|
Name |
Accession |
Description |
Interval |
E-value |
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-324 |
0e+00 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 592.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 1 MTPLPLLEVSKLKMHFD------AGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTN 74
Cdd:COG4608 2 AMAEPLLEVRDLKKHFPvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 75 LHALSEKEQFAFNRKLQMIFQDPYASLNPRMTVREIILEPMEIHNLYnTHKARLLVVDELLEAVGLHPDFGSRYPHEFSG 154
Cdd:COG4608 82 ITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLA-SKAERRERVAELLELVGLRPEHADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 155 GQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEIT 234
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 235 ESGTLYREPLHPYTKALLSSIPIPDPelEDKRERILLKGELPSPVNPPSGCVFRTRCPEAMPECGESRPQLQEIEPGRFV 314
Cdd:COG4608 241 PRDELYARPLHPYTQALLSAVPVPDP--ERRRERIVLEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREVGPGHQV 318
|
330
....*....|
gi 1239365521 315 ACHLYRNAET 324
Cdd:COG4608 319 ACHLAEEGSG 328
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-324 |
0e+00 |
|
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: 503.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDaGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQP---TEGSVVYRGTNLHALSEKE 82
Cdd:COG0444 1 LLEVRNLKVYFP-TRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 83 QFAF-NRKLQMIFQDPYASLNPRMTVREIILEPMEIHNLYNTHKARLLVVdELLEAVGLHP--DFGSRYPHEFSGGQRQR 159
Cdd:COG0444 80 LRKIrGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAI-ELLERVGLPDpeRRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 160 IGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTL 239
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 240 YREPLHPYTKALLSSIPIPDPeleDKRERILLKGELPSPVNPPSGCVFRTRCPEAMPECGESRPQLQEIEPGRFVACHLY 319
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDP---DGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGHRVACHLY 315
|
....*
gi 1239365521 320 RNAET 324
Cdd:COG0444 316 EEEAP 320
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-316 |
6.20e-160 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 449.93 E-value: 6.20e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDA--------GKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLH 76
Cdd:PRK15079 7 VLLEVADLKVHFDIkdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 77 ALSEKEQFAFNRKLQMIFQDPYASLNPRMTVREIILEPMEIhnlYNTHKARLLV---VDELLEAVGLHPDFGSRYPHEFS 153
Cdd:PRK15079 87 GMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRT---YHPKLSRQEVkdrVKAMMLKVGLLPNLINRYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 154 GGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEI 233
Cdd:PRK15079 164 GGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVEL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 234 TESGTLYREPLHPYTKALLSSIPIPDPELEDKRERILLKGELPSPVNPPSGCVFRTRCPEAMPECGESRPQLQeiepGRF 313
Cdd:PRK15079 244 GTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLE----GSF 319
|
....*.
gi 1239365521 314 ---VAC 316
Cdd:PRK15079 320 rhaVSC 325
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-261 |
6.83e-145 |
|
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: 418.54 E-value: 6.83e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQF 84
Cdd:COG1123 259 PLLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFNRKLQMIFQDPYASLNPRMTVREIILEPMEIHNLYNTHKARLLVvDELLEAVGLHPDFGSRYPHEFSGGQRQRIGIAR 164
Cdd:COG1123 339 ELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERV-AELLERVGLPPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 165 ALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREPL 244
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
250
....*....|....*..
gi 1239365521 245 HPYTKALLSSIPIPDPE 261
Cdd:COG1123 498 HPYTRALLAAVPSLDPA 514
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
5-317 |
6.40e-140 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 398.95 E-value: 6.40e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDA-----GKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALS 79
Cdd:PRK11308 4 PLLQAIDLKKHYPVkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 80 EKEQFAFNRKLQMIFQDPYASLNPRMTVREIILEPMEIH-NLynTHKARLLVVDELLEAVGLHPDFGSRYPHEFSGGQRQ 158
Cdd:PRK11308 84 PEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINtSL--SAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 159 RIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGT 238
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 239 LYREPLHPYTKALLSSIPIPDPelEDKRERILLKGELPSPVNPPSGCVFRTRCPEAMPECGESRPQLQEIEpGRFVACH 317
Cdd:PRK11308 242 IFNNPRHPYTQALLSATPRLNP--DDRRERIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYD-GRLVACF 317
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-259 |
6.18e-130 |
|
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: 380.95 E-value: 6.18e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGK---KRTV---KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLyQPTEGSVVYRGTNLHAL 78
Cdd:COG4172 274 PLLEARDLKVWFPIKRglfRRTVghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 79 SEKEQFAFNRKLQMIFQDPYASLNPRMTVREIILEPMEIHNLYNTHKARLLVVDELLEAVGLHPDFGSRYPHEFSGGQRQ 158
Cdd:COG4172 353 SRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQ 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 159 RIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGhmmEITESG- 237
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDG---KVVEQGp 509
|
250 260
....*....|....*....|....
gi 1239365521 238 --TLYREPLHPYTKALLSSIPIPD 259
Cdd:COG4172 510 teQVFDAPQHPYTRALLAAAPLLE 533
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-233 |
7.04e-124 |
|
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: 354.50 E-value: 7.04e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDaGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFA 85
Cdd:cd03257 1 LLEVKNLSVSFP-TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 86 FNRKLQMIFQDPYASLNPRMTVREIILEPMEIHNLYNTHKARLLVVDELLEAVGLHPDFGSRYPHEFSGGQRQRIGIARA 165
Cdd:cd03257 80 RRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 166 LSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEI 233
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-261 |
1.37e-117 |
|
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: 339.09 E-value: 1.37e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDAGKKRtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKeqfA 85
Cdd:COG1124 1 MLEVRNLSVSYGQGGRR-VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK---A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 86 FNRKLQMIFQDPYASLNPRMTVREIILEPMEIHNLYNtHKARllvVDELLEAVGLHPDFGSRYPHEFSGGQRQRIGIARA 165
Cdd:COG1124 77 FRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPD-REER---IAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 166 LSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREPLH 245
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
250
....*....|....*.
gi 1239365521 246 PYTKALLSSIPIPDPE 261
Cdd:COG1124 233 PYTRELLAASLAFERA 248
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-322 |
3.24e-94 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 292.14 E-value: 3.24e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGK------KRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHAL 78
Cdd:PRK10261 312 PILQVRNLVTRFPLRSgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 79 SEKEQFAFNRKLQMIFQDPYASLNPRMTVREIILEPMEIHNLYNTHKARLLVVdELLEAVGLHPDFGSRYPHEFSGGQRQ 158
Cdd:PRK10261 392 SPGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVA-WLLERVGLLPEHAWRYPHEFSGGQRQ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 159 RIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGT 238
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRA 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 239 LYREPLHPYTKALLSSIPIPDPElEDKRERILLKGELPSPVNPpsgcvfRTRCPEAMPecgesrpqLQEIEPGRFVACHL 318
Cdd:PRK10261 551 VFENPQHPYTRKLMAAVPVADPS-RQRPQRVLLSDDLPSNIHL------RGEEVAAVS--------LQCVGPGHYVAQPQ 615
|
....
gi 1239365521 319 YRNA 322
Cdd:PRK10261 616 SEYA 619
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-274 |
2.28e-91 |
|
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: 282.34 E-value: 2.28e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 1 MTPLPLLEVSKLKMHFDAGKkRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQP----TEGSVVYRGTNLH 76
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQGG-GTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 77 ALSEKEQfafnRKLQ-----MIFQDPYASLNPRMTVREIILEPMEIHNLYNTHKARLLVVdELLEAVGLhPDFGSR---Y 148
Cdd:COG4172 80 GLSEREL----RRIRgnriaMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARAL-ELLERVGI-PDPERRldaY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 149 PHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:COG4172 154 PHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQG 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1239365521 229 HMMEITESGTLYREPLHPYTKALLSSIPIPDPELEDKRERILLKGE 274
Cdd:COG4172 234 EIVEQGPTAELFAAPQHPYTRKLLAAEPRGDPRPVPPDAPPLLEAR 279
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-317 |
1.45e-80 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 248.10 E-value: 1.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFdAGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQP---TEGSVVYRGTNLHALSEK 81
Cdd:PRK09473 11 ALLDVKDLRVTF-STPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 82 EqfaFNR----KLQMIFQDPYASLNPRMTVREIILEPMEIHNLYNTHKARLLVVdELLEAVGLhPDFGSR---YPHEFSG 154
Cdd:PRK09473 90 E---LNKlraeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESV-RMLDAVKM-PEARKRmkmYPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 155 GQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEIT 234
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 235 ESGTLYREPLHPYTKALLSSIPIPDPELEdkrERILLKGELPSPVNPPSGCVFRTRCPEAMPECgESRPQLQEIEPGRFV 314
Cdd:PRK09473 245 NARDVFYQPSHPYSIGLLNAVPRLDAEGE---SLLTIPGNPPNLLRLPKGCPFQPRCPHAMEIC-SSAPPLEEFGPGRLR 320
|
...
gi 1239365521 315 ACH 317
Cdd:PRK09473 321 ACF 323
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-254 |
1.16e-78 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 240.89 E-value: 1.16e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGK----KRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLhalsE 80
Cdd:COG4167 3 ALLEVRNLSKTFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL----E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 81 KEQFAFNRKL-QMIFQDPYASLNPRMTVREIILEPMEIhnlyNTH---KARLLVVDELLEAVGLHPDFGSRYPHEFSGGQ 156
Cdd:COG4167 79 YGDYKYRCKHiRMIFQDPNTSLNPRLNIGQILEEPLRL----NTDltaEEREERIFATLRLVGLLPEHANFYPHMLSSGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 157 RQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITES 236
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKT 234
|
250
....*....|....*...
gi 1239365521 237 GTLYREPLHPYTKALLSS 254
Cdd:COG4167 235 AEVFANPQHEVTKRLIES 252
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
6-317 |
1.40e-76 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 237.72 E-value: 1.40e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFdAGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLY----QPTEGSVVYRGTNLHALSEK 81
Cdd:PRK11022 3 LLNVDKLSVHF-GDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 82 EQfafnRKL-----QMIFQDPYASLNPRMTVREIILEPMEIHNLYNtHKARLLVVDELLEAVGLhPDFGSR---YPHEFS 153
Cdd:PRK11022 82 ER----RNLvgaevAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGN-KKTRRQRAIDLLNQVGI-PDPASRldvYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 154 GGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEI 233
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 234 TESGTLYREPLHPYTKALLSSIpipdPEL-EDKRERILLKGELPSPVNPPSGCVFRTRCPEAMPECGESRPQLQEIePGR 312
Cdd:PRK11022 236 GKAHDIFRAPRHPYTQALLRAL----PEFaQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNML-AGR 310
|
....*
gi 1239365521 313 FVACH 317
Cdd:PRK11022 311 QSKCH 315
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-260 |
1.08e-75 |
|
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: 233.54 E-value: 1.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDAG----KKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEK 81
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 82 EQFAFNRKLQMIFQDPYASLNPRMTVREIILEPMEiHNLYNTHKARLLVVDELLEAVGLHPDFGSRYPHEFSGGQRQRIG 161
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLR-HLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 162 IARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYR 241
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
250
....*....|....*....
gi 1239365521 242 EPlHPYTKALLSSIPIPDP 260
Cdd:TIGR02769 241 FK-HPAGRNLQSAVLPEHP 258
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-253 |
2.10e-75 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 240.76 E-value: 2.10e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGK---KRTV---KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYqPTEGSVVYRGTNLHAL 78
Cdd:PRK15134 274 PLLDVEQLQVAFPIRKgilKRTVdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 79 SEKEQFAFNRKLQMIFQDPYASLNPRMTVREIILEPMEIHNLYNTHKARLLVVDELLEAVGLHPDFGSRYPHEFSGGQRQ 158
Cdd:PRK15134 353 NRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQ 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 159 RIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGT 238
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCER 512
|
250
....*....|....*
gi 1239365521 239 LYREPLHPYTKALLS 253
Cdd:PRK15134 513 VFAAPQQEYTRQLLA 527
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-268 |
3.51e-73 |
|
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: 234.80 E-value: 3.51e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 1 MTPLplLEVSKLKMHFDAGkkrTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPT---EGSVVYRGTNLHA 77
Cdd:COG1123 1 MTPL--LEVRDLSVRYPGG---DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 78 LSEKEQfafNRKLQMIFQDPYASLNPrMTVREIILEPMEIHNLynTHKARLLVVDELLEAVGLhPDFGSRYPHEFSGGQR 157
Cdd:COG1123 76 LSEALR---GRRIGMVFQDPMTQLNP-VTVGDQIAEALENLGL--SRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 158 QRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESG 237
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260 270
....*....|....*....|....*....|.
gi 1239365521 238 TLYREPlhpytkALLSSIPIPDPELEDKRER 268
Cdd:COG1123 229 EILAAP------QALAAVPRLGAARGRAAPA 253
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-255 |
1.63e-71 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 222.64 E-value: 1.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 4 LPLLEVSKLKMHFDAG---KKRTVKAV-DGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALS 79
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsGKHQHQTVlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 80 EKEQFAFNRKLQMIFQDPYASLNPRMTVREIILEPMEiHNLYNTHKARLLVVDELLEAVGLHPDFGSRYPHEFSGGQRQR 159
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLR-HLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 160 IGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMME---ITES 236
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqpVGDK 239
|
250
....*....|....*....
gi 1239365521 237 GTLYreplHPYTKALLSSI 255
Cdd:PRK10419 240 LTFS----SPAGRVLQNAV 254
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-325 |
5.18e-68 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 215.92 E-value: 5.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 4 LPLLEVSKLKMHFDAGKKRtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQP----TEGSVVYRGTNLHALS 79
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGR-VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 80 EKEQFAF-NRKLQMIFQDPYASLNPRMTVREIILEPMEIHNL----YNTHKARLLVVDELLEAVGL--HPDFGSRYPHEF 152
Cdd:COG4170 80 PRERRKIiGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFkgkwWQRFKWRKKRAIELLHRVGIkdHKDIMNSYPHEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 153 SGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMME 232
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 233 ITESGTLYREPLHPYTKALLSSIPIPDPELEDKRERILLKGELPSPVNPPSGCVFRTRCPEAMPECGESrPQLQEIEpGR 312
Cdd:COG4170 240 SGPTEQILKSPHHPYTKALLRSMPDFRQPLPHKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVET-PRLRKIK-GH 317
|
330
....*....|...
gi 1239365521 313 FVACHLYRNAETK 325
Cdd:COG4170 318 EFACHFPLNMEEK 330
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-269 |
1.18e-67 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 215.33 E-value: 1.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDaGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAF 86
Cdd:COG1135 2 IELENLSKTFP-TKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDpyASLNPRMTVREIILEPMEIHNLynTHKARLLVVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARAL 166
Cdd:COG1135 81 RRKIGMIFQH--FNLLSSRTVAENVALPLEIAGV--PKAEIRKRVAELLELVGL-SDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 167 SLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGhmmEITESGTLY---REP 243
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENG---RIVEQGPVLdvfANP 232
|
250 260
....*....|....*....|....*.
gi 1239365521 244 LHPYTKALLSSIPIPDPElEDKRERI 269
Cdd:COG1135 233 QSELTRRFLPTVLNDELP-EELLARL 257
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
18-246 |
4.60e-63 |
|
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: 199.73 E-value: 4.60e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 18 AGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAFNRKLQMIFQDp 97
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQH- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 98 YASLNPRmTVREIILEPMEIHNLYNTHKARLlvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADE 177
Cdd:cd03258 91 FNLLSSR-TVFENVALPLEIAGVPKAEIEER--VLELLELVGLE-DKADAYPAQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 178 PISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGhmmEITESGTLYREPLHP 246
Cdd:cd03258 167 ATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKG---EVVEEGTVEEVFANP 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-222 |
1.62e-59 |
|
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: 190.39 E-value: 1.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAGKKRtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAF 86
Cdd:cd03255 1 IELKNLSKTYGGGGEK-VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 -NRKLQMIFQDPYasLNPRMTVREIILEPMEIHNLynTHKARLLVVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARA 165
Cdd:cd03255 80 rRRHIGFVFQSFN--LLPDLTALENVELPLLLAGV--PKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365521 166 LSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHiSDRI 222
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRI 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-222 |
2.49e-59 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 189.87 E-value: 2.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGKkRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQF 84
Cdd:COG1136 3 PLLELRNLTKSYGTGE-GEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AF-NRKLQMIFQDPYasLNPRMTVREIILEPMEIHNLynTHKARLLVVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIA 163
Cdd:COG1136 82 RLrRRHIGFVFQFFN--LLPELTALENVALPLLLAGV--SRKERRERARELLERVGL-GDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 164 RALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHiSDRI 222
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRV 214
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-254 |
2.96e-59 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 191.16 E-value: 2.96e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHF--DAG--KKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGtnlHALSEK 81
Cdd:PRK15112 4 LLEVRNLSKTFryRTGwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 82 EQFAFNRKLQMIFQDPYASLNPRMTVREIILEPMEIhNLYNTHKARLLVVDELLEAVGLHPDFGSRYPHEFSGGQRQRIG 161
Cdd:PRK15112 81 DYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRL-NTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 162 IARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYR 241
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
250
....*....|...
gi 1239365521 242 EPLHPYTKALLSS 254
Cdd:PRK15112 240 SPLHELTKRLIAG 252
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-247 |
5.80e-59 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 193.01 E-value: 5.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 1 MTPlPLLEVSKLKMHFDagkkrTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSe 80
Cdd:COG3842 1 MAM-PALELENVSKRYG-----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 81 keqfAFNRKLQMIFQDpYAsLNPRMTVREIILEPMEIHNLYNTHKARLlvVDELLEAVGLhPDFGSRYPHEFSGGQRQRI 160
Cdd:COG3842 74 ----PEKRNVGMVFQD-YA-LFPHLTVAENVAFGLRMRGVPKAEIRAR--VAELLELVGL-EGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 161 GIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHD----LSMvkhiSDRIGVMYLGHMMEITES 236
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLAL----ADRIAVMNDGRIEQVGTP 220
|
250
....*....|.
gi 1239365521 237 GTLYREPLHPY 247
Cdd:COG3842 221 EEIYERPATRF 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
18-269 |
1.31e-58 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 191.94 E-value: 1.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 18 AGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAFNRKLQMIFQDp 97
Cdd:PRK11153 12 PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQH- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 98 YASLNPRmTVREIILEPMEIHNLYNTH-KARllvVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVAD 176
Cdd:PRK11153 91 FNLLSSR-TVFDNVALPLELAGTPKAEiKAR---VTELLELVGL-SDKADRYPAQLSGGQKQRVAIARALASNPKVLLCD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 177 EPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREPLHPYTKALLSSIp 256
Cdd:PRK11153 166 EATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQST- 244
|
250
....*....|...
gi 1239365521 257 IPDPELEDKRERI 269
Cdd:PRK11153 245 LHLDLPEDYLARL 257
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-238 |
6.74e-58 |
|
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: 186.72 E-value: 6.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDagkKRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQF 84
Cdd:COG1127 4 PMIEVRNLTKSFG---DRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFNRKLQMIFQDP--YASlnprMTVREIILEPMEIHNLYNTHKARLLvVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGI 162
Cdd:COG1127 79 ELRRRIGMLFQGGalFDS----LTVFENVAFPLREHTDLSEAEIREL-VLEKLELVGL-PGAADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365521 163 ARALSLNPEFIVADEPISALD-VSVqAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHmmeITESGT 238
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGK---IIAEGT 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-261 |
1.93e-56 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 191.07 E-value: 1.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHF-DAGKKRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYqPT------EGSVVYRGTN-LH 76
Cdd:PRK15134 4 PLLAIENLSVAFrQQQTVRTV--VNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESlLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 77 ALSEKEQFAFNRKLQMIFQDPYASLNPRMTVREIILEPMEIHNLYNTHKARLLVVDeLLEAVGLHPDFG--SRYPHEFSG 154
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILN-CLDRVGIRQAAKrlTDYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 155 GQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEIT 234
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQN 239
|
250 260
....*....|....*....|....*..
gi 1239365521 235 ESGTLYREPLHPYTKALLSSIPIPDPE 261
Cdd:PRK15134 240 RAATLFSAPTHPYTQKLLNSEPSGDPV 266
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-225 |
1.40e-55 |
|
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: 180.36 E-value: 1.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDaGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALsekeqfaf 86
Cdd:cd03293 1 LEVRNVSKTYG-GGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDPyaSLNPRMTVREIILEPMEIHNLynTHKARLLVVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARAL 166
Cdd:cd03293 72 GPDRGYVFQQD--ALLPWLTVLDNVALGLELQGV--PKAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 167 SLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-238 |
2.95e-54 |
|
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: 177.31 E-value: 2.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDagkKRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAF 86
Cdd:cd03261 1 IELRGLTKSFG---GRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDpyASLNPRMTVREIILEPMEIHNLYNTHKARLLVVdELLEAVGLHPDfGSRYPHEFSGGQRQRIGIARAL 166
Cdd:cd03261 76 RRRMGMLFQS--GALFDSLTVFENVAFPLREHTRLSEEEIREIVL-EKLEAVGLRGA-EDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 167 SLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHmmeITESGT 238
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGK---IVAEGT 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-256 |
5.77e-54 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 186.60 E-value: 5.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDAgKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVV-------YRGTNLHAL 78
Cdd:PRK10261 12 VLAVENLNIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrRRSRQVIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 79 SEKEQFAFNR----KLQMIFQDPYASLNPRMTVREIILEPMEIHNLYNTHKArLLVVDELLEAVGLhPD---FGSRYPHE 151
Cdd:PRK10261 91 SEQSAAQMRHvrgaDMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEA-MVEAKRMLDQVRI-PEaqtILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 152 FSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMM 231
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260
....*....|....*....|....*
gi 1239365521 232 EITESGTLYREPLHPYTKALLSSIP 256
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVP 273
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-256 |
1.39e-53 |
|
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: 176.68 E-value: 1.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAFNRK-LQMIFQDpYAsLNPR 104
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKkISMVFQS-FA-LLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 MTVREIILEPMEIHNLynTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDV 184
Cdd:cd03294 117 RTVLENVAFGLEVQGV--PRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 185 SVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREPLHPYTKALLSSIP 256
Cdd:cd03294 194 LIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVD 265
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-325 |
2.50e-53 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 178.07 E-value: 2.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 4 LPLLEVSKLKMHFDAGKKrTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRL----YQPTEGSVVYRGTNLHALS 79
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDG-WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 80 EKEQfafnRKL-----QMIFQDPYASLNPRMTVREIILEPM-------EIHNLYNTHKARLLvvdELLEAVGL--HPDFG 145
Cdd:PRK15093 80 PRER----RKLvghnvSMIFQEPQSCLDPSERVGRQLMQNIpgwtykgRWWQRFGWRKRRAI---ELLHRVGIkdHKDAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 146 SRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 226 YLGHMMEITESGTLYREPLHPYTKALLSSIPIPDPELEDKRERILLKGELPSPVNPPSGCVFRTRCPEAMPECGESrPQL 305
Cdd:PRK15093 233 YCGQTVETAPSKELVTTPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIET-PRL 311
|
330 340
....*....|....*....|
gi 1239365521 306 QEIEpGRFVACHLYRNAETK 325
Cdd:PRK15093 312 TGAK-NHLYACHFPLNMEEE 330
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-225 |
3.11e-53 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 175.28 E-value: 3.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 1 MTPL-PLLEVSKLKMHFDAGKKRTVkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALS 79
Cdd:COG1116 1 MSAAaPALELRGVSKRFPTGGGGVT-ALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 80 ekeqfafnRKLQMIFQDPyaSLNPRMTVREIILEPMEIHNLynTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQR 159
Cdd:COG1116 80 --------PDRGVVFQEP--ALLPWLTVLDNVALGLELRGV--PKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239365521 160 IGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
25-243 |
9.88e-53 |
|
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: 173.64 E-value: 9.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDpyASLNPR 104
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LRRKIGYVIQQ--IGLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 MTVRE-IILEPMEIHNLYNTHKARllvVDELLEAVGLHPD-FGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISAL 182
Cdd:cd03295 90 MTVEEnIALVPKLLKWPKEKIRER---ADELLALVGLDPAeFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239365521 183 DVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREP 243
Cdd:cd03295 167 DPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
24-225 |
1.47e-51 |
|
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: 169.62 E-value: 1.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 24 VKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfafnRKLQMIFQDPyaSLNP 103
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER-----RNIGMVFQDY--ALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 104 RMTVREIILEPMEIHNLYNTHKARllVVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALD 183
Cdd:cd03259 86 HLTVAENIAFGLKLRGVPKAEIRA--RVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1239365521 184 VSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:cd03259 163 AKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVM 204
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-243 |
1.73e-51 |
|
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: 170.11 E-value: 1.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDagkkrTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSekeqfAF 86
Cdd:cd03300 1 IELENVSKFYG-----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP-----PH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDpYAsLNPRMTVREIILEPMEIHNL-YNTHKARllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARA 165
Cdd:cd03300 71 KRPVNTVFQN-YA-LFPHLTVFENIAFGLRLKKLpKAEIKER---VAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 166 LSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREP 243
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-222 |
6.18e-50 |
|
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: 166.20 E-value: 6.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAGKKrtvkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAF 86
Cdd:cd03256 1 IEVENLSKTYPNGKK----ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDPyaSLNPRMTVREIILEPM-EIHNLYNT-----HKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRI 160
Cdd:cd03256 77 RRQIGMIFQQF--NLIERLSVLENVLSGRlGRRSTWRSlfglfPKEEKQRALAALERVGLL-DKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 161 GIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRI 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-222 |
9.06e-50 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 166.00 E-value: 9.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGKKrtvkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQF 84
Cdd:COG3638 1 PMLELRNLSKRYPGGTP----ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFNRKLQMIFQDPYasLNPRMTVreiilepmeIHN-----LYNTHKARLLV----------VDELLEAVGLhPDFGSRYP 149
Cdd:COG3638 77 RLRRRIGMIFQQFN--LVPRLSV---------LTNvlagrLGRTSTWRSLLglfppedrerALEALERVGL-ADKAYQRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 150 HEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRI 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
24-229 |
1.04e-49 |
|
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: 163.51 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 24 VKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALsEKEQFAFNRKLQMIFQDPyaSLNP 103
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLRRRIGMVFQDF--ALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 104 RMTVREIILEPMeihnlynthkarllvvdelleavglhpdfgsryphefSGGQRQRIGIARALSLNPEFIVADEPISALD 183
Cdd:cd03229 90 HLTVLENIALGL-------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1239365521 184 VSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGH 229
Cdd:cd03229 133 PITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-255 |
1.52e-48 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 162.47 E-value: 1.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHAlSEKEQFA 85
Cdd:COG1126 1 MIEIENLHKSFGD-----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 86 FNRKLQMIFQdpyaSLN--PRMTVRE-IILEPMEIHNLyNTHKARLLVVdELLEAVGLhPDFGSRYPHEFSGGQRQRIGI 162
Cdd:COG1126 75 LRRKVGMVFQ----QFNlfPHLTVLEnVTLAPIKVKKM-SKAEAEERAM-ELLERVGL-ADKADAYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 163 ARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGhmmEITESGT---L 239
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGG---RIVEEGPpeeF 223
|
250
....*....|....*.
gi 1239365521 240 YREPLHPYTKALLSSI 255
Cdd:COG1126 224 FENPQHERTRAFLSKV 239
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-225 |
3.28e-48 |
|
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: 162.14 E-value: 3.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLkmHFDAGKKRtvkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqFA 85
Cdd:COG1120 1 MLEAENL--SVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE-LA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 86 fnRKLQMIFQDPYASLNprMTVREIIL---EPMeiHNLYNTHKAR-LLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIG 161
Cdd:COG1120 75 --RRIAYVPQEPPAPFG--LTVRELVAlgrYPH--LGLFGRPSAEdREAVEEALERTGLE-HLADRPVDELSGGERQRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 162 IARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLL 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
20-229 |
6.76e-48 |
|
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: 159.94 E-value: 6.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 20 KKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDPYA 99
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE---LRRKVGLVFQNPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 100 SL-NPrmTVREIILEPMEihNLYNTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEP 178
Cdd:cd03225 87 QFfGP--TVEEEVAFGLE--NLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1239365521 179 ISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGH 229
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-239 |
1.39e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 160.23 E-value: 1.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEkeqfAF 86
Cdd:COG1131 1 IEVRGLTKRYGD-----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA----EV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDPyaSLNPRMTVREIILEPMEIHNL-YNTHKARllvVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARA 165
Cdd:COG1131 72 RRRIGYVPQEP--ALYPDLTVRENLRFFARLYGLpRKEARER---IDELLELFGL-TDAADRKVGTLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 166 LSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGhmmEITESGTL 239
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKG---RIVADGTP 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
24-225 |
2.19e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 159.42 E-value: 2.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 24 VKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDPYASL-N 102
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE---LRRKVGLVFQNPDDQLfA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 103 PrmTVREII--------LEPMEIhnlynthKARllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIV 174
Cdd:COG1122 91 P--TVEEDVafgpenlgLPREEI-------RER---VEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1239365521 175 ADEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVL 207
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-230 |
3.19e-46 |
|
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: 156.94 E-value: 3.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHalseKEQFA 85
Cdd:COG4555 1 MIEVENLSKKYGK-----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR----KEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 86 FNRKLQMIFQDPYasLNPRMTVREIILEPMEIHNLynTHKARLLVVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARA 165
Cdd:COG4555 72 ARRQIGVLPDERG--LYDRLTVRENIRYFAELYGL--FDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 166 LSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-222 |
4.56e-46 |
|
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: 156.30 E-value: 4.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDAGKKrtvkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFA 85
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ----ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 86 FNRKLQMIFQDpYAsLNPRMTVREIILEP-MEIHNLYNT-----HKARLLVVDELLEAVGLhPDFGSRYPHEFSGGQRQR 159
Cdd:TIGR02315 77 LRRRIGMIFQH-YN-LIERLTVLENVLHGrLGYKPTWRSllgrfSEEDKERALSALERVGL-ADKAYQRADQLSGGQQQR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 160 IGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRI 216
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
9-225 |
7.67e-46 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 157.56 E-value: 7.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 9 VSKlkmHFDAGKKrtvkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNR 88
Cdd:COG1125 7 VTK---RYPDGTV----AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE---LRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 89 K----LQMIfqdpyaSLNPRMTVRE-IILEPM-------EIhnlynthKARllvVDELLEAVGLHPD-FGSRYPHEFSGG 155
Cdd:COG1125 77 RigyvIQQI------GLFPHMTVAEnIATVPRllgwdkeRI-------RAR---VDELLELVGLDPEeYRDRYPHELSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 156 QRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:COG1125 141 QQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-247 |
3.36e-45 |
|
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: 154.03 E-value: 3.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaf 86
Cdd:cd03296 3 IEVRNVSKRFGD-----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 nRKLQMIFQDpYAsLNPRMTVREII-----LEPMEIHNLYNTHKARllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIG 161
Cdd:cd03296 74 -RNVGFVFQH-YA-LFRHMTVFDNVafglrVKPRSERPPEAEIRAK---VHELLKLVQLD-WLADRYPAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 162 IARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYR 241
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
....*.
gi 1239365521 242 EPLHPY 247
Cdd:cd03296 227 HPASPF 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-243 |
1.10e-44 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 155.69 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRG----TNLHALseke 82
Cdd:COG1118 3 IEVRNISKRFGS-----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlfTNLPPR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 83 qfafNRKLQMIFQDpYAsLNPRMTVREIILEPMEIHNLYNTHKARllVVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGI 162
Cdd:COG1118 74 ----ERRVGFVFQH-YA-LFPHMTVAENIAFGLRVRPPSKAEIRA--RVEELLELVQL-EGLADRYPSQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 163 ARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYRE 242
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
.
gi 1239365521 243 P 243
Cdd:COG1118 225 P 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-178 |
1.99e-44 |
|
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: 148.95 E-value: 1.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKeqfAFNRKLQMIFQDPyaSLNPRMT 106
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK---SLRKEIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 107 VREIILEPMEIHNLYNTHK-ARLLVVDELLEAVGLHPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEP 178
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKdARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
42-280 |
3.75e-44 |
|
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: 153.80 E-value: 3.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 42 LVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLhalseKEQFAFNRKLQMIFQDpYAsLNPRMTVREIILEPMEIHNLY 121
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-----TNVPPHLRHINMVFQS-YA-LFPHMTVEENVAFGLKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 122 N-THKARllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKE 200
Cdd:TIGR01187 74 RaEIKPR---VLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 201 KGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREPLHPYTKALLSSIPIPD-PELEDKRERILLKGELPSPV 279
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEaTVIERKSEQVVLAGVEGRRC 229
|
.
gi 1239365521 280 N 280
Cdd:TIGR01187 230 D 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
25-237 |
3.90e-44 |
|
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: 150.79 E-value: 3.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLY-----QPTEGSVVYRGTNLHALSEKEqFAFNRKLQMIFQDPya 99
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDV-LELRRRVGMVFQKP-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 100 slNP-RMTVREIILEPMEIHnLYNTHKARLLVVDELLEAVGLHPDFGSR-YPHEFSGGQRQRIGIARALSLNPEFIVADE 177
Cdd:cd03260 91 --NPfPGSIYDNVAYGLRLH-GIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 178 PISALDVSVQAQVVNLLKRLQKEkgLTFLFIAHDLSMVKHISDRIGVMYLGhmmEITESG 237
Cdd:cd03260 168 PTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNG---RLVEFG 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
23-233 |
4.66e-44 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 150.10 E-value: 4.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 23 TVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfafnRKLQMIFQDpYAsLN 102
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-----RDIAMVFQN-YA-LY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 103 PRMTVREIILEPMEIHNLYN-------THKARLLVVDELLeavglhpdfgSRYPHEFSGGQRQRIGIARALSLNPEFIVA 175
Cdd:cd03301 85 PHMTVYDNIAFGLKLRKVPKdeidervREVAELLQIEHLL----------DRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 176 DEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEI 233
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-230 |
5.92e-44 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 148.70 E-value: 5.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFdaGKKrtvKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHalseKEQFAF 86
Cdd:cd03230 1 IEVRNLSKRY--GKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDPyaSLNPRMTVREIIlepmeihnlynthkarllvvdelleavglhpdfgsryphEFSGGQRQRIGIARAL 166
Cdd:cd03230 72 KRRIGYLPEEP--SLYENLTVRENL---------------------------------------KLSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 167 SLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-228 |
1.77e-43 |
|
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: 149.51 E-value: 1.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfAF 86
Cdd:cd03219 1 LEVRGLTKRFGG-----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE--IA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDPyaSLNPRMTVREIILEPMEIHNLYNTHKARLLV--------VDELLEAVGLHpDFGSRYPHEFSGGQRQ 158
Cdd:cd03219 74 RLGIGRTFQIP--RLFPELTVLENVMVAAQARTGSGLLLARARReerearerAEELLERVGLA-DLADRPAGELSYGQQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 159 RIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-243 |
1.85e-43 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 152.53 E-value: 1.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaf 86
Cdd:COG3839 4 LELENVSKSYGG-----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 nRKLQMIFQDpYAsLNPRMTVREIILEPMEIHNLYNTHKARLlvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARAL 166
Cdd:COG3839 75 -RNIAMVFQS-YA-LYPHMTVYENIAFPLKLRKVPKAEIDRR--VREAAELLGLE-DLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 167 SLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHD----LSMvkhiSDRIGVMYLGHMMEItesGT---L 239
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQV---GTpeeL 221
|
....
gi 1239365521 240 YREP 243
Cdd:COG3839 222 YDRP 225
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
25-249 |
1.91e-43 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 153.08 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKE-QFAFNRKLQMIFQDpyASLNP 103
Cdd:TIGR01186 7 KGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElREVRRKKIGMVFQQ--FALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 104 RMTVRE---IILEPMEIHNLYNTHKARllvvdELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPIS 180
Cdd:TIGR01186 85 HMTILQntsLGPELLGWPEQERKEKAL-----ELLKLVGL-EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 181 ALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREPLHPYTK 249
Cdd:TIGR01186 159 ALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVE 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
24-237 |
2.52e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 148.66 E-value: 2.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 24 VKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAFNRKLQMIFQDpyASLNP 103
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD--FRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 104 RMTVREIILEPMEIHNLynTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALD 183
Cdd:COG2884 93 DRTVYENVALPLRVTGK--SRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 184 VSVQAQVVNLLKRLQKeKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESG 237
Cdd:COG2884 170 PETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARG 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-228 |
3.02e-43 |
|
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: 149.42 E-value: 3.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSekeQF 84
Cdd:COG0411 3 PLLEVRGLTKRFGG-----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP---PH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFNRK-LQMIFQDPyaSLNPRMTVREIILEPMEIHNLYNTHKARLLV-------------VDELLEAVGLHpDFGSRYPH 150
Cdd:COG0411 75 RIARLgIARTFQNP--RLFPELTVLENVLVAAHARLGRGLLAALLRLprarreerearerAEELLERVGLA-DRADEPAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 151 EFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFG 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
28-230 |
3.05e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 148.04 E-value: 3.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 28 DGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDPYAslnPRMTV 107
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE---WRRQVAYVPQEPAL---WGGTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 108 REIILEPMEIHNL-YNTHKARllvvdELLEAVGLHPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSV 186
Cdd:COG4619 91 RDNLPFPFQLRERkFDRERAL-----ELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPEN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1239365521 187 QAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:COG4619 166 TRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
26-247 |
3.51e-43 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 148.79 E-value: 3.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfafnRKLQMIFQDpYAsLNPRM 105
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARD-----RKIGFVFQH-YA-LFKHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 106 TVREIILEPMEI--HNLYNThKARllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALD 183
Cdd:TIGR00968 88 TVRDNIAFGLEIrkHPKAKI-KAR---VEELLELVQLE-GLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 184 VSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREPLHPY 247
Cdd:TIGR00968 163 AKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPF 226
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
20-228 |
3.67e-43 |
|
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: 148.27 E-value: 3.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 20 KKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAF-NRKLQMIFQdpY 98
Cdd:TIGR02211 14 GKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLrNKKLGFIYQ--F 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 99 ASLNPRMTVREIILEPMEIHNLYNTHKARLlvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEP 178
Cdd:TIGR02211 92 HHLLPDFTALENVAMPLLIGKKSVKEAKER--AYEMLEKVGLE-HRINHRPSELSGGERQRVAIARALVNQPSLVLADEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1239365521 179 ISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHIsDRIGVMYLG 228
Cdd:TIGR02211 169 TGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDG 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
22-225 |
4.36e-43 |
|
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: 146.37 E-value: 4.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 22 RTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDPYasL 101
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LRKNIAYVPQDPF--L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 102 nPRMTVREIILepmeihnlynthkarllvvdelleavglhpdfgsryphefSGGQRQRIGIARALSLNPEFIVADEPISA 181
Cdd:cd03228 88 -FSGTIRENIL----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1239365521 182 LDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHiSDRIGVM 225
Cdd:cd03228 127 LDPETEALILEALRALAKGK--TVIVIAHRLSTIRD-ADRIIVL 167
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-271 |
2.11e-41 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 148.06 E-value: 2.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSekeqf 84
Cdd:PRK11607 18 PLLEIRNLTKSFDG-----QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFNRKLQMIFQDpYAsLNPRMTVREIILEPMEIHNLYNTH-KARllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIA 163
Cdd:PRK11607 88 PYQRPINMMFQS-YA-LFPHMTVEQNIAFGLKQDKLPKAEiASR---VNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 164 RALSLNPEFIVADEPISALDVSV----QAQVVNLLKRLqkekGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTL 239
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
250 260 270
....*....|....*....|....*....|..
gi 1239365521 240 YREPLHPYTKALLSSIPIPDPELEDKRERILL 271
Cdd:PRK11607 238 YEHPTTRYSAEFIGSVNVFEGVLKERQEDGLV 269
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
22-238 |
5.27e-41 |
|
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: 151.91 E-value: 5.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 22 RTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDPY--- 98
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS---LRRQIGVVLQDVFlfs 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 99 ASL-------NPRMTVREIIlepmeihnlynthkarllvvdELLEAVGLHpDFGSRYPH-----------EFSGGQRQRI 160
Cdd:COG2274 563 GTIrenitlgDPDATDEEII---------------------EAARLAGLH-DFIEALPMgydtvvgeggsNLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 161 GIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGhmmEITESGT 238
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRL-ADRIIVLDKG---RIVEDGT 692
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-255 |
7.09e-41 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 143.53 E-value: 7.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 1 MTPLPLLEVSKLKMHFDAGKkrtvkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRG-----TNL 75
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRK-----GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 76 HALSEKEQfafnRKLQ-----MIFQDPYASLnpRMTVRE--IILEP-MEI-HNLYNTHKARLLvvdELLEAVGLHPDFGS 146
Cdd:PRK11701 76 YALSEAER----RRLLrtewgFVHQHPRDGL--RMQVSAggNIGERlMAVgARHYGDIRATAG---DWLERVEIDAARID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 147 RYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMY 226
Cdd:PRK11701 147 DLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMK 226
|
250 260 270
....*....|....*....|....*....|..
gi 1239365521 227 LGHmmeITESGTLYR---EPLHPYTKALLSSI 255
Cdd:PRK11701 227 QGR---VVESGLTDQvldDPQHPYTQLLVSSV 255
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-229 |
1.12e-40 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 141.51 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFdaGKKrtvKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHAlSEKEQFAF 86
Cdd:cd03262 1 IEIKNLHKSF--GDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDpyASLNPRMTVRE-IILEPMEIHNLyNTHKARLLVVdELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARA 165
Cdd:cd03262 75 RQKVGMVFQQ--FNLFPHLTVLEnITLAPIKVKGM-SKAEAEERAL-ELLEKVGL-ADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 166 LSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGH 229
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-225 |
1.53e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 145.16 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqf 84
Cdd:COG1129 3 PLLEMRGISKSFGG-----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFNRKLQMIFQDPyaSLNPRMTVREiilepmeihNLY-NTHKARLLVVD---------ELLEAVGLHPDfgsryPH---- 150
Cdd:COG1129 76 AQAAGIAIIHQEL--NLVPNLSVAE---------NIFlGREPRRGGLIDwramrrrarELLARLGLDID-----PDtpvg 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 151 EFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:COG1129 140 DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-236 |
1.67e-39 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 139.11 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 2 TPLPLLEVSKLKMHFDAGKKRtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEK 81
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGE-LTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 82 EQFAF-NRKLQMIFQdpyaS--LNPRMTVREIILEPMEIHNLYNTH-KARllvvdELLEAVGLhpdfGSR---YPHEFSG 154
Cdd:COG4181 83 ARARLrARHVGFVFQ----SfqLLPTLTALENVMLPLELAGRRDARaRAR-----ALLERVGL----GHRldhYPAQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 155 GQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMMEIT 234
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDT 228
|
..
gi 1239365521 235 ES 236
Cdd:COG4181 229 AA 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
25-229 |
3.18e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 135.84 E-value: 3.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFafnRKLQMIFQdpyaslnpr 104
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR---RRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 mtvreiilepmeihnlynthkarllvvdelleavglhpdfgsrypheFSGGQRQRIGIARALSLNPEFIVADEPISALDV 184
Cdd:cd00267 81 -----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1239365521 185 SVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGH 229
Cdd:cd00267 114 ASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
26-238 |
5.21e-39 |
|
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: 144.90 E-value: 5.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKeqfAFNRKLQMIFQDPYasLnPRM 105
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPA---SWRRQIAWVPQNPY--L-FAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 106 TVREIILepmeihnLYNTH--KARLLvvdELLEAVGLHpDFGSRYPH-------E----FSGGQRQRIGIARALSLNPEF 172
Cdd:COG4988 426 TIRENLR-------LGRPDasDEELE---AALEAAGLD-EFVAALPDgldtplgEggrgLSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239365521 173 IVADEPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGHmmeITESGT 238
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGR---IVEQGT 554
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-227 |
5.62e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.91 E-value: 5.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 1 MTPLPLLEVSKLKMHFDagkkrTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSE 80
Cdd:COG1121 1 MMMMPAIELENLTVSYG-----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 81 K-----EQFAFNRKLqmifqdpyaslnPrMTVREIILepMeihNLYNTH-------KARLLVVDELLEAVGLHpDFGSRY 148
Cdd:COG1121 76 RigyvpQRAEVDWDF------------P-ITVRDVVL--M---GRYGRRglfrrpsRADREAVDEALERVGLE-DLADRP 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 149 PHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRigVMYL 227
Cdd:COG1121 137 IGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDR--VLLL 212
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-230 |
6.48e-39 |
|
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: 135.25 E-value: 6.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfAF 86
Cdd:cd03216 1 LELRGITKRFGG-----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--AR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQdpyaslnprmtvreiilepmeihnlynthkarllvvdelleavglhpdfgsrypheFSGGQRQRIGIARAL 166
Cdd:cd03216 74 RAGIAMVYQ--------------------------------------------------------LSVGERQMVEIARAL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 167 SLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:cd03216 98 ARNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-238 |
1.23e-38 |
|
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: 136.59 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 15 HFDAGKKRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIF 94
Cdd:cd03254 9 NFSYDEKKPV--LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS---LRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 95 QDPYasLNPRmTVREIIlepmeihnLYNTHKARLLVVDELLEAVGLHpDFGSRYP-----------HEFSGGQRQRIGIA 163
Cdd:cd03254 84 QDTF--LFSG-TIMENI--------RLGRPNATDEEVIEAAKEAGAH-DFIMKLPngydtvlgengGNLSQGERQLLAIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 164 RALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGhmmEITESGT 238
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDG---KIIEEGT 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
25-242 |
2.01e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 143.38 E-value: 2.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKE---QFAfnrklqMIFQDPY--A 99
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrrQIG------VVPQDTFlfS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 100 slnprMTVREiilepmeihNL-YNTHKARLLVVDELLEAVGLHpDFGSRYPH-----------EFSGGQRQRIGIARALS 167
Cdd:COG1132 428 -----GTIRE---------NIrYGRPDATDEEVEEAAKAAQAH-EFIEALPDgydtvvgergvNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 168 LNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGhmmEITESGT--------- 238
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRN-ADRILVLDDG---RIVEQGTheellargg 566
|
....
gi 1239365521 239 LYRE 242
Cdd:COG1132 567 LYAR 570
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-230 |
2.74e-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: 134.10 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 21 KRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfafnrklqmifqdpyas 100
Cdd:cd03214 11 GRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 101 lnprmtvreiilepmeihnlynthKARLL-VVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPI 179
Cdd:cd03214 71 ------------------------LARKIaYVPQALELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1239365521 180 SALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-243 |
6.44e-38 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 138.54 E-value: 6.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDagkkrTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSekeqf 84
Cdd:PRK09452 13 PLVELRGISKSFD-----GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFNRKLQMIFQDpYAsLNPRMTVREIILEPMEIHNLYNTH-KARllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIA 163
Cdd:PRK09452 83 AENRHVNTVFQS-YA-LFPHMTVFENVAFGLRMQKTPAAEiTPR---VMEALRMVQLE-EFAQRKPHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 164 RALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHD----LSMvkhiSDRIGVMYLGHMMEITESGTL 239
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM----SDRIVVMRDGRIEQDGTPREI 232
|
....
gi 1239365521 240 YREP 243
Cdd:PRK09452 233 YEEP 236
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-255 |
1.04e-37 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 134.96 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGKkrtvkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRG-----TNLHALS 79
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGK-----GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaeLELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 80 EKEQFAFNR-KLQMIFQDPYASLnpRMTVR---EIILEPMEIHNlynTHKARL-LVVDELLEAVGLHPDFGSRYPHEFSG 154
Cdd:TIGR02323 77 EAERRRLMRtEWGFVHQNPRDGL--RMRVSagaNIGERLMAIGA---RHYGNIrATAQDWLEEVEIDPTRIDDLPRAFSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 155 GQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEIT 234
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
250 260
....*....|....*....|.
gi 1239365521 235 ESGTLYREPLHPYTKALLSSI 255
Cdd:TIGR02323 232 LTDQVLDDPQHPYTQLLVSSI 252
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
25-229 |
6.71e-37 |
|
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: 133.35 E-value: 6.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAFNRKLQMIFQDPYASLNpR 104
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPEHQLF-E 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 MTV-REIILEPMeihNL-YNTHKARLLVvDELLEAVGLHPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISAL 182
Cdd:TIGR04521 98 ETVyKDIAFGPK---NLgLSEEEAEERV-KEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1239365521 183 DVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGH 229
Cdd:TIGR04521 174 DPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGK 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
36-225 |
9.91e-37 |
|
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: 131.26 E-value: 9.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 36 EGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGT-------NLHALSEKeqfafnRKLQMIFQDpyASLNPRMTVR 108
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkKINLPPQQ------RKIGLVFQQ--YALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 109 EIILEPMEIHnlynTHKARLLVVDELLEAVGLHPdFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQA 188
Cdd:cd03297 94 ENLAFGLKRK----RNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 1239365521 189 QVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
27-254 |
3.58e-36 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 130.98 E-value: 3.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQP----TEGSVVYRGTNLHALSEKeqfafNRKLQMIFQDPYASLN 102
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR-----GRKIATIMQNPRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 103 PRMTVREIILEPMEIHNLYNThKARLLvvdELLEAVGLH--PDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPIS 180
Cdd:PRK10418 94 PLHTMHTHARETCLALGKPAD-DATLT---AALEAVGLEnaARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 181 ALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREPLHPYTKALLSS 254
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
30-238 |
7.01e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 129.75 E-value: 7.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNL---HALSEKEQFAFNRKLQMIFQDpYaSLNPRMT 106
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELRRNVGMVFQQ-Y-NLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 107 VREIILE-PMEIHNLYNTH-KARllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDV 184
Cdd:PRK11124 99 VQQNLIEaPCRVLGLSKDQaLAR---AEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 185 SVQAQVVNLLKRLQkEKGLTFLFIAHDLSMVKHISDRIGVMYLGHmmeITESGT 238
Cdd:PRK11124 175 EITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGH---IVEQGD 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-219 |
3.59e-35 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 127.62 E-value: 3.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGKKRTvKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQF 84
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSVQT-DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AF-NRKLQMIFQdpYASLNPRMTVREIILEPMEIHNLYN---THKARllvvdELLEAVGLHPDFGSRyPHEFSGGQRQRI 160
Cdd:PRK11629 83 ELrNQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKKPaeiNSRAL-----EMLAAVGLEHRANHR-PSELSGGERQRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 161 GIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHIS 219
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-228 |
4.20e-35 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 127.10 E-value: 4.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDagkkrTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLhalsEKEQFAF 86
Cdd:cd03265 1 IEVENLVKKYG-----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV----VREPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDPyaSLNPRMTVREiilePMEIH-NLYNTHKARLLV-VDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIAR 164
Cdd:cd03265 72 RRRIGIVFQDL--SVDDELTGWE----NLYIHaRLYGVPGAERRErIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 165 ALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:cd03265 145 SLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-257 |
4.51e-35 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 131.69 E-value: 4.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAFNRK-LQMIFQDpyASLNPR 104
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQS--FALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 MTVREIILEPMEIHNLYNTHKARLLVvdELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDV 184
Cdd:PRK10070 121 MTVLDNTAFGMELAGINAEERREKAL--DALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 185 SVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREPLHPYTKALLSSIPI 257
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDI 270
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
26-222 |
9.58e-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: 126.11 E-value: 9.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGtnlhalseKEQFAFNRKLQMIFQDPYASLNPRM 105
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG--------KPLEKERKRIGYVPQRRSIDRDFPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 106 TVREIILEPMEIH-----NLYNTHKARllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPIS 180
Cdd:cd03235 86 SVRDVVLMGLYGHkglfrRLSKADKAK---VDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1239365521 181 ALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRI 222
Cdd:cd03235 162 GVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRV 202
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
27-233 |
1.45e-34 |
|
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: 126.30 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALS-EKEQFAFnrklqmIFQDpYAsLNPRM 105
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPpEKRDISY------VPQN-YA-LFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 106 TVREIILEPMeIHNLYNTHK--------ARLLVVDELLEavglhpdfgsRYPHEFSGGQRQRIGIARALSLNPEFIVADE 177
Cdd:cd03299 87 TVYKNIAYGL-KKRKVDKKEierkvleiAEMLGIDHLLN----------RKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239365521 178 PISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEI 233
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-238 |
3.17e-34 |
|
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: 125.04 E-value: 3.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 21 KRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHAL---SEKEQFAFNRKLQMIFQDp 97
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYtlaSLRRQIGLVSQDVFLFND- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 98 yaslnprmTVREIIlepmeihnLYNTHKARLLVVDELLEAVGLHpDFGSRYPHEF-----------SGGQRQRIGIARAL 166
Cdd:cd03251 91 --------TVAENI--------AYGRPGATREEVEEAARAANAH-EFIMELPEGYdtvigergvklSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 167 SLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGhmmEITESGT 238
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDG---KIVERGT 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-253 |
1.27e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.38 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFdaGKKrtvKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLY--QP---TEGSVVYRGTNLHAlS 79
Cdd:COG1117 10 PKIEVRNLNVYY--GDK---QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPgarVEGEILLDGEDIYD-P 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 80 EKEQFAFNRKLQMIFQDPyaslNP-RMTVREIILEPMEIHNLYNthKARLlvvDEL----LEAVG--------LHpdfgs 146
Cdd:COG1117 84 DVDVVELRRRVGMVFQKP----NPfPKSIYDNVAYGLRLHGIKS--KSEL---DEIveesLRKAAlwdevkdrLK----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 147 RYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALD-VSVqAQVVNLLKRLQKEkgLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:COG1117 150 KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpIST-AKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFF 226
|
250 260
....*....|....*....|....*...
gi 1239365521 226 YLGHMMEITESGTLYREPLHPYTKALLS 253
Cdd:COG1117 227 YLGELVEFGPTEQIFTNPKDKRTEDYIT 254
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-238 |
1.30e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 124.74 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGKKRtvkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTnlhALSEKEQF 84
Cdd:PRK13635 4 EIIRVEHISFRYPDAATY---ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFNRKLQMIFQdpyaslNPR-----MTVREIILEPMEIHNLynTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQR 159
Cdd:PRK13635 78 DVRRQVGMVFQ------NPDnqfvgATVQDDVAFGLENIGV--PREEMVERVDQALRQVGME-DFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 160 IGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLGhmmEITESGT 238
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKG---EILEEGT 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
21-243 |
2.34e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 125.99 E-value: 2.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 21 KRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKeqfafNRKLQMIFQDpYAs 100
Cdd:PRK11432 18 SNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-----QRDICMVFQS-YA- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 101 LNPRMTVREIILEPMEIHNLYNTH-KARllvVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPI 179
Cdd:PRK11432 89 LFPHMSLGENVGYGLKMLGVPKEErKQR---VKEALELVDL-AGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 180 SALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREP 243
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-238 |
4.66e-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: 4.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 15 HFDAGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIF 94
Cdd:cd03249 7 SFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRW---LRSQIGLVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 95 QDP--YAslnprMTVREIIlepmeihnLYNTHKARLLVVDELLEAVGLHpDFGSRYPHEF-----------SGGQRQRIG 161
Cdd:cd03249 84 QEPvlFD-----GTIAENI--------RYGKPDATDEEVEEAAKKANIH-DFIMSLPDGYdtlvgergsqlSGGQKQRIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365521 162 IARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQkeKGLTFLFIAHDLSMVKHiSDRIGVMYLGHmmeITESGT 238
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRN-ADLIAVLQNGQ---VVEQGT 220
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-232 |
5.55e-33 |
|
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: 121.17 E-value: 5.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFdaGKKRtvkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKeqfaf 86
Cdd:cd03268 1 LKTNDLTKTY--GKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDPyaSLNPRMTVREiilepmeihNLYNTHKARLL---VVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIA 163
Cdd:cd03268 71 LRRIGALIEAP--GFYPNLTARE---------NLRLLARLLGIrkkRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 164 RALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMME 232
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
22-243 |
5.67e-33 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 125.11 E-value: 5.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 22 RTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQP--TEGSVVYRGTNL-HALSEKeqfafnRKLQMIFQDpY 98
Cdd:TIGR03258 18 NTV--LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLtHAPPHK------RGLALLFQN-Y 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 99 AsLNPRMTVREIILEPMEIHNLYNTHKARLlvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEP 178
Cdd:TIGR03258 89 A-LFPHLKVEDNVAFGLRAQKMPKADIAER--VADALKLVGLG-DAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239365521 179 ISALDVSVQAQVVNLLKRLQKE-KGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREP 243
Cdd:TIGR03258 165 LSALDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAP 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-238 |
1.50e-32 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 126.80 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGKKrtvKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQF 84
Cdd:COG4987 332 PSLELEDVSFRYPGAGR---PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 afnRKLQMIFQDPY--ASlnprmTVREiilepmeihNLynthkarLLVV-----DEL---LEAVGLHpDFGSRYPH---- 150
Cdd:COG4987 409 ---RRIAVVPQRPHlfDT-----TLRE---------NL-------RLARpdatdEELwaaLERVGLG-DWLAALPDgldt 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 151 -------EFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHIsDRIG 223
Cdd:COG4987 464 wlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERM-DRIL 540
|
250
....*....|....*
gi 1239365521 224 VMYLGHmmeITESGT 238
Cdd:COG4987 541 VLEDGR---IVEQGT 552
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
30-238 |
2.19e-32 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 120.50 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNL---HALSEKEQFAFNRKLQMIFQDpYaSLNPRMT 106
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQQ-Y-NLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 107 VREIILE-PMEIHNLynTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVS 185
Cdd:COG4161 99 VMENLIEaPCKVLGL--SKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 186 VQAQVVNLLKRLQkEKGLTFLFIAHDLSMVKHISDRIGVMYLGHmmeITESGT 238
Cdd:COG4161 176 ITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGR---IIEQGD 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-225 |
2.36e-32 |
|
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: 120.00 E-value: 2.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 24 VKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNlhalsekeqfafnrklqmifqdpYASLNP 103
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTD-----------------------IRQLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 104 RMTVREIILEPMEIHNLYNTHK-----ARLLVVDE-LLEAV---GLHpDFGSRYPHEF-----------SGGQRQRIGIA 163
Cdd:cd03245 74 ADLRRNIGYVPQDVTLFYGTLRdnitlGAPLADDErILRAAelaGVT-DFVNKHPNGLdlqigergrglSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 164 RALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKhISDRIGVM 225
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLD-LVDRIIVM 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-230 |
2.65e-32 |
|
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: 119.43 E-value: 2.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 23 TVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAFNRKLQMIFQDpyASLN 102
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 103 PRMTVREIILEPMEIhnLYNTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISAL 182
Cdd:cd03292 91 PDRNVYENVAFALEV--TGVPPREIRKRVPAALELVGLS-HKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239365521 183 DVSVQAQVVNLLKRLQKeKGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:cd03292 168 DPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-225 |
2.85e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 125.52 E-value: 2.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqf 84
Cdd:COG3845 4 PALELRGITKRFGG-----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFNRKLQMIFQDPyaSLNPRMTVRE-IIL--EPMEIHNLyNTHKARLLvVDELLEAVGLH--PDfgsRYPHEFSGGQRQR 159
Cdd:COG3845 77 AIALGIGMVHQHF--MLVPNLTVAEnIVLglEPTKGGRL-DRKAARAR-IRELSERYGLDvdPD---AKVEDLSVGEQQR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 160 IGIARALSLNPEFIVADEPISALdvsVQAQVVNL---LKRLqKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVL---TPQEADELfeiLRRL-AAEGKSIIFITHKLREVMAIADRVTVL 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-253 |
3.84e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 120.46 E-value: 3.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFdaGKKRTVKavdGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLH---------A 77
Cdd:PRK10619 6 LNVIDLHKRY--GEHEVLK---GVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 78 LSEKEQFAFNR-KLQMIFQdpYASLNPRMTVREIILE-PMEIHNLyNTHKARLLVVdELLEAVGLHPDFGSRYPHEFSGG 155
Cdd:PRK10619 81 VADKNQLRLLRtRLTMVFQ--HFNLWSHMTVLENVMEaPIQVLGL-SKQEARERAV-KYLAKVGIDERAQGKYPVHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 156 QRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITE 235
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
250
....*....|....*...
gi 1239365521 236 SGTLYREPLHPYTKALLS 253
Cdd:PRK10619 236 PEQLFGNPQSPRLQQFLK 253
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-211 |
4.38e-32 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 118.74 E-value: 4.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDagkKRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEkeqf 84
Cdd:COG4133 1 MMLEAENLSCRRG---ERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFNRKLQMIFqdPYASLNPRMTVREiilepmeihNL------YNTHKARLLVvDELLEAVGLHPdFGSRYPHEFSGGQRQ 158
Cdd:COG4133 72 DYRRRLAYLG--HADGLKPELTVRE---------NLrfwaalYGLRADREAI-DEALEAVGLAG-LADLPVRQLSAGQKR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 159 RIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRlQKEKGLTFLFIAHD 211
Cdd:COG4133 139 RVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-233 |
6.42e-32 |
|
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: 124.53 E-value: 6.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYR-GTNLHALSEK-- 81
Cdd:TIGR03269 278 PIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPgp 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 82 -EQFAFNRKLQMIFQDpyASLNPRMTVREIILEPMEIHNLYNTHKARLLVVdelLEAVGLHPDFG----SRYPHEFSGGQ 156
Cdd:TIGR03269 358 dGRGRAKRYIGILHQE--YDLYPHRTVLDNLTEAIGLELPDELARMKAVIT---LKMVGFDEEKAeeilDKYPDELSEGE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365521 157 RQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEI 233
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-238 |
1.53e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.41 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDAGkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLhALSEKEQFA 85
Cdd:PRK13639 1 ILETRDLKYSYPDG----TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 86 FNRKLQMIFQDPYASLNPRMTVREIILEPMeihNLYNTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARA 165
Cdd:PRK13639 76 VRKTVGIVFQNPDDQLFAPTVEEDVAFGPL---NLGLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 166 LSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGhmmEITESGT 238
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDG---KIIKEGT 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-228 |
2.07e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 116.97 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 13 KMHFDAGKKRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHAlseKEQFafnRKLQM 92
Cdd:cd03226 4 NISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERR---KSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 93 IFQDPYASLNpRMTVR-EIILEPMEIHNLYNThkarllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPE 171
Cdd:cd03226 76 VMQDVDYQLF-TDSVReELLLGLKELDAGNEQ-------AETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365521 172 FIVADEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRigVMYLG 228
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDR--VLLLA 200
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
22-238 |
2.79e-31 |
|
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: 123.29 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 22 RTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHAL---SEKEQFAFNRKLQMIFQDPY 98
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYtlaSLRRQVALVSQDVVLFNDTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 99 ASlN-----PRMTVREIILEPMEIHNLYNthkarllVVDELLEavGLHPDFGSRyPHEFSGGQRQRIGIARALSLNPEFI 173
Cdd:TIGR02203 423 AN-NiaygrTEQADRAEIERALAAAYAQD-------FVDKLPL--GLDTPIGEN-GVLLSGGQRQRLAIARALLKDAPIL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 174 VADEPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGhmmEITESGT 238
Cdd:TIGR02203 492 ILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVVMDDG---RIVERGT 550
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
27-233 |
2.80e-31 |
|
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: 117.18 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGtnlhalseKEQFAFNRKLQMIFQDpyASLNPRMT 106
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG--------KQITEPGPDRMVVFQN--YSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 107 VREIILEPMEIHNLYNTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSV 186
Cdd:TIGR01184 71 VRENIALAVDRVLPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 187 QAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVM------YLGHMMEI 233
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILEV 202
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
26-238 |
4.08e-31 |
|
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: 117.20 E-value: 4.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLhALSEKEqfAFNRKLQMIFQ---------- 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL-ALADPA--WLRRQVGVVLQenvlfnrsir 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 96 DPYASLNPRMTVREIILEP---------MEIHNLYNThkarllVVDEllEAVGLhpdfgsryphefSGGQRQRIGIARAL 166
Cdd:cd03252 94 DNIALADPGMSMERVIEAAklagahdfiSELPEGYDT------IVGE--QGAGL------------SGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 167 SLNPEFIVADEPISALDVSVQAQVVNLLKRLQkeKGLTFLFIAHDLSMVKHiSDRIGVMYLGhmmEITESGT 238
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKN-ADRIIVMEKG---RIVEQGS 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-211 |
4.45e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 117.66 E-value: 4.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDaGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEkeqf 84
Cdd:COG4525 2 SMLTVRHVSVRYP-GGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 afNRKLqmIFQDpyASLNPRMTVREIILEPMEIHNLynTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIAR 164
Cdd:COG4525 77 --DRGV--VFQK--DALLPWLNVLDNVAFGLRLRGV--PKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1239365521 165 ALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHD 211
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
41-247 |
5.55e-31 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 119.45 E-value: 5.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 41 GLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHAlSEKEQF--AFNRKLQMIFQDpyASLNPRMTVREIILEPMEih 118
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD-SRKGIFlpPEKRRIGYVFQE--ARLFPHLSVRGNLRYGMK-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 119 nlYNTHKARLLVVDELLEAVGLHPDFGsRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQ 198
Cdd:TIGR02142 102 --RARPSERRISFERVIELLGIGHLLG-RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1239365521 199 KEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREPLHPY 247
Cdd:TIGR02142 179 AEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
25-225 |
6.20e-31 |
|
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: 123.05 E-value: 6.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDP---YASL 101
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAD---LRRNIGYVPQDPrlfYGTL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 102 nprmtvREiilepmeihNLynTHKARLLVVDELLEAV---GLHpDFGSRYPHEF-----------SGGQRQRIGIARALS 167
Cdd:TIGR03375 556 ------RD---------NI--ALGAPYADDEEILRAAelaGVT-EFVRRHPDGLdmqigergrslSGGQRQAVALARALL 617
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 168 LNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKhISDRIGVM 225
Cdd:TIGR03375 618 RDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLLD-LVDRIIVM 672
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-243 |
6.83e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 119.42 E-value: 6.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDagkkRTvKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaf 86
Cdd:PRK10851 3 IEIANIKKSFG----RT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 nRKLQMIFQDpYAsLNPRMTVREII---LEPMEIHNLYNTHKARLLVVdELLEAVGLhPDFGSRYPHEFSGGQRQRIGIA 163
Cdd:PRK10851 74 -RKVGFVFQH-YA-LFRHMTVFDNIafgLTVLPRRERPNAAAIKAKVT-QLLEMVQL-AHLADRYPAQLSGGQKQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 164 RALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREP 243
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-228 |
7.02e-31 |
|
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: 115.93 E-value: 7.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDAgKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHalseKEQFA 85
Cdd:cd03266 1 MITADALTKRFRD-VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 86 FNRKLQMIFQDpyASLNPRMTVREIILEPMEIHNLYNTH-KARllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIAR 164
Cdd:cd03266 76 ARRRLGFVSDS--TGLYDRLTARENLEYFAGLYGLKGDElTAR---LEELADRLGME-ELLDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 165 ALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
8-238 |
1.57e-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: 121.35 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 8 EVSKLKMHFDAGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFN 87
Cdd:TIGR02204 337 EIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAE---LR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 88 RKLQMIFQDP---YASL-------NPRMTVREIILepmeihnlynthKARLLVVDELLEAV--GLHPDFGSRyPHEFSGG 155
Cdd:TIGR02204 414 ARMALVPQDPvlfAASVmenirygRPDATDEEVEA------------AARAAHAHEFISALpeGYDTYLGER-GVTLSGG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 156 QRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGhmmEITE 235
Cdd:TIGR02204 481 QRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGR--TTLIIAHRLATVLK-ADRIVVMDQG---RIVA 554
|
...
gi 1239365521 236 SGT 238
Cdd:TIGR02204 555 QGT 557
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-222 |
2.44e-30 |
|
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: 114.84 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 1 MTPLplLEVSKL----KMHFDAGKKRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYR----G 72
Cdd:COG4778 1 MTTL--LEVENLsktfTLHLQGGKRLPV--LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 73 TNLHALSEKE-------------QFafnrkLQMIfqdpyaslnPRMTVREIILEPMeIHNLYNTHKARLLVvDELLEAVG 139
Cdd:COG4778 77 VDLAQASPREilalrrrtigyvsQF-----LRVI---------PRVSALDVVAEPL-LERGVDREEARARA-RELLARLN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 140 LHPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHIS 219
Cdd:COG4778 141 LPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVA 219
|
...
gi 1239365521 220 DRI 222
Cdd:COG4778 220 DRV 222
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
26-225 |
3.99e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.57 E-value: 3.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGtnLHALSEKEQFAFNRKLQMIFQDPYASLnprm 105
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIRNKAGMVFQNPDNQI---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 106 tVREII------------LEPMEIhnlynthKARllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFI 173
Cdd:PRK13633 99 -VATIVeedvafgpenlgIPPEEI-------RER---VDESLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 174 VADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHiSDRIGVM 225
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVM 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
25-238 |
5.09e-30 |
|
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: 114.25 E-value: 5.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLhalSEKEQFAFNRKLQMIFQDpyaslnpr 104
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI---REVTLDSLRRAIGVVPQD-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 mTV--REIILepmeihnlYNTHKARLLVVDELLEAV----GLHpDFGSRYPHEF-----------SGGQRQRIGIARALS 167
Cdd:cd03253 84 -TVlfNDTIG--------YNIRYGRPDATDEEVIEAakaaQIH-DKIMRFPDGYdtivgerglklSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239365521 168 LNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGhmmEITESGT 238
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDG---RIVERGT 218
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
229-318 |
6.92e-30 |
|
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: 108.99 E-value: 6.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 229 HMMEITESGTLYREPLHPYTKALLSSIPIPDpelEDKRERILLKGELPSPVNPPSGCVFRTRCPEAMPECGESRPQLQEI 308
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIK---KRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEI 77
|
90
....*....|
gi 1239365521 309 EPGRFVACHL 318
Cdd:TIGR01727 78 AEGHRVACHL 87
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
6-222 |
8.10e-30 |
|
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: 113.25 E-value: 8.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLK----MHFDAGKKRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYR----GTNLHA 77
Cdd:TIGR02324 1 LLEVEDLSktftLHQQGGVRLPV--LKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRhegaWVDLAQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 78 LSEKEQFAFnRKLQMIFQDPYASLNPRMTVREIILEPMeIHNLYNTHKARLlVVDELLEAVGLHPDFGSRYPHEFSGGQR 157
Cdd:TIGR02324 79 ASPREVLEV-RRKTIGYVSQFLRVIPRVSALEVVAEPL-LERGVPREAARA-RARELLARLNIPERLWHLPPATFSGGEQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 158 QRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:TIGR02324 156 QRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEA-KARGAALIGIFHDEEVRELVADRV 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6-225 |
1.30e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 114.06 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDagKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGtnlHALSEKEQFA 85
Cdd:PRK13650 4 IIEVKNLTFKYK--EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 86 FNRKLQMIFQDPYASLnPRMTVREIILEPMEIHNL-YNTHKARllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIAR 164
Cdd:PRK13650 79 IRHKIGMVFQNPDNQF-VGATVEDDVAFGLENKGIpHEEMKER---VNEALELVGMQ-DFKEREPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239365521 165 ALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKhISDRIGVM 225
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVM 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-231 |
1.61e-29 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 112.21 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFdagKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHalseKEQFAF 86
Cdd:cd03263 1 LQIRNLTKTY---KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDpyASLNPRMTVREIILEPMEIHNLYNTHKArlLVVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARAL 166
Cdd:cd03263 74 RQSLGYCPQF--DALFDELTVREHLRFYARLKGLPKSEIK--EEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 167 SLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHISDRIGVMYLGHMM 231
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
31-222 |
2.26e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 112.16 E-value: 2.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 31 TFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfafnRKLQMIFQDpyASLNPRMTVREI 110
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-----RPVSMLFQE--NNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 111 I---LEP-MeihNLYNTHKARllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSV 186
Cdd:COG3840 92 IglgLRPgL---KLTAEQRAQ---VEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPAL 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 1239365521 187 QAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:COG3840 165 RQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRV 200
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-253 |
2.84e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 112.54 E-value: 2.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 4 LPLLEVSKLKMHFdagKKRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHA-LSEKE 82
Cdd:PRK11264 1 MSAIEVKNLVKKF---HGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTaRSLSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 83 QFAFNRKLQ----MIFQDpyASLNPRMTVREIILE-PMEIHNlyNTHKARLLVVDELLEAVGLHPDfGSRYPHEFSGGQR 157
Cdd:PRK11264 76 QKGLIRQLRqhvgFVFQN--FNLFPHRTVLENIIEgPVIVKG--EPKEEATARARELLAKVGLAGK-ETSYPRRLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 158 QRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKgLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESG 237
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
|
250
....*....|....*.
gi 1239365521 238 TLYREPLHPYTKALLS 253
Cdd:PRK11264 230 ALFADPQQPRTRQFLE 245
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-242 |
3.57e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 113.34 E-value: 3.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALS-EKEQFAFNRKLQMIFQDPYASLNP 103
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkDKYIRPVRKRIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 104 RMTVREIILEP----MEIHNLynthKARLLvvdELLEAVGLHPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPI 179
Cdd:PRK13646 101 DTVEREIIFGPknfkMNLDEV----KNYAH---RLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 180 SALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYRE 242
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-229 |
5.22e-29 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 110.75 E-value: 5.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFdaGKKRtvkAVDGVTFQIREGeTFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGtnlHALSEKEQfAF 86
Cdd:cd03264 1 LQLENLTKRY--GKKR---ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG---QDVLKQPQ-KL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDPyaSLNPRMTVREIiLEPMEIhnLYNTHKARL-LVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARA 165
Cdd:cd03264 71 RRRIGYLPQEF--GVYPNFTVREF-LDYIAW--LKGIPSKEVkARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 166 LSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHISDRIGVMYLGH 229
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-237 |
6.47e-29 |
|
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: 110.70 E-value: 6.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 10 SKLKMHFDAGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGtNLHALsekeqFAFNrk 89
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSL-----LGLG-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 90 lqmifqdpyASLNPRMTVREIILEPMEIHNLynTHKARLLVVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARALSLN 169
Cdd:cd03220 93 ---------GGFNPELTGRENIYLNGRLLGL--SRKEIDEKIDEIIEFSEL-GDFIDLPVKTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 170 PEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGhmmEITESG 237
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKG---KIRFDG 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-240 |
1.00e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 111.72 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDagKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHAlseKEQFA 85
Cdd:PRK13642 4 ILEVENLVFKYE--KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 86 FNRKLQMIFQDPYASLnPRMTVREIILEPMEIHNLynTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARA 165
Cdd:PRK13642 79 LRRKIGMVFQNPDNQF-VGATVEDDVAFGMENQGI--PREEMIKRVDEALLAVNML-DFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 166 LSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMMEITESGTLY 240
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-253 |
1.85e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 110.64 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFdaGKKrtvKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRL--YQP---TEGSVVYRGTNLHAlS 79
Cdd:PRK14239 4 PILQVSDLSVYY--NKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYS-P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 80 EKEQFAFNRKLQMIFQDPyaslNP-RMTVREIILEPMEIHNLYNthKARL-LVVDELLEAVGLHPDFGSRYpHE----FS 153
Cdd:PRK14239 78 RTDTVDLRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIKD--KQVLdEAVEKSLKGASIWDEVKDRL-HDsalgLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 154 GGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEkgLTFLFIAHDLSMVKHISDRIGVMYLGHMMEI 233
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEY 228
|
250 260
....*....|....*....|
gi 1239365521 234 TESGTLYREPLHPYTKALLS 253
Cdd:PRK14239 229 NDTKQMFMNPKHKETEDYIS 248
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-230 |
1.94e-28 |
|
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: 109.29 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFdagkkRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGtnlhalsEKEQFAF 86
Cdd:cd03269 1 LEVENVTKRF-----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-------KPLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDpyASLNPRMTVREIILEPMEIHNLynTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARAL 166
Cdd:cd03269 69 RNRIGYLPEE--RGLYPKMKVIDQLVYLAQLKGL--KKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 167 SLNPEFIVADEPISALDVsVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:cd03269 144 IHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
29-238 |
2.33e-28 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 110.28 E-value: 2.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 29 GVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGT----------NLHALSEKEQFAFNRKLQMIFQdpy 98
Cdd:COG4598 26 GVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpdrdgELVPADRRQLQRIRTRLGMVFQ--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 99 aSLN--PRMTVREIILE-PmeIHNLYNTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVA 175
Cdd:COG4598 103 -SFNlwSHMTVLENVIEaP--VHVLGRPKAEAIERAEALLAKVGLA-DKRDAYPAHLSGGQQQRAAIARALAMEPEVMLF 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 176 DEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRigVMYLgHMMEITESGT 238
Cdd:COG4598 179 DEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSH--VVFL-HQGRIEEQGP 237
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
25-228 |
4.28e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.14 E-value: 4.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLhaLSEKEQFAFNRK-LQMIFQDPYASLNP 103
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI--TDKKVKLSDIRKkVGLVFQYPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 104 RMTVREIILEPM-------EIHNLynthkarllvVDELLEAVGL-HPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVA 175
Cdd:PRK13637 99 ETIEKDIAFGPInlglseeEIENR----------VKRAMNIVGLdYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 176 DEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:PRK13637 169 DEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKG 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-238 |
5.86e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.11 E-value: 5.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 21 KRTVKAVDGVtfqIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHA-LSEKEQFAFNRKLQMIFQDPYA 99
Cdd:PRK13634 20 RRALYDVNVS---IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgKKNKKLKPLRKKVGIVFQFPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 100 SLNPRMTVREIILEPMeihNLYNTHKARLLVVDELLEAVGLHPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPI 179
Cdd:PRK13634 97 QLFEETVEKDICFGPM---NFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 180 SALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGhmmEITESGT 238
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKG---TVFLQGT 229
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
28-242 |
7.60e-28 |
|
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: 113.90 E-value: 7.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 28 DGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALsekEQFAFNRKLQMIFQdpyaslNPRmtv 107
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL---DVQAVRRQLGVVLQ------NGR--- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 108 reiiLEPMEIHNlyNTHKARLLVVDELLEA---VGLHPDFgSRYP---H--------EFSGGQRQRIGIARALSLNPEFI 173
Cdd:TIGR03797 538 ----LMSGSIFE--NIAGGAPLTLDEAWEAarmAGLAEDI-RAMPmgmHtvisegggTLSGGQRQRLLIARALVRKPRIL 610
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 174 VADEPISALDVSVQAQVVNLLKRLQkekgLTFLFIAHDLSMVKHiSDRIGVMYLGhmmEITESGTlYRE 242
Cdd:TIGR03797 611 LFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAG---RVVQQGT-YDE 670
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
5-225 |
1.48e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 108.15 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEkEQF 84
Cdd:PRK11300 4 PLLSVSGLMMRFGG-----LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG-HQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AfNRKLQMIFQDpyASLNPRMTVREIILEPME-------IHNLYNTHKARLLVVDEL------LEAVGLHpDFGSRYPHE 151
Cdd:PRK11300 78 A-RMGVVRTFQH--VRLFREMTVIENLLVAQHqqlktglFSGLLKTPAFRRAESEALdraatwLERVGLL-EHANRQAGN 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 152 FSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
27-232 |
1.66e-27 |
|
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: 112.91 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLhALSE------------KEQFAFNRKLQmif 94
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDL-AIADpawlrrqmgvvlQENVLFSRSIR--- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 95 qDPYASLNPRMTVREIIlepmeihnlyntHKARLlvvdelleaVGLHpDFGSRYPHEF-----------SGGQRQRIGIA 163
Cdd:TIGR01846 549 -DNIALCNPGAPFEHVI------------HAAKL---------AGAH-DFISELPQGYntevgekganlSGGQRQRIAIA 605
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 164 RALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQkeKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMME 232
Cdd:TIGR01846 606 RALVGNPRILIFDEATSALDYESEALIMRNMREIC--RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAE 671
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-225 |
1.69e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.94 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDagkKRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSeKEQF 84
Cdd:PRK13548 1 AMLEARNLSVRLG---GRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWS-PAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AfnRKLQMIFQdpYASLNPRMTVREIILEPMEIHNLYNTHKARLlvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIAR 164
Cdd:PRK13548 75 A--RRRAVLPQ--HSSLSFPFTVEEVVAMGRAPHGLSRAEDDAL--VAAALAQVDLA-HLAGRDYPQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365521 165 AL------SLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:PRK13548 148 VLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLL 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-249 |
1.95e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 107.69 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDagkkrTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQ-----PTEGSVVYRGTNLHALSEK 81
Cdd:PRK14247 4 IEIRDLKVSFG-----QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 82 EqfaFNRKLQMIFQDPYASlnPRMTVREIILEPMEIHNLYNTHKARLLVVDELLEAVGLHPDFGSRY---PHEFSGGQRQ 158
Cdd:PRK14247 79 E---LRRRVQMVFQIPNPI--PNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 159 RIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEkgLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGT 238
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
250
....*....|.
gi 1239365521 239 LYREPLHPYTK 249
Cdd:PRK14247 232 VFTNPRHELTE 242
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-230 |
2.07e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 108.66 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDagkkrTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHAlSEKEQFAF 86
Cdd:COG4152 2 LELKGLTKRFG-----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-EDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 ---NRklqmifqdpyaSLNPRMTVREIILEPMEIHNLyNTHKARlLVVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIA 163
Cdd:COG4152 76 lpeER-----------GLYPKMKVGEQLVYLARLKGL-SKAEAK-RRADEWLERLGL-GDRANKKVEELSKGNQQKVQLI 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 164 RALSLNPEFIVADEPISALD-VSVQAqVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDpVNVEL-LKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
28-237 |
3.49e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 106.72 E-value: 3.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 28 DGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQfAFNRKLQMIFQDPYasLNPRMTV 107
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER-LIRQEAGMVFQQFY--LFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 108 RE-IILEPMEIHNLYNTHKARLlvVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSV 186
Cdd:PRK09493 95 LEnVMFGPLRVRGASKEEAEKQ--ARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1239365521 187 QAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHmmeITESG 237
Cdd:PRK09493 172 RHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGR---IAEDG 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-225 |
3.79e-27 |
|
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: 109.03 E-value: 3.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHAlSEKEQF--AFNRKLQMIFQDpyASLNPRMTV 107
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD-SARGIFlpPHRRRIGYVFQE--ARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 108 REiilepmeihNLYNTHK-----ARLLVVDELLEAVGLHP--DfgsRYPHEFSGGQRQRIGIARALSLNPEFIVADEPIS 180
Cdd:COG4148 95 RG---------NLLYGRKrapraERRISFDEVVELLGIGHllD---RRPATLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1239365521 181 ALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:COG4148 163 ALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLL 207
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-253 |
3.98e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.85 E-value: 3.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQ-----PTEGSVVYRGTNLHAlSEKEQFAFNRKLQMIFQdpYASL 101
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYS-PDVDPIEVRREVGMVFQ--YPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 102 NPRMTVREIILEPMEIHNLYNTHKARLLVVDELLEAVGLHPDFGSR---YPHEFSGGQRQRIGIARALSLNPEFIVADEP 178
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 179 ISALDVSVQAQVVNLLKRLQKEkgLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREPLHPYTKALLS 253
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVT 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-224 |
5.12e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 110.79 E-value: 5.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 1 MTPlPLLEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYqPT---EGSVVYRGTNLHA 77
Cdd:PRK13549 1 MME-YLLEMKNITKTFGG-----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 78 LSEKEQfafNRK-LQMIFQDpyASLNPRMTVREIIL---EPMEIHNL-YNTHKARllvVDELLEAVGLHPDFGSRYpHEF 152
Cdd:PRK13549 74 SNIRDT---ERAgIAIIHQE--LALVKELSVLENIFlgnEITPGGIMdYDAMYLR---AQKLLAQLKLDINPATPV-GNL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 153 SGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGV 224
Cdd:PRK13549 145 GLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICV 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-222 |
8.93e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 105.92 E-value: 8.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 2 TPLPLLEVSKlkmHFdaGKKRTVKAVDgvtFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEK 81
Cdd:PRK11247 11 TPLLLNAVSK---RY--GERTVLNQLD---LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 82 eqfafnrkLQMIFQDpyASLNPRMTVreiilepmeIHN----LYNTHKARLLvvdELLEAVGLhPDFGSRYPHEFSGGQR 157
Cdd:PRK11247 83 --------TRLMFQD--ARLLPWKKV---------IDNvglgLKGQWRDAAL---QALAAVGL-ADRANEWPAALSGGQK 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 158 QRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRV 204
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-249 |
9.13e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 106.28 E-value: 9.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTLGRVLMRLYQ------PTEGSVVYRGTNLHALsekEQFAFNRKLQMIFQDPyaSLNP 103
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQI---DAIKLRKEVGMVFQQP--NPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 104 RMTVREIILEPMEIHNLYNTHKARLlVVDELLEAVGLHPDFGSRY---PHEFSGGQRQRIGIARALSLNPEFIVADEPIS 180
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIKK-IVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 181 ALDVSVQAQVVNLLKRLQKEkgLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREPLHPYTK 249
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-238 |
1.28e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 110.05 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 16 FDAGKKRTvkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKeqfAFNRKLQMIFQ 95
Cdd:PRK13657 342 FSYDNSRQ--GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA---SLRRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 96 DpyASLNPRmTVREIIL------EPMEIHnlynthkarllvvdELLEAVGLHpDFGSRYPHEF-----------SGGQRQ 158
Cdd:PRK13657 417 D--AGLFNR-SIEDNIRvgrpdaTDEEMR--------------AAAERAQAH-DFIERKPDGYdtvvgergrqlSGGERQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 159 RIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQkeKGLTFLFIAHDLSMVKHiSDRIGVMYLGHmmeITESGT 238
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-ADRILVFDNGR---VVESGS 552
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-230 |
2.27e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 104.19 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAFNRKLQMIFQDPYASLNpr 104
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 MTVREIILEPMEIHNLYNTHKARLlvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDV 184
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRRR--VSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1239365521 185 SVQAQVVNLLKRLQKeKGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:PRK10908 171 ALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
27-225 |
2.49e-26 |
|
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: 102.68 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDpyaslnprmt 106
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE---LGDHVGYLPQD---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 107 vreiilepmeihnlynthkarllvvDELLEavglhpdfGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSV 186
Cdd:cd03246 85 -------------------------DELFS--------GSIAENILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190
....*....|....*....|....*....|....*....
gi 1239365521 187 QAQVVNLLKRLqKEKGLTFLFIAHDLSMVKhISDRIGVM 225
Cdd:cd03246 132 ERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVL 168
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-239 |
3.65e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 103.99 E-value: 3.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLkmHFDAGKKRTVKavdGVTFQIREGETFGLVGESGCGKSTLGRVLM--RLYQPTEGSVVYRGTNLHALSEKEQF 84
Cdd:COG0396 1 LEIKNL--HVSVEGKEILK---GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSPDERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 afNRKLQMIFQDP------------YASLNPRmtvREIILEPMEIHNLynthkarllvVDELLEAVGLHPDFGSRYPHE- 151
Cdd:COG0396 76 --RAGIFLAFQYPveipgvsvsnflRTALNAR---RGEELSAREFLKL----------LKEKMKELGLDEDFLDRYVNEg 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 152 FSGGQRQRIGIARALSLNPEFIVADEPISALDV-SVQAqVVNLLKRLqKEKGLTFLFIAHDLSMVKHIS-DRIGVMYLGH 229
Cdd:COG0396 141 FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdALRI-VAEGVNKL-RSPDRGILIITHYQRILDYIKpDFVHVLVDGR 218
|
250
....*....|
gi 1239365521 230 mmeITESGTL 239
Cdd:COG0396 219 ---IVKSGGK 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
37-231 |
5.67e-26 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 104.10 E-value: 5.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 37 GETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKeqfAFNRKLQMIFQD-PYASlnpRMTVREIIlepm 115
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK---AFARKVAYLPQQlPAAE---GMTVRELV---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 116 eIHNLYNTHKA--RLLV-----VDELLEAVGLHPdFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQA 188
Cdd:PRK10575 107 -AIGRYPWHGAlgRFGAadrekVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1239365521 189 QVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMM 231
Cdd:PRK10575 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-233 |
7.87e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 103.92 E-value: 7.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGKKrtvKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqf 84
Cdd:PRK13632 6 VMIKVENVSFSYPNSEN---NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 aFNRKLQMIFQdpyaslNPR-----MTVREIILEPMEiHNLYNTHKARLlVVDELLEAVGLHpDFGSRYPHEFSGGQRQR 159
Cdd:PRK13632 81 -IRKKIGIIFQ------NPDnqfigATVEDDIAFGLE-NKKVPPKKMKD-IIDDLAKKVGME-DYLDKEPQNLSGGQKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 160 IGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKhISDRIGVMYLGHMMEI 233
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQ 223
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-243 |
7.89e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 105.70 E-value: 7.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 1 MTPLPLLEVSKlkmHFDAGkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSE 80
Cdd:PRK11650 1 MAGLKLQAVRK---SYDGK----TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 81 KEqfafnRKLQMIFQDpYAsLNPRMTVReiilEPMEiHNLYN------------THKARLLVVDELLEavglhpdfgsRY 148
Cdd:PRK11650 74 AD-----RDIAMVFQN-YA-LYPHMSVR----ENMA-YGLKIrgmpkaeieervAEAARILELEPLLD----------RK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 149 PHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:PRK11650 132 PRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGG 211
|
250
....*....|....*...
gi 1239365521 229 HMMEItesGT---LYREP 243
Cdd:PRK11650 212 VAEQI---GTpveVYEKP 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-225 |
9.54e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.08 E-value: 9.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqf 84
Cdd:PRK09536 2 PMIDVSDLSVEFGD-----TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 aFNRKLQMIFQDpyASLNPRMTVREIIlePMEIHnlynTHKARL--------LVVDELLEAVGLhPDFGSRYPHEFSGGQ 156
Cdd:PRK09536 75 -ASRRVASVPQD--TSLSFEFDVRQVV--EMGRT----PHRSRFdtwtetdrAAVERAMERTGV-AQFADRPVTSLSGGE 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 157 RQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:PRK09536 145 RQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLL 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-238 |
1.44e-25 |
|
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: 101.74 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAf 86
Cdd:cd03224 1 LEVENLNAGYGK-----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 nRKLQMIFQDPyaSLNPRMTVREIILepMEIHNLYNTHKARLLvvDELLEavgLHPDFGSRYPH---EFSGGQRQRIGIA 163
Cdd:cd03224 75 -AGIGYVPEGR--RIFPELTVEENLL--LGAYARRRAKRKARL--ERVYE---LFPRLKERRKQlagTLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 164 RALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHmmeITESGT 238
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGR---VVLEGT 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-256 |
1.49e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 107.12 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGKKrTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALS----- 79
Cdd:PRK10535 3 ALLELKDIRRSYPSGEE-QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadala 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 80 --EKEQFAFnrklqmIFQDPYasLNPRMTVreiiLEPMEIHNLY--NTHKARLLVVDELLEAVGLhpdfGSR---YPHEF 152
Cdd:PRK10535 82 qlRREHFGF------IFQRYH--LLSHLTA----AQNVEVPAVYagLERKQRLLRAQELLQRLGL----EDRveyQPSQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 153 SGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQkEKGLTFLFIAHDlSMVKHISDRIGVMYLGHMMe 232
Cdd:PRK10535 146 SGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV- 222
|
250 260
....*....|....*....|....
gi 1239365521 233 iTESGTLYREPLHPYTKALLSSIP 256
Cdd:PRK10535 223 -RNPPAQEKVNVAGGTEPVVNTAS 245
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
29-243 |
1.68e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 107.12 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 29 GVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTnlhALSEKEQFAFNRKLQMIFQDPyasLNPRMTVR 108
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV---PLVQYDHHYLHRQVALVGQEP---VLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 109 EIILepmeiHNLYNTHKARLLVVdelLEAVGLHpDFGSRYPHEF-----------SGGQRQRIGIARALSLNPEFIVADE 177
Cdd:TIGR00958 573 ENIA-----YGLTDTPDEEIMAA---AKAANAH-DFIMEFPNGYdtevgekgsqlSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239365521 178 PISALDVSVQAqvvnLLKRLQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMMEITESGTLYREP 243
Cdd:TIGR00958 644 ATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-225 |
1.80e-25 |
|
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: 106.76 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 2 TPLP----LLEVSKLKMHFDAGKKRTVKavdGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHA 77
Cdd:COG4618 322 MPLPrpkgRLSVENLTVVPPGSKRPILR---GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 78 LsEKEQFAfnrklQMIF---QDPyaSLNPRmTVREIIlepmeihnlynthkARLLVVD--ELLEA---VGLHpDFGSRYP 149
Cdd:COG4618 399 W-DREELG-----RHIGylpQDV--ELFDG-TIAENI--------------ARFGDADpeKVVAAaklAGVH-EMILRLP 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 150 HEF-----------SGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHi 218
Cdd:COG4618 455 DGYdtrigeggarlSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA- 532
|
....*..
gi 1239365521 219 SDRIGVM 225
Cdd:COG4618 533 VDKLLVL 539
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-233 |
2.53e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 101.70 E-value: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 20 KKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTnLHALsekeqFAFNrklqmifqdpyA 99
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSAL-----LELG-----------A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 100 SLNPRMTVREiilepmeihNLYntHKARLL-----VVDELLEAVglhpdfgsrypHEFSG--------------GQRQRI 160
Cdd:COG1134 98 GFHPELTGRE---------NIY--LNGRLLglsrkEIDEKFDEI-----------VEFAElgdfidqpvktyssGMRARL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 161 GIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEI 233
Cdd:COG1134 156 AFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-225 |
4.16e-25 |
|
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: 105.45 E-value: 4.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 2 TPLPLLEVSKLKMHFDAgkkrTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEK 81
Cdd:TIGR02857 317 APASSLEFSGVSVAYPG----RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 82 ---EQFAfnrklqmifqdpYASLNPRM---TVREIIL------EPMEIHNlynthKARLLVVDELLEAV--GLHPDFGSR 147
Cdd:TIGR02857 393 swrDQIA------------WVPQHPFLfagTIAENIRlarpdaSDAEIRE-----ALERAGLDEFVAALpqGLDTPIGEG 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 148 yPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQkeKGLTFLFIAHDLSmVKHISDRIGVM 225
Cdd:TIGR02857 456 -GAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLA-LAALADRIVVL 529
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
27-211 |
5.83e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.86 E-value: 5.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQP---TEGSVVYRGTNLHALSeKEQfafnRKLQMIFQDPYasLNP 103
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALP-AEQ----RRIGILFQDDL--LFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 104 RMTVREIIL--EPMEIhnlynTHKARLLVVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISA 181
Cdd:COG4136 90 HLSVGENLAfaLPPTI-----GRAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
170 180 190
....*....|....*....|....*....|
gi 1239365521 182 LDVSVQAQVVNLLKRLQKEKGLTFLFIAHD 211
Cdd:COG4136 164 LDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
26-242 |
6.04e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.37 E-value: 6.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYrgtNLHALSEKEQFAFNRKLQMIFQDPYASLNPRm 105
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY---NNQAITDDNFEKLRKHIGIVFQNPDNQFVGS- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 106 TVREIILEPMEIHNLynTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVS 185
Cdd:PRK13648 100 IVKYDVAFGLENHAV--PYDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365521 186 VQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHiSDRIGVMylghmmeitESGTLYRE 242
Cdd:PRK13648 177 ARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVM---------NKGTVYKE 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
6-242 |
6.62e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 101.73 E-value: 6.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDAGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALS-EKEQF 84
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFNRKLQMIFQDPYASLNPRMTVREIILEPmeiHNLYNTHKARLLVVDELLEAVGLHPDFGSRYPHEFSGGQRQRIGIAR 164
Cdd:PRK13643 81 PVRKKVGVVFQFPESQLFEETVLKDVAFGP---QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 165 ALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQkEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYRE 242
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-224 |
7.45e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 104.61 E-value: 7.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 24 VKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfAFNRKLQMIFQDpyASLNP 103
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA--ALAAGVAIIYQE--LHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 104 RMTVREiilepmeihNLYNTH-KARLLVVD---------ELLEAVGLHPDfgsryPH----EFSGGQRQRIGIARALSLN 169
Cdd:PRK11288 93 EMTVAE---------NLYLGQlPHKGGIVNrrllnyearEQLEHLGVDID-----PDtplkYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 170 PEFIVADEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGV 224
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITV 212
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-238 |
8.44e-25 |
|
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: 99.91 E-value: 8.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAGKkrtvkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQ--- 83
Cdd:TIGR03410 1 LEVSNLNVYYGQSH-----ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERara 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 84 -FAFNRKLQMIFqdpyaslnPRMTVREIILEPMEihNLYNTHKArllVVDELLEavgLHP---DFGSRYPHEFSGGQRQR 159
Cdd:TIGR03410 76 gIAYVPQGREIF--------PRLTVEENLLTGLA--ALPRRSRK---IPDEIYE---LFPvlkEMLGRRGGDLSGGQQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 160 IGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGhmmEITESGT 238
Cdd:TIGR03410 140 LAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERG---RVVASGA 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
25-228 |
1.14e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.58 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDPYASLNPr 104
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---VRSKVGLVFQDPDDQVFS- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 MTVRE-IILEPMeihNLYNTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALD 183
Cdd:PRK13647 95 STVWDdVAFGPV---NMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1239365521 184 VSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:PRK13647 171 PRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
12-221 |
1.19e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 99.66 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 12 LKMHFDagkkrtvkavdgvtFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNlHALSEKEQfafnRKLQ 91
Cdd:PRK10771 14 LPMRFD--------------LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSR----RPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 92 MIFQDpyASLNPRMTVREII---LEPmeihNLYNTHKARLLVVDeLLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSL 168
Cdd:PRK10771 75 MLFQE--NNLFSHLTVAQNIglgLNP----GLKLNAAQREKLHA-IARQMGIE-DLLARLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 169 NPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDR 221
Cdd:PRK10771 147 EQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPR 199
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-231 |
1.84e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.70 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 19 GKKRTVkavDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDPy 98
Cdd:PRK11231 13 GTKRIL---NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ---LARRLALLPQHH- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 99 asLNPR-MTVREIIL---EPmeihnlYNTHKARLLVVDELLEAVGLHP----DFGSRYPHEFSGGQRQRIGIARALSLNP 170
Cdd:PRK11231 86 --LTPEgITVRELVAygrSP------WLSLWGRLSAEDNARVNQAMEQtrinHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239365521 171 EFIVADEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMM 231
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
29-225 |
1.89e-24 |
|
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: 99.08 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 29 GVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGtnlHALSEKEQFAFNRKLQMIFQDPyaSLNPRmTVR 108
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG---KPISQYEHKYLHSKVSLVGQEP--VLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 109 EIIlepmeihnLYNTHKARLLVVDELLEAVGLHpDFGSRYPHEF-----------SGGQRQRIGIARALSLNPEFIVADE 177
Cdd:cd03248 106 DNI--------AYGLQSCSFECVKEAAQKAHAH-SFISELASGYdtevgekgsqlSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239365521 178 PISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHiSDRIGVM 225
Cdd:cd03248 177 ATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVL 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-230 |
1.90e-24 |
|
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: 97.89 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHfdagkkrtvKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqf 84
Cdd:cd03215 3 PVLEVRGLSVK---------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFNRKLQMIFQDPYAS-LNPRMTVRE-IILepmeihnlynthkARLLvvdelleavglhpdfgsryphefSGGQRQRIGI 162
Cdd:cd03215 72 AIRAGIAYVPEDRKREgLVLDLSVAEnIAL-------------SSLL-----------------------SGGNQQKVVL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 163 ARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:cd03215 116 ARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-242 |
2.25e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.18 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqf 84
Cdd:COG3845 256 VVLEVENLSVRDDRG----VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE-- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 afNRKLQM--IFQDPYAS-LNPRMTVRE-IIL-----EPMEIHNLYNTHKARLLvVDELLEavglhpDFGSRYPHE---- 151
Cdd:COG3845 330 --RRRLGVayIPEDRLGRgLVPDMSVAEnLILgryrrPPFSRGGFLDRKAIRAF-AEELIE------EFDVRTPGPdtpa 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 152 --FSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGH 229
Cdd:COG3845 401 rsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
250
....*....|...
gi 1239365521 230 MMEITESGTLYRE 242
Cdd:COG3845 480 IVGEVPAAEATRE 492
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-232 |
4.60e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.52 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHA-LSEKEQFAFNRKLQMIFQDPYASLNP 103
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKKLRKKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 104 RMTVREIILEPMEIHnlYNTHKARLLVVdELLEAVGLHPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALD 183
Cdd:PRK13641 101 NTVLKDVEFGPKNFG--FSEDEAKEKAL-KWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1239365521 184 VSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMME 232
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
25-237 |
5.85e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 96.23 E-value: 5.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEkeqfAFNRKLQMIFQDPYaslnpr 104
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK----ALSSLISVLNQRPY------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 mtvreiilepmeihnLYNThkarllvvdELLEAVGLhpdfgsryphEFSGGQRQRIGIARALSLNPEFIVADEPISALDV 184
Cdd:cd03247 86 ---------------LFDT---------TLRNNLGR----------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 185 SVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHIsDRIGVMYLGhmmEITESG 237
Cdd:cd03247 132 ITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENG---KIIMQG 178
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
27-238 |
6.13e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 98.23 E-value: 6.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqFAfnRKLQMIFQDPyaSLNPRMT 106
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRE-LA--KRLAILRQEN--HINSRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 107 VREiilepmeihnL-----YNTHKARL-----LVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVAD 176
Cdd:COG4604 92 VRE----------LvafgrFPYSKGRLtaedrEIIDEAIAYLDLE-DLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 177 EPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGhmmEITESGT 238
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDG---RVVAQGT 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-231 |
9.38e-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: 97.40 E-value: 9.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 15 HFDAGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGtnLHALSEKEQFA------FNR 88
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRKKFLrrigvvFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 89 KLQMIFQDPyaslnprmtVREIILEPMEIHNL-YNTHKARLlvvDELLEAVGLHP--DFGSRyphEFSGGQRQRIGIARA 165
Cdd:cd03267 103 KTQLWWDLP---------VIDSFYLLAAIYDLpPARFKKRL---DELSELLDLEEllDTPVR---QLSLGQRMRAEIAAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239365521 166 LSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMM 231
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-230 |
1.45e-23 |
|
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: 100.89 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 19 GKKRTVKavdGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALsEKEQFAfnRKLQMIFQDpy 98
Cdd:TIGR01842 329 GKKPTLR---GISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQW-DRETFG--KHIGYLPQD-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 99 ASLNPRmTVREII------LEPMEIhnlynTHKARLLVVDELLEAV--GLHPDFGSRyPHEFSGGQRQRIGIARALSLNP 170
Cdd:TIGR01842 401 VELFPG-TVAENIarfgenADPEKI-----IEAAKLAGVHELILRLpdGYDTVIGPG-GATLSGGQRQRIALARALYGDP 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 171 EFIVADEPISALDVSVQAQVVNLLKRLQKeKGLTFLFIAHDLSMVKHIsDRIGVMYLGHM 230
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEQALANAIKALKA-RGITVVVITHRPSLLGCV-DKILVLQDGRI 531
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-238 |
1.88e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.32 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLkmHFDAGKKrtvKAVDGVTFQIREGEtFGLV-GESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSE--- 80
Cdd:PRK10247 6 PLLQLQNV--GYLAGDA---KILNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 81 KEQFAFNRKLQMIFQDpyaslnprmTVREIILEPMEIHNLYNTHKArlLVVDelLEAVGLHPDFGSRYPHEFSGGQRQRI 160
Cdd:PRK10247 80 RQQVSYCAQTPTLFGD---------TVYDNLIFPWQIRNQQPDPAI--FLDD--LERFALPDTILTKNIAELSGGEKQRI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 161 GIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVM-YLGHMMEITESGT 238
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQpHAGEMQEARYELA 225
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
27-238 |
1.88e-23 |
|
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: 100.79 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAfnrKLQMIFQDpyASLNpRMT 106
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLAN---SVAMVDQD--IFLF-EGT 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 107 VREIIlepmeihNLYNTHKARLLVVDELLEAVgLHPDFGSR---YPHE-------FSGGQRQRIGIARALSLNPEFIVAD 176
Cdd:TIGR03796 569 VRDNL-------TLWDPTIPDADLVRACKDAA-IHDVITSRpggYDAElaegganLSGGQRQRLEIARALVRNPSILILD 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 177 EPISALDVSVQAQVVNLLKRlqkeKGLTFLFIAHDLSMVKHiSDRIGVMYLGhmmEITESGT 238
Cdd:TIGR03796 641 EATSALDPETEKIIDDNLRR----RGCTCIIVAHRLSTIRD-CDEIIVLERG---KVVQRGT 694
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-240 |
2.07e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.38 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 1 MTPLPL-----LEVSKLKMHFDAGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSV------- 68
Cdd:PRK13631 11 KVPNPLsddiiLRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 69 -----VYRGTNLHALSEKEQFAFNRKL-QMIFQDPYASLNPRMTVREIILEP--MEIHNLYNTHKARLLvvdelLEAVGL 140
Cdd:PRK13631 91 gdkknNHELITNPYSKKIKNFKELRRRvSMVFQFPEYQLFKDTIEKDIMFGPvaLGVKKSEAKKLAKFY-----LNKMGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 141 HPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRlQKEKGLTFLFIAHDLSMVKHISD 220
Cdd:PRK13631 166 DDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVAD 244
|
250 260
....*....|....*....|
gi 1239365521 221 RIGVMYLGhmmEITESGTLY 240
Cdd:PRK13631 245 EVIVMDKG---KILKTGTPY 261
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-238 |
2.53e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.18 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 21 KRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDPYAS 100
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE---VRKFVGLVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 101 LNPRMTVREIILEPMEIHNLYNTHKARllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPIS 180
Cdd:PRK13652 91 IFSPTVEQDIAFGPINLGLDEETVAHR---VSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 181 ALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGhmmEITESGT 238
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKG---RIVAYGT 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-212 |
2.65e-23 |
|
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: 100.13 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGKKrtvkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqf 84
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPP----VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 aFNRKLQMIFQDP--YASlnprmTVREiilepmeihnlyNTHKARLLVVDE----LLEAVGLHPDFGSRyPH-------- 150
Cdd:TIGR02868 407 -VRRRVSVCAQDAhlFDT-----TVRE------------NLRLARPDATDEelwaALERVGLADWLRAL-PDgldtvlge 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 151 ---EFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLkrLQKEKGLTFLFIAHDL 212
Cdd:TIGR02868 468 ggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
26-225 |
3.33e-23 |
|
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: 95.64 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTN-----LHALsekeqfafNRKLQMIFQDPyas 100
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskigLHDL--------RSRISIIPQDP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 101 LNPRMTVREiILEPMEIH------------NLYNTHKARLLVVDELLEAVGLHpdfgsrypheFSGGQRQRIGIARALSL 168
Cdd:cd03244 88 VLFSGTIRS-NLDPFGEYsdeelwqalervGLKEFVESLPGGLDTVVEEGGEN----------LSVGQRQLLCLARALLR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365521 169 NPEFIVADEPISALDVSVQAQVVNLLKRlqKEKGLTFLFIAHDLSMVKHiSDRIGVM 225
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVL 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-229 |
3.42e-23 |
|
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: 95.69 E-value: 3.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFdagKKRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQfaf 86
Cdd:cd03218 1 LRAENLSKRY---GKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 nRKLQMIFQDPYASLNPRMTVREIILEPMEIHNLYNTHKARLLvvDELLEAVGLHP---DFGSRypheFSGGQRQRIGIA 163
Cdd:cd03218 73 -ARLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKL--EELLEEFHITHlrkSKASS----LSGGERRRVEIA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365521 164 RALSLNPEFIVADEPISALD-VSVQaQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGH 229
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDpIAVQ-DIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
231-298 |
3.67e-23 |
|
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: 90.54 E-value: 3.67e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 231 MEITESGTLYREPLHPYTKALLSSIPIPDPEledKRERILLKGELPSPVNPPSGCVFRTRCPEAMPEC 298
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPP---KRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-273 |
5.30e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.21 E-value: 5.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFafnRKL-QMIFQDPYASLNPR 104
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGI---RKLvGIVFQNPETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 mTVRE--------IILEPMEIHNLynthkarllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVAD 176
Cdd:PRK13644 94 -TVEEdlafgpenLCLPPIEIRKR----------VDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 177 EPISALDVSVQAQVVNLLKRLQkEKGLTFLFIAHDLSMVkHISDRIGVMYLGHMMeitesgtLYREPLHPYTKALLSSIP 256
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKIV-------LEGEPENVLSDVSLQTLG 232
|
250
....*....|....*..
gi 1239365521 257 IPDPELEDKRERILLKG 273
Cdd:PRK13644 233 LTPPSLIELAENLKMHG 249
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-262 |
8.05e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 96.23 E-value: 8.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEK--EQFAFNRKLQMIFQDPYASLN 102
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVKRLRKEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 103 PRMTVREIILEPMeihNLYNTHKARLLVVDELLEAVGLHPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISAL 182
Cdd:PRK13645 105 QETIEKDIAFGPV---NLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 183 DVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYReplhpyTKALLSSIPIPDPEL 262
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS------NQELLTKIEIDPPKL 255
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-249 |
8.37e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.49 E-value: 8.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 4 LPLLEVSKLKMHFDagkkrTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQ-----PTEGSVVYRGTNLHal 78
Cdd:PRK14258 5 IPAIKVNNLSFYYD-----TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 79 seKEQFAFNR---KLQMIFQDPyaSLNPrMTVREIILEPMEIHNLYNThkarlLVVDELLEAVGLHPDFGSRYPH----- 150
Cdd:PRK14258 78 --ERRVNLNRlrrQVSMVHPKP--NLFP-MSVYDNVAYGVKIVGWRPK-----LEIDDIVESALKDADLWDEIKHkihks 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 151 --EFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMY-- 226
Cdd:PRK14258 148 alDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgn 227
|
250 260
....*....|....*....|....*.
gi 1239365521 227 ---LGHMMEITESGTLYREPLHPYTK 249
Cdd:PRK14258 228 enrIGQLVEFGLTKKIFNSPHDSRTR 253
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-237 |
1.44e-22 |
|
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: 93.36 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLkmHFDAGKKRTVKavdGVTFQIREGETFGLVGESGCGKSTLGRVLMRL--YQPTEGSVVYRGTNLHALSEKEQF 84
Cdd:cd03217 1 LEIKDL--HVSVGGKEILK---GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AfnRKLQMIFQdpyaslnprmtvreiilEPMEIHNLYNthkarllvvDELLeavglhpdfgsRYPHE-FSGGQRQRIGIA 163
Cdd:cd03217 76 R--LGIFLAFQ-----------------YPPEIPGVKN---------ADFL-----------RYVNEgFSGGEKKRNEIL 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 164 RALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHI-SDRIGVMYLGHmmeITESG 237
Cdd:cd03217 117 QLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGR---IVKSG 187
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-215 |
1.89e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.15 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVY---RGTNLHALSEKEQ 83
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 84 F------------------AFNRKLQMIFQDPYASLNPRMTVREIILEPMEihnlYNTHKARLL-VVDELLEAVGLHPDF 144
Cdd:PRK13651 83 VleklviqktrfkkikkikEIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVS----MGVSKEEAKkRAAKYIELVGLDESY 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239365521 145 GSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMV 215
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNV 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
12-222 |
2.41e-22 |
|
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: 92.94 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 12 LKMHFDagkkrtvkavdgvtFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfafnRKLQ 91
Cdd:cd03298 13 QPMHFD--------------LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-----RPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 92 MIFQDpyASLNPRMTVREII---LEPmeihNLYNTHKARLlVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSL 168
Cdd:cd03298 74 MLFQE--NNLFAHLTVEQNVglgLSP----GLKLTAEDRQ-AIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 169 NPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:cd03298 146 DKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRV 199
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
26-267 |
2.66e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.48 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQP---TEGSVVYRGTNLhalSEKEQFAFNRKLQMIFQDPYASLn 102
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITL---TAKTVWDIREKVGIVFQNPDNQF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 103 PRMTVREIILEPMEihNLYNTHKARLLVVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISAL 182
Cdd:PRK13640 98 VGATVGDDVAFGLE--NRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 183 DVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMM------EITESGTLYRE-----PLHPYTKAL 251
Cdd:PRK13640 175 DPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLaqgspvEIFSKVEMLKEigldiPFVYKLKNK 253
|
250
....*....|....*...
gi 1239365521 252 L--SSIPIPDpELEDKRE 267
Cdd:PRK13640 254 LkeKGISVPQ-EINTEEK 270
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
6-211 |
2.82e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 93.30 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDAGKKRtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFA 85
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHE-LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 86 FN-RKLQMIFQDpyASLNPRMTVREIILEPMEIHNlYNTHKARLLVVdELLEAVGLhpdfGSRYPH---EFSGGQRQRIG 161
Cdd:PRK10584 85 LRaKHVGFVFQS--FMLIPTLNALENVELPALLRG-ESSRQSRNGAK-ALLEQLGL----GKRLDHlpaQLSGGEQQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1239365521 162 IARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHD 211
Cdd:PRK10584 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
6-228 |
3.01e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.53 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDAGkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHaLSEKEQFA 85
Cdd:PRK13636 5 ILKVEELNYNYSDG----THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 86 FNRKLQMIFQDPYASLNPRMTVREIILEPMeihNLYNTHKARLLVVDELLEAVGLHPdFGSRYPHEFSGGQRQRIGIARA 165
Cdd:PRK13636 80 LRESVGMVFQDPDNQLFSASVYQDVSFGAV---NLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 166 LSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEG 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-217 |
3.68e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 97.41 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAgkKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTnlHALSEKEQFAF 86
Cdd:PTZ00265 383 IQFKNVRFHYDT--RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS--HNLKDINLKWW 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDP-----------------------------------YASLNPRMTVR-------EIILEPMEIHNLYNTH 124
Cdd:PTZ00265 459 RSKIGVVSQDPllfsnsiknnikyslyslkdlealsnyynedgndsQENKNKRNSCRakcagdlNDMSNTTDSNELIEMR 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 125 KARLLVVD----ELLEAVGLHpDFGSRYPHEF-----------SGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQ 189
Cdd:PTZ00265 539 KNYQTIKDsevvDVSKKVLIH-DFVSALPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
|
250 260
....*....|....*....|....*...
gi 1239365521 190 VVNLLKRLQKEKGLTFLFIAHDLSMVKH 217
Cdd:PTZ00265 618 VQKTINNLKGNENRITIIIAHRLSTIRY 645
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-238 |
3.89e-22 |
|
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: 92.74 E-value: 3.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSekeqf 84
Cdd:COG0410 2 PMLEVENLHAGYGG-----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLP----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFNR-KL--------QMIFqdpyaslnPRMTVREiilepmeihNL----YNTHKARllVVDELLEAV-GLHPDFGSRYPH 150
Cdd:COG0410 72 PHRIaRLgigyvpegRRIF--------PSLTVEE---------NLllgaYARRDRA--EVRADLERVyELFPRLKERRRQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 151 ---EFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYL 227
Cdd:COG0410 133 ragTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLER 211
|
250
....*....|.
gi 1239365521 228 GhmmEITESGT 238
Cdd:COG0410 212 G---RIVLEGT 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-239 |
5.53e-22 |
|
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: 96.05 E-value: 5.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQ--PTEGSVVYRGTNLHALSEKEQ 83
Cdd:TIGR02633 1 LLEMKGIVKTFGG-----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 84 FAfnRKLQMIFQDpyASLNPRMTVREIILEPMEI-HNLYNTH-KARLLVVDELLEAVGLHPDFGSRYPHEFSGGQRQRIG 161
Cdd:TIGR02633 76 ER--AGIVIIHQE--LTLVPELSVAENIFLGNEItLPGGRMAyNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 162 IARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTL 239
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-238 |
8.84e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.89 E-value: 8.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 16 FDAGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAFNRK-LQMIF 94
Cdd:PRK13649 12 YQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKkVGLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 95 QDPYASLNPRMTVREIILEPmeiHNLYNTHKARLLVVDELLEAVGLHPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIV 174
Cdd:PRK13649 92 QFPESQLFEETVLKDVAFGP---QNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 175 ADEPISALDVSVQAQVVNLLKRLQkEKGLTFLFIAHDLSMVKHISDRIGVMYLGHmmeITESGT 238
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGK---LVLSGK 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-248 |
9.30e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.85 E-value: 9.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFdAGKKrtvkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEG-----SVVYRGTNLhaLS 79
Cdd:PRK14271 20 PAMAAVNLTLGF-AGKT----VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 80 EKEQFAFNRKLQMIFQDPyaslNP-RMTVREIILEPMEIHNLYNTHKARLLVVDELLEaVGLH---PDFGSRYPHEFSGG 155
Cdd:PRK14271 93 YRDVLEFRRRVGMLFQRP----NPfPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTE-VGLWdavKDRLSDSPFRLSGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 156 QRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEkgLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITE 235
Cdd:PRK14271 168 QQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGP 245
|
250
....*....|...
gi 1239365521 236 SGTLYREPLHPYT 248
Cdd:PRK14271 246 TEQLFSSPKHAET 258
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-225 |
1.31e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 95.24 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKeqF 84
Cdd:PRK09700 4 PYISMAGIGKSFGP-----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK--L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFNRKLQMIFQDpyASLNPRMTVREiilepmeihNLYnthKARLL--------VVD---------ELLEAVGLHPDFGSR 147
Cdd:PRK09700 77 AAQLGIGIIYQE--LSVIDELTVLE---------NLY---IGRHLtkkvcgvnIIDwremrvraaMMLLRVGLKVDLDEK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 148 YPhEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:PRK09700 143 VA-NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVM 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
30-243 |
1.46e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.94 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfafnRKLQMIFQDpYAsLNPRMTVRE 109
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-----RGVGMVFQS-YA-LYPHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 110 II--------LEPMEIHNLYNtHKARLLVVDELLEavglhpdfgsRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISA 181
Cdd:PRK11000 95 NMsfglklagAKKEEINQRVN-QVAEVLQLAHLLD----------RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 182 LDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREP 243
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-213 |
2.41e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.59 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 21 KRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDpyAS 100
Cdd:PRK10253 19 KYTV--AENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE---VARRIGLLAQN--AT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 101 LNPRMTVREIILEPMEIHNLYNTH--KARLLVVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEP 178
Cdd:PRK10253 92 TPGDITVQELVARGRYPHQPLFTRwrKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190
....*....|....*....|....*....|....*
gi 1239365521 179 ISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLS 213
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLN 205
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
25-238 |
2.41e-21 |
|
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: 94.81 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDPYaslnpr 104
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT---LRQFINYLPQEPY------ 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 mTVREIILEPMEIHNLYNTHKARLLVVDELLE--------AVGLHPDFgSRYPHEFSGGQRQRIGIARALSLNPEFIVAD 176
Cdd:TIGR01193 559 -IFSGSILENLLLGAKENVSQDEIWAACEIAEikddienmPLGYQTEL-SEEGSSISGGQKQRIALARALLTDSKVLILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 177 EPISALDVSVQAQVVNLLKRLQKEkglTFLFIAHDLSMVKHiSDRIGVMYLGhmmEITESGT 238
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHG---KIIEQGS 691
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
34-228 |
2.47e-21 |
|
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: 90.31 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 34 IREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfafnRKLQMIFQDpyASLNPRMTVREII-- 111
Cdd:TIGR01277 21 VADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ-----RPVSMLFQE--NNLFAHLTVRQNIgl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 112 -LEPMEIHNLYNTHKarllvVDELLEAVGLhPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQV 190
Cdd:TIGR01277 94 gLHPGLKLNAEQQEK-----VVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1239365521 191 VNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:TIGR01277 168 LALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQG 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-240 |
2.66e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.61 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 29 GVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHaLSEKEQFAFNRKLQMIFQDP-----YASLNP 103
Cdd:PRK13638 19 GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQVATVFQDPeqqifYTDIDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 104 RM--TVREIILEPMEIhnlynthkARLlvVDELLEAVGlhpdfGSRYPHE----FSGGQRQRIGIARALSLNPEFIVADE 177
Cdd:PRK13638 98 DIafSLRNLGVPEAEI--------TRR--VDEALTLVD-----AQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 178 PISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLY 240
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-238 |
3.66e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 93.71 E-value: 3.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVL--MRLYQPTEGSVVYR------------- 71
Cdd:TIGR03269 1 IEVKNLTKKFDG-----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHvalcekcgyverp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 72 ---GTN--------------LHALSEKEQFAFNRKLQMIFQDPYAsLNPRMTVREIILEPMEIHNlYNTHKARLLVVDeL 134
Cdd:TIGR03269 76 skvGEPcpvcggtlepeevdFWNLSDKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALEEIG-YEGKEAVGRAVD-L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 135 LEAVGLhpdfGSRYPH---EFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHD 211
Cdd:TIGR03269 153 IEMVQL----SHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHW 228
|
250 260
....*....|....*....|....*..
gi 1239365521 212 LSMVKHISDRIGVMYLGhmmEITESGT 238
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENG---EIKEEGT 252
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
28-220 |
4.20e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.98 E-value: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 28 DGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAFNRKLQMIFQDpyASLNPRMTV 107
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS--GALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 108 REIILEPMEIHNLYNTHKARLLVVDELlEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQ 187
Cdd:PRK11831 102 FDNVAYPLREHTQLPAPLLHSTVMMKL-EAVGLR-GAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM 179
|
170 180 190
....*....|....*....|....*....|...
gi 1239365521 188 AQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISD 220
Cdd:PRK11831 180 GVLVKLISELNSALGVTCVVVSHDVPEVLSIAD 212
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-232 |
4.33e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.93 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNL--HALSE-KEQFAFNRKLQMIFQD------ 96
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdYTLASlRNQVALVSQNVHLFNDtianni 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 97 PYASlNPRMTVREIIlepmeihnlyntHKARLLVVDELLEAV--GLHPDFGsryphE----FSGGQRQRIGIARALSLNP 170
Cdd:PRK11176 438 AYAR-TEQYSREQIE------------EAARMAYAMDFINKMdnGLDTVIG-----EngvlLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 171 EFIVADEPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGHMME 232
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVE 558
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
28-238 |
5.75e-21 |
|
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: 93.35 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 28 DGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSekeQFAFNRKLQMIFQDpyaslnprmTV 107
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT---QASLRAAIGIVPQD---------TV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 108 reiilepmeIHN---LYNTHKARLLVVDELLEAVG----LHpDFGSRYPHEF-----------SGGQRQRIGIARALSLN 169
Cdd:COG5265 443 ---------LFNdtiAYNIAYGRPDASEEEVEAAAraaqIH-DFIESLPDGYdtrvgerglklSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 170 PEFIVADEPISALDV----SVQAQvvnlLKRLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGHmmeITESGT 238
Cdd:COG5265 513 PPILIFDEATSALDSrterAIQAA----LREVARGR--TTLVIAHRLSTIVD-ADEILVLEAGR---IVERGT 575
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
27-212 |
6.56e-21 |
|
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: 89.76 E-value: 6.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYR------GTNLHALseKEQFAF-NRKLQMIFQdpya 99
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLfgerrgGEDVWEL--RKRIGLvSPALQLRFP---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 100 slnPRMTVREIIL-----------EPMEIHnlynTHKARllvvdELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSL 168
Cdd:COG1119 93 ---RDETVLDVVLsgffdsiglyrEPTDEQ----RERAR-----ELLELLGLA-HLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1239365521 169 NPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDL 212
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHV 203
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-212 |
7.45e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.76 E-value: 7.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFdAGKKrtvkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQfa 85
Cdd:PRK11248 1 MLQISHLYADY-GGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERG-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 86 fnrklqMIFQDpyASLNPRMTVREIILEPMEIHNLynTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARA 165
Cdd:PRK11248 74 ------VVFQN--EGLLPWRNVQDNVAFGLQLAGV--EKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1239365521 166 LSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDL 212
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-224 |
8.28e-21 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 89.77 E-value: 8.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 34 IREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVvyrGTNLHALSEKEQfafnrklqmifqdpYASLNPRMTVREI--- 110
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKPQ--------------YIKADYEGTVRDLlss 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 111 ILEPMEIHNLYNTHKARLLVVDELLEavglhpdfgsRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQV 190
Cdd:cd03237 85 ITKDFYTHPYFKTEIAKPLQIEQILD----------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190
....*....|....*....|....*....|....
gi 1239365521 191 VNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGV 224
Cdd:cd03237 155 SKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-222 |
1.18e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.53 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 20 KKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHalseKEQFAFNRKLQMIF----Q 95
Cdd:COG4586 31 EYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPF----KRRKEFARRIGVVFgqrsQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 96 dpyasLNPRMTVREI--ILEpmEIHNL-YNTHKARLlvvDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEF 172
Cdd:COG4586 107 -----LWWDLPAIDSfrLLK--AIYRIpDAEYKKRL---DELVELLDLG-ELLDTPVRQLSLGQRMRCELAAALLHRPKI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1239365521 173 IVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRV 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
8-213 |
1.29e-20 |
|
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: 87.61 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 8 EVSKLKMHFDAGKKRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLM--RLYQPTEGSVVYRGTNLHAlsekeqFA 85
Cdd:cd03213 8 NLTVTVKSSPSKSGKQL--LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDK------RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 86 FNRKLQMIFQDPYasLNPRMTVREiilepmeihNLYNTHKARllvvdelleavGLhpdfgsryphefSGGQRQRIGIARA 165
Cdd:cd03213 80 FRKIIGYVPQDDI--LHPTLTVRE---------TLMFAAKLR-----------GL------------SGGERKRVSIALE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239365521 166 LSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLS 213
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPS 172
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-203 |
4.04e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.39 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFdagKKRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSekeqf 84
Cdd:COG1137 2 MTLEAENLVKSY---GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFNR-KLQMIF--QDPyaSLNPRMTVREIILEPMEIHNLynTHKARLLVVDELLEavglhpDFG-----SRYPHEFSGGQ 156
Cdd:COG1137 72 MHKRaRLGIGYlpQEA--SIFRKLTVEDNILAVLELRKL--SKKEREERLEELLE------EFGithlrKSKAYSLSGGE 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239365521 157 RQRIGIARALSLNPEFIVADEPISALD-VSVqAQVVNLLKRLqKEKGL 203
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHL-KERGI 187
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
26-215 |
6.98e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.75 E-value: 6.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSekeqfafnrklqmifqdPYASLNPR- 104
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYV-----------------PQRSEVPDs 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 --MTVREII-------LEPMEIHnlynTHKARLlVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVA 175
Cdd:NF040873 70 lpLTVRDLVamgrwarRGLWRRL----TRDDRA-AVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1239365521 176 DEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMV 215
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELV 182
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
26-220 |
3.24e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.60 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQ--PT---EGSVVYRGTNLHAlSEKEQFAFNRKLQMIFQDPyas 100
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKP--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 101 lNPrmtVREIILEPMEIHNLYNTHKARLlvvDELLE----AVGLHPDFGSRYPHE---FSGGQRQRIGIARALSLNPEFI 173
Cdd:PRK14243 101 -NP---FPKSIYDNIAYGARINGYKGDM---DELVErslrQAALWDEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1239365521 174 VADEPISALDVSVQAQVVNLLKRLQKEkgLTFLFIAHDLSMVKHISD 220
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-225 |
3.53e-19 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 84.06 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTnlhalsekeqFAf 86
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS----------IA- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 nrklqmifqdpYASLNP---RMTVREIIL--EPMEihnlynthKARLlvvDELLEAVGLHPDFgSRYPH-------E--- 151
Cdd:cd03250 70 -----------YVSQEPwiqNGTIRENILfgKPFD--------EERY---EKVIKACALEPDL-EILPDgdlteigEkgi 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365521 152 -FSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVN--LLKRLQKEKglTFLFIAHDLSMVKHiSDRIGVM 225
Cdd:cd03250 127 nLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQLLPH-ADQIVVL 200
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
26-232 |
6.29e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 87.46 E-value: 6.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHAL---SEKEQFAFNRKLQMIFQDPYASL- 101
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqldSWRSRLAVVSQTPFLFSDTVANNi 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 102 ---NPRMTVREIilepmeihnlynTHKARLLVV--DELLEAVGLHPDFGSRYPHeFSGGQRQRIGIARALSLNPEFIVAD 176
Cdd:PRK10789 410 algRPDATQQEI------------EHVARLASVhdDILRLPQGYDTEVGERGVM-LSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239365521 177 EPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGHMME 232
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTE-ASEILVMQHGHIAQ 529
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-228 |
6.72e-19 |
|
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: 83.86 E-value: 6.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 19 GKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQP---TEGSVVYRGTNLHALSEKEQFAFNRklqmifQ 95
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQKCVAYVR------Q 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 96 DPYasLNPRMTVREIIL--EPMEIHNLYNTHKARLLVVDELLEAVGlHPDFGSRYPHEFSGGQRQRIGIARALSLNPEFI 173
Cdd:cd03234 89 DDI--LLPGLTVRETLTytAILRLPRKSSDAIRKKRVEDVLLRDLA-LTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 174 VADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSG 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
28-211 |
1.15e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.27 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 28 DGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYR-GTNLHALSekeqfafnrklqmifQDPYasLNPRMT 106
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLP---------------QEPP--LDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 107 VREIIL----------------------------------EPMEIHNLYNTHkARllvVDELLEAVGLHPDFGSRYPHEF 152
Cdd:COG0488 78 VLDTVLdgdaelraleaeleeleaklaepdedlerlaelqEEFEALGGWEAE-AR---AEEILSGLGFPEEDLDRPVSEL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 153 SGGQRQRIGIARALSLNPEFIVADEPISALDV-SVQAqvvnLLKRLQKEKGlTFLFIAHD 211
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEW----LEEFLKNYPG-TVLVVSHD 208
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
27-210 |
1.17e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.40 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVvyrgtnlhalsekeqfAFNRKLQMIF--QDPYAslnPR 104
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI----------------ARPAGARVLFlpQRPYL---PL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 MTVREIILEPmEIHNLYNTHKARllvvdELLEAVGLHP-----DFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPI 179
Cdd:COG4178 440 GTLREALLYP-ATAEAFSDAELR-----EALEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190
....*....|....*....|....*....|..
gi 1239365521 180 SALDVSVQAQvvnLLKRLQKE-KGLTFLFIAH 210
Cdd:COG4178 514 SALDEENEAA---LYQLLREElPGTTVISVGH 542
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-212 |
1.21e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 83.98 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEkeqfaf 86
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMI---FQDPYASLNPRMTVREiilepmeihNL---YNTHKARLLV--VD--------ELLEAVG------LHPDF 144
Cdd:COG1101 76 YKRAKYIgrvFQDPMMGTAPSMTIEE---------NLalaYRRGKRRGLRrgLTkkrrelfrELLATLGlglenrLDTKV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239365521 145 GSrypheFSGGQRQrigiarALSL------NPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDL 212
Cdd:COG1101 147 GL-----LSGGQRQ------ALSLlmatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-224 |
1.77e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 86.00 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 24 VKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYqPT---EGSVVYRGT--NLHALSEKEQfafnRKLQMIFQDpy 98
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcRFKDIRDSEA----LGIVIIHQE-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 99 ASLNPRMTVREIILepmeihnLYNTHkARLLVVD---------ELLEAVGLHPDfgsryPHEFSG----GQRQRIGIARA 165
Cdd:NF040905 87 LALIPYLSIAENIF-------LGNER-AKRGVIDwnetnrrarELLAKVGLDES-----PDTLVTdigvGKQQLVEIAKA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 166 LSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGV 224
Cdd:NF040905 154 LSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITV 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-224 |
1.82e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 86.02 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 33 QIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTnlhaLSEKEQfafnrklqmifqdpYASLNPRMTVREIIl 112
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK----ISYKPQ--------------YIKPDYDGTVEDLL- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 113 epMEIH-----NLYNTHKARLLVVDELLEavglhpdfgsRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQ 187
Cdd:PRK13409 422 --RSITddlgsSYYKSEIIKPLQLERLLD----------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
170 180 190
....*....|....*....|....*....|....*..
gi 1239365521 188 AQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGV 224
Cdd:PRK13409 490 LAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
32-222 |
2.00e-18 |
|
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: 82.59 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 32 FQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHA-------LSEKEQFAFNRKLQMifqdPYASLNPR 104
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKgwrhigyVPQRHEFAWDFPISV----AHTVMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 MTVreiilepmeIHNLYNTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDV 184
Cdd:TIGR03771 77 TGH---------IGWLRRPCVADFAAVRDALRRVGLT-ELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDM 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 1239365521 185 SVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRI 222
Cdd:TIGR03771 147 PTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV 183
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
25-233 |
2.18e-18 |
|
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: 82.07 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 25 KAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTN-----LHALsekeqfafNRKLQMIFQDPYA 99
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDistipLEDL--------RSSLTIIPQDPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 100 SLNprmTVReiilEPMEIHNLYNThkarllvvDELLEAVGLhpdfgSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPI 179
Cdd:cd03369 94 FSG---TIR----SNLDPFDEYSD--------EEIYGALRV-----SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239365521 180 SALDVSVQAqvvnLLKRLQKE--KGLTFLFIAHDLSMVKHIsDRIGVMYLGHMMEI 233
Cdd:cd03369 154 ASIDYATDA----LIQKTIREefTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEY 204
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-238 |
2.42e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.65 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 22 RTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEkeqfafnrklqmifqdpyASL 101
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE------------------AAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 102 NPRMTVReiilePMEIHNLYNTHKARLLVVD---------ELLEAVGLHPDF------------GSRyphEFSGGQRQRI 160
Cdd:PRK11160 413 RQAISVV-----SQRVHLFSATLRDNLLLAApnasdealiEVLQQVGLEKLLeddkglnawlgeGGR---QLSGGEQRRL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 161 GIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHIsDRIGVMYLGhmmEITESGT 238
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQF-DRICVMDNG---QIIEQGT 556
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
27-229 |
5.13e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.34 E-value: 5.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEkeqfAFNRKLQMIFQdpYASLNPRMT 106
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR----LARARIGVVPQ--FDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 107 VREIILepmeIHNLYNTHKARLL--VVDELLEAVGLHPDFGSRYPhEFSGGQRQRIGIARALSLNPEFIVADEPISALDV 184
Cdd:PRK13536 131 VRENLL----VFGRYFGMSTREIeaVIPSLLEFARLESKADARVS-DLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1239365521 185 SVQAQVVNLLKRLQKeKGLTFLFIAHDLSMVKHISDRIGVMYLGH 229
Cdd:PRK13536 206 HARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-238 |
5.84e-18 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 82.00 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 1 MTPLPLLEVSKLKMHFDagkkrTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLM--RLYQPTEGSVVYRGTNLHAL 78
Cdd:CHL00131 2 NKNKPILEIKNLHASVN-----ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 79 sEKEQFAfNRKLQMIFQDPY------------ASLNPRMTVREII-LEPMEIhnlynthkarLLVVDELLEAVGLHPDFG 145
Cdd:CHL00131 77 -EPEERA-HLGIFLAFQYPIeipgvsnadflrLAYNSKRKFQGLPeLDPLEF----------LEIINEKLKLVGMDPSFL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 146 SRYPHE-FSGGQRQRIGIARALSLNPEFIVADEPISALDVS---VQAQVVNLLKRLQKekglTFLFIAHDLSMVKHIS-D 220
Cdd:CHL00131 145 SRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSEN----SIILITHYQRLLDYIKpD 220
|
250
....*....|....*...
gi 1239365521 221 RIGVMYLGhmmEITESGT 238
Cdd:CHL00131 221 YVHVMQNG---KIIKTGD 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
40-231 |
1.13e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 82.61 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 40 FGLvgeSGCGKSTLGRVLMRLYQPTEGSVVYrgtNLHALSEKEQFAF----NRKLQMIFQDpyASLNPRMTVREiilepm 115
Cdd:PRK11144 30 FGR---SGAGKTSLINAISGLTRPQKGRIVL---NGRVLFDAEKGIClppeKRRIGYVFQD--ARLFPHYKVRG------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 116 eihNL-YNTHKARLLVVDELLEAVGLHPDFgSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLL 194
Cdd:PRK11144 96 ---NLrYGMAKSMVAQFDKIVALLGIEPLL-DRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1239365521 195 KRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMM 231
Cdd:PRK11144 172 ERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
31-210 |
1.48e-17 |
|
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: 78.73 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 31 TFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYrgtnlhalSEKEQFAFnrklqmIFQDPYAslnPRMTVREI 110
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--------PEGEDLLF------LPQRPYL---PLGTLREQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 111 ILepmeihnlynthkarllvvdelleavglhpdfgsrYP--HEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQA 188
Cdd:cd03223 84 LI-----------------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|..
gi 1239365521 189 QVVNLLkrlqKEKGLTFLFIAH 210
Cdd:cd03223 129 RLYQLL----KELGITVISVGH 146
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-224 |
1.62e-17 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 83.30 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 33 QIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVvyrGTNLhALSEKEQfafnrklqmifqdpYASLNPRMTVREIil 112
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDL-KISYKPQ--------------YISPDYDGTVEEF-- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 113 epmeihnLYNTHKARL---LVVDELLEAVGLHPDFgSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQ 189
Cdd:COG1245 422 -------LRSANTDDFgssYYKTEIIKPLGLEKLL-DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 493
|
170 180 190
....*....|....*....|....*....|....*
gi 1239365521 190 VVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGV 224
Cdd:COG1245 494 VAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
29-196 |
2.59e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 29 GVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAfnrklqmifqdpYAS----LNPR 104
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH------------YLGhrnaMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 MTVREIILEPMEIHNlynthkARLLVVDELLEAVGLHPDFGSRYpHEFSGGQRQRIGIARALSLN-PEFIVaDEPISALD 183
Cdd:PRK13539 88 LTVAENLEFWAAFLG------GEELDIAAALEAVGLAPLAHLPF-GYLSAGQKRRVALARLLVSNrPIWIL-DEPTAALD 159
|
170
....*....|...
gi 1239365521 184 VSVQAQVVNLLKR 196
Cdd:PRK13539 160 AAAVALFAELIRA 172
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-235 |
4.22e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.60 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLkmhfdagkkRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQ- 83
Cdd:COG1129 255 VVLEVEGL---------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAi 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 84 ---FAF---NRKLQMIFQDpyaslnprMTVRE-IILEPME--IHNLYNTHKARLLVVDELLEAVGLhpdfgsRYPH---- 150
Cdd:COG1129 326 ragIAYvpeDRKGEGLVLD--------LSIREnITLASLDrlSRGGLLDRRRERALAEEYIKRLRI------KTPSpeqp 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 151 --EFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:COG1129 392 vgNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMREG 470
|
250
....*....|...
gi 1239365521 229 HMM------EITE 235
Cdd:COG1129 471 RIVgeldreEATE 483
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-225 |
8.48e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 8.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKE-Q 83
Cdd:PRK10762 3 ALLQLKGIDKAFPG-----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 84 FAfnrKLQMIFQDpyasLN--PRMTVREIILEPMEIHNLYNT--HKARLLVVDELLEAVGLhpDFGSRYP-HEFSGGQRQ 158
Cdd:PRK10762 78 EA---GIGIIHQE----LNliPQLTIAENIFLGREFVNRFGRidWKKMYAEADKLLARLNL--RFSSDKLvGELSIGEQQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365521 159 RIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVF 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-229 |
1.46e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 1 MTPLPLLEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSE 80
Cdd:PRK15439 6 TTAPPLLCARSISKQYSG-----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 81 KEQFAFNrkLQMIFQDPYasLNPRMTVREIILEPMEihnlynTHKARLLVVDELLEAVGLHPDfgsryPHEFSG----GQ 156
Cdd:PRK15439 81 AKAHQLG--IYLVPQEPL--LFPNLSVKENILFGLP------KRQASMQKMKQLLAALGCQLD-----LDSSAGslevAD 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 157 RQRIGIARALSLNPEFIVADEPISALdvsVQAQVVNLLKRLQK--EKGLTFLFIAHDLSMVKHISDRIGVMYLGH 229
Cdd:PRK15439 146 RQIVEILRGLMRDSRILILDEPTASL---TPAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGT 217
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
30-225 |
2.31e-16 |
|
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: 76.60 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAFNRklqmiFQDPYASLNPRM---T 106
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNR-----YSVAYAAQKPWLlnaT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 107 VREIILepmeIHNLYNTHKARLLVvdellEAVGLHPDFgSRYPH-----------EFSGGQRQRIGIARALSLNPEFIVA 175
Cdd:cd03290 95 VEENIT----FGSPFNKQRYKAVT-----DACSLQPDI-DLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 176 DEPISALDVSVQAQVVN--LLKRLQKEKgLTFLFIAHDLSMVKHiSDRIGVM 225
Cdd:cd03290 165 DDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKLQYLPH-ADWIIAM 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-222 |
5.34e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAgkkRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVyRGTNLhalsekeQF 84
Cdd:COG0488 314 KVLELEGLSKSYGD---KTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETV-------KI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFnrklqmiF-QDpYASLNPRMTVREIILEPMEihNLYNTHkARllvvdELLEAVGLHPDFGSRYPHEFSGGQRQRIGIA 163
Cdd:COG0488 381 GY-------FdQH-QEELDPDKTVLDELRDGAP--GGTEQE-VR-----GYLGRFLFSGDDAFKPVGVLSGGEKARLALA 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 164 RALSLNPEFIVADEPISALDV-SVQAqvvnLLKRLQKEKGlTFLFIAHDLSMVKHISDRI 222
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIeTLEA----LEEALDDFPG-TVLLVSHDRYFLDRVATRI 499
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
5-210 |
1.34e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.39 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFDAGKKRTVKAVDGVtfqIREGETFGLVGESGCGKSTLGRVLMrLYQPT----EGSVVYRGTNLHALSE 80
Cdd:TIGR00955 22 QLVSRLRGCFCRERPRKHLLKNVSGV---AKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKEM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 81 KEQFAFNRKLQMIFqdpyaslnPRMTVRE--IILEPMEIHNLYnTHKARLLVVDELLEAVGL----HPDFGSRYPHE-FS 153
Cdd:TIGR00955 98 RAISAYVQQDDLFI--------PTLTVREhlMFQAHLRMPRRV-TKKEKRERVDEVLQALGLrkcaNTRIGVPGRVKgLS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365521 154 GGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAH 210
Cdd:TIGR00955 169 GGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIH 224
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
11-249 |
1.61e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 77.24 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 11 KLK-MHFDAGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGT-NLHALSekeqfafnr 88
Cdd:PRK13545 23 KLKdLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaALIAIS--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 89 klqmifqdpyASLNPRMTVreiiLEPMEIHNLYNTHKARllVVDELLEAVGLHPDFGsRYPHE----FSGGQRQRIGIAR 164
Cdd:PRK13545 94 ----------SGLNGQLTG----IENIELKGLMMGLTKE--KIKEIIPEIIEFADIG-KFIYQpvktYSSGMKSRLGFAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 165 ALSLNPEFIVADEpisALDVSVQAQVVNLLKRLQ--KEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMME---ITESGTL 239
Cdd:PRK13545 157 SVHINPDILVIDE---ALSVGDQTFTKKCLDKMNefKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEygdIKEVVDH 233
|
250
....*....|
gi 1239365521 240 YREPLHPYTK 249
Cdd:PRK13545 234 YDEFLKKYNQ 243
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-225 |
1.99e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.61 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 3 PLPLLEVSKLKMHFDAgkkRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGtnlHALSEKE 82
Cdd:PRK13537 4 SVAPIDFRNVEKRYGD---KLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG---EPVPSRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 83 QFAfNRKLQMIFQdpYASLNPRMTVREIILepmeIHNLY---NTHKARLLvVDELLEAVGLHPDFGSRYpHEFSGGQRQR 159
Cdd:PRK13537 76 RHA-RQRVGVVPQ--FDNLDPDFTVRENLL----VFGRYfglSAAAARAL-VPPLLEFAKLENKADAKV-GELSGGMKRR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239365521 160 IGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKeKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVI 211
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
30-238 |
2.42e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.42 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTLGRVLMRlYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDPyaSLnPRMTVRE 109
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPES---WRKHLSWVGQNP--QL-PHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 110 IILepMEIHNLYNTHkarllvVDELLEAVGLHpDFGSRYPH-----------EFSGGQRQRIGIARALSLNPEFIVADEP 178
Cdd:PRK11174 442 NVL--LGNPDASDEQ------LQQALENAWVS-EFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 179 ISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHIsDRIGVMYLGhmmEITESGT 238
Cdd:PRK11174 513 TASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDG---QIVQQGD 566
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
30-246 |
2.64e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.38 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVyrgtnlhalsEKEQFAFNRKLQMIFQDPYASLnprmTV-R 108
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------RNGKLRIGYVPQKLYLDTTLPL----TVnR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 109 EIILEPmeihnlyNTHKARLLVVDELLEAVGLHpdfgsRYP-HEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQ 187
Cdd:PRK09544 89 FLRLRP-------GTKKEDILPALKRVQAGHLI-----DAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 188 AQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRigVMYLGHmmEITESGTLYREPLHP 246
Cdd:PRK09544 157 VALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDE--VLCLNH--HICCSGTPEVVSLHP 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
30-242 |
3.70e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAF-------NRKLQMIFQDPYASLN 102
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARglvylpeDRQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 103 PRMTVreiilepmeiHN---LYNTHKARLLVVDELLEAVGL---HPDFGSRyphEFSGGQRQRIGIARALSLNPEFIVAD 176
Cdd:PRK15439 362 VCALT----------HNrrgFWIKPARENAVLERYRRALNIkfnHAEQAAR---TLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239365521 177 EPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHMmeiteSGTLYRE 242
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI-----SGALTGA 488
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
26-220 |
8.76e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAFnrklqmIFQDPYASLNPRM 105
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAY------VPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 106 TVREIILEPMEIH-NLYNTHKAR-LLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALD 183
Cdd:PRK15056 96 LVEDVVMMGRYGHmGWLRRAKKRdRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1239365521 184 VSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISD 220
Cdd:PRK15056 175 VKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
29-212 |
9.42e-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: 71.62 E-value: 9.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 29 GVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKeqfafnRKLQMIFQDPYASLNPRMTVR 108
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE------PHENILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 109 EiilepmEIHNLYNTHKARLLVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQA 188
Cdd:TIGR01189 92 E------NLHFWAAIHGGAQRTIEDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|....
gi 1239365521 189 QVVNLLKRLQKEKGLTFLFIAHDL 212
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTHQDL 188
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-225 |
1.28e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.38 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 24 VKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfAFNRKLQMIFQDpyasLN- 102
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALENGISMVHQE----LNl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 103 --PRMTVREIILEPMEIHNLYNTHKARLLVVDELLEAVGLHPDfgsryPHE----FSGGQRQRIGIARALSLNPEFIVAD 176
Cdd:PRK10982 85 vlQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDID-----PRAkvatLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1239365521 177 EPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-210 |
1.32e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.91 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 8 EVSKLKMHFDAGKKRTVKAV-DGVTFQIREGETFGLVGESGCGKSTLGRVLMRLY--QPTEGSVVYrgtnlhalsekeqf 84
Cdd:COG2401 26 RVAIVLEAFGVELRVVERYVlRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV-------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 afnrklqmifqdPYASLNPRMTVREIILepmeihnlyntHKARLLVVDELLEAVGLH-PDFGSRYPHEFSGGQRQRIGIA 163
Cdd:COG2401 92 ------------PDNQFGREASLIDAIG-----------RKGDFKDAVELLNAVGLSdAVLWLRRFKELSTGQKFRFRLA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239365521 164 RALSLNPEFIVADEPISALDVSVqAQVVNL-LKRLQKEKGLTFLFIAH 210
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDRQT-AKRVARnLQKLARRAGITLVVATH 195
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-226 |
1.62e-14 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 72.01 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 35 REGETFGLVGESGCGKSTLGRVLMRLYQPTEGSV-----------VYRGTNLHALSEKeqfAFNRKLQMIFQDPYASLNP 103
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNYFTK---LLEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 104 RM---TVREIILEPMEIHNLynthkarllvvDELLEAVGLHPDFgSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPIS 180
Cdd:cd03236 101 KAvkgKVGELLKKKDERGKL-----------DELVDQLELRHVL-DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1239365521 181 ALDVSVQAQVVNLLKRLQKEKGlTFLFIAHDLSMVKHISDRIGVMY 226
Cdd:cd03236 169 YLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
18-231 |
4.04e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.69 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 18 AGKKRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFafNRKLQMIFQDp 97
Cdd:PRK10895 12 AYKGRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA--RRGIGYLPQE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 98 yASLNPRMTVREIILEPMEIHNLYNTHKaRLLVVDELLEAVG---LHPDFGsrypHEFSGGQRQRIGIARALSLNPEFIV 174
Cdd:PRK10895 87 -ASIFRRLSVYDNLMAVLQIRDDLSAEQ-REDRANELMEEFHiehLRDSMG----QSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 175 ADEPISALDvsvQAQVVNLLKRLQ--KEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMM 231
Cdd:PRK10895 161 LDEPFAGVD---PISVIDIKRIIEhlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
28-222 |
5.56e-14 |
|
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: 68.24 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 28 DGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVyrgtnlhalsekeqfafnrklqmifqdpyaslnprmtv 107
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-------------------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 108 reiilepmeihnlynthkarllvvdelleavgLHPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQ 187
Cdd:cd03221 59 --------------------------------WGSTVKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI 106
|
170 180 190
....*....|....*....|....*....|....*
gi 1239365521 188 AQVVNLLKRLQKekglTFLFIAHDLSMVKHISDRI 222
Cdd:cd03221 107 EALEEALKEYPG----TVILVSHDRYFLDQVATKI 137
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-231 |
5.92e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.25 E-value: 5.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLgrvLMRL--YQPTEGSVVYRGTNLHALSEKEQfafNRKLQMIFQDPYASLNpr 104
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTL---LARMagLLPGQGEILLNGRPLSDWSAAEL---ARHRAYLSQQQSPPFA-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 MTVREIIlepmeihNLYNTHKARL----LVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARAL-----SLNPE--FI 173
Cdd:COG4138 84 MPVFQYL-------ALHQPAGASSeaveQLLAQLAEALGLE-DKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 174 VADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMM 231
Cdd:COG4138 156 LLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-230 |
6.89e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 6.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDAGKkrtvkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTE---------GSVVYRGTNLH 76
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ-----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 77 ALSEKEQfafnRKLQMIFQDpyASLNPRMTVRE-IILEPMEIHNLYNT--------HKARLLvvdELLEAVGLhPDFGSR 147
Cdd:PRK09984 79 RDIRKSR----ANTGYIFQQ--FNLVNRLSVLEnVLIGALGSTPFWRTcfswftreQKQRAL---QALTRVGM-VHFAHQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 148 YPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMYL 227
Cdd:PRK09984 149 RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQ 228
|
...
gi 1239365521 228 GHM 230
Cdd:PRK09984 229 GHV 231
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
27-217 |
7.62e-14 |
|
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: 72.09 E-value: 7.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLM--------RLYQPTEGSVVYrgtnlhalsekeqfafnrklqmIFQDPY 98
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFY----------------------VPQRPY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 99 ASLNprmTVREIILEPMEIHNLynthKARLL---VVDELLEAVGLHP--------DFGSRYPHEFSGGQRQRIGIARALS 167
Cdd:TIGR00954 526 MTLG---TLRDQIIYPDSSEDM----KRRGLsdkDLEQILDNVQLTHilereggwSAVQDWMDVLSGGEKQRIAMARLFY 598
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1239365521 168 LNPEFIVADEPISALDVSVQAQVVNLLkrlqKEKGLTFLFIAHDLSMVKH 217
Cdd:TIGR00954 599 HKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSHRKSLWKY 644
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
28-194 |
2.51e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 28 DGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEkeqfAFNRklQMIFQDPYASLNPRMTV 107
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD----EYHQ--DLLYLGHQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 108 REIILEPMEIHNLYNTHKARllvvdELLEAVGLhpdfgSRY---P-HEFSGGQRQRIGIARALSLNPEFIVADEPISALD 183
Cdd:PRK13538 92 LENLRFYQRLHGPGDDEALW-----EALAQVGL-----AGFedvPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170
....*....|.
gi 1239365521 184 VSVQAQVVNLL 194
Cdd:PRK13538 162 KQGVARLEALL 172
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-230 |
3.97e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAF-------NRK-----LQMif 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANgivyiseDRKrdglvLGM-- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 95 qdpyaSLNPRMTV---REIILEPMEIHnlyntHKARLLVVDELLEAvglhpdFGSRYPH------EFSGGQRQRIGIARA 165
Cdd:PRK10762 346 -----SVKENMSLtalRYFSRAGGSLK-----HADEQQAVSDFIRL------FNIKTPSmeqaigLLSGGNQQKVAIARG 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 166 LSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
5-242 |
2.14e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 5 PLLEVSKLKMHFdaGKkrtVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNL----HALSE 80
Cdd:PRK11614 4 VMLSFDKVSAHY--GK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwqTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 81 KEQFAFNRKLQMIFQdpyaslnpRMTVREiilepmeihNLY--NTHKARLLVVDELLEAVGLHPDFGSRYPHE---FSGG 155
Cdd:PRK11614 79 REAVAIVPEGRRVFS--------RMTVEE---------NLAmgGFFAERDQFQERIKWVYELFPRLHERRIQRagtMSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 156 QRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHM-MEIT 234
Cdd:PRK11614 142 EQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVvLEDT 220
|
....*...
gi 1239365521 235 ESGTLYRE 242
Cdd:PRK11614 221 GDALLANE 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-232 |
2.54e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.69 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 29 GVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDPYASLNprmTVR 108
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD---LRRVLSIIPQSPVLFSG---TVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 109 eIILEPMEIHNLYNTHKArlLVVDELLEAVGLHPdFG-----SRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALD 183
Cdd:PLN03232 1328 -FNIDPFSEHNDADLWEA--LERAHIKDVIDRNP-FGldaevSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1239365521 184 VSVQAqvvnLLKRLQKE--KGLTFLFIAHDLSMVKHiSDRIGVMYLGHMME 232
Cdd:PLN03232 1404 VRTDS----LIQRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLE 1449
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-244 |
3.67e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 67.28 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTnlhalsekeqFAFNRKLQMIFQDpyaslnprmT 106
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----------VAYVPQQAWIQND---------S 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 107 VREIIL--EPMEIHNLYNTHKARLLVVD-ELLEAvGLHPDFGSRYPHeFSGGQRQRIGIARALSLNPEFIVADEPISALD 183
Cdd:TIGR00957 715 LRENILfgKALNEKYYQQVLEACALLPDlEILPS-GDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 184 VSVQAQVV-NLLKRLQKEKGLTFLFIAHDLSMVKHIsDRIGVMYLGhmmEITESGTlYREPL 244
Cdd:TIGR00957 793 AHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGG---KISEMGS-YQELL 849
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
29-222 |
4.82e-12 |
|
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: 64.05 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 29 GVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHalseKEQFAFNRKLQMIFQDPyaSLNPRMTVR 108
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD----FQRDSIARGLLYLGHAP--GIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 109 EiilepmEIHNLYNTHKARllVVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQA 188
Cdd:cd03231 92 E------NLRFWHADHSDE--QVEEALARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180 190
....*....|....*....|....*....|....
gi 1239365521 189 QVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-226 |
5.04e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.37 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 34 IREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVV-----------YRGTNLHA----LSEKEQFAFnRKLQMIFQDPY 98
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEeepswdevlkrFRGTELQNyfkkLYNGEIKVV-HKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 99 ASlnpRMTVREIilepmeihnLYNTHKARLLvvDELLEAVGLHPdFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEP 178
Cdd:PRK13409 175 VF---KGKVREL---------LKKVDERGKL--DEVVERLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239365521 179 ISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHISDRIGVMY 226
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIAY 285
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-222 |
1.49e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.41 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTLgrvLMRL--YQPTEGSVVYRGTNLHALSEKEQfAFNRKLqMIFQDPYASLNPrmtv 107
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTL---LARMagLLPGSGSIQFAGQPLEAWSAAEL-ARHRAY-LSQQQTPPFAMP---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 108 reiILEPMEIHNLYNTHKARLL-VVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARAL-----SLNPE--FIVADEPI 179
Cdd:PRK03695 86 ---VFQYLTLHQPDKTRTEAVAsALNEVAEALGLD-DKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1239365521 180 SALDVSVQAQVVNLLKRLQkEKGLTFLFIAHDLSMVKHISDRI 222
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRV 203
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
26-232 |
1.96e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.74 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGET--------------FGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKeqfAFNRKLQ 91
Cdd:PRK10790 342 DIDNVSFAYRDDNLvlqninlsvpsrgfVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---VLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 92 MIFQDPY---ASLNPRMTV-REIILEpmeihnlynthkarllVVDELLEAV-----------GLHPDFGSRyPHEFSGGQ 156
Cdd:PRK10790 419 MVQQDPVvlaDTFLANVTLgRDISEE----------------QVWQALETVqlaelarslpdGLYTPLGEQ-GNNLSVGQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239365521 157 RQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGHMME 232
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-230 |
2.19e-11 |
|
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: 64.46 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 6 LLEVSKLKMHFDAGKKRtvKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPT-EGSVVYRGTNLHALSEKEQF 84
Cdd:TIGR02633 257 ILEARNLTCWDVINPHR--KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AF-------NRKLQMIFQDPYASLNPRMTVREIILEPMEIHNlynthKARLLVVDELLEAVGL---HPDFGSRyphEFSG 154
Cdd:TIGR02633 335 RAgiamvpeDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDA-----AAELQIIGSAIQRLKVktaSPFLPIG---RLSG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239365521 155 GQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:TIGR02633 407 GNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
29-233 |
2.98e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.76 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 29 GVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDPYASLNprmTVR 108
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD---LRKVLGIIPQAPVLFSG---TVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 109 eIILEPMEIHNlynthKARLLvvdELLEAVGLHpDFGSRYP-----------HEFSGGQRQRIGIARALSLNPEFIVADE 177
Cdd:PLN03130 1331 -FNLDPFNEHN-----DADLW---ESLERAHLK-DVIRRNSlgldaevseagENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 178 PISALDVSVQAqvvnLLKRLQKE--KGLTFLFIAHDLSMVKHiSDRIGVMYLGHMMEI 233
Cdd:PLN03130 1401 ATAAVDVRTDA----LIQKTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEF 1453
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
29-232 |
3.38e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.50 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 29 GVTFQIREGETFGLVGESGCGKSTLGRVLM--RLYQPTEGSVVYRGTNLHALSEKEQFAfnRKLQMIFQDPY-------- 98
Cdd:PRK09580 19 GLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAG--EGIFMAFQYPVeipgvsnq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 99 ----ASLNPRMTVREiiLEPMEIHNLYNthkarllVVDELLEAVGLHPDFGSRYPHE-FSGGQRQRIGIARALSLNPEFI 173
Cdd:PRK09580 97 fflqTALNAVRSYRG--QEPLDRFDFQD-------LMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 174 VADEPISALDVSVQAQVVNLLKRLQKEKgLTFLFIAHDLSMVKHIS-DRIGVMYLGHMME 232
Cdd:PRK09580 168 ILDESDSGLDIDALKIVADGVNSLRDGK-RSFIIVTHYQRILDYIKpDYVHVLYQGRIVK 226
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
30-216 |
3.91e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.50 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLhalsEKEQFAFNRklQMIFQDPYASLNPRMTVRE 109
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQK--QLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 110 iilepmeiHNLYNTH-KARLLVVDEL--LEAVGLHPDFGSRYpheFSGGQRQRIGIARALSLNPEFIVADEPISALDVSV 186
Cdd:PRK13540 94 --------NCLYDIHfSPGAVGITELcrLFSLEHLIDYPCGL---LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180 190
....*....|....*....|....*....|
gi 1239365521 187 QAQVVNLLKRLQKEKGLTFLFIAHDLSMVK 216
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSHQDLPLNK 192
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-222 |
4.36e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 32 FQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVY-----------------RGTNLHALSE--KEQF----AFNR 88
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeqdlivarlqqdpprnvEGTVYDFVAEgiEEQAeylkRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 89 KLQMIFQDPYAS-LNPRMTVREIIlepmEIHNLYNThKARllvVDELLEAVGLHPDfgsRYPHEFSGGQRQRIGIARALS 167
Cdd:PRK11147 104 ISHLVETDPSEKnLNELAKLQEQL----DHHNLWQL-ENR---INEVLAQLGLDPD---AALSSLSGGWLRKAALGRALV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 168 LNPEFIVADEPISALDVSVQAQVVNLLKRLQKekglTFLFIAHDLSMVKHISDRI 222
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRI 223
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-235 |
4.96e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 62.14 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 20 KKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGtnlhalsEKEQFAFNrklqmifqdpyA 99
Cdd:PRK13546 33 KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-------EVSVIAIS-----------A 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 100 SLNPRMTVreiiLEPMEIHNLYNTHKARLL--VVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADE 177
Cdd:PRK13546 95 GLSGQLTG----IENIEFKMLCMGFKRKEIkaMTPKIIEFSELG-EFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 178 pisALDVSVQAQVVNLLKRLQ--KEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITE 235
Cdd:PRK13546 170 ---ALSVGDQTFAQKCLDKIYefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-230 |
6.23e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 60.74 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 9 VSKLKMHFDAGKKR-TVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVL---MRLYQPTEGSVVYRGTNLHalsekeQF 84
Cdd:cd03233 4 LSWRNISFTTGKGRsKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYK------EF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 AFNRKLQMIFQDPYASLNPRMTVREIIlepmeihnlynthkarllvvdelleavglhpDF-----GSRYPHEFSGGQRQR 159
Cdd:cd03233 78 AEKYPGEIIYVSEEDVHFPTLTVRETL-------------------------------DFalrckGNEFVRGISGGERKR 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 160 IGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLS-MVKHISDRIGVMYLGHM 230
Cdd:cd03233 127 VSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQ 198
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
30-224 |
1.55e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTLGRVLMRLYQ-------------------------PTEGSVVYRGTNLHALSEKEQF 84
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgDEEQNVGMKNVNEFSLTKEGGS 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 85 A-----FNRKLQMIFQD----PYASLNPRMTVREIILEPMEIH-NLYNTHK--------------ARLLVVDELLEAVGL 140
Cdd:PTZ00265 1267 GedstvFKNSGKILLDGvdicDYNLKDLRNLFSIVSQEPMLFNmSIYENIKfgkedatredvkraCKFAAIDEFIESLPN 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 141 HPDFG-SRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHiS 219
Cdd:PTZ00265 1347 KYDTNvGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-S 1425
|
....*
gi 1239365521 220 DRIGV 224
Cdd:PTZ00265 1426 DKIVV 1430
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-230 |
1.61e-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: 62.34 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLhalsEKEQFAFNRKLQMIFQdpYASLNPRM 105
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCPQ--HNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 106 TVREIILepmeihnLYNTHKAR-----LLVVDELLEAVGLHPDFGSRyPHEFSGGQRQRIGIARALSLNPEFIVADEPIS 180
Cdd:TIGR01257 1019 TVAEHIL-------FYAQLKGRsweeaQLEMEAMLEDTGLHHKRNEE-AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1239365521 181 ALDVSVQAQVVNLLkrLQKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHM 230
Cdd:TIGR01257 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
29-225 |
2.49e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.72 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 29 GVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEqfaFNRKLQMIFQDPYASLNprmTVR 108
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE---LRRQFSMIPQDPVLFDG---TVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 109 EiilepmeihNLYNTHKARLLVVDELLEAVGLHP--------------DFGSRYphefSGGQRQRIGIARA-LSLNPEFI 173
Cdd:PTZ00243 1402 Q---------NVDPFLEASSAEVWAALELVGLRErvasesegidsrvlEGGSNY----SVGQRQLMCMARAlLKKGSGFI 1468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239365521 174 VADEPIS----ALDVSVQAQVVNLLkrlqkeKGLTFLFIAHDLSMVKHIsDRIGVM 225
Cdd:PTZ00243 1469 LMDEATAnidpALDRQIQATVMSAF------SAYTVITIAHRLHTVAQY-DKIIVM 1517
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-213 |
2.59e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 20 KKRTVkaVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQptegSVVYRGTNLhALSEKEQFAFNRKLQMIFQDPYa 99
Cdd:PLN03211 79 QERTI--LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQ----GNNFTGTIL-ANNRKPTKQILKRTGFVTQDDI- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 100 sLNPRMTVRE--IILEPMEIHNLYnTHKARLLVVDELLEAVGL----HPDFGSRYPHEFSGGQRQRIGIARALSLNPEFI 173
Cdd:PLN03211 151 -LYPHLTVREtlVFCSLLRLPKSL-TKQEKILVAESVISELGLtkceNTIIGNSFIRGISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1239365521 174 VADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLS 213
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMHQPS 267
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-238 |
2.60e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.68 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTL-GRVLMRLYQPTEGSVVYRGTnlhalsekeqFAFNRKLQMIFQdpyaslnprMTVR 108
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLiSAMLGELPPRSDASVVIRGT----------VAYVPQVSWIFN---------ATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 109 EIIL--EPMEIHNLYNTHKARLLVVDELLEAVGLHPDFGSRYPHeFSGGQRQRIGIARALSLNPEFIVADEPISALDVSV 186
Cdd:PLN03130 697 DNILfgSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1239365521 187 QAQVVNllKRLQKE-KGLTFLFIAHDLSMVKHIsDRIgvmYLGHMMEITESGT 238
Cdd:PLN03130 776 GRQVFD--KCIKDElRGKTRVLVTNQLHFLSQV-DRI---ILVHEGMIKEEGT 822
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-272 |
3.48e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 32 FQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSeKEQfafnrkLQMIFQDPYASLNPRM------ 105
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS-FEQ------LQKLVSDEWQRNNTDMlspged 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 106 ----TVREIILEpmeihnlyNTHKARLlvVDELLEAVGLHPDFGSRYPHeFSGGQRQRIGIARALSLNPEFIVADEPISA 181
Cdd:PRK10938 97 dtgrTTAEIIQD--------EVKDPAR--CEQLAQQFGITALLDRRFKY-LSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 182 LDVSVQAQVVNLLKRLQKeKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEITESGTLYREPL-----HPYTkalLSSIP 256
Cdd:PRK10938 166 LDVASRQQLAELLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALvaqlaHSEQ---LEGVQ 241
|
250 260
....*....|....*....|...
gi 1239365521 257 IPDPE-------LEDKRERILLK 272
Cdd:PRK10938 242 LPEPDepsarhaLPANEPRIVLN 264
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-226 |
4.85e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.57 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 35 REGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVV-----------YRGTNLH----ALSEKEQFAfNRKLQMIfqdpya 99
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepswdevlkrFRGTELQdyfkKLANGEIKV-AHKPQYV------ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 100 SLNPRM---TVREIiLEPmeihnlYNTHKarllVVDELLEAVGLHPdFGSRYPHEFSGGQRQRIGIARALSLNPEFIVAD 176
Cdd:COG1245 170 DLIPKVfkgTVREL-LEK------VDERG----KLDELAEKLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1239365521 177 EPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMY 226
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-183 |
1.27e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.37 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHA-----------LSEkeqfAFnrklqmif 94
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAgdiatrrrvgyMSQ----AF-------- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 95 qdpyaSLNPRMTVREiilepmeihNLyNTHkARLL---------VVDELLEAVGLHPDFGSRyPHEFSGGQRQRIGIARA 165
Cdd:NF033858 349 -----SLYGELTVRQ---------NL-ELH-ARLFhlpaaeiaaRVAEMLERFDLADVADAL-PDSLPLGIRQRLSLAVA 411
|
170
....*....|....*...
gi 1239365521 166 LSLNPEFIVADEPISALD 183
Cdd:NF033858 412 VIHKPELLILDEPTSGVD 429
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
34-226 |
1.39e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 56.43 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 34 IREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYrgtnlhalsekeqfafnrklqmifqdpyaslnPRMTvreIILE 113
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW--------------------------------DGIT---PVYK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 114 PMEIhnlynthkarllvvdelleavglhpdfgsryphEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNL 193
Cdd:cd03222 67 PQYI---------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA 113
|
170 180 190
....*....|....*....|....*....|...
gi 1239365521 194 LKRLQKEKGLTFLFIAHDLSMVKHISDRIGVMY 226
Cdd:cd03222 114 IRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-225 |
1.39e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.91 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 21 KRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLM-RLYQPTE-------GSVVYRGTNLHALSEKEQFAFNRKLQM 92
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 93 IFQDPYAslnprMTVREIIL---EPMEIHNLYNTHKARLlVVDELLEAVGLHPDFGsRYPHEFSGGQRQRIGIARALS-- 167
Cdd:PRK13547 91 AAQPAFA-----FSAREIVLlgrYPHARRAGALTHRDGE-IAWQALALAGATALVG-RDVTTLSGGELARVQFARVLAql 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 168 -------LNPEFIVADEPISALDVSVQAQVVNLLKRLQKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:PRK13547 164 wpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAML 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-215 |
3.32e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.42 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTN-----LHALsekeqfafNRKLQMIFQDPYA-SLNP 103
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNiakigLHDL--------RFKITIIPQDPVLfSGSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 104 RMTvreiiLEPMEIHNLYNTHKArllvvdelLEAVGLHpDFGSRYP----HE-------FSGGQRQRIGIARALSLNPEF 172
Cdd:TIGR00957 1377 RMN-----LDPFSQYSDEEVWWA--------LELAHLK-TFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1239365521 173 IVADEPISALDVSVQaqvvNLLK---RLQKEKgLTFLFIAHDLSMV 215
Cdd:TIGR00957 1443 LVLDEATAAVDLETD----NLIQstiRTQFED-CTVLTIAHRLNTI 1483
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-222 |
3.92e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.69 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 37 GETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYrgtnlhalsekeqfafnrklqmifqdpyasLNPRMTVREIILEpme 116
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY------------------------------IDGEDILEEVLDQ--- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 117 ihnlynthkarllvvdelleavgLHPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQV-----V 191
Cdd:smart00382 49 -----------------------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeL 105
|
170 180 190
....*....|....*....|....*....|....*.
gi 1239365521 192 NLLKRLQKEKGLTFLFIAHDLSM-----VKHISDRI 222
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNDEKDlgpalLRRRFDRR 141
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-228 |
6.64e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.33 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTN-LHALSEKEQfafnrklQMIFQDPYASLNPR 104
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISDVHQ-------NMGYCPQFDAIDDL 2026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 105 MTVREiilepmeihNLYNTHKARLLVVDEL-------LEAVGLHPdFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADE 177
Cdd:TIGR01257 2027 LTGRE---------HLYLYARLRGVPAEEIekvanwsIQSLGLSL-YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1239365521 178 PISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-242 |
7.30e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 15 HFDAGKKRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTE-GSVVYRGTnlhalsekeqFAFNRKLQMI 93
Cdd:PLN03232 621 YFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGS----------VAYVPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 94 FQdpyaslnprMTVREIILEPMEIHNlynTHKARLLVVDELLEAVGLHP-----DFGSRYPHeFSGGQRQRIGIARALSL 168
Cdd:PLN03232 691 FN---------ATVRENILFGSDFES---ERYWRAIDVTALQHDLDLLPgrdltEIGERGVN-ISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 169 NPEFIVADEPISALDVSVQAQVVNLLKRlQKEKGLTFLFIAHDLSMVKHIsDRIGVMYLGHM------MEITESGTLYRE 242
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIkeegtfAELSKSGSLFKK 835
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
7-232 |
9.72e-09 |
|
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: 55.30 E-value: 9.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAGKKRTVKAVDGVtfqIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKeqfAF 86
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAY---IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLH---TL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDPYA-------SLNPRMTVREIIL-EPMEIHNLYNTHKARLLVVDELLEAVGlhpdfgsrypHEFSGGQRQ 158
Cdd:cd03288 94 RSRLSIILQDPILfsgsirfNLDPECKCTDDRLwEALEIAQLKNMVKSLPGGLDAVVTEGG----------ENFSVGQRQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239365521 159 RIGIARALSLNPEFIVADEPISALDVSVQaqvvNLLKR--LQKEKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMME 232
Cdd:cd03288 164 LFCLARAFVRKSSILIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVE 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-225 |
1.27e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 23 TVKAVDG------VTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAF-------NRK 89
Cdd:PRK11288 259 RLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgimlcpeDRK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 90 LQMIFqdPYASlnprmtVREIILEPMEIHNLynthKARLLVvDELLEAvglhpDFGSRY--------PH------EFSGG 155
Cdd:PRK11288 339 AEGII--PVHS------VADNINISARRHHL----RAGCLI-NNRWEA-----ENADRFirslniktPSreqlimNLSGG 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 156 QRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVM 225
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVM 469
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-222 |
1.85e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.56 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSEKEQFAFNRKLQMIFQD---PYASLNP 103
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIDgdrEYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 104 RMTVREIILEPMEIHNLYN--------THKARllvVDELLEAVGLHPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVA 175
Cdd:PRK10636 97 QLHDANERNDGHAIATIHGkldaidawTIRSR---AASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1239365521 176 DEPISALDVSVqaqVVNLLKRLQKEKGlTFLFIAHDLSMVKHISDRI 222
Cdd:PRK10636 174 DEPTNHLDLDA---VIWLEKWLKSYQG-TLILISHDRDFLDPIVDKI 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
41-211 |
2.31e-08 |
|
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: 55.33 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 41 GLVGESGCGKSTLGRVLMRLYQPTEGSVVyrgtnlhalsekeqFAFNRKLQMIFQDPYasLNPRMTVREIILEPM----- 115
Cdd:TIGR03719 35 GVLGLNGAGKSTLLRIMAGVDKDFNGEAR--------------PQPGIKVGYLPQEPQ--LDPTKTVRENVEEGVaeikd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 116 ------EIHNLYN----------THKARLlvvDELLEAVGLHpDFGS---------RYP------HEFSGGQRQRIGIAR 164
Cdd:TIGR03719 99 aldrfnEISAKYAepdadfdklaAEQAEL---QEIIDAADAW-DLDSqleiamdalRCPpwdadvTKLSGGERRRVALCR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239365521 165 ALSLNPEFIVADEPISALDvsvqAQVVNLLKR-LQKEKGlTFLFIAHD 211
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLD----AESVAWLERhLQEYPG-TVVAVTHD 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-233 |
2.57e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 21 KRTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALSE----KEQFAF---NRKLQMI 93
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavKKGMAYiteSRRDNGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 94 FqdPYASLNPRMTV-REIILEPME-IHNLYNTHKARLLVvDELLEAVGLHPDFGSRYPHEFSGGQRQRIGIARALSLNPE 171
Cdd:PRK09700 353 F--PNFSIAQNMAIsRSLKDGGYKgAMGLFHEVDEQRTA-ENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239365521 172 FIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHISDRIGVMYLGHMMEI 233
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
7-245 |
3.22e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.36 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAgkkrtVKAVDGVTFQIREGETFGLVGESGCGKSTlGRVLMRLYQPTEGSVVYR----GTNLHALseKE 82
Cdd:NF000106 14 VEVRGLVKHFGE-----VKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRf*twCANRRAL--RR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 83 QFAFNRKLQMIFQDPYASL-NPRMTVREIILEPMEIhnlynthKARllvVDELLEAVGLHPDFGsRYPHEFSGGQRQRIG 161
Cdd:NF000106 86 TIG*HRPVR*GRRESFSGReNLYMIGR*LDLSRKDA-------RAR---ADELLERFSLTEAAG-RAAAKYSGGMRRRLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 162 IARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEkGLTFLF----------IAHDLSMVkhisDRIGVMYLGHMM 231
Cdd:NF000106 155 LAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLttqymeeaeqLAHELTVI----DRGRVIADGKVD 229
|
250
....*....|....*..
gi 1239365521 232 EI-TESG--TLYREPLH 245
Cdd:NF000106 230 ELkTKVGgrTLQIRPAH 246
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-211 |
3.54e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSvVYRGTnlhalsekeqfafnrKLQMIFQDPY-ASLNPRM 105
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR-IHCGT---------------KLEVAYFDQHrAELDPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 106 TVREIILEpmeihnlyntHKARLLVVDELLEAVGLHPDF-----GSRYP-HEFSGGQRQRIGIARaLSLNP-EFIVADEP 178
Cdd:PRK11147 399 TVMDNLAE----------GKQEVMVNGRPRHVLGYLQDFlfhpkRAMTPvKALSGGERNRLLLAR-LFLKPsNLLILDEP 467
|
170 180 190
....*....|....*....|....*....|...
gi 1239365521 179 ISALDVsvqaQVVNLLKRLQKEKGLTFLFIAHD 211
Cdd:PRK11147 468 TNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-234 |
1.48e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.67 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 26 AVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGtnlHALSEKEQFAFNRKLQMIFQDPY---ASLN 102
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG---KPVTAEQPEDYRKLFSAVFTDFHlfdQLLG 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 103 PRMTVREIILEPMEIHNLYNTHKARLlvVDELLEAVglhpdfgsryphEFSGGQRQRIGIARALSLNPEFIVADEpiSAL 182
Cdd:PRK10522 415 PEGKPANPALVEKWLERLKMAHKLEL--EDGRISNL------------KLSKGQKKRLALLLALAEERDILLLDE--WAA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1239365521 183 DVSVQAQVV---NLLKRLQkEKGLTFLFIAHDLSMVKHiSDRIGVMYLGHMMEIT 234
Cdd:PRK10522 479 DQDPHFRREfyqVLLPLLQ-EMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSELT 531
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-229 |
3.65e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.83 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYRGTnlhaLSEKEQFAF----NRKLQMIFQDPYASLNPRM 105
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR----ISFSPQTSWimpgTIKDNIIFGLSYDEYRYTS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 106 TVREIILEPmEIHNLYNTHKARLLvvdelleavglhpDFGSryphEFSGGQRQRIGIARALSLNPEFIVADEPISALDVS 185
Cdd:TIGR01271 521 VIKACQLEE-DIALFPEKDKTVLG-------------EGGI----TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1239365521 186 VQAQVV-NLLKRLQKEKglTFLFIAHDLSMVKHiSDRIGVMYLGH 229
Cdd:TIGR01271 583 TEKEIFeSCLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEGV 624
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-228 |
7.41e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 22 RTVKAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQ-PTEGSVVYRGTNLHALSEKEQFAFN-------RKLQMI 93
Cdd:PRK13549 273 PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGiamvpedRKRDGI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 94 FQD-------PYASLNpRMTVREIILEPMEIHNLyNTHKARLLVvdelleavglhpdfgsRYPHEF------SGGQRQRI 160
Cdd:PRK13549 353 VPVmgvgkniTLAALD-RFTGGSRIDDAAELKTI-LESIQRLKV----------------KTASPElaiarlSGGNQQKA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 161 GIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRLQKEkGLTFLFIAHDLSMVKHISDRIGVMYLG 228
Cdd:PRK13549 415 VLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-191 |
2.27e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 29 GVTFQIREGETFGLVGESGCGKSTLGRVLM--RLYQPTEGSVVYRGTnlhalsEKEQFAFNRKLQMIFQDPYASlnPRMT 106
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGF------PKKQETFARISGYCEQNDIHS--PQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 107 VREIILE------PMEIhnlynTHKARLLVVDELLE----------AVGLHPDFGsrypheFSGGQRQRIGIARALSLNP 170
Cdd:PLN03140 970 VRESLIYsaflrlPKEV-----SKEEKMMFVDEVMElveldnlkdaIVGLPGVTG------LSTEQRKRLTIAVELVANP 1038
|
170 180
....*....|....*....|.
gi 1239365521 171 EFIVADEPISALDVSVQAQVV 191
Cdd:PLN03140 1039 SIIFMDEPTSGLDARAAAIVM 1059
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-197 |
2.65e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 18 AGKKRTVKAVDGVtfqIREGETFGLVGESGCGKSTLgrvLMRLYQPTEGSVVYRGT---NLHALSEkeqfAFNRKLQMIF 94
Cdd:TIGR00956 773 KEKRVILNNVDGW---VKPGTLTALMGASGAGKTTL---LNVLAERVTTGVITGGDrlvNGRPLDS----SFQRSIGYVQ 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 95 QDPYASlnPRMTVREIIL------EPMEI----HNLYNTHKARLLVVDELLEAVGLHPDFGsrypheFSGGQRQRIGIAR 164
Cdd:TIGR00956 843 QQDLHL--PTSTVRESLRfsaylrQPKSVskseKMEYVEEVIKLLEMESYADAVVGVPGEG------LNVEQRKRLTIGV 914
|
170 180 190
....*....|....*....|....*....|....
gi 1239365521 165 ALSLNPEFIV-ADEPISALDVSVQAQVVNLLKRL 197
Cdd:TIGR00956 915 ELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
30-217 |
2.66e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.01 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVvyrgtnlhaLSEkeqfafnRKLQMIFQDPYAsLNPrmTVRE 109
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAE-------RSIAYVPQQAWI-MNA--TVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 110 IIL--EPMEIHNLYNTHKARLLVVDELLEAVGLHPDFGSRYPHeFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQ 187
Cdd:PTZ00243 740 NILffDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818
|
170 180 190
....*....|....*....|....*....|..
gi 1239365521 188 AQVVN--LLKRLqkeKGLTFLFIAHDLSMVKH 217
Cdd:PTZ00243 819 ERVVEecFLGAL---AGKTRVLATHQVHVVPR 847
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
34-68 |
2.95e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 48.64 E-value: 2.95e-06
10 20 30
....*....|....*....|....*....|....*
gi 1239365521 34 IREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSV 68
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
153-236 |
2.99e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 153 SGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLLKRL-QKEKGLtfLFIAHDLSMVKHISDRIGVMYLGHMM 231
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGLVA 470
|
....*
gi 1239365521 232 EITES 236
Cdd:PRK10982 471 GIVDT 475
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
34-133 |
3.56e-06 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 45.80 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 34 IREGETFG-LVGESGCGKSTLGRVLMRLYQPTEGSVVYrgTNLHALSEKEQFAfnRKLQMIFQDPYASLNPRMTVREIIl 112
Cdd:pfam13401 1 IRFGAGILvLTGESGTGKTTLLRRLLEQLPEVRDSVVF--VDLPSGTSPKDLL--RALLRALGLPLSGRLSKEELLAAL- 75
|
90 100
....*....|....*....|.
gi 1239365521 113 epmeIHNLYNTHKARLLVVDE 133
Cdd:pfam13401 76 ----QQLLLALAVAVVLIIDE 92
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
36-245 |
1.37e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 36 EGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVY-RGTNLHALSEkEQFAF------------NRKLQMIFQDP---YA 99
Cdd:PRK15064 26 GGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKLRQ-DQFAFeeftvldtvimgHTELWEVKQERdriYA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 100 slNPRMT------VREIILEPMEIHNlYnTHKARllvVDELLEAVGLHPDFGSRYPHEFSGGQRQRIGIARALSLNPEFI 173
Cdd:PRK15064 105 --LPEMSeedgmkVADLEVKFAEMDG-Y-TAEAR---AGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDIL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 174 VADEPISALDVSvqaqVVNLLKRLQKEKGLTFLFIAHD---LSMV-KHISD------RIgvmYLGHMMEITESGTLYREP 243
Cdd:PRK15064 178 LLDEPTNNLDIN----TIRWLEDVLNERNSTMIIISHDrhfLNSVcTHMADldygelRV---YPGNYDEYMTAATQARER 250
|
..
gi 1239365521 244 LH 245
Cdd:PRK15064 251 LL 252
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
134-184 |
4.70e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 4.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1239365521 134 LLEAVGLHPDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDV 184
Cdd:PLN03073 327 ILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
7-222 |
6.22e-05 |
|
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: 43.08 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHfdagkkrtvkAVDGVTFQIREGETFGLVGESGCGKSTLgrvlmrlyqptegsvvyrgtnlhalsekeqfaf 86
Cdd:cd03238 1 LTVSGANVH----------NLQNLDVSIPLNVLVVVTGVSGSGKSTL--------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 nrklqmIFQDPYASLNPRMtvreiilepmeIHNLYNTHKARLLVVDEL--LEAVGLHPDFGSRYPHEFSGGQRQRIGIAR 164
Cdd:cd03238 38 ------VNEGLYASGKARL-----------ISFLPKFSRNKLIFIDQLqfLIDVGLGYLTLGQKLSTLSGGELQRVKLAS 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 165 ALSLNPE--FIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHiSDRI 222
Cdd:cd03238 101 ELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSS-ADWI 158
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
102-222 |
1.19e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.63 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 102 NPRMTVREIilepMEIHNLYNTHKARLLVVDEL--LEAVGLHPDFGSRYPHEFSGGQRQRIGIARAL--SLNPEFIVADE 177
Cdd:cd03270 90 NPRSTVGTV----TEIYDYLRLLFARVGIRERLgfLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIgsGLTGVLYVLDE 165
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1239365521 178 PISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVKHiSDRI 222
Cdd:cd03270 166 PSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA-ADHV 208
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-237 |
1.28e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 7 LEVSKLKMHFDAGKkrtvkAVDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVvyrgtnlhalsekeQFAF 86
Cdd:PRK15064 320 LEVENLTKGFDNGP-----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------------KWSE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 87 NRKLQMIFQDPYASLNPRMTVreiilepMEIHNLYNTHK----------ARLLVV-DELLEAVGLhpdfgsrypheFSGG 155
Cdd:PRK15064 381 NANIGYYAQDHAYDFENDLTL-------FDWMSQWRQEGddeqavrgtlGRLLFSqDDIKKSVKV-----------LSGG 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 156 QRQRIGIARALSLNPEFIVADEPISALDV-SVQAqvVNLlkRLQKEKGlTFLFIAHDLSMVKHISDRIgvmylghmMEIT 234
Cdd:PRK15064 443 EKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIES--LNM--ALEKYEG-TLIFVSHDREFVSSLATRI--------IEIT 509
|
...
gi 1239365521 235 ESG 237
Cdd:PRK15064 510 PDG 512
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
153-226 |
3.07e-04 |
|
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: 40.81 E-value: 3.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 153 SGGQRQRIGIARALSL---NPE-FIVADEPISALDVSVQAQVVNLLKRLQKeKGLTFLFIAHDLSMVKhISDRIGVMY 226
Cdd:cd03227 79 SGGEKELSALALILALaslKPRpLYILDEIDRGLDPRDGQALAEAILEHLV-KGAQVIVITHLPELAE-LADKLIHIK 154
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
27-184 |
3.94e-04 |
|
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: 41.84 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 27 VDGVTFQIREGETFGLVGESGCGKSTLGRVLMRLYQPTEGSVVYrGTNLHaLSEKEQFafnRKlqmifqdpyaSLNPRMT 106
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK-LAYVDQS---RD----------ALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 107 VREIILEPMEIHNLYNThkarllvvdelleavglhpDFGSR-YPHEF--------------SGGQRQRIGIARALSLNPE 171
Cdd:TIGR03719 403 VWEEISGGLDIIKLGKR-------------------EIPSRaYVGRFnfkgsdqqkkvgqlSGGERNRVHLAKTLKSGGN 463
|
170
....*....|...
gi 1239365521 172 FIVADEPISALDV 184
Cdd:TIGR03719 464 VLLLDEPTNDLDV 476
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-183 |
8.55e-04 |
|
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: 41.05 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 30 VTFQIREGETFGLVGESGCGKSTLGRVLMRLYQpTEGSVVYRGTNLHALS-EKEQFAFNRKLQMIF---------QDPYA 99
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTlQTWRKAFGVIPQKVFifsgtfrknLDPYE 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 100 slnpRMTVREI--ILEPMEIHNLYNTHKARLlvvDELLEAVGlhpdfgsrypHEFSGGQRQRIGIARALSLNPEFIVADE 177
Cdd:TIGR01271 1317 ----QWSDEEIwkVAEEVGLKSVIEQFPDKL---DFVLVDGG----------YVLSNGHKQLMCLARSILSKAKILLLDE 1379
|
....*.
gi 1239365521 178 PISALD 183
Cdd:TIGR01271 1380 PSAHLD 1385
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
61-273 |
1.02e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 61 YQPTEGSVVYRGTNLHALSEK---EQFAFNRKLQmifqdpyasLNPRmtvREIILEPM--EIhnlynthKARLlvvdELL 135
Cdd:TIGR00630 416 LKPEALAVTVGGKSIADVSELsirEAHEFFNQLT---------LTPE---EKKIAEEVlkEI-------RERL----GFL 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 136 EAVGLHPDFGSRYPHEFSGGQRQRIGIARAL--SLNPEFIVADEPISALDVSVQAQVVNLLKRLQKeKGLTFLFIAHDLS 213
Cdd:TIGR00630 473 IDVGLDYLSLSRAAGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEHDED 551
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239365521 214 MVKHiSDRIGVMYLG---HMMEITESGTLyREPL---HPYTKALLS---SIPIPDPELEDKRERILLKG 273
Cdd:TIGR00630 552 TIRA-ADYVIDIGPGageHGGEVVASGTP-EEILanpDSLTGQYLSgrkKIEVPAERRPGNGKFLTLKG 618
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
44-194 |
2.42e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.31 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 44 GESGCGKSTLGRVLMRLYQPTEGSVVYRGTNLHALsekeqfafnrklqmifQDPYAS-------LNPRMTVREIILEPME 116
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI----------------AKPYCTyighnlgLKLEMTVFENLKFWSE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239365521 117 IHNLYNThkarllvVDELLEAVGLHpDFGSRYPHEFSGGQRQRIGIARALSLNPEFIVADEPISALDVSVQAQVVNLL 194
Cdd:PRK13541 97 IYNSAET-------LYAAIHYFKLH-DLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
153-216 |
3.16e-03 |
|
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: 38.75 E-value: 3.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365521 153 SGGQRQRIGIARALSL---NPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVK 216
Cdd:cd03271 171 SGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHNLDVIK 236
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| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
153-216 |
3.40e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 3.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239365521 153 SGGQRQRIGIARALS---LNPEFIVADEPISALDVSVQAQVVNLLKRLqKEKGLTFLFIAHDLSMVK 216
Cdd:TIGR00630 831 SGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNLDVIK 896
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| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-178 |
4.44e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 38.95 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 24 VKAVDGVTFQIREGETFGLVGESGCGKSTL------------GRVL-----MRlyQPTEGSVVYR---------GTNL-H 76
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLlsliagarkiqqGRVEvlggdMA--DARHRRAVCPriaympqglGKNLyP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239365521 77 ALSEKE--QFaFNRklqmIF-QDPyaslnprmtvREiilepmeihnlyntHKARllvVDELLEAVGLHPdFGSRYPHEFS 153
Cdd:NF033858 92 TLSVFEnlDF-FGR----LFgQDA----------AE--------------RRRR---IDELLRATGLAP-FADRPAGKLS 138
|
170 180
....*....|....*....|....*
gi 1239365521 154 GGQRQRIGIARALSLNPEFIVADEP 178
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEP 163
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