLAQQVGIRpEYLDRLP---H--------AFSGGQRQ 151
Cdd:TIGR03797 517 LAGLDVQavrrqlgvvLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLA-EDIRAMPmgmHtvisegggTLSGGQRQ 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 152 RIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRnltyVLISHNVSVVRHmSDRVAVMYLGQIVELGETQQ 231
Cdd:TIGR03797 596 RLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR----IVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
31-227 |
6.02e-25 |
|
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: 99.88 E-value: 6.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN----------YSRRDGKQHngMQMVFQDPL-------S 93
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSilidgvdiskIGLHDLRSR--ISIIPQDPVlfsgtirS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 94 SLDPrlpvwriitepvwIQKRSSERERRILaedlaQQVGIRpEYLDRLPHA-----------FSGGQRQRIAIARALSSE 162
Cdd:cd03244 97 NLDP-------------FGEYSDEELWQAL-----ERVGLK-EFVESLPGGldtvveeggenLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740855357 163 PDVIVLDEPTSALDISVQAQILNLLVSlqARRNLTYVLISHNVSVVRHmSDRVAVMYLGQIVELG 227
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-227 |
8.97e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 99.76 E-value: 8.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSfparknwlgkVTERVhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGmlQPsqgNYSRRDGK------ 79
Cdd:COG0396 1 LEIKNLHVS----------VEGKE-ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG--HP---KYEVTSGSilldge 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 80 ----------QHNGMQMVFQDPlssldPRLP------VWRIITEPVwIQKRSSERERRILAEDLAQQVGIRPEYLDR-LP 142
Cdd:COG0396 65 dilelspderARAGIFLAFQYP-----VEIPgvsvsnFLRTALNAR-RGEELSAREFLKLLKEKMKELGLDEDFLDRyVN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 143 HAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDI-SVQ--AQILNLLVSlqarRNLTYVLISHNVSVVRHMS-DRVAVM 218
Cdd:COG0396 139 EGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdALRivAEGVNKLRS----PDRGILIITHYQRILDYIKpDFVHVL 214
|
....*....
gi 740855357 219 YLGQIVELG 227
Cdd:COG0396 215 VDGRIVKSG 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
30-224 |
9.46e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.56 E-value: 9.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 30 HALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNySRRDGKQH----------NGMQMV---------FQD 90
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGE-IRLDGKPVrirsprdairAGIAYVpedrkgeglVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 91 -------PLSSLDpRLPVWRIItepvwiqkrSSERERRIlAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEP 163
Cdd:COG1129 345 lsireniTLASLD-RLSRGGLL---------DRRRERAL-AEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740855357 164 DVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIV 224
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
29-237 |
1.03e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 102.42 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 29 VHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQHN-------GMQMVFQDplSSLDPRLPV 101
Cdd:PRK11000 16 VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGEKRMNdvppaerGVGMVFQS--YALYPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 102 WRIITEPVWIQK-RSSERERRI--LAEDLaqQVGirpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDIS 178
Cdd:PRK11000 93 AENMSFGLKLAGaKKEEINQRVnqVAEVL--QLA---HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 179 VQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPA 237
Cdd:PRK11000 168 LRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-224 |
2.03e-24 |
|
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: 98.94 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 26 TERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN--------YSRRDGKQHNgMQMVFQDPlSSLDP 97
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEvrvaglvpWKRRKKFLRR-IGVVFGQK-TQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 98 RLPV---WRIITEPVWIQKRSSERERRILAEDLaqQVGirpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSA 174
Cdd:cd03267 109 DLPVidsFYLLAAIYDLPPARFKKRLDELSELL--DLE---ELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 740855357 175 LDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIV 224
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
22-225 |
2.06e-24 |
|
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: 98.06 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 22 LGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNysrrdgkqhngmqmVFQDPLSSLDPRLPV 101
Cdd:cd03268 6 LTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGE--------------ITFDGKSYQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 102 WRI---ITEPVWIQKRSSERERRILA----------EDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVL 168
Cdd:cd03268 72 RRIgalIEAPGFYPNLTARENLRLLArllgirkkriDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 169 DEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVE 225
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
9-236 |
2.31e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 103.26 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 9 QDVHVSFPARKNwlgkvterVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrDGKQ-------- 80
Cdd:TIGR00958 482 QDVSFSYPNRPD--------VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-DGVPlvqydhhy 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 81 -HNGMQMVFQDPLssldprlpVW-RIITEPVWIQKRSSERERRILAedlAQQVGIRpEYLDRLPHAF-----------SG 147
Cdd:TIGR00958 553 lHRQVALVGQEPV--------LFsGSVRENIAYGLTDTPDEEIMAA---AKAANAH-DFIMEFPNGYdtevgekgsqlSG 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 148 GQRQRIAIARALSSEPDVIVLDEPTSALDisvqAQILNLLVSLQARRNLTYVLISHNVSVVRHmSDRVAVMYLGQIVELG 227
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
....*....
gi 740855357 228 ETQQVLTHP 236
Cdd:TIGR00958 696 THKQLMEDQ 704
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-227 |
2.58e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 102.73 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARKnwlgkvtervHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnYSRRDGKQHNGM 84
Cdd:PRK13657 334 AVEFDDVSFSYDNSR----------QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSG-RILIDGTDIRTV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 85 QM---------VFQDPLSsLDprlpvwRIITEPVWIQKRSSERERRILAEDLAQQVgirpEYLDRLPHAF---------- 145
Cdd:PRK13657 403 TRaslrrniavVFQDAGL-FN------RSIEDNIRVGRPDATDEEMRAAAERAQAH----DFIERKPDGYdtvvgergrq 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 146 -SGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqaRRNLTYVLISHNVSVVRHmSDRVAVMYLGQIV 224
Cdd:PRK13657 472 lSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTVRN-ADRILVFDNGRVV 548
|
...
gi 740855357 225 ELG 227
Cdd:PRK13657 549 ESG 551
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
32-236 |
3.55e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.52 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG-----------NYSRRDGKQ-HNGMQMVFQDPLSSLdprl 99
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGtitiagyhitpETGNKNLKKlRKKVSLVFQFPEAQL---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 100 pVWRIITEPVWIQKRS---SERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALD 176
Cdd:PRK13641 99 -FENTVLKDVEFGPKNfgfSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 177 ISVQAQILNLLVSLQaRRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHP 236
Cdd:PRK13641 178 PEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
32-263 |
6.51e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 98.65 E-value: 6.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNY----------SRRDGKQHNGMqmVFQDPLSSLdprlpV 101
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteeNVWDIRHKIGM--VFQNPDNQF-----V 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 102 WRIITEPVWI---QKRSSERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDIS 178
Cdd:PRK13650 96 GATVEDDVAFgleNKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 179 VQAQILNLLVSLQARRNLTYVLISHNVSVVRhMSDRVAVMYLGQIVELGETQQVLTHPAH--------PYTRLLLDSVPK 250
Cdd:PRK13650 175 GRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNDllqlgldiPFTTSLVQSLRQ 253
|
250
....*....|...
gi 740855357 251 TGAPLAEDLVLRK 263
Cdd:PRK13650 254 NGYDLPEGYLTEK 266
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-234 |
6.65e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 101.83 E-value: 6.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARKNwlgkvtervHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKqhngm 84
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQ---------PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI-LLNGQ----- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 85 qmvfqdPLSSLDPRlpVWR----IITEPVWIQKrSSERERRILAEDLA---------QQVGIR-----PEYLD------- 139
Cdd:PRK11160 403 ------PIADYSEA--ALRqaisVVSQRVHLFS-ATLRDNLLLAAPNAsdealievlQQVGLEklledDKGLNawlgegg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 140 RlphAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLvsLQARRNLTYVLISHNVSVVRHMsDRVAVMY 219
Cdd:PRK11160 474 R---QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELL--AEHAQNKTVLMITHRLTGLEQF-DRICVMD 547
|
250
....*....|....*
gi 740855357 220 LGQIVELGETQQVLT 234
Cdd:PRK11160 548 NGQIIEQGTHQELLA 562
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-232 |
8.77e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 101.01 E-value: 8.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 22 LGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN-------YSRRDGK--QHNGMQMVFQ--- 89
Cdd:PRK09700 11 IGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTitinninYNKLDHKlaAQLGIGIIYQels 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 90 --DPLSSLDpRLPVWRIITEPVWIQKRSSERERRILAEDLAQQVGIRPEyLDRLPHAFSGGQRQRIAIARALSSEPDVIV 167
Cdd:PRK09700 91 viDELTVLE-NLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 168 LDEPTSALdisVQAQILNLLVSLQARRN--LTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQV 232
Cdd:PRK09700 169 MDEPTSSL---TNKEVDYLFLIMNQLRKegTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-205 |
1.45e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 96.39 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG-------NYSRRDGKQHNGMQ-----MVFQDPLssLDPRL 99
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGevslvgqPLHQMDEEARAKLRakhvgFVFQSFM--LIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 100 PVWRIITEPVWIqKRSSERERRILAEDLAQQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISV 179
Cdd:PRK10584 104 NALENVELPALL-RGESSRQSRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180
....*....|....*....|....*.
gi 740855357 180 QAQILNLLVSLQARRNLTYVLISHNV 205
Cdd:PRK10584 182 GDKIADLLFSLNREHGTTLILVTHDL 207
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
20-246 |
2.34e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 98.23 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 20 NWLGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnYSRRDGKQHNGMQ-------MVFQdpl 92
Cdd:PRK10851 6 ANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSG-HIRFHGTDVSRLHardrkvgFVFQ--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 93 ssldpRLPVWRIIT--EPVWIQKRSSERERRILAEDLAQQVG-----IRPEYL-DRLPHAFSGGQRQRIAIARALSSEPD 164
Cdd:PRK10851 82 -----HYALFRHMTvfDNIAFGLTVLPRRERPNAAAIKAKVTqllemVQLAHLaDRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 165 VIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAhpyTRLL 244
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPA---TRFV 233
|
..
gi 740855357 245 LD 246
Cdd:PRK10851 234 LE 235
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
31-218 |
3.36e-23 |
|
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: 99.28 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNySRRDGKqhngmqmvfqdPLSSLDPRlpVWR------- 103
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS-IAVNGV-----------PLADADAD--SWRdqiawvp 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 104 --------IITEPVWIQKR---SSERERRILAEDLAQQVGIRPEYLDRL----PHAFSGGQRQRIAIARALSSEPDVIVL 168
Cdd:TIGR02857 403 qhpflfagTIAENIRLARPdasDAEIREALERAGLDEFVAALPQGLDTPigegGAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 740855357 169 DEPTSALDISVQAQILNLLvsLQARRNLTYVLISHNVSVVRHMsDRVAVM 218
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEAL--RALAQGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
31-235 |
4.19e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 96.62 E-value: 4.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHNGMQ-------------MVFQDPLSSLDP 97
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKkikevkrlrkeigLVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 98 RLPVWRIITEPVWIQKRSSERERRIlaEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDI 177
Cdd:PRK13645 106 ETIEKDIAFGPVNLGENKQEAYKKV--PELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 740855357 178 SVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTH 235
Cdd:PRK13645 184 KGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
28-215 |
5.42e-23 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL 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 C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 94.77 E-value: 5.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 28 RVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnysrRDGKQHNG--MQMVFQDPLSSLD--------- 96
Cdd:TIGR02324 20 RLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSG----RILVRHEGawVDLAQASPREVLEvrrktigyv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 97 -------PRLPVWRIITEPvwIQKRSSERER-RILAEDLAQQVGIrPEYLDRLPHA-FSGGQRQRIAIARALSSEPDVIV 167
Cdd:TIGR02324 96 sqflrviPRVSALEVVAEP--LLERGVPREAaRARARELLARLNI-PERLWHLPPAtFSGGEQQRVNIARGFIADYPILL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 740855357 168 LDEPTSALDISVQAQILNLLVSLQARRnLTYVLISHNVSVVRHMSDRV 215
Cdd:TIGR02324 173 LDEPTASLDAANRQVVVELIAEAKARG-AALIGIFHDEEVRELVADRV 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
30-227 |
6.10e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.57 E-value: 6.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 30 HALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNY-------SRRDGKQHNGM-QMVFQDPlsslDPRL-- 99
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrevNAENEKWVRSKvGLVFQDP----DDQVfs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 100 -PVWRIIT-EPVWIQKRSSERERRilAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDI 177
Cdd:PRK13647 95 sTVWDDVAfGPVNMGLDKDEVERR--VEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 740855357 178 SVQAQILNLLVSLQaRRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELG 227
Cdd:PRK13647 172 RGQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-216 |
7.66e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.21 E-value: 7.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARKnwlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsrrdgKQHNGM 84
Cdd:COG0488 315 VLELEGLSKSYGDKT-----------LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-----KLGETV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 85 QMVF--QDpLSSLDPRLPVWRIItepvwiqKRSSERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSE 162
Cdd:COG0488 379 KIGYfdQH-QEELDPDKTVLDEL-------RDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 740855357 163 PDVIVLDEPTSALDISVQAQILNLLVSLQArrnlTYVLISHNvsvvRHMSDRVA 216
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEALEEALDDFPG----TVLLVSHD----RYFLDRVA 496
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
31-205 |
8.19e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.77 E-value: 8.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQHNG----MQMVFQDplsslDPRLPvWRIIT 106
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI-TLDGKPVEGpgaeRGVVFQN-----EGLLP-WRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 107 EPV--WIQKRSSER-ERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQI 183
Cdd:PRK11248 89 DNVafGLQLAGVEKmQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180
....*....|....*....|..
gi 740855357 184 LNLLVSLQARRNLTYVLISHNV 205
Cdd:PRK11248 168 QTLLLKLWQETGKQVLLITHDI 189
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-232 |
9.29e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.20 E-value: 9.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 28 RVHALNG-----LDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN-------YSRRDGKQ--HNGMQMVFQDPLS 93
Cdd:PRK15439 270 TVEDLTGegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRimlngkeINALSTAQrlARGLVYLPEDRQS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 94 S---LDPRLpVWRII-----TEPVWIQKRsseRERRILaEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDV 165
Cdd:PRK15439 350 SglyLDAPL-AWNVCalthnRRGFWIKPA---RENAVL-ERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 166 IVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQV 232
Cdd:PRK15439 425 LIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
32-227 |
9.76e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 93.87 E-value: 9.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQpSQGNYSRR---DGKQHNGMQmvFQDPLSSLD------PRLPVW 102
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE-GGGTTSGQilfNGQPRKPDQ--FQKCVAYVRqddillPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 103 RIITEPVWI--QKRSSERERRILAEDLA-QQVGIRPEYLDRLPhAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISV 179
Cdd:cd03234 100 ETLTYTAILrlPRKSSDAIRKKRVEDVLlRDLALTRIGGNLVK-GISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 740855357 180 QAQILNLLVSLqARRNLTYVLISHN-VSVVRHMSDRVAVMYLGQIVELG 227
Cdd:cd03234 179 ALNLVSTLSQL-ARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-224 |
3.76e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 93.23 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPArknwlGKVTERvHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQHNGMQ 85
Cdd:COG1101 2 LELKNLSKTFNP-----GTVNEK-RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSI-LIDGKDVTKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 ---------MVFQDPLSSLDPRLPV-----------------WRIitepvwiqkRSSERE--RRILA------ED-LAQQ 130
Cdd:COG1101 75 eykrakyigRVFQDPMMGTAPSMTIeenlalayrrgkrrglrRGL---------TKKRRElfRELLAtlglglENrLDTK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 131 VGirpeYLdrlphafSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRH 210
Cdd:COG1101 146 VG----LL-------SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALD 214
|
250
....*....|....
gi 740855357 211 MSDRVAVMYLGQIV 224
Cdd:COG1101 215 YGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
29-225 |
3.89e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.62 E-value: 3.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 29 VHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnYSRRDGKQ---------HNGMQMVFQDPLSSLdprl 99
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG-KVKIDGELltaenvwnlRRKIGMVFQNPDNQF---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 100 pVWRIITEPV--WIQKRSSERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDI 177
Cdd:PRK13642 95 -VGATVEDDVafGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 740855357 178 SVQAQILNLLVSLQARRNLTYVLISHNVSVVRHmSDRVAVMYLGQIVE 225
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIK 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
32-216 |
1.18e-21 |
|
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: 88.66 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGkqhngmqmvfqdplssldprlpvwriitepvwi 111
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 112 qkrssererrilaedlaqqvgIRPEYLDRLphafSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQ 191
Cdd:cd03221 63 ---------------------VKIGYFEQL----SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYP 117
|
170 180
....*....|....*....|....*
gi 740855357 192 ArrnlTYVLISHNvsvvRHMSDRVA 216
Cdd:cd03221 118 G----TVILVSHD----RYFLDQVA 134
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-224 |
1.89e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.79 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARKnwlgkvtERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNY-------SRRD 77
Cdd:PRK10535 4 LLELKDIRRSYPSGE-------EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYrvagqdvATLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 78 G-------KQHNGMqmVFQDplSSLDPRLPVWRIITEPVwIQKRSSERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQR 150
Cdd:PRK10535 77 AdalaqlrREHFGF--IFQR--YHLLSHLTAAQNVEVPA-VYAGLERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740855357 151 QRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNlTYVLISHNVSVVRHmSDRVAVMYLGQIV 224
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
47-241 |
2.12e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 91.70 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 47 IVGESGCGKSTLAQLLMGMLQPSQGN-------------YSRRDGKQ-HNGMQMVFQDP----LSSLDPRLPVWRIitep 108
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGYrysgdvllggrsiFNYRDVLEfRRRVGMLFQRPnpfpMSIMDNVLAGVRA---- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 109 vwiQKRSSERERRILAEDLAQQVGIRPEYLDRL---PHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILN 185
Cdd:PRK14271 128 ---HKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 740855357 186 LLVSLQARrnLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPAHPYT 241
Cdd:PRK14271 205 FIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
35-244 |
2.14e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 94.14 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 35 LDLQIRQGETLGIVGESGCGKSTLAQLLMGMLqPSQGNYsrrdgkQHNGMqmvfqdPLSSLDPrlPVWR-----IITEPV 109
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSL------KINGI------ELRELDP--ESWRkhlswVGQNPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 110 WIQkrSSERERRILA---------EDLAQQVGIRpEYLDRLPH-----------AFSGGQRQRIAIARALSSEPDVIVLD 169
Cdd:PRK11174 434 LPH--GTLRDNVLLGnpdasdeqlQQALENAWVS-EFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740855357 170 EPTSALDISVQAQILNLLvsLQARRNLTYVLISHNVSVVRHMsDRVAVMYLGQIVELGETQQvLTHPAHPYTRLL 244
Cdd:PRK11174 511 EPTASLDAHSEQLVMQAL--NAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAE-LSQAGGLFATLL 581
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-271 |
2.29e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.37 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFparknwlGKVTervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGkqhngmq 85
Cdd:PRK09536 4 IDVSDLSVEF-------GDTT----VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV-LVAG------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 mvfqDPLSSLDPRLPVWRIITEP-------------VWIQKRSSERER--------RILAEDLAQQVGIrPEYLDRLPHA 144
Cdd:PRK09536 65 ----DDVEALSARAASRRVASVPqdtslsfefdvrqVVEMGRTPHRSRfdtwtetdRAAVERAMERTGV-AQFADRPVTS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 145 FSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIV 224
Cdd:PRK09536 140 LSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVR 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 740855357 225 ELGETQQVLTHPAHPYT---RLLLDSVPKTGAPLAedlvlrkTELPGNRT 271
Cdd:PRK09536 219 AAGPPADVLTADTLRAAfdaRTAVGTDPATGAPTV-------TPLPDPDR 261
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
9-223 |
2.36e-21 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 90.22 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 9 QDVHVSFPARKNwlgkvterVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQ-------- 80
Cdd:cd03248 15 QNVTFAYPTRPD--------TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-LLDGKPisqyehky 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 81 -HNGMQMVFQDP-LSSldprlpvwRIITEPVWIQKRSSERERRILAEDLAQQVGIRPEyldrLPHAF-----------SG 147
Cdd:cd03248 86 lHSKVSLVGQEPvLFA--------RSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISE----LASGYdtevgekgsqlSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740855357 148 GQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRnlTYVLISHNVSVVRHmSDRVAVMYLGQI 223
Cdd:cd03248 154 GQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
28-227 |
2.49e-21 |
|
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: 89.65 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 28 RVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnYSRRDGKqhnGMQMVFQDPLSSL-DPR--LPVWRI 104
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSG-EVLFDGK---PLDIAARNRIGYLpEERglYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 105 ITEPVWIQ--KRSSERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDiSVQAQ 182
Cdd:cd03269 88 IDQLVYLAqlKGLKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD-PVNVE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 740855357 183 ILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELG 227
Cdd:cd03269 166 LLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-235 |
4.96e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 91.30 E-value: 4.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 29 VHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYS---------RRDGKQHNGMqmVF-QDplSSLDPR 98
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvpfkrRKEFARRIGV--VFgQR--SQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 99 LPVW---RIITEpvwIQKRSSERERRILAEdLAQQVGIRpEYLDR----LphafSGGQRQRIAIARALSSEPDVIVLDEP 171
Cdd:COG4586 111 LPAIdsfRLLKA---IYRIPDAEYKKRLDE-LVELLDLG-ELLDTpvrqL----SLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740855357 172 TSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTH 235
Cdd:COG4586 182 TIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-227 |
5.74e-21 |
|
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: 89.13 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 8 LQDVHVSFPARK---------NWLGKVTE--RVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRR 76
Cdd:cd03220 3 LENVSKSYPTYKggssslkklGILGRKGEvgEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 77 dGKQHN--GMQMVFQDPLSSLDPRLPVWRI--ITepvwiQKRSSERERRIlaEDLAqQVGirpEYLDRLPHAFSGGQRQR 152
Cdd:cd03220 83 -GRVSSllGLGGGFNPELTGRENIYLNGRLlgLS-----RKEIDEKIDEI--IEFS-ELG---DFIDLPVKTYSSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740855357 153 IAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNlTYVLISHNVSVVRHMSDRVAVMYLGQIVELG 227
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-210 |
6.36e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.95 E-value: 6.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPArknwlGKVTervhaLNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQhngmq 85
Cdd:COG4178 363 LALEDLTLRTPD-----GRPL-----LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGAR----- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 MVF--QDP---LSSLDprlpvwRIITEPVWIQKRSSERERRILaedlaQQVGIrPEYLDRL------PHAFSGGQRQRIA 154
Cdd:COG4178 428 VLFlpQRPylpLGTLR------EALLYPATAEAFSDAELREAL-----EAVGL-GHLAERLdeeadwDQVLSLGEQQRLA 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 740855357 155 IARALSSEPDVIVLDEPTSALDISVQAQILNLLvsLQARRNLTYVLISHNVSVVRH 210
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLL--REELPGTTVISVGHRSTLAAF 549
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
31-235 |
6.87e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.77 E-value: 6.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrDGkqHNgmqmvFQD-PLSSLDPRLPVwriITEPV 109
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-DG--HD-----LRDyTLASLRNQVAL---VSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 110 ------------WIQKRSSERERRILAEDLAQQVgirpEYLDRLPHAF-----------SGGQRQRIAIARALSSEPDVI 166
Cdd:PRK11176 427 hlfndtianniaYARTEQYSREQIEEAARMAYAM----DFINKMDNGLdtvigengvllSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 167 VLDEPTSALDISVQAQILNLLVSLQarRNLTYVLISHNVSVVRHmSDRVAVMYLGQIVELGETQQVLTH 235
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQ 568
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
224-289 |
9.61e-21 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 83.99 E-value: 9.61e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740855357 224 VELGETQQVLTHPAHPYTRLLLDSVPKTGAPLAEdLVLRKTELPGNRTLPEGCFFRDRCPLAIRGC 289
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRP-LYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-233 |
1.05e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.68 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG---------NYSRRD---GKQHngMQMVFQDPLSSLdprl 99
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGavlwqgkplDYSKRGllaLRQQ--VATVFQDPEQQI---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 100 pVWRIITEPVWIQKRS-----SERERRI-LAEDLAQQVGIRPEYLDRLPHafsgGQRQRIAIARALSSEPDVIVLDEPTS 173
Cdd:PRK13638 91 -FYTDIDSDIAFSLRNlgvpeAEITRRVdEALTLVDAQHFRHQPIQCLSH----GQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 174 ALDISVQAQILNLLVSLQARRNLTyVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVL 233
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
32-234 |
1.44e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.92 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrDGKqhngmqmvfqdPLSSLDPR--------LPVWR 103
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFL-GDK-----------PISMLSSRqlarrlalLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 104 IITEPVWIQK--------------RSSERERRILAEDLaQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLD 169
Cdd:PRK11231 86 LTPEGITVRElvaygrspwlslwgRLSAEDNARVNQAM-EQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740855357 170 EPTSALDISVQAQILNLLVSLQARRNlTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLT 234
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
28-218 |
2.32e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 87.49 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 28 RVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnysrrdgkqhngmQMVFQDPLSSLD----------- 96
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSG-------------SILVRHDGGWVDlaqaspreila 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 97 ----------------PRLPVWRIITEPVwIQKRSSERERRILAEDLAQQVGIrPEYLDRLPHA-FSGGQRQRIAIARAL 159
Cdd:COG4778 90 lrrrtigyvsqflrviPRVSALDVVAEPL-LERGVDREEARARARELLARLNL-PERLWDLPPAtFSGGEQQRVNIARGF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 160 SSEPDVIVLDEPTSALDISVQAQILNLLVSLQArRNLTYVLISHNVSVVRHMSDRVAVM 218
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKA-RGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
30-224 |
2.97e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.24 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 30 HALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG-------NYSRRDGKQ----HNGMQMVFQDPLSSLDPR 98
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGkiwfsghDITRLKNREvpflRRQIGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 99 lpVWRIITEPVWIQKRSSERERRILAEDLaQQVGIrpeyLDR---LPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSAL 175
Cdd:PRK10908 96 --VYDNVAIPLIIAGASGDDIRRRVSAAL-DKVGL----LDKaknFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 740855357 176 DISVQAQILNLLVSLQaRRNLTYVLISHNVSVVRHMSDRVAVMYLGQIV 224
Cdd:PRK10908 169 DDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-262 |
3.14e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.55 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIR-----QGETlGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDG---KQHNGMQM---------VFQDPlss 94
Cdd:PRK11144 10 LGDLCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKGICLppekrrigyVFQDA--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 95 ldpRL-PVWRIITEPVWIQKRSSererRILAEDLAQQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTS 173
Cdd:PRK11144 86 ---RLfPHYKVRGNLRYGMAKSM----VAQFDKIVALLGIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 174 ALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQV--------------------- 232
Cdd:PRK11144 158 SLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVwassamrpwlpkeeqssilkv 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 740855357 233 ---LTHPAHPYTRLLLDS----VPKTGAPLAEDLVLR 262
Cdd:PRK11144 238 tvlEHHPHYAMTALALGDqhlwVNKLDAPLGTALRIR 274
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
30-237 |
4.51e-20 |
|
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: 86.83 E-value: 4.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 30 HALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN-------------YSRRdgkqHNGMQMVFQDP----- 91
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKilldgqditklpmHKRA----RLGIGYLPQEAsifrk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 92 LSSLDPRLPVWRIITEPvwiqkrssERERRILAEDLAQQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEP 171
Cdd:cd03218 90 LTVEENILAVLEIRGLS--------KKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740855357 172 TSALD-ISVQaQILNLLVSLqARRNLTyVLIS-HNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPA 237
Cdd:cd03218 161 FAGVDpIAVQ-DIQKIIKIL-KDRGIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-215 |
1.06e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.02 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 23 GKVTERVhaLNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRdGKQHNGM-----------QMVFQDP 91
Cdd:PRK11629 18 GSVQTDV--LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN-GQPMSKLssaakaelrnqKLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 92 LSSLDPRLPVWRIITEPVWI-QKRSSERERRilAEDLAQQVGIRPEYLDRlPHAFSGGQRQRIAIARALSSEPDVIVLDE 170
Cdd:PRK11629 95 FHHLLPDFTALENVAMPLLIgKKKPAEINSR--ALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 740855357 171 PTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRV 215
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
32-236 |
1.55e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 85.47 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQHNGMQM----------------VFQdplssl 95
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI-FLDGEDITHLPMhkrarlgigylpqeasIFR------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 96 dpRLPVW---RIITEpvwIQKRSSErERRILAEDLAQQVGIrpEYL-DRLPHAFSGGQRQRIAIARALSSEPDVIVLDEP 171
Cdd:COG1137 92 --KLTVEdniLAVLE---LRKLSKK-EREERLEELLEEFGI--THLrKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740855357 172 TSALD-ISV---QAQILNLlvslqARRNLTyVLIS-HNV----SVVrhmsDRVAVMYLGQIVELGETQQVLTHP 236
Cdd:COG1137 164 FAGVDpIAVadiQKIIRHL-----KERGIG-VLITdHNVretlGIC----DRAYIISEGKVLAEGTPEEILNNP 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-222 |
2.08e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.45 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEFLLALQDVHVSFPArknwlgkvterVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGmLQPSqGNYS---RRD 77
Cdd:PRK13549 1 MMEYLLEMKNITKTFGG-----------VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPH-GTYEgeiIFE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 78 GK----------QHNGMQMVFQDplSSLDPRLPVWRII---TEPV------WiqKRSSERERRILAE-----DLAQQVGi 133
Cdd:PRK13549 68 GEelqasnirdtERAGIAIIHQE--LALVKELSVLENIflgNEITpggimdY--DAMYLRAQKLLAQlkldiNPATPVG- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 134 rpeyldrlphAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQArRNLTYVLISHNVSVVRHMSD 213
Cdd:PRK13549 143 ----------NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISD 211
|
....*....
gi 740855357 214 RVAVMYLGQ 222
Cdd:PRK13549 212 TICVIRDGR 220
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
37-233 |
2.61e-19 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 84.52 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 37 LQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNY---SRRDGKQHNGMQMVFQDPLSSLDPRLPVWRIITEPV---- 109
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVkvaGASPGKGWRHIGYVPQRHEFAWDFPISVAHTVMSGRtghi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 110 -WIqkRSSERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLV 188
Cdd:TIGR03771 81 gWL--RRPCVADFAAVRDALRRVGLT-ELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 740855357 189 SLQARRNlTYVLISHNVSVVRHMSDRVaVMYLGQIVELGETQQVL 233
Cdd:TIGR03771 158 ELAGAGT-AILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQ 200
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-227 |
3.01e-19 |
|
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: 87.95 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 12 HVSF---PARKnwlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG-----NYSRRDGKQ--- 80
Cdd:COG5265 362 NVSFgydPERP-----------ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGrilidGQDIRDVTQasl 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 81 HNGMQMVFQDPLSSLDPrlpvwriITEPVWIQKRSSERERRILAEDLAQqvgIRpEYLDRLPHAF-----------SGGQ 149
Cdd:COG5265 431 RAAIGIVPQDTVLFNDT-------IAYNIAYGRPDASEEEVEAAARAAQ---IH-DFIESLPDGYdtrvgerglklSGGE 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740855357 150 RQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRnlTYVLISHNVSVVRHmSDRVAVMYLGQIVELG 227
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-217 |
6.81e-19 |
|
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: 84.00 E-value: 6.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 39 IRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnysrrdgkqhngmqmvfqdplsslDPRLPVWRIITEPVWIQKRSSER 118
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG------------------------DIEIELDTVSYKPQYIKADYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 119 ERRILAEDLaQQVGIRPEY-------------LDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQaqiln 185
Cdd:cd03237 78 VRDLLSSIT-KDFYTHPYFkteiakplqieqiLDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR----- 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 740855357 186 LLVSLQARR-----NLTYVLISHNVSVVRHMSDRVAV 217
Cdd:cd03237 152 LMASKVIRRfaennEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-233 |
1.64e-18 |
|
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: 86.15 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHNGMQMVFQDplSSLDPRLPVWRIITEPVWi 111
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQN--DSLRENILFGKALNEKYY- 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 112 qkRSSERERRILAEDLAQQVGIRPEYLDRLPHaFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQ 191
Cdd:TIGR00957 731 --QQVLEACALLPDLEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPE 807
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 740855357 192 AR-RNLTYVLISHNVSVVRHMsDRVAVMYLGQIVELGETQQVL 233
Cdd:TIGR00957 808 GVlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 849
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
6-227 |
2.41e-18 |
|
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: 82.31 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSfparknwlgkvTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGmlQPS----QGNYSRR----- 76
Cdd:TIGR01978 1 LKIKDLHVS-----------VEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKgqdll 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 77 ----DGKQHNGMQMVFQDPLSSldPRLPVWRIITEPVWIQkRSSERERRI-------LAEDLAQQVGIRPEYLDR-LPHA 144
Cdd:TIGR01978 68 elepDERARAGLFLAFQYPEEI--PGVSNLEFLRSALNAR-RSARGEEPLdlldfekLLKEKLALLDMDEEFLNRsVNEG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 145 FSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMS-DRVAVMYLGQI 223
Cdd:TIGR01978 145 FSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRL-REPDRSFLIITHYQRLLNYIKpDYVHVLLDGRI 223
|
....
gi 740855357 224 VELG 227
Cdd:TIGR01978 224 VKSG 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-247 |
3.35e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 82.85 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 29 VHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnYSRRDGKqhngmqmvfqdPLSSLD------------ 96
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSG-EVLWDGE-----------PLDPEDrrrigylpeerg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 97 --PRLPVWRIItepVWI-----QKRSSERERrilAEDLAQQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLD 169
Cdd:COG4152 82 lyPKMKVGEQL---VYLarlkgLSKAEAKRR---ADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 170 EPTSALD-ISVQAqILNLLVSLqaRRNLTYVLIS-HNVSVVRHMSDRVAVMYLGQIVELGETQQVLThpAHPYTRLLLDS 247
Cdd:COG4152 155 EPFSGLDpVNVEL-LKDVIREL--AAKGTTVIFSsHQMELVEELCDRIVIINKGRKVLSGSVDEIRR--QFGRNTLRLEA 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-227 |
4.76e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 80.65 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSfparknwlgkVTERvHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGmlQPSqgnYSRRDGKqhngmq 85
Cdd:cd03217 1 LEIKDLHVS----------VGGK-EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPK---YEVTEGE------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 MVFQDP-LSSLDPrlpvwriitepvwiqkrsSERERRILAedLAQQV-----GIR-PEYLDRLPHAFSGGQRQRIAIARA 158
Cdd:cd03217 59 ILFKGEdITDLPP------------------EERARLGIF--LAFQYppeipGVKnADFLRYVNEGFSGGEKKRNEILQL 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 159 LSSEPDVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHM-SDRVAVMYLGQIVELG 227
Cdd:cd03217 119 LLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
35-203 |
5.27e-18 |
|
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: 79.51 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 35 LDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrdgKQHNGMQMVFQDPLssldprLPVWRiitepvwiqkr 114
Cdd:cd03223 20 LSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---PEGEDLLFLPQRPY------LPLGT----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 115 ssererrilaedLAQQVgIRPEYldrlpHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQArr 194
Cdd:cd03223 80 ------------LREQL-IYPWD-----DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGI-- 139
|
....*....
gi 740855357 195 nlTYVLISH 203
Cdd:cd03223 140 --TVISVGH 146
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-236 |
6.76e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.31 E-value: 6.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARKnwlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGkqhngM 84
Cdd:PRK09544 4 LVSLENVSVSFGQRR-----------VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK-----L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 85 QMVFQDPLSSLDPRLPvwriITEPVWIQKRSSERERRILAEDLAQQVGirpEYLDRLPHAFSGGQRQRIAIARALSSEPD 164
Cdd:PRK09544 68 RIGYVPQKLYLDTTLP----LTVNRFLRLRPGTKKEDILPALKRVQAG---HLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740855357 165 VIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYlGQIVELGETQQVLTHP 236
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVVSLHP 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-231 |
1.23e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.83 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 22 LGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQ---------GNYSRRDGK---------QHNG 83
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRlardirksrANTG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 84 ---MQMVFQDPLSSLDPRL-------PVWRIITEpvWIQKRSSERERRILAedlaqQVGIRPEYLDRLPhAFSGGQRQRI 153
Cdd:PRK09984 90 yifQQFNLVNRLSVLENVLigalgstPFWRTCFS--WFTREQKQRALQALT-----RVGMVHFAHQRVS-TLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740855357 154 AIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQ 231
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
12-233 |
1.35e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 83.23 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 12 HVSFPARKNwlgkvtERVhaLNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGK-----QH----N 82
Cdd:PRK10790 345 NVSFAYRDD------NLV--LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI-RLDGRplsslSHsvlrQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 83 GMQMVFQDPL---SSLDPRLPVWRIITEP-VWiqkRSSERER-----RILAEDLAQQVGirpEYLDRLphafSGGQRQRI 153
Cdd:PRK10790 416 GVAMVQQDPVvlaDTFLANVTLGRDISEEqVW---QALETVQlaelaRSLPDGLYTPLG---EQGNNL----SVGQKQLL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 154 AIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqaRRNLTYVLISHNVSVVRHmSDRVAVMYLGQIVELGETQQVL 233
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
31-234 |
1.66e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.70 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYS-----RRDGKQHNGMQMVFQDplSSLDPRLPVwriI 105
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqpTRQALQKNLVAYVPQS--EEVDWSFPV---L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 106 TEPV----------WIqKRSSERERRILAEDLAQqVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSAL 175
Cdd:PRK15056 97 VEDVvmmgryghmgWL-RRAKKRDRQIVTAALAR-VDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 176 DISVQAQILNLLVSLQArRNLTYVLISHNVSVVRHMSDrVAVMYLGQIVELGETQQVLT 234
Cdd:PRK15056 174 DVKTEARIISLLRELRD-EGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFT 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-224 |
1.83e-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: 82.57 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 29 VHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGML-------------QPSQGNYSRRdgKQHNGMQMVFQDplSSL 95
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgtwdgeiywsgSPLKASNIRD--TERAGIVIIHQE--LTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 96 DPRLPVWRII---TEPVWIQKRSSERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPT 172
Cdd:TIGR02633 90 VPELSVAENIflgNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 740855357 173 SALDISVQAQILNLLVSLQArRNLTYVLISHNVSVVRHMSDRVAVMYLGQIV 224
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-176 |
6.97e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.83 E-value: 6.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPARKnwlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnysrrdgkqhngm 84
Cdd:PRK10247 7 LLQLQNVGYLAGDAK-----------ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSG------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 85 QMVFQ-DPLSSLDP---RLPVWRIITEPV-------------WiQKRSSERERRILAEDLAqQVGIRPEYLDRLPHAFSG 147
Cdd:PRK10247 63 TLLFEgEDISTLKPeiyRQQVSYCAQTPTlfgdtvydnlifpW-QIRNQQPDPAIFLDDLE-RFALPDTILTKNIAELSG 140
|
170 180
....*....|....*....|....*....
gi 740855357 148 GQRQRIAIARALSSEPDVIVLDEPTSALD 176
Cdd:PRK10247 141 GEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-225 |
7.64e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 7.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPArknwlgkvterVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMlqpsqgnYSRRDGKQH-NG 83
Cdd:PRK10762 4 LLQLKGIDKAFPG-----------VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGI-------YTRDAGSILyLG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 84 MQMVFQDPLSS-------------LDPRLPvwriITEPVWIQKRSSERERRIL-------AEDLAQQVGIRPEYlDRLPH 143
Cdd:PRK10762 66 KEVTFNGPKSSqeagigiihqelnLIPQLT----IAENIFLGREFVNRFGRIDwkkmyaeADKLLARLNLRFSS-DKLVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 144 AFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQAR-RNLTYvlISHNVSVVRHMSDRVAVMYLGQ 222
Cdd:PRK10762 141 ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQgRGIVY--ISHRLKEIFEICDDVTVFRDGQ 218
|
....
gi 740855357 223 -IVE 225
Cdd:PRK10762 219 fIAE 222
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-234 |
9.54e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.96 E-value: 9.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSfparknwlgkvtervHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLqPSQGN----------YSR 75
Cdd:COG4138 1 LQLNDVAVA---------------GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEillngrplsdWSA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 76 RDGKQHNGMQMVFQDPLSSLdprlPVWRIITepVWIQKRSSERERRILAEDLAQQVGIRPeYLDRLPHAFSGGQRQRIAI 155
Cdd:COG4138 65 AELARHRAYLSQQQSPPFAM----PVFQYLA--LHQPAGASSEAVEQLLAQLAEALGLED-KLSRPLTQLSGGEWQRVRL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 156 ARAL-------SSEPDVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGE 228
Cdd:COG4138 138 AAVLlqvwptiNPEGQLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGE 216
|
....*.
gi 740855357 229 TQQVLT 234
Cdd:COG4138 217 TAEVMT 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-235 |
1.13e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 23 GKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsrrdgkQHNGMQMVFQDPLSSLD------ 96
Cdd:PRK11288 11 GKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI------LIDGQEMRFASTTAALAagvaii 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 97 -------PRLPVwriiTEPVWI----QKRSSERERRILAEDLAQqvgirpeyLDRL-----PHA----FSGGQRQRIAIA 156
Cdd:PRK11288 85 yqelhlvPEMTV----AENLYLgqlpHKGGIVNRRLLNYEAREQ--------LEHLgvdidPDTplkyLSIGQRQMVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 157 RALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQAR-RNLTYVliSHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTH 235
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEgRVILYV--SHRMEEIFALCDAITVFKDGRYVATFDDMAQVDR 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-233 |
1.57e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.91 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 2 SEFLLALQDVHVSFPARKnwlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQH 81
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRT-----------LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 82 NGMQMVFQDPLSSLDPRLPVWRIIT--EPVWIQK----------RSSERERrilAEDLAQQVGIRPeYLDRLPHAFSGGQ 149
Cdd:PRK10575 77 SWSSKAFARKVAYLPQQLPAAEGMTvrELVAIGRypwhgalgrfGAADREK---VEEAISLVGLKP-LAHRLVDSLSGGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 150 RQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGET 229
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
|
....
gi 740855357 230 QQVL 233
Cdd:PRK10575 233 AELM 236
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
31-227 |
1.91e-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: 76.30 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrDGKQHNGMqmvfqdPLSSLDPRLPVwrIITEPVw 110
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDISTI------PLEDLRSSLTI--IPQDPT- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 111 iqkrssererrILAEDLAQQVGIRPEYLDRLPHA----------FSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQ 180
Cdd:cd03369 93 -----------LFSGTIRSNLDPFDEYSDEEIYGalrvsegglnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 740855357 181 AQILNLLVSLQArrNLTYVLISHNVSVVRHMsDRVAVMYLGQIVELG 227
Cdd:cd03369 162 ALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
222-307 |
2.55e-16 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 72.78 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 222 QIVELGETQQVLTHPAHPYTRLLLDSVPKTGAPlAEDLVlrktELPGN----RTLPEGCFFRDRCPLAIRGCENKQ-ILL 296
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKR-DRKLI----SIPGEvpslINLPSGCRFYPRCPYAQDECRKEPpALV 75
|
90
....*....|.
gi 740855357 297 SSESGCEVRCW 307
Cdd:TIGR01727 76 EIAEGHRVACH 86
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
32-287 |
4.41e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.15 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRD----GKQHNGMQMVFQDP-LSSLDPRLPVwriiT 106
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQRVGVVPqFDNLDPDFTV----R 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 107 EPVWIQKR----SSERERRILAEDLaqQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQ 182
Cdd:PRK13537 99 ENLLVFGRyfglSAAAARALVPPLL--EFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 183 ILNLLVSLQARRNlTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTH-----------PAHPYTRLLLdsvpkt 251
Cdd:PRK13537 177 MWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESeigcdvieiygPDPVALRDEL------ 249
|
250 260 270
....*....|....*....|....*....|....*.
gi 740855357 252 gAPLAEdlvlrKTELPGNRTLpegCFFRDRCPLAIR 287
Cdd:PRK13537 250 -APLAE-----RTEISGETLF---CYVRDPEPLHAR 276
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
40-219 |
5.08e-16 |
|
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: 76.25 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 40 RQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNysrrdgkqhngmqmvFQDPlssldprlPVWRIITEpvwiQKRSSERE 119
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---------------FDDP--------PDWDEILD----EFRGSELQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 120 ---RRILAEDLaqQVGIRPEYLDRLPHAF-------------------------------------SGGQRQRIAIARAL 159
Cdd:cd03236 77 nyfTKLLEGDV--KVIVKPQYVDLIPKAVkgkvgellkkkdergkldelvdqlelrhvldrnidqlSGGELQRVAIAAAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740855357 160 SSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNltYVL-ISHNVSVVRHMSDRVAVMY 219
Cdd:cd03236 155 ARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDN--YVLvVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
31-242 |
6.32e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.97 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLL--MGMLQPS---QGNYSRRDGKQHNG----------MQMVFQDPLssl 95
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNLYAPdvdpvevrrrIGMVFQKPN--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 96 dprlPVWRIITEPVWIQKRSSERERRI--LAEDLAQQVGIRPEYLDRLPH---AFSGGQRQRIAIARALSSEPDVIVLDE 170
Cdd:PRK14243 102 ----PFPKSIYDNIAYGARINGYKGDMdeLVERSLRQAALWDEVKDKLKQsglSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 171 PTSALDISVQAQILNLLVSLqaRRNLTYVLISHNVSVVRHMSDRVAVM---------YLGQIVELGETQQVLTHPAHPYT 241
Cdd:PRK14243 178 PCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQAT 255
|
.
gi 740855357 242 R 242
Cdd:PRK14243 256 R 256
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
29-225 |
6.70e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.91 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 29 VHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGmLQPSqGNYsrrDGKQH-NGMQMVFQDPLSS------------- 94
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPH-GSY---EGEILfDGEVCRFKDIRDSealgiviihqela 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 95 LDPRLPvwriITEPVWIQKRSSER------ERRILAEDLAQQVGirpeyLDRLPHAFSG----GQRQRIAIARALSSEPD 164
Cdd:NF040905 89 LIPYLS----IAENIFLGNERAKRgvidwnETNRRARELLAKVG-----LDESPDTLVTdigvGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740855357 165 VIVLDEPTSALDISVQAQILNLLVSLQArRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVE 225
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-270 |
8.09e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 8.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSFPArknwlgkvterVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHN-- 82
Cdd:PRK15439 11 LLCARSISKQYSG-----------VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 83 -------GMQMVFQDPLssLDPRLPVWRIItepVWIQKRSSERERRIlaEDLAQQVGIRpeyLDrlPHAFSG----GQRQ 151
Cdd:PRK15439 80 pakahqlGIYLVPQEPL--LFPNLSVKENI---LFGLPKRQASMQKM--KQLLAALGCQ---LD--LDSSAGslevADRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 152 RIAIARALSSEPDVIVLDEPTSALdisVQAQILNLLVSLQARRNLTY--VLISHNVSVVRHMSDRVAVMYLGQIVELGET 229
Cdd:PRK15439 148 IVEILRGLMRDSRILILDEPTASL---TPAETERLFSRIRELLAQGVgiVFISHKLPEIRQLADRISVMRDGTIALSGKT 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 740855357 230 QQVLThpahpytrlllDSVPKTGAPLAEDLVLRKT-----ELPGNR 270
Cdd:PRK15439 225 ADLST-----------DDIIQAITPAAREKSLSASqklwlELPGNR 259
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
38-217 |
9.73e-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: 77.52 E-value: 9.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 38 QIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnysrrdgkqhngmqmvfqdplsSLDPRLpvwRIITEPVWIQKRSSE 117
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG----------------------EVDEDL---KISYKPQYISPDYDG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 118 RERRILAEDLAQQVG--------IRPEYLDRLPHA----FSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILN 185
Cdd:COG1245 417 TVEEFLRSANTDDFGssyykteiIKPLGLEKLLDKnvkdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAK 496
|
170 180 190
....*....|....*....|....*....|..
gi 740855357 186 LLVSLQARRNLTYVLISHNVSVVRHMSDRVAV 217
Cdd:COG1245 497 AIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
39-234 |
1.20e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 39 IRQGETLGIVGESGCGKSTLAQLLMGMLQ-PSQGNYsRRDGKQ----------HNGMQMVFQD-PLSSLDPRLPVWRIIT 106
Cdd:PRK13549 285 LRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEI-FIDGKPvkirnpqqaiAQGIAMVPEDrKRDGIVPVMGVGKNIT 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 107 EPVWiqKRSSERERrilAEDLAQQVGIRpEYLDRL----PHAF------SGGQRQRIAIARALSSEPDVIVLDEPTSALD 176
Cdd:PRK13549 364 LAAL--DRFTGGSR---IDDAAELKTIL-ESIQRLkvktASPElaiarlSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740855357 177 ISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQI----VELGETQ-QVLT 234
Cdd:PRK13549 438 VGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVLVMHEGKLkgdlINHNLTQeQVME 499
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
37-233 |
1.45e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.54 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 37 LQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRD---------GKQHNGMQMVFQDPlsSLDPRLPVWRIITE 107
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplhARARRGIGYLPQEA--SIFRRLSVYDNLMA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 108 PVWIQKRSSERERRILAEDLAQQVGIrpEYL-DRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALD-ISVqAQILN 185
Cdd:PRK10895 102 VLQIRDDLSAEQREDRANELMEEFHI--EHLrDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpISV-IDIKR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 740855357 186 LLVSLQaRRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVL 233
Cdd:PRK10895 179 IIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
32-218 |
1.56e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 74.29 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQpsqgnysRRDGKQH--NGMQMVFQDPLSSLDPRLPVWRIITEPv 109
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ-------TLEGKVHwsNKNESEPSFEATRSRNRYSVAYAAQKP- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 110 WIQKRSSErERRILAEDLAQQ--------VGIRPEyLDRLPHA-----------FSGGQRQRIAIARALSSEPDVIVLDE 170
Cdd:cd03290 89 WLLNATVE-ENITFGSPFNKQrykavtdaCSLQPD-IDLLPFGdqteigerginLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 740855357 171 PTSALDISV-----QAQILNLLvsLQARRnlTYVLISHNVSVVRHmSDRVAVM 218
Cdd:cd03290 167 PFSALDIHLsdhlmQEGILKFL--QDDKR--TLVLVTHKLQYLPH-ADWIIAM 214
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
31-236 |
1.93e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.67 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnysrrdgkqhngmQMVFQD-PLSSLdpRLPVWR----II 105
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG-------------DIRFHDiPLTKL--QLDSWRsrlaVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 106 TEPVWIQK----------RSSERERRIlaEDLAQQVGIRPEYLdRLPHAF-----------SGGQRQRIAIARALSSEPD 164
Cdd:PRK10789 395 SQTPFLFSdtvannialgRPDATQQEI--EHVARLASVHDDIL-RLPQGYdtevgergvmlSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740855357 165 VIVLDEPTSALDISVQAQILNLLVslQARRNLTYVLISHNVSVVRHmSDRVAVMYLGQIVELGETQQVLTHP 236
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
40-219 |
2.36e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 76.36 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 40 RQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDG-----KQHNGMQMvfQDPLSSL-DPRLpvwRIITEPVWIQ- 112
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSwdevlKRFRGTEL--QDYFKKLaNGEI---KVAHKPQYVDl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 113 -------------KRSSERERrilAEDLAQQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISv 179
Cdd:COG1245 172 ipkvfkgtvrellEKVDERGK---LDELAEKLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY- 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 740855357 180 qaQILNLlvslqAR--RNLT----YVL-ISHNVSVVRHMSDRVAVMY 219
Cdd:COG1245 247 --QRLNV-----ARliRELAeegkYVLvVEHDLAILDYLADYVHILY 286
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
38-217 |
2.40e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.39 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 38 QIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN------------YSRRDgkqhngMQMVFQDPLSSLDPRL---PVW 102
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEvdpelkisykpqYIKPD------YDGTVEDLLRSITDDLgssYYK 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 103 RIITEPVWIqkrssererrilaEDLAQQvgirpeYLDRLphafSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQ 182
Cdd:PRK13409 435 SEIIKPLQL-------------ERLLDK------NVKDL----SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180 190
....*....|....*....|....*....|....*
gi 740855357 183 ILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAV 217
Cdd:PRK13409 492 VAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-219 |
2.52e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.39 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 39 IRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDG-----KQHNGMQMvfQDPLSSL-DPRLpvwRIITEPVWIQ 112
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSwdevlKRFRGTEL--QNYFKKLyNGEI---KVVHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 113 --------------KRSSERERrilAEDLAQQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDIS 178
Cdd:PRK13409 171 lipkvfkgkvrellKKVDERGK---LDEVVERLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 740855357 179 vqaQILNLlvslqAR--RNLT---YVL-ISHNVSVVRHMSDRVAVMY 219
Cdd:PRK13409 247 ---QRLNV-----ARliRELAegkYVLvVEHDLAVLDYLADNVHIAY 285
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-231 |
3.19e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 28 RVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQP-SQGNYSRR-DGKQHNGMQM------VFQDPLssLDPRL 99
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgVKGSGSVLlNGMPIDAKEMraisayVQQDDL--FIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 100 PVWR--IITEPVWIQKRSSERERRILAEDLAQQVGIR---------PEYLDRLphafSGGQRQRIAIARALSSEPDVIVL 168
Cdd:TIGR00955 115 TVREhlMFQAHLRMPRRVTKKEKRERVDEVLQALGLRkcantrigvPGRVKGL----SGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740855357 169 DEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQ 231
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
41-221 |
3.34e-15 |
|
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: 71.64 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 41 QGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsrrdgkqhngmqmvfqdplssldprlpvwrIITEPVWIQKRSSERER 120
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV------------------------------IYIDGEDILEEVLDQLL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 121 RIlaedlaqqvgirpeYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQIL-----NLLVSLQARRN 195
Cdd:smart00382 51 LI--------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLLKSEKN 116
|
170 180 190
....*....|....*....|....*....|.
gi 740855357 196 LTYVLISHNVSV-----VRHMSDRVAVMYLG 221
Cdd:smart00382 117 LTVILTTNDEKDlgpalLRRRFDRRIVLLLI 147
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-256 |
3.59e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 22 LGKVTERVHALNG------LDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQ----------HNGMQ 85
Cdd:PRK11288 253 LGEVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQV-YLDGKPidirsprdaiRAGIM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 MVFQD-------PLSSLDPRLPV--------WRIITEPVWiqkrssERErriLAEDLAQQVGIRPEYLDRLPHAFSGGQR 150
Cdd:PRK11288 332 LCPEDrkaegiiPVHSVADNINIsarrhhlrAGCLINNRW------EAE---NADRFIRSLNIKTPSREQLIMNLSGGNQ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 151 QRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVelGEtq 230
Cdd:PRK11288 403 QKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA--GE-- 477
|
250 260
....*....|....*....|....*.
gi 740855357 231 qvLTHPAHPYTRLLLDSVPKTGAPLA 256
Cdd:PRK11288 478 --LAREQATERQALSLALPRTSAAVA 501
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
31-203 |
3.72e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.78 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQHNGMQMVFQDPL------SSLDPRLPVWri 104
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV-RWNGTPLAEQRDEPHENIlylghlPGLKPELSAL-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 105 itEPVWIQKRSSERERRILAEDLAQqVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQIL 184
Cdd:TIGR01189 92 --ENLHFWAAIHGGAQRTIEDALAA-VGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLA 167
|
170
....*....|....*....
gi 740855357 185 NLLVSLQARRNLTyVLISH 203
Cdd:TIGR01189 168 GLLRAHLARGGIV-LLTTH 185
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-227 |
5.06e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 72.20 E-value: 5.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 19 KNWLGKVTERVhaLNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGmlqpsqgnysRRDGKQHNGMQMVFQDPLSsldpr 98
Cdd:cd03213 14 KSSPSKSGKQL--LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG----------RRTGLGVSGEVLINGRPLD----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 99 lpvwriitePVWIQKRSS--ERERRILA-----EDLAQQVGIRpeyldrlphAFSGGQRQRIAIARALSSEPDVIVLDEP 171
Cdd:cd03213 77 ---------KRSFRKIIGyvPQDDILHPtltvrETLMFAAKLR---------GLSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 172 TSALDISVQAQILNLLVSLqARRNLTYVLISHNVS-VVRHMSDRVAVMYLGQIVELG 227
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
36-233 |
8.41e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 74.67 E-value: 8.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 36 DLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRR-----------------DGKQHNGMQMVFQDPLsslDPR 98
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfshitrlsfeqlqklvsDEWQRNNTDMLSPGED---DTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 99 LPVWRIItepvwiQKRSSERERrilAEDLAQQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDIS 178
Cdd:PRK10938 100 RTTAEII------QDEVKDPAR---CEQLAQQFGITA-LLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 740855357 179 VQAQILNLLVSLQArRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVL 233
Cdd:PRK10938 170 SRQQLAELLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
35-234 |
9.71e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.71 E-value: 9.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 35 LDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN----------YSRRDGKQHNGMqmVFQDPLSSLDprLPVWRI 104
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHvwldgehiqhYASKEVARRIGL--LAQNATTPGD--ITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 105 IT------EPVWIQKRSSERERRILAedlAQQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDIS 178
Cdd:PRK10253 102 VArgryphQPLFTRWRKEDEEAVTKA---MQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 740855357 179 VQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLT 234
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
31-236 |
1.19e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 72.33 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQHNGM--QMV--------FQDPlssldpRLP 100
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI-LLRGQHIEGLpgHQIarmgvvrtFQHV------RLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 101 VWRIITEPVWIQK------------------RSSERERRILAEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSE 162
Cdd:PRK11300 93 REMTVIENLLVAQhqqlktglfsgllktpafRRAESEALDRAATWLERVGLL-EHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740855357 163 PDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHP 236
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-233 |
1.42e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.88 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 23 GKVTERVHALNGLDL-----QIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG----------NYSRRDGKQhNGMQMV 87
Cdd:PRK10762 254 GEVRLKVDNLSGPGVndvsfTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGyvtldghevvTRSPQDGLA-NGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 88 FQD----------------PLSSLDPRLPVWRIItepvwiqKRSSERerrILAEDLAQQVGIRPEYLDRLPHAFSGGQRQ 151
Cdd:PRK10762 333 SEDrkrdglvlgmsvkenmSLTALRYFSRAGGSL-------KHADEQ---QAVSDFIRLFNIKTPSMEQAIGLLSGGNQQ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 152 RIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQArRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVelGE--- 228
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKA-EGLSIILVSSEMPEVLGMSDRILVMHEGRIS--GEftr 479
|
....*...
gi 740855357 229 ---TQQVL 233
Cdd:PRK10762 480 eqaTQEKL 487
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
32-234 |
1.43e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.04 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN---------------YSRRDG--KQHNGMQMvfqdplss 94
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEvlvdgldvattpsreLAKRLAilRQENHINS-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 95 ldpRLPVwriiTEPV------WIQKRSSERERRILAEDLAQQ--VGIRPEYLDRLphafSGGQRQRIAIARALSSEPDVI 166
Cdd:COG4604 89 ---RLTV----RELVafgrfpYSKGRLTAEDREIIDEAIAYLdlEDLADRYLDEL----SGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740855357 167 VLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLT 234
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-232 |
1.45e-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: 74.07 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 22 LGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGM--LQPSQG----NYSR-----------RDGKQ--HN 82
Cdd:TIGR03269 6 LTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGriiyHVALcekcgyverpsKVGEPcpVC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 83 GMQMVFQDpLSSLDPRLPVWRIITEPVWIQKRSS---ERERRIL--------------------AEDLAQQVGIRpeylD 139
Cdd:TIGR03269 86 GGTLEPEE-VDFWNLSDKLRRRIRKRIAIMLQRTfalYGDDTVLdnvlealeeigyegkeavgrAVDLIEMVQLS----H 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 140 RLPHA---FSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVA 216
Cdd:TIGR03269 161 RITHIardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*.
gi 740855357 217 VMYLGQIVELGETQQV 232
Cdd:TIGR03269 241 WLENGEIKEEGTPDEV 256
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
35-236 |
1.52e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 35 LDLQIRQGETLGIVGESGCGKSTLAQLLMGMLqPSQG----------NYSRRDGKQHNGMQMVFQDPLSSldprLPVWRI 104
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGsiqfagqpleAWSAAELARHRAYLSQQQTPPFA----MPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 105 ITEPVWIQKRSSERERRIlaEDLAQQVGIRPEyLDRLPHAFSGG--QRQRIA-----IARALSSEPDVIVLDEPTSALDI 177
Cdd:PRK03695 90 LTLHQPDKTRTEAVASAL--NEVAEALGLDDK-LGRSVNQLSGGewQRVRLAavvlqVWPDINPAGQLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 178 SVQAqILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHP 236
Cdd:PRK03695 167 AQQA-ALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-233 |
1.84e-14 |
|
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: 73.71 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 25 VTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHN----------GMQMVFQD-PLS 93
Cdd:TIGR02633 269 INPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDirnpaqairaGIAMVPEDrKRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 94 SLDPRLPVWRIITEPV-----WIQKRSSERERRILAEDLaQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVL 168
Cdd:TIGR02633 349 GIVPILGVGKNITLSVlksfcFKMRIDAAAELQIIGSAI-QRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 169 DEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQI----VELGETQ-QVL 233
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQL-AQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLkgdfVNHALTQeQVL 496
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
35-248 |
2.71e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.33 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 35 LDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGN----------YSR-RDGKQHNGMQMVFQDplSSLDPRLPVWR 103
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEilfdgenipaMSRsRLYTVRKRMSMLFQS--GALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 104 IITEPVwiqkrsseRERRILAEDLAQQ--------VGIRPEyLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSAL 175
Cdd:PRK11831 104 NVAYPL--------REHTQLPAPLLHStvmmkleaVGLRGA-AKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740855357 176 DISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTHPaHPYTRLLLDSV 248
Cdd:PRK11831 175 DPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFLDGI 246
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-225 |
4.31e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.79 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 18 RKNWLGKVTervhaLNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYS-------RRDGKQHNGMQMVFQd 90
Cdd:PRK13536 48 SKSYGDKAV-----VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvpARARLARARIGVVPQ- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 91 pLSSLDPRLPVwriiTEPVWIQKR---SSERERRILAEDLAQQVGIRPEYLDRLPHaFSGGQRQRIAIARALSSEPDVIV 167
Cdd:PRK13536 122 -FDNLDLEFTV----RENLLVFGRyfgMSTREIEAVIPSLLEFARLESKADARVSD-LSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 168 LDEPTSALDISVQAQILNLLVSLQArRNLTYVLISHNVSVVRHMSDRVAVMYLG-QIVE 225
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGrKIAE 253
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-227 |
7.15e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.06 E-value: 7.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 1 MSEFLLALQDVHVSFPARKnwlgkvtervhALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMG-----------MLQPS 69
Cdd:CHL00131 3 KNKPILEIKNLHASVNENE-----------ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykilegdiLFKGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 70 QGNYSRRDGKQHNGMQMVFQDP------------------------LSSLDPrLPVWRIITEPVwiqkrssererrilae 125
Cdd:CHL00131 72 SILDLEPEERAHLGIFLAFQYPieipgvsnadflrlaynskrkfqgLPELDP-LEFLEIINEKL---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 126 dlaQQVGIRPEYLDR-LPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHN 204
Cdd:CHL00131 135 ---KLVGMDPSFLSRnVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHY 210
|
250 260
....*....|....*....|....
gi 740855357 205 VSVVRHMS-DRVAVMYLGQIVELG 227
Cdd:CHL00131 211 QRLLDYIKpDYVHVMQNGKIIKTG 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
35-210 |
8.45e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.98 E-value: 8.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 35 LDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDgkQHN-----------GMQMVFQDPL----------- 92
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND--SHNlkdinlkwwrsKIGVVSQDPLlfsnsiknnik 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 93 ------------------------SSLDPRLPVWRIITEPVWIQKRSSERERRILAE------------DLAQQVGIRpE 136
Cdd:PTZ00265 482 yslyslkdlealsnyynedgndsqENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRknyqtikdsevvDVSKKVLIH-D 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 137 YLDRLPHAF-----------SGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNV 205
Cdd:PTZ00265 561 FVSALPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
....*
gi 740855357 206 SVVRH 210
Cdd:PTZ00265 641 STIRY 645
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
34-187 |
1.21e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.36 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 34 GLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHNGM---QMVFQDPLSSLDPRLPVWRIITepVW 110
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaeACHYLGHRNAMKPALTVAENLE--FW 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740855357 111 IQKRSSERERrilAEDLAQQVGIRPeyLDRLPHAF-SGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLL 187
Cdd:PRK13539 98 AAFLGGEELD---IAAALEAVGLAP--LAHLPFGYlSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
28-224 |
1.28e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.14 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 28 RVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrDGKQHNGMQMVfqdplssldprlpvwRIITE 107
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVF-DGKDITDWQTA---------------KIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 108 PVWIQKRSSERERRILAEDLAQQVGI---RPEYLDRLPHAF-----------------SGGQRQRIAIARALSSEPDVIV 167
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFfaeRDQFQERIKWVYelfprlherriqragtmSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 168 LDEPTSALDISVQAQILNLLVSLQArRNLTYVLISHNVSVVRHMSDRVAVMYLGQIV 224
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-203 |
1.55e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.45 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 25 VTERV---HALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGmlqpsqgnysRRDGKQHNGMQMVFQDPLSSLDPrlpv 101
Cdd:COG2401 36 VELRVverYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG----------ALKGTPVAGCVDVPDNQFGREAS---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 102 wriITEPVWIqKRSSERERRILAedlaqQVGIRPEYL-DRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDiSVQ 180
Cdd:COG2401 102 ---LIDAIGR-KGDFKDAVELLN-----AVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD-RQT 171
|
170 180
....*....|....*....|....
gi 740855357 181 AQILNLLVSLQARR-NLTYVLISH 203
Cdd:COG2401 172 AKRVARNLQKLARRaGITLVVATH 195
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-235 |
1.60e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.06 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPS--QGNYSRRDGKQHNGMQ----MVFQDPLssLDPRLPVWR-- 103
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILkrtgFVTQDDI--LYPHLTVREtl 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 104 IITEPVWIQKRSSERERRILAEDLAQQVGIRPEYLDRLPHAF----SGGQRQRIAIARALSSEPDVIVLDEPTSALDISV 179
Cdd:PLN03211 162 VFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 180 QAQILNLLVSLqARRNLTYVLISHNVSV-VRHMSDRVAVMYLGQIVELGETQQVLTH 235
Cdd:PLN03211 242 AYRLVLTLGSL-AQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFGKGSDAMAY 297
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
39-219 |
2.84e-13 |
|
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: 66.83 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 39 IRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSrrdgkqhngmqmvfqdplssldprlpvWRIITepvwiqkrsser 118
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE---------------------------WDGIT------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 119 errilaedlaqqVGIRPEYLDrlphaFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTY 198
Cdd:cd03222 63 ------------PVYKPQYID-----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTA 125
|
170 180
....*....|....*....|.
gi 740855357 199 VLISHNVSVVRHMSDRVAVMY 219
Cdd:cd03222 126 LVVEHDLAVLDYLSDRIHVFE 146
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
32-238 |
4.92e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.93 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSqgnySRRDGKQHNGMQMVFQDPLSSLD-PRLPVWRII----T 106
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGG----GAPRGARVTGDVTLNGEPLAAIDaPRLARLRAVlpqaA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 107 EPVWI--------------QKRS---SERERRILAEDLAQqVGIRPeYLDRLPHAFSGGQRQRIAIARALS--------- 160
Cdd:PRK13547 93 QPAFAfsareivllgryphARRAgalTHRDGEIAWQALAL-AGATA-LVGRDVTTLSGGELARVQFARVLAqlwpphdaa 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740855357 161 SEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLThPAH 238
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT-PAH 247
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
46-213 |
4.93e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.15 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 46 GIVGESGCGKSTLAQLLMGMLQPSQGNYS----RRDGKQHNGmQMVFQDpLSSLDPRL----PVWRIITE--PVWIQKRS 115
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVSldpnERLGKLRQD-QFAFEE-FTVLDTVImghtELWEVKQErdRIYALPEM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 116 SER--------------------ERRilAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSAL 175
Cdd:PRK15064 109 SEEdgmkvadlevkfaemdgytaEAR--AGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 740855357 176 DISV---QAQILNllvslqaRRNLTYVLISH-----NvSVVRHMSD 213
Cdd:PRK15064 187 DINTirwLEDVLN-------ERNSTMIIISHdrhflN-SVCTHMAD 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
32-222 |
5.75e-13 |
|
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: 67.96 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsrrdgkQHNGmQMVFQDPLSSLDPRLPVWRIITEPVWI 111
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------KHSG-RISFSSQFSWIMPGTIKENIIFGVSYD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 112 QKRSserERRILAEDLAQQVGIRPEYlDRLPHA-----FSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNL 186
Cdd:cd03291 126 EYRY---KSVVKACQLEEDITKFPEK-DNTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFES 201
|
170 180 190
....*....|....*....|....*....|....*..
gi 740855357 187 LV-SLQArrNLTYVLISHNVSVVRhMSDRVAVMYLGQ 222
Cdd:cd03291 202 CVcKLMA--NKTRILVTSKMEHLK-KADKILILHEGS 235
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
32-193 |
6.38e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 66.36 E-value: 6.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYS--------RRDGKQHN----GMQMVFQDPLSSLDpRL 99
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlnggpldfQRDSIARGllylGHAPGIKTTLSVLE-NL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 100 PVWRII--TEPVWiqkrssererrilaEDLAQqVGIRPeYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDI 177
Cdd:cd03231 95 RFWHADhsDEQVE--------------EALAR-VGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170
....*....|....*.
gi 740855357 178 SVQAQILNLLVSLQAR 193
Cdd:cd03231 159 AGVARFAEAMAGHCAR 174
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-232 |
1.49e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.50 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNySRRDGKQ--------HNGMQMVFQdpLSSLDPRLPVw 102
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGD-ATVAGKSiltnisdvHQNMGYCPQ--FDAIDDLLTG- 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 103 riiTEPVWIQKR-----SSERERriLAEDLAQQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDI 177
Cdd:TIGR01257 2030 ---REHLYLYARlrgvpAEEIEK--VANWSIQSLGLSL-YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 740855357 178 SVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQV 232
Cdd:TIGR01257 2104 QARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-217 |
2.26e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.75 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 8 LQDVHVSFPARKNwlgkvterVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGML--------------------- 66
Cdd:PTZ00265 1168 IMDVNFRYISRPN--------VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtne 1239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 67 QPSQGN------------YSRRDGKQHNGMQMVFQ-------DPLSSLDPRLPVWR-----IITEPVWIQKRSSE----- 117
Cdd:PTZ00265 1240 QDYQGDeeqnvgmknvneFSLTKEGGSGEDSTVFKnsgkillDGVDICDYNLKDLRnlfsiVSQEPMLFNMSIYEnikfg 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 118 RERRILaEDL--AQQVGIRPEYLDRLPHAF-----------SGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQIL 184
Cdd:PTZ00265 1320 KEDATR-EDVkrACKFAAIDEFIESLPNKYdtnvgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1398
|
250 260 270
....*....|....*....|....*....|...
gi 740855357 185 NLLVSLQARRNLTYVLISHNVSVVRHmSDRVAV 217
Cdd:PTZ00265 1399 KTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1430
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-265 |
6.11e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 6.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrDGKQHNGMQMVFQDPLSSLDPRLPVW-----RIIT 106
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMI-DDCDVAKFGLTDLRRVLSIIPQSPVLfsgtvRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 107 EPVwiqkrsSERERRILAEDLaQQVGIRpEYLDRLP-----------HAFSGGQRQRIAIARALSSEPDVIVLDEPTSAL 175
Cdd:PLN03232 1331 DPF------SEHNDADLWEAL-ERAHIK-DVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 176 DISVQAQILNLLvsLQARRNLTYVLISHNVSVVRHmSDRVAVMYLGQIVELGETQQVLTHPAHPYTRLLLDSVPKTGAPL 255
Cdd:PLN03232 1403 DVRTDSLIQRTI--REEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPANAQYL 1479
|
250
....*....|
gi 740855357 256 AeDLVLRKTE 265
Cdd:PLN03232 1480 S-NLVFERRE 1488
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
28-215 |
6.16e-12 |
|
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: 63.11 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 28 RVHALNGLDLQIRQGETLGIVGESGCGKSTLAQ-----LLMGMLQPSQGNYSRRdgkqhngmQMVFQDPLSSLdprlpvw 102
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNeglyaSGKARLISFLPKFSRN--------KLIFIDQLQFL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 103 riitepvwiqkrssererrilaedlaQQVGIRPEYLDRLPHAFSGGQRQRIAIARAL--SSEPDVIVLDEPTSALDISVQ 180
Cdd:cd03238 72 --------------------------IDVGLGYLTLGQKLSTLSGGELQRVKLASELfsEPPGTLFILDEPSTGLHQQDI 125
|
170 180 190
....*....|....*....|....*....|....*
gi 740855357 181 AQILNLLVSLQARRNlTYVLISHNVSVVRHmSDRV 215
Cdd:cd03238 126 NQLLEVIKGLIDLGN-TVILIEHNLDVLSS-ADWI 158
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
32-221 |
8.17e-12 |
|
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: 66.09 E-value: 8.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsrrdgkQHNGmQMVFQDPLSSLDPRLPVWRIITEPVWI 111
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI------KHSG-RISFSPQTSWIMPGTIKDNIIFGLSYD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 112 QKRSSERerrILAEDLAQQVGIRPEYlDRLPH-----AFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQIL-N 185
Cdd:TIGR01271 515 EYRYTSV---IKACQLEEDIALFPEK-DKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFeS 590
|
170 180 190
....*....|....*....|....*....|....*...
gi 740855357 186 LLVSLQArrNLTYVLIShnvSVVRHM--SDRVAVMYLG 221
Cdd:TIGR01271 591 CLCKLMS--NKTRILVT---SKLEHLkkADKILLLHEG 623
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-228 |
1.00e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.66 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 5 LLALQDVHVSfparknwlgkvTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGmlqpsqgnysrRDGKQHNGM 84
Cdd:PRK09580 1 MLSIKDLHVS-----------VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG-----------REDYEVTGG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 85 QMVFQ-DPLSSLDPR----LPVWRIITEPVWIQKRSSE----------RERR-----------ILAEDLAQQVGIRPEYL 138
Cdd:PRK09580 59 TVEFKgKDLLELSPEdragEGIFMAFQYPVEIPGVSNQfflqtalnavRSYRgqepldrfdfqDLMEEKIALLKMPEDLL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 139 DR-LPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNlTYVLISHNVSVVRHMS-DRVA 216
Cdd:PRK09580 139 TRsVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTHYQRILDYIKpDYVH 217
|
250
....*....|..
gi 740855357 217 VMYLGQIVELGE 228
Cdd:PRK09580 218 VLYQGRIVKSGD 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
30-226 |
2.58e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.19 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 30 HALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQhngMQMVFQDPlsSLDPRLPVWRIITEPV 109
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIK---VGYLPQEP--QLDPTKTVRENVEEGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 110 WIQKRSSERERRI-------------LAE---------------DLAQQVGIRPEYLdRLP------HAFSGGQRQRIAI 155
Cdd:TIGR03719 94 AEIKDALDRFNEIsakyaepdadfdkLAAeqaelqeiidaadawDLDSQLEIAMDAL-RCPpwdadvTKLSGGERRRVAL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740855357 156 ARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQArrnlTYVLISHNvsvvRHMSDRVAvmylGQIVEL 226
Cdd:TIGR03719 173 CRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTHD----RYFLDNVA----GWILEL 231
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-227 |
2.83e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.41 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG----------NYSRRDGKQHngMQMVFQDPL-------SS 94
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGeirvngreigAYGLRELRRQ--FSMIPQDPVlfdgtvrQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 95 LDPRL-----PVWRIItEPVWIQKR-SSERErrilaedlaqqvGIRPEYLDRLPHaFSGGQRQRIAIARA-LSSEPDVIV 167
Cdd:PTZ00243 1404 VDPFLeassaEVWAAL-ELVGLRERvASESE------------GIDSRVLEGGSN-YSVGQRQLMCMARAlLKKGSGFIL 1469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 168 LDEPTSALDISVQAQILNLLVSlqARRNLTYVLISHNVSVVRHMsDRVAVMYLGQIVELG 227
Cdd:PTZ00243 1470 MDEATANIDPALDRQIQATVMS--AFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMG 1526
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
38-203 |
3.69e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 38 QIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnysrrdgKQHNGMQM---VFQDPLSSLDPRlpvwRIITEPVWIQKR 114
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG-------RIHCGTKLevaYFDQHRAELDPE----KTVMDNLAEGKQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 115 SSE---RERRILAedlaqqvgirpeYL-DRLPH---------AFSGGQRQRIAIARALSSEPDVIVLDEPTSALDIsvqa 181
Cdd:PRK11147 410 EVMvngRPRHVLG------------YLqDFLFHpkramtpvkALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV---- 473
|
170 180
....*....|....*....|..
gi 740855357 182 QILNLLVSLQARRNLTYVLISH 203
Cdd:PRK11147 474 ETLELLEELLDSYQGTVLLVSH 495
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
36-224 |
4.68e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 36 DLQIRQGETLGIVGESGCGKSTLAQLLMG--MLQPSQGNY------SR------RD-----------GKQHNG------- 83
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGevLLDDGRIIYeqdlivARlqqdppRNvegtvydfvaeGIEEQAeylkryh 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 84 --MQMVFQDP-------LSSLDPRLP---VWRIitepvwiqkrsserERRIlaEDLAQQVGIRPeylDRLPHAFSGGQRQ 151
Cdd:PRK11147 103 diSHLVETDPseknlneLAKLQEQLDhhnLWQL--------------ENRI--NEVLAQLGLDP---DAALSSLSGGWLR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740855357 152 RIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQArrnlTYVLISHNVSVVRHMSDRVAVMYLGQIV 224
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-233 |
1.14e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.66 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQ------HN---GMQMVFQDPL---SSLDPRL 99
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI-IIDGLNiakiglHDlrfKITIIPQDPVlfsGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 100 -PVWRIITEPVWiqkrssererriLAEDLAQQVGIRPEYLDRLPHA-------FSGGQRQRIAIARALSSEPDVIVLDEP 171
Cdd:TIGR00957 1381 dPFSQYSDEEVW------------WALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740855357 172 TSALDIS----VQAQILNLLvslqarRNLTYVLISHNVSVVRHMSdRVAVMYLGQIVELGETQQVL 233
Cdd:TIGR00957 1449 TAAVDLEtdnlIQSTIRTQF------EDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLL 1507
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
30-235 |
2.17e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.44 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 30 HALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsrrDGKQHNGMQMVFqdplSSLDPRLPVWRIITEPV 109
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV---DIKGSAALIAIS----SGLNGQLTGIENIELKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 110 WIQKRSSERERRILAE--DLAqQVGirpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLL 187
Cdd:PRK13545 111 LMMGLTKEKIKEIIPEiiEFA-DIG---KFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 740855357 188 VSLQaRRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTH 235
Cdd:PRK13545 187 NEFK-EQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
31-176 |
2.20e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.68 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG--------------NYSRRDGKqhngMQMVFqdplsSLD 96
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeawlfgqpvdagdiATRRRVGY----MSQAF-----SLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 97 PRLPVW-------RIITEPvwiqkrSSERERRIlaEDLAQQVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLD 169
Cdd:NF033858 352 GELTVRqnlelhaRLFHLP------AAEIAARV--AEMLERFDLA-DVADALPDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
....*..
gi 740855357 170 EPTSALD 176
Cdd:NF033858 423 EPTSGVD 429
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
34-187 |
2.65e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.05 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 34 GLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYS------RRDGKQHNGmQMVFQDPLSSLDPRLPVWRIITe 107
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepiRRQRDEYHQ-DLLYLGHQPGIKTELTALENLR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 108 pvWIQKRSSERERRILAEDLAQqVGIRpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLL 187
Cdd:PRK13538 97 --FYQRLHGPGDDEALWEALAQ-VGLA-GFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-235 |
3.40e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.44 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 16 PARKNwlgkvtERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrdgkqHNGMQMVFQDplSSL 95
Cdd:PRK13546 30 PKHKN------KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDR-----NGEVSVIAIS--AGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 96 DPRLPVWRIITEPVWIQKRSSERERRILAEDLA-QQVGirpEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSA 174
Cdd:PRK13546 97 SGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEfSELG---EFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740855357 175 LDISVQAQILNLLVSLQARrNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLTH 235
Cdd:PRK13546 174 GDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
6-244 |
3.45e-10 |
|
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: 59.54 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFparKNWLGKVTERVHALngldlqIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrDGKQhngmq 85
Cdd:cd03288 20 IKIHDLCVRY---ENNLKPVLKHVKAY------IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI-DGID----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 mVFQDPLSSLDPRLPVwrIITEPVWIQ---------KRSSERERRILAEDLAQ---QVGIRPEYLDRL----PHAFSGGQ 149
Cdd:cd03288 85 -ISKLPLHTLRSRLSI--ILQDPILFSgsirfnldpECKCTDDRLWEALEIAQlknMVKSLPGGLDAVvtegGENFSVGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 150 RQRIAIARALSSEPDVIVLDEPTSALDISVQaQILNLLVsLQARRNLTYVLISHNVSVVRHmSDRVAVMYLGQIVELGET 229
Cdd:cd03288 162 RQLFCLARAFVRKSSILIMDEATASIDMATE-NILQKVV-MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTP 238
|
250
....*....|....*
gi 740855357 230 QQVLTHPAHPYTRLL 244
Cdd:cd03288 239 ENLLAQEDGVFASLV 253
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
15-231 |
3.49e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 15 FPARKNWLGKVTERVHALNGLD--------LQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKQ------ 80
Cdd:PRK10982 239 FPDKENKPGEVILEVRNLTSLRqpsirdvsFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTI-TLHGKKinnhna 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 81 ----HNGMQMV----------------FQDPLSSLDPRLPVWRIITEpvwiQKRSSERERRILAEDL---AQQVGIrpey 137
Cdd:PRK10982 318 neaiNHGFALVteerrstgiyayldigFNSLISNIRNYKNKVGLLDN----SRMKSDTQWVIDSMRVktpGHRTQI---- 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 138 ldrlpHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAV 217
Cdd:PRK10982 390 -----GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILV 463
|
250
....*....|....*..
gi 740855357 218 MYLGQ---IVELGETQQ 231
Cdd:PRK10982 464 MSNGLvagIVDTKTTTQ 480
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-224 |
3.82e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 29 VHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG---------NYSRRDGKQHNGMQMVFQD-----PLSS 94
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGsilfqgkeiDFKSSKEALENGISMVHQElnlvlQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 95 LDprlPVW--RIITEPVWIQKRSSERERRILAEDLAQQVGIRPEYLDrlphaFSGGQRQRIAIARALSSEPDVIVLDEPT 172
Cdd:PRK10982 91 MD---NMWlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 740855357 173 SALDISVQAQILNLLVSLQaRRNLTYVLISHNVSVVRHMSDRVAVMYLGQIV 224
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
32-234 |
4.17e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.57 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDG------KQHngmQMVF----QDPLSSLdprlpv 101
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGiklgyfAQH---QLEFlradESPLQHL------ 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 102 wriitepVWIQKRSSERERRilaeDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQA 181
Cdd:PRK10636 399 -------ARLAPQELEQKLR----DYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 182 QILNLLVSLQArrnlTYVLISHNVSVVRHMSDRVAVMYLGQIV----ELGETQQVLT 234
Cdd:PRK10636 468 ALTEALIDFEG----ALVVVSHDRHLLRSTTDDLYLVHDGKVEpfdgDLEDYQQWLS 520
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-295 |
4.90e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.80 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 31 ALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHNGMQMVFQD----PLSS-LDPRLPVWRII 105
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSlgmcPQHNiLFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 106 TEPVWIQKRSSErERRILAEDLAQQVGIRPEYlDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILN 185
Cdd:TIGR01257 1025 LFYAQLKGRSWE-EAQLEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 186 LLvsLQARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGetqqvlthpahpyTRLLLDSVPKTGAPLAedLVLRKTE 265
Cdd:TIGR01257 1103 LL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG-------------TPLFLKNCFGTGFYLT--LVRKMKN 1165
|
250 260 270
....*....|....*....|....*....|....*.
gi 740855357 266 LPGNRTLPEGCF------FRDRCPLAIRGCENKQIL 295
Cdd:TIGR01257 1166 IQSQRGGCEGTCsctskgFSTRCPARVDEITPEQVL 1201
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-227 |
5.10e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnysrrdgkqhngmqmvfqdplSSLDPRLPVWRIITEPvWI 111
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAET---------------------SSVVIRGSVAYVPQVS-WI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 112 QKrSSERERRILAEDL-------AQQVGIRPEYLDRLPHA-----------FSGGQRQRIAIARALSSEPDVIVLDEPTS 173
Cdd:PLN03232 691 FN-ATVRENILFGSDFeserywrAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 740855357 174 ALDISVQAQILNLLVSlQARRNLTYVLISHNVSVVRHMsDRVAVMYLGQIVELG 227
Cdd:PLN03232 770 ALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEG 821
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-234 |
6.03e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 19 KNWLGKVTERVhalNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMlQPSQGNYSRRDGKQ----------HNGMQMVF 88
Cdd:PRK09700 269 RNVTSRDRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGV-DKRAGGEIRLNGKDisprspldavKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 89 QD-------PLSSLDPRLPVWRIITEPVWiqKRS----SERERRILAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIAR 157
Cdd:PRK09700 345 ESrrdngffPNFSIAQNMAISRSLKDGGY--KGAmglfHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISK 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 158 ALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLT 234
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMS 498
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-71 |
9.90e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 59.43 E-value: 9.90e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740855357 6 LALQDVHVSFPARKNwlgkvtERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQG 71
Cdd:COG4615 328 LELRGVTYRYPGEDG------DEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESG 387
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
39-204 |
2.22e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.26 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 39 IRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrdgKQHNGMQMVFQDplsslDPRLPVwriitePVWIQKRSSER 118
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---PGNWQLAWVNQE-----TPALPQ------PALEYVIDGDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 119 ERRILAEDLAQQ----------------------------------VGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPD 164
Cdd:PRK10636 90 EYRQLEAQLHDAnerndghaiatihgkldaidawtirsraasllhgLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 740855357 165 VIVLDEPTSALDISVQAQILNLLVSLQArrnlTYVLISHN 204
Cdd:PRK10636 170 LLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHD 205
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-237 |
2.41e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.06 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 6 LALQDVHVSFPARKnwlgkvtervHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYsRRDGKqhngmq 85
Cdd:PRK10522 323 LELRNVTFAYQDNG----------FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI-LLDGK------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 86 mvfqdPLSSLDPRlpVWR-----IITEpVWIQKRSSERERRILAEDLAQQVGIRPEYLDRLPHA--------FSGGQRQR 152
Cdd:PRK10522 386 -----PVTAEQPE--DYRklfsaVFTD-FHLFDQLLGPEGKPANPALVEKWLERLKMAHKLELEdgrisnlkLSKGQKKR 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 153 IAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNLTYVLISHNVSVVrHMSDRVAVMYLGQIVEL-GETQQ 231
Cdd:PRK10522 458 LALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQLSELtGEERD 536
|
....*.
gi 740855357 232 VLTHPA 237
Cdd:PRK10522 537 AASRDA 542
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-216 |
3.70e-09 |
|
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: 57.64 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGkqhngMQMVFQDPL-SSLDPRLPVWRIITE--- 107
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET-----VKLAYVDQSrDALDPNKTVWEEISGgld 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 108 -----PVWIQKRSSERERRILAEDLAQQVGIrpeyldrlphaFSGGQRQRIAIARALSSEPDVIVLDEPTSALDIsvqaq 182
Cdd:TIGR03719 413 iiklgKREIPSRAYVGRFNFKGSDQQKKVGQ-----------LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----- 476
|
170 180 190
....*....|....*....|....*....|....*..
gi 740855357 183 ilNLLVSL-QARRNL--TYVLISHNvsvvRHMSDRVA 216
Cdd:TIGR03719 477 --ETLRALeEALLNFagCAVVISHD----RWFLDRIA 507
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
146-227 |
4.02e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 146 SGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSlQARRNLTYVLISHNVSVVRHMsDRVAVMYLGQIVE 225
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKE 819
|
..
gi 740855357 226 LG 227
Cdd:PLN03130 820 EG 821
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
29-238 |
4.13e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.05 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 29 VHALNGLDLQIRQGETLGIVGESGCGKSTLAqLLMGMLQPSQGNYS-------------RRDGKQHNGMQMVFQDPLSSL 95
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPwrf*twcanrralRRTIG*HRPVR*GRRESFSGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 96 DPRLPVWRIITepvwiqkrSSERERRILAEDLAQQVGIrPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSAL 175
Cdd:NF000106 105 ENLYMIGR*LD--------LSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740855357 176 DISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHMSDRVAVMYLGQIVELGETQQVLT---------HPAH 238
Cdd:NF000106 176 DPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTkvggrtlqiRPAH 246
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
32-210 |
4.21e-09 |
|
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: 57.45 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLmGMLQPSQGnySRRDGKQHNGMQMVFQDPLSSLdprlpvwRIITEPVWI 111
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYG--GRLTKPAKGKLFYVPQRPYMTL-------GTLRDQIIY 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 112 QKRSSERERRILAE-DLAQqvgirpeYLD--RLPH----------------AFSGGQRQRIAIARALSSEPDVIVLDEPT 172
Cdd:TIGR00954 538 PDSSEDMKRRGLSDkDLEQ-------ILDnvQLTHilereggwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|....*...
gi 740855357 173 SALDISVQAQILNLLvslqARRNLTYVLISHNVSVVRH 210
Cdd:TIGR00954 611 SAVSVDVEGYMYRLC----REFGITLFSVSHRKSLWKY 644
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-188 |
8.25e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.41 E-value: 8.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 34 GLDLQIRqgetLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQhngMQMVFQDPLSSLD----PRLPVWRIITEpV 109
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVR---MAVFSQHHVDGLDlssnPLLYMMRCFPG-V 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 110 WIQKRSSERERRILAEDLAQQvgirPEYldrlphAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDI-SVQAQILNLLV 188
Cdd:PLN03073 603 PEQKLRAHLGSFGVTGNLALQ----PMY------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdAVEALIQGLVL 672
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-228 |
8.47e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.71 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNysrrdgkqhngmqmvfqdplssldprlpVW--RIIT--- 106
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR----------------------------VWaeRSIAyvp 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 107 EPVWIQK---RSS------ERERRI--------LAEDLAQQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLD 169
Cdd:PTZ00243 728 QQAWIMNatvRGNilffdeEDAARLadavrvsqLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 740855357 170 EPTSALDISVQAQILNLLVsLQARRNLTYVLISHNVSVVRHmSDRVAVMYLGQIVELGE 228
Cdd:PTZ00243 808 DPLSALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGS 864
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-265 |
1.03e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.67 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRrDGKQHNGMQMVFQDPLSSLDPRLPVW-----RIIT 106
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILI-DGCDISKFGLMDLRKVLGIIPQAPVLfsgtvRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 107 EP--------VWiqkRSSERE------RRilaedlaQQVGIRPEYLDRlPHAFSGGQRQRIAIARALSSEPDVIVLDEPT 172
Cdd:PLN03130 1334 DPfnehndadLW---ESLERAhlkdviRR-------NSLGLDAEVSEA-GENFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 173 SALDISVQAQILNLLvsLQARRNLTYVLISHNVSVVRHmSDRVAVMYLGQIVELGETQQVLTHPAHPYTRLlldsVPKTG 252
Cdd:PLN03130 1403 AAVDVRTDALIQKTI--REEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEGSAFSKM----VQSTG 1475
|
250
....*....|....*.
gi 740855357 253 APLAE---DLVLRKTE 265
Cdd:PLN03130 1476 AANAQylrSLVFGGDE 1491
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
135-177 |
2.53e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 2.53e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 740855357 135 PEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDI 177
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
46-176 |
1.10e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 46 GIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQhngMQMVFQDPLssLDPRLPVWRIITEPVWIQKRSSERERRI--- 122
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIK---VGYLPQEPQ--LDPEKTVRENVEEGVAEVKAALDRFNEIyaa 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 123 ----------LAE---------------DLAQQVGIRPEYLdRLPHA------FSGGQRQRIAIARALSSEPDVIVLDEP 171
Cdd:PRK11819 112 yaepdadfdaLAAeqgelqeiidaadawDLDSQLEIAMDAL-RCPPWdakvtkLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
....*
gi 740855357 172 TSALD 176
Cdd:PRK11819 191 TNHLD 195
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-176 |
1.15e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGmlQPSQGnYS-------RRDG--------KQHNGMqmvfqdpLSS-- 94
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQG-YSndltlfgRRRGsgetiwdiKKHIGY-------VSSsl 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 95 -LDPRL--PVWRIIT----EPVWIQKRSSERERRilaedLAQQvgirpeYLDRL---------P-HAFSGGQrQRIA-IA 156
Cdd:PRK10938 346 hLDYRVstSVRNVILsgffDSIGIYQAVSDRQQK-----LAQQ------WLDILgidkrtadaPfHSLSWGQ-QRLAlIV 413
|
170 180
....*....|....*....|
gi 740855357 157 RALSSEPDVIVLDEPTSALD 176
Cdd:PRK10938 414 RALVKHPTLLILDEPLQGLD 433
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
32-186 |
4.18e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.05 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHNGMQmvfQDPLSSLDPRLPVWRIITEpvWI 111
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYA---QDHAYDFENDLTLFDWMSQ--WR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 112 QKRSSERE-RRIL------AEDLAQQVGIrpeyldrlphaFSGGQRQRIAIARALSSEPDVIVLDEPTSALDI-SVQAqi 183
Cdd:PRK15064 410 QEGDDEQAvRGTLgrllfsQDDIKKSVKV-----------LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIES-- 476
|
...
gi 740855357 184 LNL 186
Cdd:PRK15064 477 LNM 479
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
145-224 |
6.97e-07 |
|
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: 48.80 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 145 FSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLvslqarRNLTYVLisHNVSVVR---------HMSDRV 215
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCI------RTMADVL--KTTTFVSlyqasdeiyDLFDKV 190
|
....*....
gi 740855357 216 AVMYLGQIV 224
Cdd:cd03233 191 LVLYEGRQI 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-205 |
1.11e-06 |
|
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: 50.29 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 19 KNWLGKVTERVHA-LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQpSQGNYSRrDGKQHNGMQmvfqdplssldp 97
Cdd:TIGR01271 1221 QGLTAKYTEAGRAvLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQI-DGVSWNSVT------------ 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 98 rLPVWR----IITEPVWI-----QKRSSERERRILAE--DLAQQVGIR------PEYLDRL----PHAFSGGQRQRIAIA 156
Cdd:TIGR01271 1287 -LQTWRkafgVIPQKVFIfsgtfRKNLDPYEQWSDEEiwKVAEEVGLKsvieqfPDKLDFVlvdgGYVLSNGHKQLMCLA 1365
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 740855357 157 RALSSEPDVIVLDEPTSALDiSVQAQILNLLVSlQARRNLTYVLISHNV 205
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLD-PVTLQIIRKTLK-QSFSNCTVILSEHRV 1412
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-233 |
1.38e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 15 FPARKNWLGKVTERV-------------HALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMlqpSQGNY----SRRD 77
Cdd:NF040905 246 YPERTPKIGEVVFEVknwtvyhplhperKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGR---SYGRNisgtVFKD 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 78 GKQ----------HNGMQMVFQD----------------PLSSLdPRLPVWRIITEpvwiqkrssERERRIlAEDLAQQV 131
Cdd:NF040905 323 GKEvdvstvsdaiDAGLAYVTEDrkgyglnliddikrniTLANL-GKVSRRGVIDE---------NEEIKV-AEEYRKKM 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 132 GIRPEYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVRHM 211
Cdd:NF040905 392 NIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINEL-AAEGKGVIVISSELPELLGM 470
|
250 260
....*....|....*....|....*...
gi 740855357 212 SDRVAVMYLGQIVelGE------TQQVL 233
Cdd:NF040905 471 CDRIYVMNEGRIT--GElpreeaSQERI 496
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
135-213 |
1.61e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.99 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 135 PEYLDRLphafSGGQRQ------RIAIARALSSEPDVIVLDEPTSALDI-SVQAQILNLLVSLQARRNLTYVLISHNVSV 207
Cdd:cd03240 110 LDMRGRC----SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEEL 185
|
....*.
gi 740855357 208 VRHMSD 213
Cdd:cd03240 186 VDAADH 191
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
146-209 |
4.28e-06 |
|
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: 48.09 E-value: 4.28e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 146 SGGQRQRIAIARALSSE---PDVIVLDEPTSAL---DIsvqAQILNLLVSLQARRNlTYVLISHNVSVVR 209
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDKGN-TVVVIEHNLDVIK 896
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
28-215 |
4.76e-06 |
|
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: 46.87 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 28 RVHALNGLDLQIRQGETLGIVGESGCGKSTLA-QLLMGMLQ----PSQGNYSRRdgkQHNGMQMVFQDPLSSLDPRLPVw 102
Cdd:cd03270 7 REHNLKNVDVDIPRNKLVVITGVSGSGKSSLAfDTIYAEGQrryvESLSAYARQ---FLGQMDKPDVDSIEGLSPAIAI- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 103 riitepvwIQKRSSERER------------------RI-LAEDLAQQVGIRPEYL--DRLPHAFSGGQRQRIAIARALSS 161
Cdd:cd03270 83 --------DQKTTSRNPRstvgtvteiydylrllfaRVgIRERLGFLVDVGLGYLtlSRSAPTLSGGEAQRIRLATQIGS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 740855357 162 E-PDVI-VLDEPTSALDisvQAQILNLLVSLQARRNL--TYVLISHNVSVVRHmSDRV 215
Cdd:cd03270 155 GlTGVLyVLDEPSIGLH---PRDNDRLIETLKRLRDLgnTVLVVEHDEDTIRA-ADHV 208
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
28-194 |
7.09e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.43 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 28 RVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMG--MLQPSQ-----GNYSRRDGKQHNGMQMVF--QDPLSSLDPR 98
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarKIQQGRvevlgGDMADARHRRAVCPRIAYmpQGLGKNLYPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 99 LPVwriiTEPVWIQKR-----SSERERRIlaEDLAQQVGIRPeYLDRLPHAFSGGQRQRIAIARALSSEPDVIVLDEPTS 173
Cdd:NF033858 93 LSV----FENLDFFGRlfgqdAAERRRRI--DELLRATGLAP-FADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 165
|
170 180
....*....|....*....|.
gi 740855357 174 ALDISVQAQILNLLVSLQARR 194
Cdd:NF033858 166 GVDPLSRRQFWELIDRIRAER 186
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
146-209 |
8.29e-06 |
|
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: 46.45 E-value: 8.29e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 146 SGGQRQRIAIARALS---SEPDVIVLDEPTSALDISVQAQILNLLVSLQARRNlTYVLISHNVSVVR 209
Cdd:cd03271 171 SGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVIK 236
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
19-238 |
9.99e-06 |
|
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: 46.39 E-value: 9.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 19 KNWLGKVTERVHA-LNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQpSQGNYSRrDGKQHNGMQmvfqdplssldp 97
Cdd:cd03289 6 KDLTAKYTEGGNAvLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQI-DGVSWNSVP------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 98 rLPVWR----IITEPVWI------------QKRSSERERRIlaedlAQQVGIR------PEYLDRL----PHAFSGGQRQ 151
Cdd:cd03289 72 -LQKWRkafgVIPQKVFIfsgtfrknldpyGKWSDEEIWKV-----AEEVGLKsvieqfPGQLDFVlvdgGCVLSHGHKQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 152 RIAIARALSSEPDVIVLDEPTSALDiSVQAQILNLLVSlQARRNLTYVLISHNVSVVRHmSDRVAVMYLGQIVELGETQQ 231
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLD-PITYQVIRKTLK-QAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQK 222
|
....*..
gi 740855357 232 VLTHPAH 238
Cdd:cd03289 223 LLNEKSH 229
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-227 |
3.99e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 138 LDRLP-----HAFSGGQRQRIAIARAL---SSEPDVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVSVVR 209
Cdd:PRK00635 798 LDYLPlgrplSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSL-THQGHTVVIIEHNMHVVK 876
|
90
....*....|....*...
gi 740855357 210 hMSDRVavmylgqiVELG 227
Cdd:PRK00635 877 -VADYV--------LELG 885
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-177 |
5.34e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 33 NGLDLQIRQGETLGIVGESGCGKSTLAQLLMGMLQPSQGnySRRDGKQhngMQMVFQDPL-SSLDPRLPVWRIIT---EP 108
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSG--TIKIGET---VKLAYVDQSrDALDPNKTVWEEISgglDI 415
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740855357 109 VWIQKR--SSereRRILAE------DLAQQVGIrpeyldrlphaFSGGQRQRIAIARALSSEPDVIVLDEPTSALDI 177
Cdd:PRK11819 416 IKVGNReiPS---RAYVGRfnfkggDQQKKVGV-----------LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
131-277 |
5.75e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 131 VGIRPEYLDRLPHAFSGGQRQRIAIARALSSE-PDVI-VLDEPTSALDISVQAQILNLLVSLQARRNlTYVLISHNVSVV 208
Cdd:TIGR00630 475 VGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRLRDLGN-TLIVVEHDEDTI 553
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740855357 209 RHmSDRV------AVMYLGQIVELGETQQVLTHPahpytrlllDSVpkTGAPLAEDlvlRKTELPGNRTLPEGCF 277
Cdd:TIGR00630 554 RA-ADYVidigpgAGEHGGEVVASGTPEEILANP---------DSL--TGQYLSGR---KKIEVPAERRPGNGKF 613
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
10-176 |
1.19e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 10 DVHVSFPARKNWLGKVTERVHALNGLDLQIRQGETLGIVGESGCGKSTLAQLLMGM--------------LQPSQGNYSR 75
Cdd:PLN03140 874 NYFVDMPAEMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRktggyiegdirisgFPKKQETFAR 953
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 76 RDG--KQ---HNGMQMVFQDPLSSLDPRLPvwriitepvwiqKRSSERERRILAEDLAQQVgirpeYLDRLPHAFSG--- 147
Cdd:PLN03140 954 ISGycEQndiHSPQVTVRESLIYSAFLRLP------------KEVSKEEKMMFVDEVMELV-----ELDNLKDAIVGlpg 1016
|
170 180 190
....*....|....*....|....*....|....*
gi 740855357 148 ------GQRQRIAIARALSSEPDVIVLDEPTSALD 176
Cdd:PLN03140 1017 vtglstEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
149-221 |
1.19e-04 |
|
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: 42.23 E-value: 1.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740855357 149 QRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLVSLqARRNLTYVLISHNVS-VVRHMSDRVAVMYLG 221
Cdd:cd03232 113 QRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL-ADSGQAILCTIHQPSaSIFEKFDRLLLLKRG 185
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
146-235 |
3.85e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 146 SGGQRQRIAIARALSSEPDVIVLDEPTSALDISVQAQILNLLvslqarrnLTYVLISHNVSVVR---------HMSDRVA 216
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRAL--------KTSANILDTTPLVAiyqcsqdayELFDKVI 282
|
90
....*....|....*....
gi 740855357 217 VMYLGQIVELGETQQVLTH 235
Cdd:TIGR00956 283 VLYEGYQIYFGPADKAKQY 301
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
146-209 |
4.16e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 4.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740855357 146 SGGQRQRIAIARALS---SEPDVIVLDEPTSAL---DISVqaqilnLLVSLQARRNL--TYVLISHNVSVVR 209
Cdd:COG0178 828 SGGEAQRVKLASELSkrsTGKTLYILDEPTTGLhfhDIRK------LLEVLHRLVDKgnTVVVIEHNLDVIK 893
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
41-201 |
4.86e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 40.18 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 41 QGETLGIVGESGCGKSTLAQLLMGMLQPSQGNYSRRDGKQHNGMqmvfqDPLSSLDPRLPVWRIITEPvwIQKRSSERER 120
Cdd:pfam13191 23 RPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPY-----SPLLEALTREGLLRQLLDE--LESSLLEAWR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 121 RILAEDLAQQVGIRPEYLDRLPHAFsggqrQRIAIARALSSEPDVIVLDEptsaLDISVQAQiLNLLVSLQARRNLTYVL 200
Cdd:pfam13191 96 AALLEALAPVPELPGDLAERLLDLL-----LRLLDLLARGERPLVLVLDD----LQWADEAS-LQLLAALLRLLESLPLL 165
|
.
gi 740855357 201 I 201
Cdd:pfam13191 166 V 166
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
146-204 |
1.90e-03 |
|
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: 38.11 E-value: 1.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740855357 146 SGGQRQRIAIARALSS----EPDVIVLDEPTSALDISVQAQILNLLVSLQARRNlTYVLISHN 204
Cdd:cd03227 79 SGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGA-QVIVITHL 140
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
29-64 |
2.16e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.15 E-value: 2.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 740855357 29 VHALNGLDLQ--------IRQGETLGIVGESGCGKSTLAQLLMG 64
Cdd:PRK01889 174 VLAVSALDGEgldvlaawLSGGKTVALLGSSGVGKSTLVNALLG 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-187 |
2.53e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 39.71 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 32 LNGLDLQIRQGETLGIVGESGCGKSTLAQLL-----MGML---------QPSQGNYSRRDG--KQ---HNGMQMVFQDPL 92
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVItggdrlvngRPLDSSFQRSIGyvQQqdlHLPTSTVRESLR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 93 SSLDPRLPVWRIITEpvwiQKRSSERERRILA-EDLAQQ-VGIRPEYLdrlphafSGGQRQRIAIARALSSEPDVIV-LD 169
Cdd:TIGR00956 859 FSAYLRQPKSVSKSE----KMEYVEEVIKLLEmESYADAvVGVPGEGL-------NVEQRKRLTIGVELVAKPKLLLfLD 927
|
170
....*....|....*...
gi 740855357 170 EPTSALDISVQAQILNLL 187
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLM 945
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
29-66 |
3.54e-03 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 38.86 E-value: 3.54e-03
10 20 30
....*....|....*....|....*....|....*...
gi 740855357 29 VHALNGLdLQIRQGETLGIVGESGCGKSTlaqlLMGML 66
Cdd:COG1157 145 VRAIDGL-LTVGRGQRIGIFAGSGVGKST----LLGMI 177
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
29-66 |
5.88e-03 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 37.54 E-value: 5.88e-03
10 20 30
....*....|....*....|....*....|....*...
gi 740855357 29 VHALNGLdLQIRQGETLGIVGESGCGKSTlaqlLMGML 66
Cdd:cd01136 55 VRAIDGL-LTCGEGQRIGIFAGSGVGKST----LLGMI 87
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
146-241 |
6.22e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.13 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 146 SGGQRQRIAIARALSSEPD---VIVLDEPTSAL---DIsvqAQILNLLVSLQARRNlTYVLISHNVSVVRhMSDrvavmY 219
Cdd:PRK00349 832 SGGEAQRVKLAKELSKRSTgktLYILDEPTTGLhfeDI---RKLLEVLHRLVDKGN-TVVVIEHNLDVIK-TAD-----W 901
|
90 100 110
....*....|....*....|....*....|...
gi 740855357 220 L-----------GQIVELGETQQVLTHPaHPYT 241
Cdd:PRK00349 902 IidlgpeggdggGEIVATGTPEEVAKVE-ASYT 933
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
30-69 |
6.65e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.46 E-value: 6.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 740855357 30 HALNGLDLQIRQGETLG-IVGESGCGKSTLAQLLMGMLQPS 69
Cdd:COG3267 30 EALARLEYALAQGGGFVvLTGEVGTGKTTLLRRLLERLPDD 70
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
14-203 |
7.93e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 36.98 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 14 SFPARKNWLGKvtervhalnGLdlqIRQGETLGIVGESGCGKSTLA-QLLMGMLQPSQGNYSRRDGKQHNGMQMVFQDPL 92
Cdd:pfam13481 17 APPPPRRWLIK---------GL---LPAGGLGLLAGAPGTGKTTLAlDLAAAVATGKPWLGGPRVPEQGKVLYVSAEGPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740855357 93 SSLDPRLPVWRiitepvwIQKRSSERERRILAEDLaqqvgIRPEYLDRLPHAFSGGQRQRIAIARAlSSEPDVIVLDEPT 172
Cdd:pfam13481 85 DELRRRLRAAG-------ADLDLPARLLFLSLVES-----LPLFFLDRGGPLLDADVDALEAALEE-VEDPDLVVIDPLA 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 740855357 173 SALDISVQA-----QILNLLVSLQARRNLTYVLISH 203
Cdd:pfam13481 152 RALGGDENSnsdvgRLVKALDRLARRTGATVLLVHH 187
|
|
| |
