|
Name |
Accession |
Description |
Interval |
E-value |
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-295 |
0e+00 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 543.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFFTSKG-------TIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENV 73
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGlfgrtvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 74 HGrKSRSELKKFNRKMQMIFQDPYASLNPRMTVADIIAEGIDIHGLAkTRKERMAKVHELLETVGLNKEHANRYPHEFSG 153
Cdd:COG4608 83 TG-LSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLA-SKAERRERVAELLELVGLRPEHADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 154 GQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELA 233
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 234 PSDELYRNPVHPYTKALLSAIPLPDPDSEKTRQRKIYD-PS-IHDYNG----------------EEPELREVSPGHYVSC 295
Cdd:COG4608 241 PRDELYARPLHPYTQALLSAVPVPDPERRRERIVLEGDvPSpLNPPSGcrfhtrcpyaqdrcatEEPPLREVGPGHQVAC 320
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-295 |
6.40e-168 |
|
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: 468.38 E-value: 6.40e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDA---TSGEVLFNGENVHgRKSRSE 81
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLL-KLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 82 LKKF-NRKMQMIFQDPYASLNPRMTVADIIAEGIDIHGLAkTRKERMAKVHELLETVGLN--KEHANRYPHEFSGGQRQR 158
Cdd:COG0444 80 LRKIrGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGL-SKAEARERAIELLERVGLPdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 159 IGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDEL 238
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654962578 239 YRNPVHPYTKALLSAIPLPDPDSEKTRQRKIYDPSIHDY-NG----------------EEPELREVSPGHYVSC 295
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPpSGcrfhprcpyamdrcreEEPPLREVGPGHRVAC 312
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-260 |
2.73e-157 |
|
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: 448.97 E-value: 2.73e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFFT-SKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgRKSR 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLT-KLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 80 SELKKFNRKMQMIFQDPYASLNPRMTVADIIAEGIDIHGLAkTRKERMAKVHELLETVGLNKEHANRYPHEFSGGQRQRI 159
Cdd:COG1123 335 RSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLL-SRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 160 GIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELY 239
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
250 260
....*....|....*....|.
gi 654962578 240 RNPVHPYTKALLSAIPLPDPD 260
Cdd:COG1123 494 ANPQHPYTRALLAAVPSLDPA 514
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-258 |
3.35e-144 |
|
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: 416.39 E-value: 3.35e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFFTSKG-------TIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLyDATSGEVLFNGENVHGRk 77
Cdd:COG4172 275 LLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGL- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 78 SRSELKKFNRKMQMIFQDPYASLNPRMTVADIIAEGIDIHGLAKTRKERMAKVHELLETVGLNKEHANRYPHEFSGGQRQ 157
Cdd:COG4172 353 SRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQ 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 158 RIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDE 237
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQ 512
|
250 260
....*....|....*....|.
gi 654962578 238 LYRNPVHPYTKALLSAIPLPD 258
Cdd:COG4172 513 VFDAPQHPYTRALLAAAPLLE 533
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-299 |
7.84e-136 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 387.91 E-value: 7.84e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHF---------FTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHG 75
Cdd:PRK15079 8 LLEVADLKVHFdikdgkqwfWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 76 rKSRSELKKFNRKMQMIFQDPYASLNPRMTVADIIAEGIDIHGLAKTRKERMAKVHELLETVGLNKEHANRYPHEFSGGQ 155
Cdd:PRK15079 88 -MKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 156 RQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPS 235
Cdd:PRK15079 167 CQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 236 DELYRNPVHPYTKALLSAIPLPDPDSEKTRQRKIYD---PS-IHDYNG----------------EEPELrEVSPGHYVSC 295
Cdd:PRK15079 247 DEVYHNPLHPYTKALMSAVPIPDPDLERNKTIQLLEgelPSpINPPSGcvfrtrcpiagpecakTRPVL-EGSFRHAVSC 325
|
....
gi 654962578 296 SQAE 299
Cdd:PRK15079 326 LKVD 329
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-233 |
6.55e-127 |
|
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: 361.05 E-value: 6.55e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGrKSRSELKK 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLK-LSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 FNRKMQMIFQDPYASLNPRMTVADIIAEGIDIHGLAKTRKERMAKVHELLETVGLNKEHANRYPHEFSGGQRQRIGIARA 164
Cdd:cd03257 80 RRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654962578 165 LAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELA 233
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-299 |
1.06e-121 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 351.57 E-value: 1.06e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQH------FFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVH 74
Cdd:PRK11308 1 SQQPLLQAIDLKKHypvkrgLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 75 GrKSRSELKKFNRKMQMIFQDPYASLNPRMTVADIIAEGIDIHgLAKTRKERMAKVHELLETVGLNKEHANRYPHEFSGG 154
Cdd:PRK11308 81 K-ADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLIN-TSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 155 QRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAP 234
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 235 SDELYRNPVHPYTKALLSAIP--LPDPDSEK--------------------TRQRKIYDPSihdyNGEEPELREVSpGHY 292
Cdd:PRK11308 239 KEQIFNNPRHPYTQALLSATPrlNPDDRRERikltgelpsplnpppgcafnARCPRAFGRC----RQEQPQLRDYD-GRL 313
|
....*..
gi 654962578 293 VSCSQAE 299
Cdd:PRK11308 314 VACFAVE 320
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-255 |
5.35e-120 |
|
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: 344.48 E-value: 5.35e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSelkk 84
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 FNRKMQMIFQDPYASLNPRMTVADIIAEGIDIHGlaktRKERMAKVHELLETVGLNKEHANRYPHEFSGGQRQRIGIARA 164
Cdd:COG1124 77 FRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHG----LPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 165 LAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPVH 244
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
250
....*....|.
gi 654962578 245 PYTKALLSAIP 255
Cdd:COG1124 233 PYTRELLAASL 243
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-301 |
7.86e-104 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 316.03 E-value: 7.86e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 22 IKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgRKSRSELKKFNRKMQMIFQDPYASLN 101
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID-TLSPGKLQALRRDIQFIFQDPYASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 102 PRMTVADIIAEGIDIHGLAKTrKERMAKVHELLETVGLNKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISAL 181
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLLPG-KAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 182 DVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPVHPYTKALLSAIPLPDPDS 261
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVADPSR 574
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 654962578 262 EKTRQRKIYD--PSIHDYNGEEPE---LREVSPGHYVSCSQAEFA 301
Cdd:PRK10261 575 QRPQRVLLSDdlPSNIHLRGEEVAavsLQCVGPGHYVAQPQSEYA 619
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-260 |
2.34e-102 |
|
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: 309.31 E-value: 2.34e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRL--YDA--TSGEVLFNGENVHGr 76
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpDPAahPSGSILFDGQDLLG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 77 KSRSELKKF-NRKMQMIFQDPYASLNPRMTVADIIAEGIDIH-GLakTRKERMAKVHELLETVGLN--KEHANRYPHEFS 152
Cdd:COG4172 81 LSERELRRIrGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHrGL--SGAAARARALELLERVGIPdpERRLDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 153 GGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVEL 232
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
250 260
....*....|....*....|....*...
gi 654962578 233 APSDELYRNPVHPYTKALLSAIPLPDPD 260
Cdd:COG4172 239 GPTAELFAAPQHPYTRKLLAAEPRGDPR 266
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-252 |
1.78e-83 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 260.79 E-value: 1.78e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFFTSKGTIK-------AVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYdATSGEVLFNGENVHGRk 77
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNL- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 78 SRSELKKFNRKMQMIFQDPYASLNPRMTVADIIAEGIDIHGLAKTRKERMAKVHELLETVGLNKEHANRYPHEFSGGQRQ 157
Cdd:PRK15134 353 NRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQ 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 158 RIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDE 237
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCER 512
|
250
....*....|....*
gi 654962578 238 LYRNPVHPYTKALLS 252
Cdd:PRK15134 513 VFAAPQQEYTRQLLA 527
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-274 |
1.10e-82 |
|
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: 258.29 E-value: 1.10e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDkLLEIKGLKQHFftSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDAT---SGEVLFNGENVhgrk 77
Cdd:COG1123 1 MTP-LLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 78 SRSELKKFNRKMQMIFQDPYASLNPrMTVADIIAEGIDIHGLakTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQ 157
Cdd:COG1123 74 LELSEALRGRRIGMVFQDPMTQLNP-VTVGDQIAEALENLGL--SRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 158 RIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDE 237
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
250 260 270
....*....|....*....|....*....|....*..
gi 654962578 238 LYRNPvhpytkALLSAIPLPDPDSEKTRQRKIYDPSI 274
Cdd:COG1123 230 ILAAP------QALAAVPRLGAARGRAAPAAAAAEPL 260
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-253 |
2.79e-82 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 249.37 E-value: 2.79e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFFTSKG-----TIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVH--GRK 77
Cdd:COG4167 4 LLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygDYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 78 SRSelkkfnRKMQMIFQDPYASLNPRMTVADIIAEGIdIHGLAKTRKERMAKVHELLETVGLNKEHANRYPHEFSGGQRQ 157
Cdd:COG4167 84 YRC------KHIRMIFQDPNTSLNPRLNIGQILEEPL-RLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 158 RIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDE 237
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236
|
250
....*....|....*.
gi 654962578 238 LYRNPVHPYTKALLSA 253
Cdd:COG4167 237 VFANPQHEVTKRLIES 252
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-259 |
2.68e-77 |
|
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: 236.63 E-value: 2.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFFTS-----KGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKsR 79
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD-R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 80 SELKKFNRKMQMIFQDPYASLNPRMTVADIIAEGIDiHGLAKTRKERMAKVHELLETVGLNKEHANRYPHEFSGGQRQRI 159
Cdd:TIGR02769 81 KQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLR-HLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 160 GIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELY 239
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL 239
|
250 260
....*....|....*....|
gi 654962578 240 RNPvHPYTKALLSAIPLPDP 259
Cdd:TIGR02769 240 SFK-HPAGRNLQSAVLPEHP 258
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-246 |
1.78e-75 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 234.61 E-value: 1.78e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGrksrs 80
Cdd:COG3842 1 MAMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 eLKKFNRKMQMIFQDpYAsLNPRMTVADIIAEGIDIHGLAKtrKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIG 160
Cdd:COG3842 72 -LPPEKRNVGMVFQD-YA-LFPHLTVAENVAFGLRMRGVPK--AEIRARVAELLELVGL-EGLADRYPHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 161 IARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHD----LSMvkyiSDRIGVMYRGKIVELAPSD 236
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLAL----ADRIAVMNDGRIEQVGTPE 221
|
250
....*....|
gi 654962578 237 ELYRNPVHPY 246
Cdd:COG3842 222 EIYERPATRF 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-266 |
1.09e-73 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 227.26 E-value: 1.09e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHF----FTSKGTIKAV-DGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhGRKSR 79
Cdd:PRK10419 3 LLNVSGLSHHYahggLSGKHQHQTVlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL-AKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 80 SELKKFNRKMQMIFQDPYASLNPRMTVADIIAEGIDiHGLAKTRKERMAKVHELLETVGLNKEHANRYPHEFSGGQRQRI 159
Cdd:PRK10419 82 AQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLR-HLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 160 GIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELY 239
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKL 240
|
250 260
....*....|....*....|....*..
gi 654962578 240 RNPvHPYTKALLSAIPLPDPDSEKTRQ 266
Cdd:PRK10419 241 TFS-SPAGRVLQNAVLPAFPVRRRTTE 266
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-263 |
3.41e-73 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 228.46 E-value: 3.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDA---TSGEVLFNGENVHGRK 77
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 78 SRsELKKFN-RKMQMIFQDPYASLNPRMTVADIIAEGIDIH-GLAKtrKERMAKVHELLETVGL--NKEHANRYPHEFSG 153
Cdd:PRK09473 88 EK-ELNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHkGMSK--AEAFEESVRMLDAVKMpeARKRMKMYPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 154 GQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELA 233
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 244
|
250 260 270
....*....|....*....|....*....|
gi 654962578 234 PSDELYRNPVHPYTKALLSAIPLPDPDSEK 263
Cdd:PRK09473 245 NARDVFYQPSHPYSIGLLNAVPRLDAEGES 274
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-288 |
2.08e-72 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 226.50 E-value: 2.08e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhGRKSRSELKKF 85
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL-TALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDpyASLNPRMTVADIIAEGIDIHGLAKtrKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:COG1135 81 RRKIGMIFQH--FNLLSSRTVAENVALPLEIAGVPK--AEIRKRVAELLELVGL-SDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPVHP 245
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 654962578 246 YTKALLSAIPLPDPD-------SEKTRQRKIYDPSIHDYNGEEPELREVS 288
Cdd:COG1135 236 LTRRFLPTVLNDELPeellarlREAAGGGRLVRLTFVGESADEPLLSELA 285
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-242 |
2.12e-69 |
|
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: 215.14 E-value: 2.12e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhGRKSRSELKK 84
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDL-TLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 FNRKMQMIFQDpYASLNPRmTVADIIAEGIDIHGLAKtrKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARA 164
Cdd:cd03258 80 ARRRIGMIFQH-FNLLSSR-TVFENVALPLEIAGVPK--AEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 165 LAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-295 |
1.62e-68 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 216.15 E-value: 1.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYD----ATSGEVLFNGENVHGRKSRS 80
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 ELKKFNRKMQMIFQDPYASLNPRMTVADIIAEGIDIH--GLAKTRKERMAkvhELLETVGLnKEHANR---YPHEFSGGQ 155
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHqgGNKKTRRQRAI---DLLNQVGI-PDPASRldvYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 156 RQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPS 235
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654962578 236 DELYRNPVHPYTKALLSAipLPDPDSEKTRQRKI-------YD-----------PSIHDY-NGEEPELREVsPGHYVSC 295
Cdd:PRK11022 239 HDIFRAPRHPYTQALLRA--LPEFAQDKARLASLpgvvpgkYDrpngcllnprcPYATDRcRAEEPALNML-AGRQSKC 314
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-231 |
3.11e-67 |
|
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: 209.25 E-value: 3.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRksrselkkf 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDPyaSLNPRMTVADIIAEGIDIHGLAKtrKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:cd03293 72 GPDRGYVFQQD--ALLPWLTVLDNVALGLELQGVPK--AEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVM--YRGKIVE 231
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVA 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-290 |
2.64e-66 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 218.57 E-value: 2.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 2 TDKLLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLfNGENVHGRKSRS- 80
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ-CDKMLLRRRSRQv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 -ELKKFNRK---------MQMIFQDPYASLNPRMTVADIIAEGIDIH-GLAktRKERMAKVHELLETVGLNKEHA--NRY 147
Cdd:PRK10261 88 iELSEQSAAqmrhvrgadMAMIFQEPMTSLNPVFTVGEQIAESIRLHqGAS--REEAMVEAKRMLDQVRIPEAQTilSRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 148 PHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRG 227
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 228 KIVELAPSDELYRNPVHPYTKALLSAIPLPDPDSEKTRQRKIYDPSIHDYNGEEPELRE--VSPG 290
Cdd:PRK10261 246 EAVETGSVEQIFHAPQHPYTRALLAAVPQLGAMKGLDYPRRFPLISLEHPAKQEPPIEQdtVVDG 310
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-260 |
1.07e-65 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 214.57 E-value: 1.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDA-----TSGEVLFNGENVHg 75
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 76 RKSRSELKKF-NRKMQMIFQDPYASLNPRMTVADIIAEGIDIHGLAKTRKERmAKVHELLETVGLnKEHANR---YPHEF 151
Cdd:PRK15134 80 HASEQTLRGVrGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAAR-GEILNCLDRVGI-RQAAKRltdYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 152 SGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVE 231
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
250 260
....*....|....*....|....*....
gi 654962578 232 LAPSDELYRNPVHPYTKALLSAIPLPDPD 260
Cdd:PRK15134 238 QNRAATLFSAPTHPYTQKLLNSEPSGDPV 266
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-231 |
1.04e-64 |
|
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: 202.36 E-value: 1.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSelkkf 85
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 nRKMQMIFQDPyaSLNPRMTVADIIAEGIDIHGLAKtrKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:cd03259 72 -RNIGMVFQDY--ALFPHLTVAENIAFGLKLRGVPK--AEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVE 231
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-254 |
1.51e-64 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 202.92 E-value: 1.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSrsELKK 84
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKK--DINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 FNRKMQMIFQdpyaSLN--PRMTVADIIAEGIdIHGLAKTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIA 162
Cdd:COG1126 75 LRRKVGMVFQ----QFNlfPHLTVLENVTLAP-IKVKKMSKAEAEERAMELLERVGL-ADKADAYPAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 163 RALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENP 227
|
250
....*....|..
gi 654962578 243 VHPYTKALLSAI 254
Cdd:COG1126 228 QHERTRAFLSKV 239
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-251 |
4.25e-64 |
|
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: 201.75 E-value: 4.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRkSRS 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGL-SEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 ELKKFNRKMQMIFQDP--YASlnprMTVADIIAEGIDIHGlAKTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQR 158
Cdd:COG1127 76 ELYELRRRIGMLFQGGalFDS----LTVFENVAFPLREHT-DLSEAEIRELVLEKLELVGL-PGAADKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 159 IGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDEL 238
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
250
....*....|...
gi 654962578 239 YRNPvHPYTKALL 251
Cdd:COG1127 230 LASD-DPWVRQFL 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-265 |
9.73e-64 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 204.26 E-value: 9.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 7 EIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhGRKSRSELKKFN 86
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL-TALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 87 RKMQMIFQDpYASLNPRmTVADIIAEGIDIHGLAKtrKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALA 166
Cdd:PRK11153 82 RQIGMIFQH-FNLLSSR-TVFDNVALPLELAGTPK--AEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 167 VEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPVHPY 246
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPL 236
|
250 260
....*....|....*....|
gi 654962578 247 TKALL-SAIPLPDPDSEKTR 265
Cdd:PRK11153 237 TREFIqSTLHLDLPEDYLAR 256
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
16-253 |
1.74e-63 |
|
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: 200.60 E-value: 1.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 16 FTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMIFQD 95
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI----REQDPVELRRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 96 pyASLNPRMTVADIIAEGIDIHGLAKTRKERmaKVHELLETVGLN-KEHANRYPHEFSGGQRQRIGIARALAVEPDFIIA 174
Cdd:cd03295 84 --IGLFPHMTVEENIALVPKLLKWPKEKIRE--RADELLALVGLDpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654962578 175 DEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPVHPYTKALLSA 253
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-229 |
4.64e-63 |
|
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: 198.48 E-value: 4.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgRKSRSELKKF 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS-KLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 -NRKMQMIFQDPYasLNPRMTVADIIAEGIDIHGlaKTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARA 164
Cdd:cd03255 80 rRRHIGFVFQSFN--LLPDLTALENVELPLLLAG--VPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 165 LAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYiSDRIGVMYRGKI 229
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-231 |
1.99e-62 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 198.39 E-value: 1.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRksrs 80
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 elkkfNRKMQMIFQDPyaSLNPRMTVADIIAEGIDIHGLAKtrKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIG 160
Cdd:COG1116 79 -----GPDRGVVFQEP--ALLPWLTVLDNVALGLELRGVPK--AERRERARELLELVGL-AGFEDAYPHQLSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654962578 161 IARALAVEPDFIIADEPISALDV----SIQAQVVnlmkKLQRERGLTYLFIAHDLSMVKYISDRIGVMYR--GKIVE 231
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDAltreRLQDELL----RLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-247 |
2.03e-62 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 201.14 E-value: 2.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGE----NVHGRKsrse 81
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftNLPPRE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 82 lkkfnRKMQMIFQDpYAsLNPRMTVADIIAEGIDIHGLAKtrKERMAKVHELLETVGLNkEHANRYPHEFSGGQRQRIGI 161
Cdd:COG1118 75 -----RRVGFVFQH-YA-LFPHMTVAENIAFGLRVRPPSK--AEIRARVEELLELVQLE-GLADRYPSQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 162 ARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRN 241
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
....*.
gi 654962578 242 PVHPYT 247
Cdd:COG1118 225 PATPFV 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-246 |
2.92e-62 |
|
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: 198.25 E-value: 2.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 4 KLLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgRKSRSELK 83
Cdd:cd03294 19 KLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA-AMSRKELR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 84 KFNRK-MQMIFQDpYAsLNPRMTVADIIAEGIDIHGLAktRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIA 162
Cdd:cd03294 98 ELRRKkISMVFQS-FA-LLPHRTVLENVAFGLEVQGVP--RAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 163 RALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:cd03294 173 RALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
....
gi 654962578 243 VHPY 246
Cdd:cd03294 253 ANDY 256
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-243 |
8.63e-62 |
|
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: 195.92 E-value: 8.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGrksrseLKKF 85
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN------LPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDpYAsLNPRMTVADIIAEGIDIHGLAKtrKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:cd03300 71 KRPVNTVFQN-YA-LFPHLTVFENIAFGLRLKKLPK--AEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPV 243
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-246 |
5.26e-61 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 196.08 E-value: 5.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 20 GTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKsRSELKkfnRKMQMIFQDpyAS 99
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLD-PVELR---RRIGYVIQQ--IG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 100 LNPRMTVADIIAEgidIHGLAKTRKERMAK-VHELLETVGLN-KEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEP 177
Cdd:COG1125 87 LFPHMTVAENIAT---VPRLLGWDKERIRArVDELLELVGLDpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 178 ISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLS-MVKyISDRIGVMYRGKIVELAPSDELYRNPVHPY 246
Cdd:COG1125 164 FGALDPITREQLQDELLRLQRELGKTIVFVTHDIDeALK-LGDRIAVMREGRIVQYDTPEEILANPANDF 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-248 |
4.79e-60 |
|
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: 191.18 E-value: 4.79e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGrKSRSELKKF 85
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISG-LSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDpyASLNPRMTVADIIAEGIDIHGlAKTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:cd03261 76 RRRMGMLFQS--GALFDSLTVFENVAFPLREHT-RLSEEEIREIVLEKLEAVGL-RGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELyRNPVHP 245
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL-RASDDP 230
|
...
gi 654962578 246 YTK 248
Cdd:cd03261 231 LVR 233
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-255 |
7.21e-60 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 193.97 E-value: 7.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYD----ATSGEVLFNGENVHGRKSRS 80
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 ELKKFNRKMQMIFQDPYASLNPRMTVADIIAEGIDIHGL-------AKTRKERmAKvhELLETVGLnKEHA---NRYPHE 150
Cdd:COG4170 83 RRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFkgkwwqrFKWRKKR-AI--ELLHRVGI-KDHKdimNSYPHE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 151 FSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
250 260
....*....|....*....|....*
gi 654962578 231 ELAPSDELYRNPVHPYTKALLSAIP 255
Cdd:COG4170 239 ESGPTEQILKSPHHPYTKALLRSMP 263
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-231 |
1.79e-59 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 189.48 E-value: 1.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 3 DKLLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTgRTIIRLYD-ATSGEVLFNGENVHgRKSRSE 81
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTL-LNILGGLDrPTSGEVLIDGQDIS-SLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 82 LKKF-NRKMQMIFQDPYasLNPRMTVADIIAEGIDIHGLakTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIG 160
Cdd:COG1136 80 LARLrRRHIGFVFQFFN--LLPELTALENVALPLLLAGV--SRKERRERARELLERVGL-GDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654962578 161 IARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYiSDRIGVMYRGKIVE 231
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-244 |
2.35e-59 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 193.37 E-value: 2.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRselkkf 85
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDpYAsLNPRMTVADIIAEGIDIHGLAKtrKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:COG3839 74 DRNIAMVFQS-YA-LYPHMTVYENIAFPLKLRKVPK--AEIDRRVREAAELLGL-EDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHD----LSMvkyiSDRIGVMYRGKIVELAPSDELYRN 241
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDR 224
|
...
gi 654962578 242 PVH 244
Cdd:COG3839 225 PAN 227
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
1-254 |
6.92e-59 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 189.25 E-value: 6.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDK---LLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRK 77
Cdd:COG4107 1 MTNEeqpLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDRDGGPRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 78 ----SRSELKKF-NRKMQMIFQDPYASLNPRMTVADIIAEGIDIHGLAKTRKERmAKVHELLETVGLNKEHANRYPHEFS 152
Cdd:COG4107 81 lfalSEAERRRLrRTDWGMVYQNPRDGLRMDVSAGGNIAERLMAAGERHYGDIR-ARALEWLERVEIPLERIDDLPRTFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 153 GGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVEL 232
Cdd:COG4107 160 GGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVES 239
|
250 260
....*....|....*....|..
gi 654962578 233 APSDELYRNPVHPYTKALLSAI 254
Cdd:COG4107 240 GLTDQVLEDPQHPYTQLLVSSV 261
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-246 |
4.07e-58 |
|
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: 186.39 E-value: 4.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRselkkf 85
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDpYAsLNPRMTVADIIAEGIDIhglaKTRKERM------AKVHELLETVGLNKeHANRYPHEFSGGQRQRI 159
Cdd:cd03296 73 ERNVGFVFQH-YA-LFRHMTVFDNVAFGLRV----KPRSERPpeaeirAKVHELLKLVQLDW-LADRYPAQLSGGQRQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 160 GIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELY 239
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
....*..
gi 654962578 240 RNPVHPY 246
Cdd:cd03296 226 DHPASPF 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-238 |
4.65e-58 |
|
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: 185.85 E-value: 4.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKqHFFtskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDA-----TSGEVLFNGENVHGRK-SR 79
Cdd:cd03260 1 IELRDLN-VYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDvDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 80 SELKkfnRKMQMIFQDPyaslNP-RMTVADIIAEGIDIHGLaKTRKERMAKVHELLETVGLNKEHANR-YPHEFSGGQRQ 157
Cdd:cd03260 77 LELR---RRVGMVFQKP----NPfPGSIYDNVAYGLRLHGI-KLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 158 RIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErgLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDE 237
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 654962578 238 L 238
Cdd:cd03260 227 I 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-253 |
1.05e-57 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 186.53 E-value: 1.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 3 DKLLEIKGLKQHFFTSKG-----TIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVH-GR 76
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 77 KS-RSElkkfnrKMQMIFQDPYASLNPRMTVADIIAEGIDIHgLAKTRKERMAKVHELLETVGLNKEHANRYPHEFSGGQ 155
Cdd:PRK15112 82 YSyRSQ------RIRMIFQDPSTSLNPRQRISQILDFPLRLN-TDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 156 RQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPS 235
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
250
....*....|....*...
gi 654962578 236 DELYRNPVHPYTKALLSA 253
Cdd:PRK15112 235 ADVLASPLHELTKRLIAG 252
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-238 |
1.61e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 184.88 E-value: 1.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgRKSRSELKkf 85
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV--ARDPAEVR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 nRKMQMIFQDPyaSLNPRMTVADIIAEGIDIHGLakTRKERMAKVHELLETVGLNkEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:COG1131 73 -RRIGYVPQEP--ALYPDLTVRENLRFFARLYGL--PRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDEL 238
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-254 |
7.58e-57 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 183.72 E-value: 7.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 4 KLLEIKGLKQHFFTSKgtiKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRsELK 83
Cdd:COG3638 1 PMLELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGR-ALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 84 KFNRKMQMIFQDPYasLNPRMTVAD-IIAEGIDIHGLAKT-----RKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQ 157
Cdd:COG3638 77 RLRRRIGMIFQQFN--LVPRLSVLTnVLAGRLGRTSTWRSllglfPPEDRERALEALERVGL-ADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 158 RIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDE 237
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAE 233
|
250
....*....|....*..
gi 654962578 238 LyrnpvhpyTKALLSAI 254
Cdd:COG3638 234 L--------TDAVLREI 242
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
20-248 |
1.35e-54 |
|
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: 181.59 E-value: 1.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 20 GTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhGRKSRSELKKFNR-KMQMIFQDpyA 98
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENI-MKQSPVELREVRRkKIGMVFQQ--F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 99 SLNPRMTVADIIAEGIDIHGLAKtrKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPI 178
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPE--QERKEKALELLKLVGL-EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 179 SALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPVHPYTK 248
Cdd:TIGR01186 158 SALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVE 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-242 |
2.37e-54 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 176.37 E-value: 2.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKqhfFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKF 85
Cdd:COG1122 1 IELENLS---FSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI----TKKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDPYASL-NPrmTVADIIAEGIDIHGLakTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARA 164
Cdd:COG1122 74 RRKVGLVFQNPDDQLfAP--TVEEDVAFGPENLGL--PREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 165 LAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-229 |
1.09e-53 |
|
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: 174.25 E-value: 1.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSrsELKKF 85
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKK--NINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDpyASLNPRMTVADIIAEG-IDIHGLAKtrKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARA 164
Cdd:cd03262 75 RQKVGMVFQQ--FNLFPHLTVLENITLApIKVKGMSK--AEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 165 LAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKI 229
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-228 |
5.80e-53 |
|
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: 171.22 E-value: 5.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgRKSRSELKKF 85
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL--TDLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDPyaSLNPRMTVADIIAEGIdihglaktrkermakvhelletvglnkehanryphefSGGQRQRIGIARAL 165
Cdd:cd03229 75 RRRIGMVFQDF--ALFPHLTVLENIALGL-------------------------------------SGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGK 228
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-255 |
5.27e-52 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 173.84 E-value: 5.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRL----YDATSGEVLFNGENVHGRKSRS 80
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 ELKKFNRKMQMIFQDPYASLNPRMTVADIIAEGIDihglAKTRKER-MAKVH-------ELLETVGLnKEHAN---RYPH 149
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIP----GWTYKGRwWQRFGwrkrraiELLHRVGI-KDHKDamrSFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 150 EFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKI 229
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
250 260
....*....|....*....|....*.
gi 654962578 230 VELAPSDELYRNPVHPYTKALLSAIP 255
Cdd:PRK15093 238 VETAPSKELVTTPHHPYTQALIRAIP 263
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-238 |
7.09e-52 |
|
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: 170.44 E-value: 7.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftsKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKsRSELKKF 85
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLK-GKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDPyaSLNPRMTVADIIaegidIHGLAKTR-----------KERMAKVHELLETVGLnKEHANRYPHEFSGG 154
Cdd:cd03256 77 RRQIGMIFQQF--NLIERLSVLENV-----LSGRLGRRstwrslfglfpKEEKQRALAALERVGL-LDKAYQRADQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 155 QRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAP 234
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGP 228
|
....
gi 654962578 235 SDEL 238
Cdd:cd03256 229 PAEL 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
25-238 |
1.25e-51 |
|
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: 170.22 E-value: 1.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRselkKFNRKMQMIFQDPYASLNprM 104
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRR----ELARRIAYVPQEPPAPFG--L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 105 TVADIIAEGIDIH--GLAKTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALD 182
Cdd:COG1120 91 TVRELVALGRYPHlgLFGRPSAEDREAVEEALERTGL-EHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 654962578 183 VSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDEL 238
Cdd:COG1120 170 LAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-233 |
2.46e-51 |
|
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: 168.20 E-value: 2.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrSELKKF 85
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV------TDLPPK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDpYAsLNPRMTVADIIAEGIDIHGLAKtrKERMAKVHELLETVGLNkEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:cd03301 71 DRDIAMVFQN-YA-LYPHMTVYDNIAFGLKLRKVPK--DEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELA 233
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-228 |
4.14e-51 |
|
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: 167.64 E-value: 4.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 7 EIKGLkqHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFN 86
Cdd:cd03225 1 ELKNL--SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL----TKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 87 RKMQMIFQDPYASL-NPrmTVADIIAEGIDIHGLAktRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:cd03225 75 RKVGLVFQNPDDQFfGP--TVEEEVAFGLENLGLP--EEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGK 228
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-254 |
1.53e-50 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 166.90 E-value: 1.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrSELKKF 85
Cdd:TIGR00968 1 IEIANISKRF----GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDA------TRVHAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDpYAsLNPRMTVADIIAEGIDI--HGLAKTRkermAKVHELLETVGLNKeHANRYPHEFSGGQRQRIGIAR 163
Cdd:TIGR00968 71 DRKIGFVFQH-YA-LFKHLTVRDNIAFGLEIrkHPKAKIK----ARVEELLELVQLEG-LGDRYPNQLSGGQRQRVALAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 164 ALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPV 243
Cdd:TIGR00968 144 ALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPA 223
|
250
....*....|.
gi 654962578 244 HPYTKALLSAI 254
Cdd:TIGR00968 224 NPFVMSFLGEV 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
19-231 |
3.82e-50 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 165.61 E-value: 3.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 19 KGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgRKSRSELKKFNRKMQMIFQDpyA 98
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS-RLKRREIPYLRRRIGVVFQD--F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 99 SLNPRMTVADIIAEGIDIHGlaKTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPI 178
Cdd:COG2884 89 RLLPDRTVYENVALPLRVTG--KSRKEIRRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 654962578 179 SALDVSIQAQVVNLMKKLQReRGLTYLFIAHDLSMVKYISDRIGVMYRGKIVE 231
Cdd:COG2884 166 GNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-239 |
2.86e-49 |
|
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: 164.01 E-value: 2.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFFTSKGTIKAVDgltFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhGRKSRSELKK 84
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNIN---LNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDI-TKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 FNRKMQMIFQDpyASLNPRMTVADIIAEG-IDIHGLAK------TRKERMaKVHELLETVGLnKEHANRYPHEFSGGQRQ 157
Cdd:TIGR02315 77 LRRRIGMIFQH--YNLIERLTVLENVLHGrLGYKPTWRsllgrfSEEDKE-RALSALERVGL-ADKAYQRADQLSGGQQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 158 RIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDE 237
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSE 232
|
..
gi 654962578 238 LY 239
Cdd:TIGR02315 233 LD 234
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
25-253 |
6.07e-49 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 163.33 E-value: 6.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDA----TSGEVLFNGENVHGRKSRSelkkfnRKMQMIFQDPYASL 100
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRG------RKIATIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 101 NPRMTVADIIAEGidihGLAKTRKERMAKVHELLETVGLNKEH--ANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPI 178
Cdd:PRK10418 93 NPLHTMHTHARET----CLALGKPADDATLTAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 179 SALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPVHPYTKALLSA 253
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-254 |
8.43e-49 |
|
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: 165.36 E-value: 8.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 40 LVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrSELKKFNRKMQMIFQDpYAsLNPRMTVADIIAEGIDIHGL 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV------TNVPPHLRHINMVFQS-YA-LFPHMTVEENVAFGLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 120 AktRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRE 199
Cdd:TIGR01187 73 P--RAEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 200 RGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPVHPYTKALLSAI 254
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-242 |
1.58e-48 |
|
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: 161.84 E-value: 1.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRselKKF 85
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH---EIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDPyaSLNPRMTVAD--IIA------EGIDIHGLAKTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQ 157
Cdd:cd03219 74 RLGIGRTFQIP--RLFPELTVLEnvMVAaqartgSGLLLARARREEREARERAEELLERVGL-ADLADRPAGELSYGQQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 158 RIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDE 237
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
....*
gi 654962578 238 LYRNP 242
Cdd:cd03219 230 VRNNP 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-177 |
2.25e-48 |
|
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: 158.58 E-value: 2.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRksrsELKKFNRKMQMIFQDPyaSLNPRM 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD----ERKSLRKEIGYVFQDP--QLFPRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654962578 105 TVADIIAEGIDIHGLAKTRKErmAKVHELLETVGL---NKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEP 177
Cdd:pfam00005 75 TVRENLRLGLLLKGLSKREKD--ARAEEALEKLGLgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-251 |
5.93e-48 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 160.64 E-value: 5.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKK 84
Cdd:PRK09493 1 MIEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 fnRKMQMIFQDPYasLNPRMTVADIIAEG-IDIHGLAKTRKERMAKvhELLETVGLnKEHANRYPHEFSGGQRQRIGIAR 163
Cdd:PRK09493 77 --QEAGMVFQQFY--LFPHLTALENVMFGpLRVRGASKEEAEKQAR--ELLAKVGL-AERAHHYPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 164 ALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPV 243
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPP 228
|
....*...
gi 654962578 244 HPYTKALL 251
Cdd:PRK09493 229 SQRLQEFL 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-247 |
1.03e-47 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 163.58 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrS 80
Cdd:PRK09452 10 SLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI------T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 ELKKFNRKMQMIFQDpYAsLNPRMTVADIIAEGIDihgLAKTRKERMAK-VHELLETVGLnKEHANRYPHEFSGGQRQRI 159
Cdd:PRK09452 80 HVPAENRHVNTVFQS-YA-LFPHMTVFENVAFGLR---MQKTPAAEITPrVMEALRMVQL-EEFAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 160 GIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHD----LSMvkyiSDRIGVMYRGKIVELAPS 235
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM----SDRIVVMRDGRIEQDGTP 229
|
250
....*....|..
gi 654962578 236 DELYRNPVHPYT 247
Cdd:PRK09452 230 REIYEEPKNLFV 241
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-252 |
1.59e-46 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 157.12 E-value: 1.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 2 TDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYD-----ATSGEVLFNGENVHGR 76
Cdd:COG1117 8 LEPKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDGEDIYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 77 K-SRSELKkfnRKMQMIFQDPyaslNP-RMTVADIIAEGIDIHGLaKTRKERMAKVHELLETVGLNKEHANR---YPHEF 151
Cdd:COG1117 84 DvDVVELR---RRVGMVFQKP----NPfPKSIYDNVAYGLRLHGI-KSKSELDEIVEESLRKAALWDEVKDRlkkSALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 152 SGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErgLTYLFIAHDLSMVKYISDRIGVMYRGKIVE 231
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVE 233
|
250 260
....*....|....*....|.
gi 654962578 232 LAPSDELYRNPVHPYTKALLS 252
Cdd:COG1117 234 FGPTEQIFTNPKDKRTEDYIT 254
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-242 |
4.17e-46 |
|
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: 155.97 E-value: 4.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 2 TDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRse 81
Cdd:COG0411 1 SDPLLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 82 lkKFNRK-MQMIFQDPyaSLNPRMTVAD-------------IIAEGIDIHGLAKTRKERMAKVHELLETVGLnKEHANRY 147
Cdd:COG0411 75 --RIARLgIARTFQNP--RLFPELTVLEnvlvaaharlgrgLLAALLRLPRARREEREARERAEELLERVGL-ADRADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 148 PHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRG 227
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFG 229
|
250
....*....|....*.
gi 654962578 228 -KIVELAPsDELYRNP 242
Cdd:COG0411 230 rVIAEGTP-AEVRADP 244
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-238 |
5.31e-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: 155.40 E-value: 5.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgrksrSELKK 84
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-----KEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 FNRKMQMIFQDPYasLNPRMTVADIIAEGIDIHGLakTRKERMAKVHELLETVGLNkEHANRYPHEFSGGQRQRIGIARA 164
Cdd:COG4555 72 ARRQIGVLPDERG--LYDRLTVRENIRYFAELYGL--FDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654962578 165 LAVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDEL 238
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-231 |
1.49e-44 |
|
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: 150.96 E-value: 1.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKK 84
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 FNRKMQMIFQdpYASLNPRMTVADIIAEGIDIHGLAKTRKERMAKvhELLETVGLNKEhANRYPHEFSGGQRQRIGIARA 164
Cdd:TIGR02211 81 RNKKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKSVKEAKERAY--EMLEKVGLEHR-INHRPSELSGGERQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654962578 165 LAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYIsDRIGVMYRGKIVE 231
Cdd:TIGR02211 156 LVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-229 |
2.06e-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: 149.08 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgrksrSELKKF 85
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK-----KEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDPyaSLNPRMTVADIIaegidihglaktrkermakvhelletvglnkehanryphEFSGGQRQRIGIARAL 165
Cdd:cd03230 72 KRRIGYLPEEP--SLYENLTVRENL---------------------------------------KLSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKI 229
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-242 |
2.53e-44 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 154.47 E-value: 2.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrSELKKF 85
Cdd:PRK10851 3 IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV------SRLHAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDpYAsLNPRMTVADIIAEGIDIhglaKTRKER------MAKVHELLETVGLnkEH-ANRYPHEFSGGQRQR 158
Cdd:PRK10851 73 DRKVGFVFQH-YA-LFRHMTVFDNIAFGLTV----LPRRERpnaaaiKAKVTQLLEMVQL--AHlADRYPAQLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 159 IGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDEL 238
Cdd:PRK10851 145 VALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
....
gi 654962578 239 YRNP 242
Cdd:PRK10851 225 WREP 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-242 |
2.82e-44 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 154.11 E-value: 2.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRs 80
Cdd:PRK11432 2 TQKNFVVLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 elkkfNRKMQMIFQDpYAsLNPRMTVADIIAEGIDIHGLAKTrkERMAKVHELLETVGLNKeHANRYPHEFSGGQRQRIG 160
Cdd:PRK11432 77 -----QRDICMVFQS-YA-LFPHMSLGENVGYGLKMLGVPKE--ERKQRVKEALELVDLAG-FEDRYVDQISGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 161 IARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYR 240
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
..
gi 654962578 241 NP 242
Cdd:PRK11432 227 QP 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-254 |
3.00e-44 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 154.61 E-value: 3.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrSELKK 84
Cdd:PRK11607 19 LLEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL------SHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 FNRKMQMIFQDpYAsLNPRMTVADIIAEGIDIHGLAKTrkERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARA 164
Cdd:PRK11607 89 YQRPINMMFQS-YA-LFPHMTVEQNIAFGLKQDKLPKA--EIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 165 LAVEPDFIIADEPISALDVSI----QAQVVNLMKKLqrerGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYR 240
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
250
....*....|....
gi 654962578 241 NPVHPYTKALLSAI 254
Cdd:PRK11607 240 HPTTRYSAEFIGSV 253
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
25-243 |
9.88e-44 |
|
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: 149.41 E-value: 9.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrSELKKFNRKMQMIFQDpYAsLNPRM 104
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI------TNLPPEKRDISYVPQN-YA-LFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 105 TVADIIAEGIDIhgLAKTRKERMAKVHELLETVGLnkEHA-NRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDV 183
Cdd:cd03299 87 TVYKNIAYGLKK--RKVDKKEIERKVLEIAEMLGI--DHLlNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 184 SIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPV 243
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
9-268 |
5.65e-43 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 152.11 E-value: 5.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 9 KGL-KQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhGRKSRSELKKFNR 87
Cdd:PRK10070 27 QGLsKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-AKISDAELREVRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 88 K-MQMIFQDpyASLNPRMTVADIIAEGIDIHGLAKtrKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALA 166
Cdd:PRK10070 106 KkIAMVFQS--FALMPHMTVLDNTAFGMELAGINA--EERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 167 VEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPVHPY 246
Cdd:PRK10070 181 INPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
250 260
....*....|....*....|..
gi 654962578 247 TKALLSAIPLPDPDSEKTRQRK 268
Cdd:PRK10070 261 VRTFFRGVDISQVFSAKDIARR 282
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
28-253 |
1.42e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 143.74 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 28 LTFD--IFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENvHGRKSRSElkkfnRKMQMIFQDpyASLNPRMT 105
Cdd:COG3840 16 LRFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD-LTALPPAE-----RPVSMLFQE--NNLFPHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 106 VADIIAEGIDiHGLAKTRKERmAKVHELLETVGLNkEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSI 185
Cdd:COG3840 88 VAQNIGLGLR-PGLKLTAEQR-AQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 186 QAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPVHPYTKALLSA 253
Cdd:COG3840 165 RQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-248 |
3.46e-41 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 143.13 E-value: 3.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYD-----ATSGEVLFNGENVHgrksRS 80
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIF----KM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 ELKKFNRKMQMIFQDPYASlnPRMTVADIIAEGIDIHGLAKTRKERMAKVHELLETVGLNKEHANRY---PHEFSGGQRQ 157
Cdd:PRK14247 76 DVIELRRRVQMVFQIPNPI--PNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 158 RIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErgLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDE 237
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
250
....*....|.
gi 654962578 238 LYRNPVHPYTK 248
Cdd:PRK14247 232 VFTNPRHELTE 242
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-253 |
5.75e-41 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 143.02 E-value: 5.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRS----- 80
Cdd:COG4598 9 LEVRDLHKSF----GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 ----ELKKFNRKMQMIFQdpyaSLN--PRMTVADIIAEGiDIHGLAKTRKERMAKVHELLETVGL-NKEHAnrYPHEFSG 153
Cdd:COG4598 85 adrrQLQRIRTRLGMVFQ----SFNlwSHMTVLENVIEA-PVHVLGRPKAEAIERAEALLAKVGLaDKRDA--YPAHLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 154 GQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELA 233
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQG 236
|
250 260
....*....|....*....|
gi 654962578 234 PSDELYRNPVHPYTKALLSA 253
Cdd:COG4598 237 PPAEVFGNPKSERLRQFLSS 256
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-244 |
9.34e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 141.77 E-value: 9.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSR- 79
Cdd:COG1121 2 MMMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 80 ------SElkkFNRKMqmifqdpyaslnPrMTVADIIAEGIDIHG--LAKTRKERMAKVHELLETVGLnKEHANRYPHEF 151
Cdd:COG1121 78 gyvpqrAE---VDWDF------------P-ITVRDVVLMGRYGRRglFRRPSRADREAVDEALERVGL-EDLADRPIGEL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 152 SGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVE 231
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH 219
|
250 260
....*....|....*....|.
gi 654962578 232 LAPSD--------ELYRNPVH 244
Cdd:COG1121 220 GPPEEvltpenlsRAYGGPVA 240
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-254 |
2.21e-40 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 141.22 E-value: 2.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLF--NGENVHGRKS 78
Cdd:PRK11701 2 MDQPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmRDGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 79 RSELKkfnRKMQM------IFQDPYASLnpRMTV---ADI----IAEGIDIHGlaKTRkermAKVHELLETVGLNKEHAN 145
Cdd:PRK11701 78 LSEAE---RRRLLrtewgfVHQHPRDGL--RMQVsagGNIgerlMAVGARHYG--DIR----ATAGDWLERVEIDAARID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 146 RYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMY 225
Cdd:PRK11701 147 DLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMK 226
|
250 260
....*....|....*....|....*....
gi 654962578 226 RGKIVELAPSDELYRNPVHPYTKALLSAI 254
Cdd:PRK11701 227 QGRVVESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-267 |
2.24e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 142.08 E-value: 2.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLkqhFFTSKGTIK-AVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNG-----ENVH 74
Cdd:PRK13635 1 MKEEIIRVEHI---SFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 75 grksrselkKFNRKMQMIFQdpyaslNPR-----MTVADIIAEGIDIHGLAktRKERMAKVHELLETVGLnKEHANRYPH 149
Cdd:PRK13635 78 ---------DVRRQVGMVFQ------NPDnqfvgATVQDDVAFGLENIGVP--REEMVERVDQALRQVGM-EDFLNREPH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 150 EFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYiSDRIGVMYRGKI 229
Cdd:PRK13635 140 RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEI 218
|
250 260 270
....*....|....*....|....*....|....*...
gi 654962578 230 VELAPSDELYRnpvhpYTKALLsAIPLPDPDSEKTRQR 267
Cdd:PRK13635 219 LEEGTPEEIFK-----SGHMLQ-EIGLDVPFSVKLKEL 250
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-254 |
2.58e-40 |
|
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: 141.12 E-value: 2.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRK----SRS 80
Cdd:TIGR02323 3 LLQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELElyqlSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 ELKKFNR-KMQMIFQDPYASLNPRMTVADIIAEGIDIHGLAKTRKERmAKVHELLETVGLNKEHANRYPHEFSGGQRQRI 159
Cdd:TIGR02323 79 ERRRLMRtEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIR-ATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 160 GIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELY 239
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVL 237
|
250
....*....|....*
gi 654962578 240 RNPVHPYTKALLSAI 254
Cdd:TIGR02323 238 DDPQHPYTQLLVSSI 252
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
25-230 |
3.09e-40 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 138.34 E-value: 3.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSelkkfnrkmqmifqdpyaslnprm 104
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 105 tvadiiaegidihgLAKtrkeRMAKVHELLETVGLnkEH-ANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDV 183
Cdd:cd03214 71 --------------LAR----KIAYVPQALELLGL--AHlADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 654962578 184 SIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:cd03214 131 AHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-229 |
3.16e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 139.57 E-value: 3.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLkqHFFTSKGTIkaVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGenvhgrKSRSELK-- 83
Cdd:COG4619 1 LELEGL--SFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDG------KPLSAMPpp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 84 KFNRKMQMIFQDPYAslnPRMTVADIIAEGIDIHGlaktRKERMAKVHELLETVGLNKEHANRYPHEFSGGQRQRIGIAR 163
Cdd:COG4619 71 EWRRQVAYVPQEPAL---WGGTVRDNLPFPFQLRE----RKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654962578 164 ALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKI 229
Cdd:COG4619 144 ALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
24-229 |
3.47e-40 |
|
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: 139.59 E-value: 3.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 24 AVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSR----SELKKFNRKMqmifqdpyas 99
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigyvPQRRSIDRDF---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 100 lnpRMTVADIIAEGIDIH--GLAKTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEP 177
Cdd:cd03235 84 ---PISVRDVVLMGLYGHkgLFRRLSKADKAKVDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 654962578 178 ISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKI 229
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-231 |
4.16e-40 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 140.15 E-value: 4.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 20 GTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGE--NVHGRKSRSELKKFNRKMQMIFQDpY 97
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAIRELRRNVGMVFQQ-Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 98 aSLNPRMTVAD-IIAEGIDIHGLAKtrKERMAKVHELLETVGLNkEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADE 176
Cdd:PRK11124 92 -NLWPHLTVQQnLIEAPCRVLGLSK--DQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 177 PISALDVSIQAQVVNLMKKLQrERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVE 231
Cdd:PRK11124 168 PTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
25-261 |
4.27e-40 |
|
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: 143.60 E-value: 4.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLY--DATSGEVLFNGENVhgrksrSELKKFNRKMQMIFQDpYAsLNP 102
Cdd:TIGR03258 21 LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVkaAGLTGRIAIADRDL------THAPPHKRGLALLFQN-YA-LFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 103 RMTVADIIAEGIDIHGLAKTRKERmaKVHELLETVGLNkEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALD 182
Cdd:TIGR03258 93 HLKVEDNVAFGLRAQKMPKADIAE--RVADALKLVGLG-DAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 183 VSIQAQVVNLMKKLQRE-RGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPVHPYTKALLSAIPLPDPDS 261
Cdd:TIGR03258 170 ANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANILPAIA 249
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-238 |
7.05e-40 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 147.67 E-value: 7.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLkqHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENvhgrksrseLKKF 85
Cdd:COG2274 474 IELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGID---------LRQI 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 N-----RKMQMIFQDPYasLNPRmTVADIIA---EGIDihglaktrkerMAKVHELLETVGLN---KEHANRYPHE---- 150
Cdd:COG2274 543 DpaslrRQIGVVLQDVF--LFSG-TIRENITlgdPDAT-----------DEEIIEAARLAGLHdfiEALPMGYDTVvgeg 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 151 ---FSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKyISDRIGVMYRG 227
Cdd:COG2274 609 gsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIR-LADRIIVLDKG 685
|
250
....*....|.
gi 654962578 228 KIVELAPSDEL 238
Cdd:COG2274 686 RIVEDGTHEEL 696
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-242 |
3.50e-39 |
|
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: 138.74 E-value: 3.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 18 SKGT---IKAVDGLTFDIFRGETLGLVGESGCGKSTtgrtIIRLYDA----TSGEVLFNGENVHGRKsRSELKKFNRKMQ 90
Cdd:TIGR04521 11 QPGTpfeKKALDDVSLTIEDGEFVAIIGHTGSGKST----LIQHLNGllkpTSGTVTIDGRDITAKK-KKKLKDLRKKVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 91 MIFQDPYASLNpRMTVADIIAEGIDIHGLAKtrKERMAKVHELLETVGLNKEHANRYPHEFSGGQRQRIGIARALAVEPD 170
Cdd:TIGR04521 86 LVFQFPEHQLF-EETVYKDIAFGPKNLGLSE--EEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654962578 171 FIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:TIGR04521 163 VLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-252 |
3.96e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 138.18 E-value: 3.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVH-GRKSR 79
Cdd:PRK10619 1 MSENKLNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlVRDKD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 80 SELKKFNRK--------MQMIFQdpYASLNPRMTVADIIAEG-IDIHGLAKTR-KERMAKvheLLETVGLNKEHANRYPH 149
Cdd:PRK10619 77 GQLKVADKNqlrllrtrLTMVFQ--HFNLWSHMTVLENVMEApIQVLGLSKQEaRERAVK---YLAKVGIDERAQGKYPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 150 EFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQrERGLTYLFIAHDLSMVKYISDRIGVMYRGKI 229
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
250 260
....*....|....*....|...
gi 654962578 230 VELAPSDELYRNPVHPYTKALLS 252
Cdd:PRK10619 231 EEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-229 |
6.24e-39 |
|
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: 136.38 E-value: 6.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 20 GTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKsRSELKKFNRKMQMIFQDpyAS 99
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLR-GRAIPYLRRKIGVVFQD--FR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 100 LNPRMTVADIIAEGIDIHGlaKTRKERMAKVHELLETVGLNKEHaNRYPHEFSGGQRQRIGIARALAVEPDFIIADEPIS 179
Cdd:cd03292 89 LLPDRNVYENVAFALEVTG--VPPREIRKRVPAALELVGLSHKH-RALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 654962578 180 ALDVSIQAQVVNLMKKLQReRGLTYLFIAHDLSMVKYISDRIGVMYRGKI 229
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-228 |
8.01e-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: 134.29 E-value: 8.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 7 EIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgrksRSELKKFN 86
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA----KLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 87 RKMQMIFQdpyaslnprmtvadiiaegidihglaktrkermakvhelletvglnkehanrypheFSGGQRQRIGIARALA 166
Cdd:cd00267 73 RRIGYVPQ--------------------------------------------------------LSGGQRQRVALARALL 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654962578 167 VEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGK 228
Cdd:cd00267 97 LNPDLLLLDEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-228 |
1.53e-38 |
|
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: 133.66 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLkqHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKF 85
Cdd:cd03228 1 IEFKNV--SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL----RDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDPYasLnPRMTVADIIaegidihglaktrkermakvhelletvglnkehanrypheFSGGQRQRIGIARAL 165
Cdd:cd03228 75 RKNIAYVPQDPF--L-FSGTIRENI----------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKyISDRIGVMYRGK 228
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-238 |
2.52e-38 |
|
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: 134.80 E-value: 2.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksRSELKKF 85
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-----VREPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDPyaSLNPRMTVADIIAEGIDIHGLAktRKERMAKVHELLETVGLNkEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:cd03265 72 RRRIGIVFQDL--SVDDELTGWENLYIHARLYGVP--GAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDEL 238
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-252 |
2.71e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 135.65 E-value: 2.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftsKGTiKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKKF 85
Cdd:PRK11264 4 IEVKNLVKKF---HGQ-TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQ----MIFQDpyASLNPRMTVADIIAEG-IDIHGLAktRKERMAKVHELLETVGLN-KEhaNRYPHEFSGGQRQRI 159
Cdd:PRK11264 80 IRQLRqhvgFVFQN--FNLFPHRTVLENIIEGpVIVKGEP--KEEATARARELLAKVGLAgKE--TSYPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 160 GIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERgLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELY 239
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
250
....*....|...
gi 654962578 240 RNPVHPYTKALLS 252
Cdd:PRK11264 233 ADPQQPRTRQFLE 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-240 |
3.98e-38 |
|
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: 141.09 E-value: 3.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 3 DKLLEIKGLKQHFFT-SKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGE--VLFNGENVHGRKSR 79
Cdd:TIGR03269 277 EPIIKVRNVSKRYISvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 80 SELK-KFNRKMQMIFQDpyASLNPRMTVADIIAEGIDIhglaKTRKE--RMAKVHeLLETVGLNKEHA----NRYPHEFS 152
Cdd:TIGR03269 357 PDGRgRAKRYIGILHQE--YDLYPHRTVLDNLTEAIGL----ELPDElaRMKAVI-TLKMVGFDEEKAeeilDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 153 GGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVEL 232
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
....*...
gi 654962578 233 APSDELYR 240
Cdd:TIGR03269 510 GDPEEIVE 517
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-231 |
4.88e-38 |
|
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: 133.88 E-value: 4.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrSELKKF 85
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY------QKNIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDPyaSLNPRMTVAdiiaEGIDIHGLAKTRKERmaKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:cd03268 71 LRRIGALIEAP--GFYPNLTAR----ENLRLLARLLGIRKK--RIDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVE 231
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-230 |
5.39e-38 |
|
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: 133.96 E-value: 5.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 23 KAVDGLTFDI---FRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKKFNRKMQMIFQDpyAS 99
Cdd:cd03297 8 KRLPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--YA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 100 LNPRMTVADIIAEGIDIHglakTRKERMAKVHELLETVGLNKEhANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPIS 179
Cdd:cd03297 86 LFPHLNVRENLAFGLKRK----RNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 654962578 180 ALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-249 |
5.44e-38 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 134.76 E-value: 5.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 20 GTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGE--NVHGRKSRSELKKFNRKMQMIFQDpY 97
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIRLLRQKVGMVFQQ-Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 98 aSLNPRMTVAD-IIAEGIDIHGLAKtrKERMAKVHELLETVGLNkEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADE 176
Cdd:COG4161 92 -NLWPHLTVMEnLIEAPCKVLGLSK--EQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654962578 177 PISALDVSIQAQVVNLMKKLQrERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELyrnpVHPYTKA 249
Cdd:COG4161 168 PTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF----TQPQTEA 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-242 |
1.10e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 136.90 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftsKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrSELKKF 85
Cdd:PRK11650 4 LKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV------NELEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDpYAsLNPRMTVADIIAEGIDIHGLAK-TRKERMAKVHELLETVGLNKehanRYPHEFSGGQRQRIGIARA 164
Cdd:PRK11650 75 DRDIAMVFQN-YA-LYPHMSVRENMAYGLKIRGMPKaEIEERVAEAARILELEPLLD----RKPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 165 LAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-238 |
1.69e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 139.91 E-value: 1.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 16 FTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgRK-SRSELKkfnRKMQMIFQ 94
Cdd:COG1132 347 FSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI--RDlTLESLR---RQIGVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 95 DPY--AslnprMTVADIIAEG-IDIhglakTRKE-----RMAKVHEL-------LETV----GLNkehanrypheFSGGQ 155
Cdd:COG1132 422 DTFlfS-----GTIRENIRYGrPDA-----TDEEveeaaKAAQAHEFiealpdgYDTVvgerGVN----------LSGGQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 156 RQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKyISDRIGVMYRGKIVELAPS 235
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIR-NADRILVLDDGRIVEQGTH 558
|
...
gi 654962578 236 DEL 238
Cdd:COG1132 559 EEL 561
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-230 |
6.82e-37 |
|
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: 130.84 E-value: 6.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 16 FTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRselkkfnRKMQMIFQD 95
Cdd:cd03226 7 FSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR-------KSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 96 PYASLNpRMTVADIIAEGIDIHGLAKTRKErmakvhELLETVGLNKEHaNRYPHEFSGGQRQRIGIARALAVEPDFIIAD 175
Cdd:cd03226 80 VDYQLF-TDSVREELLLGLKELDAGNEQAE------TVLKDLDLYALK-ERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 176 EPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-231 |
6.99e-37 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 132.29 E-value: 6.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKS-RSelkk 84
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAdRG---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 fnrkmqMIFQDpyASLNPRMTVADIIAEGIDIHGLAKtrKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARA 164
Cdd:COG4525 80 ------VVFQK--DALLPWLNVLDNVAFGLRLRGVPK--AERRARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654962578 165 LAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVM--YRGKIVE 231
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-230 |
1.01e-36 |
|
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: 128.70 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGEnvhgrksrselkkf 85
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 nrkmqmifqdPYASLNPRmtvaDIIAEGIdihglaktrkermAKVHELletvglnkehanryphefSGGQRQRIGIARAL 165
Cdd:cd03216 63 ----------EVSFASPR----DARRAGI-------------AMVYQL------------------SVGERQMVEIARAL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:cd03216 98 ARNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-241 |
1.71e-36 |
|
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: 137.20 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKqhfFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSelkkF 85
Cdd:COG4988 337 IELEDVS---FSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS----W 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDPYasLnPRMTVADIIAegidihgLAK---TRKE-----RMAKVHELLETV--GLN---KEHANRypheFS 152
Cdd:COG4988 410 RRQIAWVPQNPY--L-FAGTIRENLR-------LGRpdaSDEEleaalEAAGLDEFVAALpdGLDtplGEGGRG----LS 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 153 GGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKyISDRIGVMYRGKIVEL 232
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLA-QADRILVLDDGRIVEQ 552
|
....*....
gi 654962578 233 APSDELYRN 241
Cdd:COG4988 553 GTHEELLAK 561
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-230 |
3.20e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 131.38 E-value: 3.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKF 85
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 -----NRkmqmifqdpyaSLNPRMTVADII---AEgidIHGLakTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQ 157
Cdd:COG4152 74 gylpeER-----------GLYPKMKVGEQLvylAR---LKGL--SKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654962578 158 RIGIARALAVEPDFIIADEPISALD-VSiqaqvVNLMKKL---QRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDpVN-----VELLKDVireLAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-252 |
5.38e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 129.96 E-value: 5.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 15 FFTSKGTIKAVDgltFDIFRGETLGLVGESGCGKSTTGRTIIRLYD-----ATSGEVLFNGENVHGRKSrsELKKFNRKM 89
Cdd:PRK14267 13 YYGSNHVIKGVD---LKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDV--DPIEVRREV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 90 QMIFQdpYASLNPRMTVADIIAEGIDIHGLAKTRKERMAKVHELLETVGLNKEHANR---YPHEFSGGQRQRIGIARALA 166
Cdd:PRK14267 88 GMVFQ--YPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 167 VEPDFIIADEPISALDVSIQAQVVNLMKKLQRErgLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPVHPY 246
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHEL 243
|
....*.
gi 654962578 247 TKALLS 252
Cdd:PRK14267 244 TEKYVT 249
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-237 |
9.71e-36 |
|
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: 128.32 E-value: 9.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHG--RKS 78
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 79 RSELKkfNRKMQMIFQdpyaS--LNPRMT----VAdIIAEgidihgLAkTRKERMAKVHELLETVGLnKEHANRYPHEFS 152
Cdd:COG4181 84 RARLR--ARHVGFVFQ----SfqLLPTLTalenVM-LPLE------LA-GRRDARARARALLERVGL-GHRLDHYPAQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 153 GGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYiSDRIGVMYRGKIVEL 232
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
....*
gi 654962578 233 APSDE 237
Cdd:COG4181 228 TAATA 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-239 |
1.11e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 129.85 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 2 TDKLLEIKGLKQHFFTSKgTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSE 81
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQ-EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL----TEEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 82 LKKFNRKMQMIFQDPYASLnPRMTVADIIAEGIDIHGLAktRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGI 161
Cdd:PRK13650 76 VWDIRHKIGMVFQNPDNQF-VGATVEDDVAFGLENKGIP--HEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 162 ARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKyISDRIGVMYRGKIVELAPSDELY 239
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELF 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-238 |
1.17e-35 |
|
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: 128.01 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksRSELKKF 85
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-----RTDRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDpyASLNPRMTVADIIAegidIHGLAK--TRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIAR 163
Cdd:cd03263 74 RQSLGYCPQF--DALFDELTVREHLR----FYARLKglPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 164 ALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDEL 238
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-252 |
2.68e-35 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 127.97 E-value: 2.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYD-----ATSGEVLFNGENVHG 75
Cdd:PRK14239 1 MTEPILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 76 RKSRS-ELKKfnrKMQMIFQDPyaslNP-RMTVADIIAEGIDIHGLaKTRKERMAKVHELLETVGLNKEHANRYpHE--- 150
Cdd:PRK14239 77 PRTDTvDLRK---EIGMVFQQP----NPfPMSIYENVVYGLRLKGI-KDKQVLDEAVEKSLKGASIWDEVKDRL-HDsal 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 151 -FSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErgLTYLFIAHDLSMVKYISDRIGVMYRGKI 229
Cdd:PRK14239 148 gLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
250 260
....*....|....*....|...
gi 654962578 230 VELAPSDELYRNPVHPYTKALLS 252
Cdd:PRK14239 226 IEYNDTKQMFMNPKHKETEDYIS 248
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
23-241 |
3.78e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 128.63 E-value: 3.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 23 KAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRseLKKFNRKMQMIFQDPYASLNP 102
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK--LSDIRKKVGLVFQYPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 103 RmTVADIIAEGIDIHGLAKTRKERmaKVHELLETVGLNKE-HANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISAL 181
Cdd:PRK13637 99 E-TIEKDIAFGPINLGLSEEEIEN--RVKRAMNIVGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 182 DVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRN 241
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-238 |
1.35e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.91 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKk 84
Cdd:COG1129 4 LLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 fnRKMQMIFQDPyaSLNPRMTVADIIAEGIDIHGLAKTRKERM-AKVHELLETVGLNkEHANRYPHEFSGGQRQRIGIAR 163
Cdd:COG1129 79 --AGIAIIHQEL--NLVPNLSVAENIFLGREPRRGGLIDWRAMrRRARELLARLGLD-IDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 164 ALAVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDEL 238
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
22-239 |
1.42e-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: 125.42 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 22 IKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKsrseLKKFNRKMQMIFQDPYasln 101
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT----LASLRRQIGLVSQDVF---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 102 prmTVADIIAEGIDIHGLAKTRKE-----RMAKVHELLETV--GLNKEHANRyPHEFSGGQRQRIGIARALAVEPDFIIA 174
Cdd:cd03251 87 ---LFNDTVAENIAYGRPGATREEveeaaRAANAHEFIMELpeGYDTVIGER-GVKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 175 DEPISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKYiSDRIGVMYRGKIVELAPSDELY 239
Cdd:cd03251 163 DEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELL 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-241 |
2.73e-34 |
|
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: 124.96 E-value: 2.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 18 SKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgrksRSELKKFNRKMQMIFQDP- 96
Cdd:cd03249 12 SRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIR----DLNLRWLRSQIGLVSQEPv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 97 -YAslnprMTVADIIAEGIDihglAKTRKE-----RMAKVHELLETV--GLNKEHANRYPhEFSGGQRQRIGIARALAVE 168
Cdd:cd03249 88 lFD-----GTIAENIRYGKP----DATDEEveeaaKKANIHDFIMSLpdGYDTLVGERGS-QLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654962578 169 PDFIIADEPISALDVS----IQAQVVNLMKklqrerGLTYLFIAHDLSMVKYiSDRIGVMYRGKIVELAPSDELYRN 241
Cdd:cd03249 158 PKILLLDEATSALDAEseklVQEALDRAMK------GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-238 |
2.75e-34 |
|
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: 124.65 E-value: 2.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 16 FTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRkSRSELKKfnrKMQMIFQD 95
Cdd:cd03254 10 FSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRS---MIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 96 PYaslnprmTVADIIAEGIDIHGLAKTRKErmakVHELLETVGLN----------KEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:cd03254 86 TF-------LFSGTIMENIRLGRPNATDEE----VIEAAKEAGAHdfimklpngyDTVLGENGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKYiSDRIGVMYRGKIVELAPSDEL 238
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-242 |
6.57e-34 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 124.33 E-value: 6.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRs 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGH- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 elkKFNRK-MQMIFQDpyASLNPRMTVAD--IIAE------GIdIHGLAKT----RKER--MAKVHELLETVGLnKEHAN 145
Cdd:PRK11300 76 ---QIARMgVVRTFQH--VRLFREMTVIEnlLVAQhqqlktGL-FSGLLKTpafrRAESeaLDRAATWLERVGL-LEHAN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 146 RYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMY 225
Cdd:PRK11300 149 RQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVN 228
|
250
....*....|....*..
gi 654962578 226 RGKIVELAPSDELYRNP 242
Cdd:PRK11300 229 QGTPLANGTPEEIRNNP 245
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-230 |
1.03e-33 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 122.86 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHG--RKSRSEL 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 KKFNRKMqmifqdpyaSLNPRMTVADIIAEGIDIHGLAktRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIA 162
Cdd:cd03266 81 GFVSDST---------GLYDRLTARENLEYFAGLYGLK--GDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 163 RALAVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
28-218 |
1.61e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 122.62 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 28 LTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKKFNRKMQMIFQdpYASLNPRMTVA 107
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ--FHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 108 DIIAEGIDIHGlaKTRKERMAKVHELLETVGLNKEhANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQA 187
Cdd:PRK11629 106 ENVAMPLLIGK--KKPAEINSRALEMLAAVGLEHR-ANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190
....*....|....*....|....*....|.
gi 654962578 188 QVVNLMKKLQRERGLTYLFIAHDLSMVKYIS 218
Cdd:PRK11629 183 SIFQLLGELNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-238 |
3.39e-33 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 121.39 E-value: 3.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRselKKF 85
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH---ERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDPyaSLNPRMTVADIIAEGIDIHGLAKtRKERMAKVHEL---LetvglnKEHANRYPHEFSGGQRQRIGIA 162
Cdd:cd03224 74 RAGIGYVPEGR--RIFPELTVEENLLLGAYARRRAK-RKARLERVYELfprL------KERRKQLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654962578 163 RALAVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDEL 238
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
31-242 |
5.99e-33 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 124.37 E-value: 5.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 31 DIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrSELKKFNRKMQMIFQDpYAsLNPRMTVADII 110
Cdd:PRK11000 25 DIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM------NDVPPAERGVGMVFQS-YA-LYPHLSVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 111 AEGIDIHGLAKT-RKERMAKVHELLETVGLnkehANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQV 189
Cdd:PRK11000 97 SFGLKLAGAKKEeINQRVNQVAEVLQLAHL----LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 654962578 190 VNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:PRK11000 173 RIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-210 |
1.08e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 119.89 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDA---TSGEVLFNGENVHGRKSRSelkkfnRKMQMIFQDPYasLN 101
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ------RRIGILFQDDL--LF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 102 PRMTVADIIAegidiHGLAKT--RKERMAKVHELLETVGLNKeHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPIS 179
Cdd:COG4136 89 PHLSVGENLA-----FALPPTigRAQRRARVEQALEEAGLAG-FADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190
....*....|....*....|....*....|.
gi 654962578 180 ALDVSIQAQVVNLMKKLQRERGLTYLFIAHD 210
Cdd:COG4136 163 KLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-246 |
1.55e-32 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 123.30 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 28 LTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKKFNRKMQMIFQDpyASLNPRMTVA 107
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE--ARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 108 DIIaegidIHGLAKTR-KERMAKVHELLETVGLnkEH-ANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSI 185
Cdd:TIGR02142 94 GNL-----RYGMKRARpSERRISFERVIELLGI--GHlLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654962578 186 QAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPVHPY 246
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-230 |
2.36e-32 |
|
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: 118.92 E-value: 2.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrselkKF 85
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----------DI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDPYASLNPRMTVADIIAEGIDIHGLakTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:cd03269 67 AARNRIGYLPEERGLYPKMKVIDQLVYLAQLKGL--KKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 166 AVEPDFIIADEPISALDvsiqaqVVN--LMKKL---QRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:cd03269 144 IHDPELLILDEPFSGLD------PVNveLLKDVireLARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-238 |
3.53e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 119.30 E-value: 3.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 29 TFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENvHGRKSRSElkkfnRKMQMIFQDpyASLNPRMTVAD 108
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSR-----RPVSMLFQE--NNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 109 IIAEGIDiHGLAKTRKERmAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQ 188
Cdd:PRK10771 91 NIGLGLN-PGLKLNAAQR-EKLHAIARQMGI-EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 654962578 189 VVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDEL 238
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-242 |
3.54e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.18 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLkqHFFTSKGTiKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgRKSRSELKK 84
Cdd:PRK13639 1 ILETRDL--KYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI--KYDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 FNRKMQMIFQDPYASL-NPrmTVADIIAEGIDIHGLAKTRKERmaKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIAR 163
Cdd:PRK13639 76 VRKTVGIVFQNPDDQLfAP--TVEEDVAFGPLNLGLSKEEVEK--RVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654962578 164 ALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-248 |
4.36e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 119.76 E-value: 4.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 13 QHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATS-----GEVLFNGENVHGRksRSELKKFNR 87
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYER--RVNLNRLRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 88 KMQMIFQDPyaSLNPrMTVADIIAEGIDIHGLAKTRK-----ERMAKVHELLETVGlNKEHANRYphEFSGGQRQRIGIA 162
Cdd:PRK14258 89 QVSMVHPKP--NLFP-MSVYDNVAYGVKIVGWRPKLEiddivESALKDADLWDEIK-HKIHKSAL--DLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 163 RALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYR-----GKIVELAPSDE 237
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKK 242
|
250
....*....|.
gi 654962578 238 LYRNPVHPYTK 248
Cdd:PRK14258 243 IFNSPHDSRTR 253
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
24-242 |
5.61e-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: 124.49 E-value: 5.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 24 AVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgRKSRSELKkfnRKMQMIFQDPY---ASL 100
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR-DLDEDDLR---RRIAVVPQRPHlfdTTL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 101 -------NPRMTVADIIA--EGIDIHGLAKTRKERmakvhelLET-VGlnkEHANRypheFSGGQRQRIGIARALAVEPD 170
Cdd:COG4987 426 renlrlaRPDATDEELWAalERVGLGDWLAALPDG-------LDTwLG---EGGRR----LSGGERRRLALARALLRDAP 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654962578 171 FIIADEPISALDVSIQAQVVNLMKKLQRERGLtyLFIAHDLSMVKYIsDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQN 560
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-239 |
8.96e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 119.43 E-value: 8.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 3 DKLLEIKGLKQHFfTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGEnvhgRKSRSEL 82
Cdd:PRK13642 2 NKILEVENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE----LLTAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 KKFNRKMQMIFQDPYASLnPRMTVADIIAEGIDIHGLAktRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIA 162
Cdd:PRK13642 77 WNLRRKIGMVFQNPDNQF-VGATVEDDVAFGMENQGIP--REEMIKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654962578 163 RALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYiSDRIGVMYRGKIVELAPSDELY 239
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-237 |
1.42e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 122.83 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRS 80
Cdd:COG3845 1 MMPPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 ELKkfnRKMQMIFQDPyaSLNPRMTVADIIAEGIDIHGLAKTRKERM-AKVHELLETVGLNKEhANRYPHEFSGGQRQRI 159
Cdd:COG3845 77 AIA---LGIGMVHQHF--MLVPNLTVAENIVLGLEPTKGGRLDRKAArARIRELSERYGLDVD-PDAKVEDLSVGEQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 160 GIARALAVEPDFIIADEPISALDvsiQAQVVNL---MKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV-ELAPS 235
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLT---PQEADELfeiLRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVgTVDTA 226
|
..
gi 654962578 236 DE 237
Cdd:COG3845 227 ET 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-241 |
2.70e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.78 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 3 DKLLEIKGLKqhFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSEL 82
Cdd:PRK13632 5 SVMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI----SKENL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 KKFNRKMQMIFQdpyaslNPR-----MTVADIIAEGIDIHGLakTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQ 157
Cdd:PRK13632 79 KEIRKKIGIIFQ------NPDnqfigATVEDDIAFGLENKKV--PPKKMKDIIDDLAKKVGM-EDYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 158 RIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVkYISDRIGVMYRGKIVELAPSDE 237
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKE 228
|
....
gi 654962578 238 LYRN 241
Cdd:PRK13632 229 ILNN 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-242 |
4.94e-31 |
|
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: 116.23 E-value: 4.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSrselkk 84
Cdd:COG0410 3 MLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 fNRKMQM----------IFqdpyaslnPRMTVADIIAEGIDIHGLAKTRKERMAKVHEL---LetvglnKEHANRYPHEF 151
Cdd:COG0410 73 -HRIARLgigyvpegrrIF--------PSLTVEENLLLGAYARRDRAEVRADLERVYELfprL------KERRRQRAGTL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 152 SGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVE 231
Cdd:COG0410 138 SGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVL 216
|
250
....*....|.
gi 654962578 232 LAPSDELYRNP 242
Cdd:COG0410 217 EGTAAELLADP 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-230 |
1.62e-30 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 114.21 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGeTLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgRKSRSELKkf 85
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV--LKQPQKLR-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 nRKMQMIFQDPyaSLNPRMTVADIIAEGIDIHGLAKtrKERMAKVHELLETVGLNkEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:cd03264 72 -RRIGYLPQEF--GVYPNFTVREFLDYIAWLKGIPS--KEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-230 |
1.66e-30 |
|
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: 114.13 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 28 LTFD--IFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrSELKKFNRKMQMIFQDpyASLNPRMT 105
Cdd:cd03298 15 MHFDltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV------TAAPPADRPVSMLFQE--NNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 106 VADIIAEGIDiHGLaKTRKERMAKVHELLETVGL-NKEhaNRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVS 184
Cdd:cd03298 87 VEQNVGLGLS-PGL-KLTAEDRQAIEVALARVGLaGLE--KRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 654962578 185 IQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:cd03298 163 LRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-229 |
2.08e-30 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 115.16 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLfngenvHGRKSRSELKKF 85
Cdd:PRK11247 13 LLLNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL------AGTAPLAEARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMqmiFQDpyASLNPRMTVadiiaegIDIHGLAKTRKERmAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:PRK11247 83 TRLM---FQD--ARLLPWKKV-------IDNVGLGLKGQWR-DAALQALAAVGL-ADRANEWPAALSGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKI 229
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-240 |
2.10e-30 |
|
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: 114.51 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 24 AVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMIFQDpyaSLNPR 103
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL----ALADPAWLRRQVGVVLQE---NVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 104 MTVADIIA---EGIDIHGLAKTrkERMAKVHELLETVGLNKEH-ANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPIS 179
Cdd:cd03252 90 RSIRDNIAladPGMSMERVIEA--AKLAGAHDFISELPEGYDTiVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654962578 180 ALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKYiSDRIGVMYRGKIVELAPSDELYR 240
Cdd:cd03252 168 ALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
26-210 |
2.21e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 113.73 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 26 DGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgrKSRSELKKfnrkmQMIFQDPYASLNPRMT 105
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR--DAREDYRR-----RLAYLGHADGLKPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 106 VADIIAEGIDIHGLAKTRkermAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSI 185
Cdd:COG4133 92 VRENLRFWAALYGLRADR----EAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
170 180
....*....|....*....|....*
gi 654962578 186 QAQVVNLMKKlQRERGLTYLFIAHD 210
Cdd:COG4133 167 VALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-280 |
2.44e-30 |
|
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: 114.10 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGEnvhgrksrsELKKFNRKMQMIFQDpyASLNPRM 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK---------QITEPGPDRMVVFQN--YSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 105 TVADIIAEGIDIHGLAKTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVS 184
Cdd:TIGR01184 70 TVRENIALAVDRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 185 IQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVM------YRGKIVElapsdelyrnpvhpytkallsaIPLPD 258
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILE----------------------VPFPR 206
|
250 260
....*....|....*....|..
gi 654962578 259 PdseKTRQRKIYDPSIHDYNGE 280
Cdd:TIGR01184 207 P---RDRLEVVEDPSYYDLRNE 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-238 |
4.28e-30 |
|
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: 119.44 E-value: 4.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 16 FTSKGT-IKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKKFNRKMQ--MI 92
Cdd:TIGR02203 338 FRYPGRdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQdvVL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 93 FQDpyaslnprmTVADIIAEGidihglaKTRKERMAKVHELLETVGLnKEHANRYPHEF-----------SGGQRQRIGI 161
Cdd:TIGR02203 418 FND---------TIANNIAYG-------RTEQADRAEIERALAAAYA-QDFVDKLPLGLdtpigengvllSGGQRQRLAI 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654962578 162 ARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKYiSDRIGVMYRGKIVELAPSDEL 238
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNEL 554
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-238 |
4.36e-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: 113.86 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 23 KAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMIFQDP------ 96
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI----REVTLDSLRRAIGVVPQDTvlfndt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 97 ------YAslNPRMTVADII--AEGIDIHglaktrkERMAKVHELLETV----GLnkehanryphEFSGGQRQRIGIARA 164
Cdd:cd03253 91 igynirYG--RPDATDEEVIeaAKAAQIH-------DKIMRFPDGYDTIvgerGL----------KLSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654962578 165 LAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVkYISDRIGVMYRGKIVELAPSDEL 238
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEEL 222
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
34-229 |
4.41e-30 |
|
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: 113.03 E-value: 4.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 34 RGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGrksrseLKKFNRKMQMIFQDpyASLNPRMTVADIIAEG 113
Cdd:TIGR01277 23 DGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG------LAPYQRPVSMLFQE--NNLFAHLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 114 IdiHGLAKTRKERMAKVHELLETVGLNkEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLM 193
Cdd:TIGR01277 95 L--HPGLKLNAEQQEKVVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 654962578 194 KKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKI 229
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-254 |
9.36e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 114.04 E-value: 9.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 40 LVGESGCGKSTTGRTIIRLYDATSG-----EVLFNGENVHGRKsrsELKKFNRKMQMIFQDPyaslNP-RMTVADIIAEG 113
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYR---DVLEFRRRVGMLFQRP----NPfPMSIMDNVLAG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 114 IDIHGLAKtRKERMAKVHELLETVGL---NKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVV 190
Cdd:PRK14271 125 VRAHKLVP-RKEFRGVAQARLTEVGLwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654962578 191 NLMKKLQRErgLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPVHPYTKALLSAI 254
Cdd:PRK14271 204 EFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGL 265
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-267 |
1.62e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 113.36 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKqhfFTSKGTIK-AVDGLTFDIFRGETLGLVGESGCGKSTTGRTI--IRLYDATSGEVLfngeNVHGRK 77
Cdd:PRK13640 1 MKDNIVEFKHVS---FTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLIngLLLPDDNPNSKI----TVDGIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 78 SRSE-LKKFNRKMQMIFQDPYASLnPRMTVADIIAEGIDIHGLAktRKERMAKVHELLETVGLnKEHANRYPHEFSGGQR 156
Cdd:PRK13640 74 LTAKtVWDIREKVGIVFQNPDNQF-VGATVGDDVAFGLENRAVP--RPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 157 QRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKyISDRIGVMYRGKIVELAPSD 236
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPV 228
|
250 260 270
....*....|....*....|....*....|.
gi 654962578 237 ELYRNPVhpytkaLLSAIPLPDPDSEKTRQR 267
Cdd:PRK13640 229 EIFSKVE------MLKEIGLDIPFVYKLKNK 253
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-243 |
2.11e-29 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 112.57 E-value: 2.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 28 LTFDIfrGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSrselKKFNRKMQMIFQD-PYASlnpRMTV 106
Cdd:PRK10575 32 LTFPA--GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS----KAFARKVAYLPQQlPAAE---GMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 107 ADIIAEG-IDIHG-LAKTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVS 184
Cdd:PRK10575 103 RELVAIGrYPWHGaLGRFGAADREKVEEAISLVGL-KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 654962578 185 IQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPV 243
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
24-230 |
2.39e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.87 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 24 AVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrKSRSELKKFNRKMQMIFQDPYASLnpr 103
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDT---SDEENLWDIRNKAGMVFQNPDNQI--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 104 mtVADIIAEGIDI--HGLAKTRKERMAKVHELLETVGLN--KEHAnryPHEFSGGQRQRIGIARALAVEPDFIIADEPIS 179
Cdd:PRK13633 99 --VATIVEEDVAFgpENLGIPPEEIRERVDESLKKVGMYeyRRHA---PHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 654962578 180 ALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYiSDRIGVMYRGKIV 230
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
40-267 |
3.14e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 112.81 E-value: 3.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 40 LVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKKFNRKMQMIFQDPYASLNPRmTVADIIAEGIDIHGL 119
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQFPEHQLFEE-TVEKDICFGPMNFGV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 120 AKTRKERMAKvhELLETVGLNKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRE 199
Cdd:PRK13634 117 SEEDAKQKAR--EMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKE 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 200 RGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPvhpytkALLSAIPLPDPDSEKTRQR 267
Cdd:PRK13634 195 KGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP------DELEAIGLDLPETVKFKRA 256
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-243 |
3.88e-29 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 111.10 E-value: 3.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrSELKKF 85
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI------TKLPMH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NR-KMQMIFQDPYASLNPRMTVADIIAEGIDIHGlaKTRKERMAKVHELLETVGLnkEH-ANRYPHEFSGGQRQRIGIAR 163
Cdd:cd03218 71 KRaRLGIGYLPQEASIFRKLTVEENILAVLEIRG--LSKKEREEKLEELLEEFHI--THlRKSKASSLSGGERRRVEIAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 164 ALAVEPDFIIADEPISALD-VSIQaQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:cd03218 147 ALATNPKFLLLDEPFAGVDpIAVQ-DIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
.
gi 654962578 243 V 243
Cdd:cd03218 225 L 225
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-234 |
5.91e-29 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 110.93 E-value: 5.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLkqHFFTSKGTIkaVDGLTFDIFRGETLGLVGESGCGKSTTGRTI--IRLYDATSGEVLFNGENVhgrksrSEL- 82
Cdd:COG0396 1 LEIKNL--HVSVEGKEI--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDI------LELs 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 --KKFNRKMQMIFQDPYASlnPRMTVADIIAEGID-IHGLAKTRKERMAKVHELLETVGLNKEHANRYPHE-FSGGQRQR 158
Cdd:COG0396 71 pdERARAGIFLAFQYPVEI--PGVSVSNFLRTALNaRRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 159 IGIARALAVEPDFIIADEPISALDV---SIQAQVVNLMkklqRERGLTYLFIAHDLSMVKYIS-DRIGVMYRGKIV---- 230
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDIdalRIVAEGVNKL----RSPDRGILIITHYQRILDYIKpDFVHVLVDGRIVksgg 224
|
....*
gi 654962578 231 -ELAP 234
Cdd:COG0396 225 kELAL 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-230 |
6.06e-29 |
|
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: 110.37 E-value: 6.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 22 IKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhGRKSRSELKkfnRKMQMIFQDP---YA 98
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI-RQLDPADLR---RNIGYVPQDVtlfYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 99 SLNPRMTVADIIAEGIDIhglakTRKERMAKVHELletvglnkehANRYPHEF-----------SGGQRQRIGIARALAV 167
Cdd:cd03245 93 TLRDNITLGAPLADDERI-----LRAAELAGVTDF----------VNKHPNGLdlqigergrglSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654962578 168 EPDFIIADEPISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKyISDRIGVMYRGKIV 230
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
25-239 |
7.48e-29 |
|
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: 116.20 E-value: 7.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGEnvhgrkSRSELKK--FNRKMQMIFQDpyASL-- 100
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGI------PREEIPRevLANSVAMVDQD--IFLfe 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 101 ----------NPRMTVADIIAEGID--IHGLAKTRKERMAkvHELLETvGLNkehanrypheFSGGQRQRIGIARALAVE 168
Cdd:TIGR03796 567 gtvrdnltlwDPTIPDADLVRACKDaaIHDVITSRPGGYD--AELAEG-GAN----------LSGGQRQRLEIARALVRN 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654962578 169 PDFIIADEPISALDVSIQAQVV-NLmkklqRERGLTYLFIAHDLSMVKYiSDRIGVMYRGKIVELAPSDELY 239
Cdd:TIGR03796 634 PSILILDEATSALDPETEKIIDdNL-----RRRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELW 699
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
23-240 |
1.45e-28 |
|
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: 114.80 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 23 KAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMIFQDP---YAS 99
Cdd:TIGR02204 354 PALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDL----RQLDPAELRARMALVPQDPvlfAAS 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 100 L--NPRMTVADIIAEGIDIHGLAKTRKERMAKVHELLET-VGlnkEHANRypheFSGGQRQRIGIARALAVEPDFIIADE 176
Cdd:TIGR02204 430 VmeNIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTyLG---ERGVT----LSGGQRQRIAIARAILKDAPILLLDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654962578 177 PISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKYiSDRIGVMYRGKIVELAPSDELYR 240
Cdd:TIGR02204 503 ATSALDAESEQLVQQALETLMKGR--TTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIA 563
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-246 |
1.54e-28 |
|
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: 109.54 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKK- 84
Cdd:TIGR03410 1 LEVSNLNVYY----GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 --FNRKMQMIFqdpyaslnPRMTVADIIAEGIDihGLAKTRKERMAKVHELLETVglnKEHANRYPHEFSGGQRQRIGIA 162
Cdd:TIGR03410 77 iaYVPQGREIF--------PRLTVEENLLTGLA--ALPRRSRKIPDEIYELFPVL---KEMLGRRGGDLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 163 RALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDK 223
|
....
gi 654962578 243 VHPY 246
Cdd:TIGR03410 224 VRRY 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-248 |
1.67e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 110.14 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 28 LTFDIFRGETLGLVGESGCGKSTTGRTIIRL---YDA---TSGEVLFNGENVHgrksRSELKKFNRKMQMIFQDPYASln 101
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIF----QIDAIKLRKEVGMVFQQPNPF-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 102 PRMTVADIIAEGIDIHGLaKTRKERMAKVHELLETVGLNKEHANRY---PHEFSGGQRQRIGIARALAVEPDFIIADEPI 178
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGI-KEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 179 SALDVSIQAQVVNLMKKLQRErgLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPVHPYTK 248
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
39-242 |
1.78e-28 |
|
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: 112.12 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 39 GLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKKFNRKMQMIFQDpyASLNPRMTVADIIAEGIDiHG 118
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQE--ARLFPHLSVRGNLLYGRK-RA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 119 LAKTRKERMAKVHELLetvGLnkEH-ANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQ 197
Cdd:COG4148 106 PRAERRISFDEVVELL---GI--GHlLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 654962578 198 RERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:COG4148 181 DELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
1.82e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 110.71 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFftSKGTiKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgrKSRS 80
Cdd:PRK13636 1 MEDYILKVEELNYNY--SDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID--YSRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 ELKKFNRKMQMIFQDPYASLNPRMTVADIIAEGIDIhGLAKtrKERMAKVHELLETVGLnkEHANRYP-HEFSGGQRQRI 159
Cdd:PRK13636 76 GLMKLRESVGMVFQDPDNQLFSASVYQDVSFGAVNL-KLPE--DEVRKRVDNALKRTGI--EHLKDKPtHCLSFGQKKRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654962578 160 GIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-221 |
1.97e-28 |
|
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: 109.06 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTdKLLEIKGLKQHFF---TSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGEN----- 72
Cdd:COG4778 1 MT-TLLEVENLSKTFTlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 73 --------VHGRksRSELKkfnrkmqmifqdpYAS--LN--PRMTVADIIAEGIDIHGLAktRKERMAKVHELLETVGLN 140
Cdd:COG4778 80 aqaspreiLALR--RRTIG-------------YVSqfLRviPRVSALDVVAEPLLERGVD--REEARARARELLARLNLP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 141 KEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQReRGLTYLFIAHDLSMVKYISDR 220
Cdd:COG4778 143 ERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKA-RGTAIIGIFHDEEVREAVADR 221
|
.
gi 654962578 221 I 221
Cdd:COG4778 222 V 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
6-242 |
5.38e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.53 E-value: 5.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFFTSKGT---IKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSEL 82
Cdd:PRK13641 1 MSIKFENVDYIYSPGTpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 KKFNRKMQMIFQDPYASLNPRMTVADIIAEGIDihgLAKTRKERMAKVHELLETVGLNKEHANRYPHEFSGGQRQRIGIA 162
Cdd:PRK13641 81 KKLRKKVSLVFQFPEAQLFENTVLKDVEFGPKN---FGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 163 RALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
25-240 |
7.88e-28 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 113.30 E-value: 7.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMIFQ---------- 94
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDL----AIADPAWLRRQMGVVLQenvlfsrsir 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 95 DPYASLNPRMTVADIIAEGidihglaktrkeRMAKVHELLETV--GLNKEHANRyPHEFSGGQRQRIGIARALAVEPDFI 172
Cdd:TIGR01846 549 DNIALCNPGAPFEHVIHAA------------KLAGAHDFISELpqGYNTEVGEK-GANLSGGQRQRIAIARALVGNPRIL 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 173 IADEPISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKYiSDRIGVMYRGKIVELAPSDELYR 240
Cdd:TIGR01846 616 IFDEATSALDYESEALIMRNMREICRGR--TVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLA 680
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-259 |
1.52e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 108.56 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 23 KAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENV-HGRKSRSELKKFNRKMQMIFQDPYASLN 101
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKIKEVKRLRKEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 102 pRMTVADIIAEGiDIHgLAKTRKERMAKVHELLETVGLNKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISAL 181
Cdd:PRK13645 105 -QETIEKDIAFG-PVN-LGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 182 DVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNpvhpytKALLSAIPLPDP 259
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN------QELLTKIEIDPP 253
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-257 |
1.63e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 107.93 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 2 TDKLLEIKGLKqhffTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRkSRSE 81
Cdd:PRK11831 4 VANLVDMRGVS----FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM-SRSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 82 LKKFNRKMQMIFQDpyASLNPRMTVADIIAEGIDIHGL---AKTRKERMAKvhelLETVGLnKEHANRYPHEFSGGQRQR 158
Cdd:PRK11831 79 LYTVRKRMSMLFQS--GALFTDMNVFDNVAYPLREHTQlpaPLLHSTVMMK----LEAVGL-RGAAKLMPSELSGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 159 IGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDEL 238
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
250 260
....*....|....*....|..
gi 654962578 239 YRNPvHPYTKALLSAI---PLP 257
Cdd:PRK11831 232 QANP-DPRVRQFLDGIadgPVP 252
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-242 |
1.77e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 112.12 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 27 GLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMIFQDPyasLNPRMTV 106
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL----VQYDHHYLHRQVALVGQEP---VLFSGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 107 ADIIAEGIDIHGLAKTRK-ERMAKVHELLE--TVGLNK---EHANryphEFSGGQRQRIGIARALAVEPDFIIADEPISA 180
Cdd:TIGR00958 572 RENIAYGLTDTPDEEIMAaAKAANAHDFIMefPNGYDTevgEKGS----QLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654962578 181 LDVSIQAQVVNLMKKlqreRGLTYLFIAHDLSMVKYiSDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:TIGR00958 648 LDAECEQLLQESRSR----ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-243 |
2.54e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 106.71 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 7 EIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRsELKKfn 86
Cdd:COG4604 3 EIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSR-ELAK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 87 rKMQMIFQDPyaSLNPRMTVADIIAEGIDIHGLAKTRKERMAKVHELLETVGLNkEHANRYPHEFSGGQRQRIGIARALA 166
Cdd:COG4604 76 -RLAILRQEN--HINSRLTVRELVAFGRFPYSKGRLTAEDREIIDEAIAYLDLE-DLADRYLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 167 VEPDFIIADEPISALDVsiqAQVVNLMKKLQR---ERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPV 243
Cdd:COG4604 152 QDTDYVLLDEPLNNLDM---KHSVQMMKLLRRladELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEV 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-242 |
4.69e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 107.63 E-value: 4.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 3 DKLLEIKGLKQhFFTSKGT--IKAVDGLTFDIFRGETLGLVGESGCGKST----------TGRTIIRLYDATSGE--VLF 68
Cdd:PRK13631 19 DIILRVKNLYC-VFDEKQEneLVALNNISYTFEKNKIYFIIGNSGSGKSTlvthfnglikSKYGTIQVGDIYIGDkkNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 69 NGENVHGRKSRSELKKFNRKMQMIFQDPYASLNPRMTVADIIAEGIDIhGLAKTRKERMAKVHelLETVGLNKEHANRYP 148
Cdd:PRK13631 98 ELITNPYSKKIKNFKELRRRVSMVFQFPEYQLFKDTIEKDIMFGPVAL-GVKKSEAKKLAKFY--LNKMGLDDSYLERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 149 HEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGK 228
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
250
....*....|....
gi 654962578 229 IVELAPSDELYRNP 242
Cdd:PRK13631 254 ILKTGTPYEIFTDQ 267
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-242 |
6.13e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.43 E-value: 6.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 16 FTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMIFQD 95
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI----TKENIREVRKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 96 PYASL-NPrmTVADIIAEGIDIHGL-AKTRKERmakVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFII 173
Cdd:PRK13652 87 PDDQIfSP--TVEQDIAFGPINLGLdEETVAHR---VSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654962578 174 ADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-240 |
6.91e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.40 E-value: 6.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 19 KGT---IKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKKFNRKMQMIFQD 95
Cdd:PRK13646 14 KGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 96 PYASLNPRMTVADIIAE----GIDIhglaktrKERMAKVHELLETVGLNKEHANRYPHEFSGGQRQRIGIARALAVEPDF 171
Cdd:PRK13646 94 PESQLFEDTVEREIIFGpknfKMNL-------DEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654962578 172 IIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYR 240
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-238 |
6.95e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 110.05 E-value: 6.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 16 FTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGrKSRSELKkfnRKMQMIFQD 95
Cdd:PRK13657 342 FSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT-VTRASLR---RNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 96 PyaslnprMTVADIIAEGIDIhGLAKTRKERM------AKVHELLET--------VGlnkEHANRypheFSGGQRQRIGI 161
Cdd:PRK13657 418 A-------GLFNRSIEDNIRV-GRPDATDEEMraaaerAQAHDFIERkpdgydtvVG---ERGRQ----LSGGERQRLAI 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654962578 162 ARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKYiSDRIGVMYRGKIVELAPSDEL 238
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDELMKGR--TTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDEL 556
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
25-237 |
9.32e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.24 E-value: 9.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgRKSRSELKKfNRKM--QmifqdpYASLNP 102
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA-DWSPAELAR-RRAVlpQ------HSSLSF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 103 RMTVADIIAEGIDIHGLAKTRKERMakVHELLETVGLnkEH-ANRYPHEFSGGQRQRIGIARALA------VEPDFIIAD 175
Cdd:PRK13548 90 PFTVEEVVAMGRAPHGLSRAEDDAL--VAAALAQVDL--AHlAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654962578 176 EPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDE 237
Cdd:PRK13548 166 EPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
5-221 |
1.03e-26 |
|
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: 104.40 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFF--TSKGT-IKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNgenvHGRKSRSE 81
Cdd:TIGR02324 1 LLEVEDLSKTFTlhQQGGVrLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVR----HEGAWVDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 82 LKKFNRKMQMI--FQDPYAS----LNPRMTVADIIAEGIDIHGLAktRKERMAKVHELLETVGLNKEHANRYPHEFSGGQ 155
Cdd:TIGR02324 77 AQASPREVLEVrrKTIGYVSqflrVIPRVSALEVVAEPLLERGVP--REAARARARELLARLNIPERLWHLPPATFSGGE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654962578 156 RQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQReRGLTYLFIAHDLSMVKYISDRI 221
Cdd:TIGR02324 155 QQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKA-RGAALIGIFHDEEVRELVADRV 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-230 |
1.28e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 104.19 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 20 GTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRsELKKFNRKMQMIFQDPYAS 99
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNR-EVPFLRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 100 LNprMTVADIIAEGIDIHGLAKTRKERmaKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPIS 179
Cdd:PRK10908 92 MD--RTVYDNVAIPLIIAGASGDDIRR--RVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 654962578 180 ALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-294 |
1.34e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 108.01 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSelkkF 85
Cdd:PRK09536 4 IDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA----A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDpyASLNPRMTVADIIAEGIDIHglaKTRKERM-----AKVHELLETVGLNKeHANRYPHEFSGGQRQRIG 160
Cdd:PRK09536 76 SRRVASVPQD--TSLSFEFDVRQVVEMGRTPH---RSRFDTWtetdrAAVERAMERTGVAQ-FADRPVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 161 IARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQrERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYR 240
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654962578 241 NP-------------VHPYTKAlLSAIPLPDPDSEKTRQrkiyDPSIHDYNGEEPELREVS----PGHYVS 294
Cdd:PRK09536 229 ADtlraafdartavgTDPATGA-PTVTPLPDPDRTEAAA----DTRVHVVGGGQPAARAVSrlvaAGASVS 294
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-211 |
1.48e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 104.78 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 24 AVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSrselkkfnrKMQMIFQDpyASLNPR 103
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA---------ERGVVFQN--EGLLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 104 MTVADIIAEGIDIHGLAKTrkERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDV 183
Cdd:PRK11248 85 RNVQDNVAFGLQLAGVEKM--QRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180
....*....|....*....|....*...
gi 654962578 184 SIQAQVVNLMKKLQRERGLTYLFIAHDL 211
Cdd:PRK11248 162 FTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-236 |
2.00e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 104.68 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFFTSKGTIkaVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSrs 80
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTV--AENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 elKKFNRKMQMIFQDpyASLNPRMTVADIIAEGIDIHG--LAKTRKERMAKVHELLETVGLNkEHANRYPHEFSGGQRQR 158
Cdd:PRK10253 77 --KEVARRIGLLAQN--ATTPGDITVQELVARGRYPHQplFTRWRKEDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654962578 159 IGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV-ELAPSD 236
Cdd:PRK10253 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVaQGAPKE 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
24-279 |
2.37e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.83 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 24 AVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMIFQDPYASLNPR 103
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI----TDDNFEKLRKHIGIVFQNPDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 104 mTVADIIAEGIDIHglAKTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDV 183
Cdd:PRK13648 100 -IVKYDVAFGLENH--AVPYDEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 184 SIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYiSDRIGVMYRGKIVELAPSDELYRNpvhpytKALLSAIPLPDPDSEK 263
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH------AEELTRIGLDLPFPIK 248
|
250
....*....|....*.
gi 654962578 264 TRQRKIYDPSIHDYNG 279
Cdd:PRK13648 249 INQMLGHQTSFLTYEG 264
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-230 |
2.96e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.01 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFFtsKGTI---KAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrSEL 82
Cdd:COG1101 2 LELKNLSKTFN--PGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV------TKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 KKFNRKMQM--IFQDPYASLNPRMTVADIIAegidihgLAKTR-----------KERMAKVHELLETVGLNKEHANRYPH 149
Cdd:COG1101 74 PEYKRAKYIgrVFQDPMMGTAPSMTIEENLA-------LAYRRgkrrglrrgltKKRRELFRELLATLGLGLENRLDTKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 150 EF-SGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLS-MVKYiSDRIGVMYRG 227
Cdd:COG1101 147 GLlSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEqALDY-GNRLIMMHEG 225
|
...
gi 654962578 228 KIV 230
Cdd:COG1101 226 RII 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-238 |
3.34e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 107.71 E-value: 3.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTI--IRLYDATSGEVLFNGENVHGRKS 78
Cdd:PRK13549 1 MMEYLLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgVYPHGTYEGEIIFEGEELQASNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 79 R-SELKkfnrKMQMIFQDpyASLNPRMTVADIIAEGIDIHGLAKTRKERM-AKVHELLETVGLNKEHANRYpHEFSGGQR 156
Cdd:PRK13549 77 RdTERA----GIAIIHQE--LALVKELSVLENIFLGNEITPGGIMDYDAMyLRAQKLLAQLKLDINPATPV-GNLGLGQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 157 QRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQReRGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSD 236
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAA 228
|
..
gi 654962578 237 EL 238
Cdd:PRK13549 229 GM 230
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-242 |
3.48e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 103.57 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftsKGTiKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHG----RKSR-- 79
Cdd:COG1137 4 LEAENLVKSY---GKR-TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmhKRARlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 80 --------SelkkfnrkmqmIFQdpyaslnpRMTVAD---IIAEgidIHGLakTRKERMAKVHELLETVGLnkEH-ANRY 147
Cdd:COG1137 80 igylpqeaS-----------IFR--------KLTVEDnilAVLE---LRKL--SKKEREERLEELLEEFGI--THlRKSK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 148 PHEFSGGQRQRIGIARALAVEPDFIIADEPISALD---VS-IQAQVVNLmkklqRERGLTYLFIAHD----LSmvkyISD 219
Cdd:COG1137 134 AYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiaVAdIQKIIRHL-----KERGIGVLITDHNvretLG----ICD 204
|
250 260
....*....|....*....|...
gi 654962578 220 RIGVMYRGKIVELAPSDELYRNP 242
Cdd:COG1137 205 RAYIISEGKVLAEGTPEEILNNP 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-229 |
4.14e-26 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 101.74 E-value: 4.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 3 DKLLEIKGLKQHfftskgtiKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSEL 82
Cdd:cd03215 2 EPVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 KK---F---NRKMQMIFQDpyaslnprMTVADIIAEGIdihglaktrkermakvheLLetvglnkehanryphefSGGQR 156
Cdd:cd03215 74 RAgiaYvpeDRKREGLVLD--------LSVAENIALSS------------------LL-----------------SGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654962578 157 QRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKI 229
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
21-237 |
4.75e-26 |
|
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: 108.03 E-value: 4.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 21 TIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgRKSRSELKkfnRKMQMIFQDP---Y 97
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIR-QIDPADLR---RNIGYVPQDPrlfY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 98 ASLnprmtvadiiAEGIDIhGLAKTRKERMAKVhelLETVGLNkEHANRYPHEF-----------SGGQRQRIGIARALA 166
Cdd:TIGR03375 553 GTL----------RDNIAL-GAPYADDEEILRA---AELAGVT-EFVRRHPDGLdmqigergrslSGGQRQAVALARALL 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654962578 167 VEPDFIIADEPISALDVSIQAQvvnLMKKLQRE-RGLTYLFIAHDLSMVKyISDRIGVMYRGKIVELAPSDE 237
Cdd:TIGR03375 618 RDPPILLLDEPTSAMDNRSEER---FKDRLKRWlAGKTLVLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQ 685
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-230 |
1.28e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.89 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 3 DKLLEIKGLkqHFFTSKGTiKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRsEL 82
Cdd:PRK13647 2 DNIIEVEDL--HFRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK-WV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 KKfnrKMQMIFQDPYASLNPrMTVADIIAEGIDIHGLakTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIA 162
Cdd:PRK13647 78 RS---KVGLVFQDPDDQVFS-STVWDDVAFGPVNMGL--DKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 163 RALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-255 |
1.98e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 105.96 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSrSELKK 84
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDA-DALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 FNRK-MQMIFQDPYasLNPRMTVAdiiaEGIDIHGL--AKTRKERMAKVHELLETVGLNkEHANRYPHEFSGGQRQRIGI 161
Cdd:PRK10535 83 LRREhFGFIFQRYH--LLSHLTAA----QNVEVPAVyaGLERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 162 ARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDlSMVKYISDRIGVMYRGKIVELAPSdelyrN 241
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPPA-----Q 228
|
250
....*....|....
gi 654962578 242 PVHPYTKALLSAIP 255
Cdd:PRK10535 229 EKVNVAGGTEPVVN 242
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-236 |
2.31e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.50 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 23 KAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKKFNRKMQMIFQDPYASLNP 102
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 103 RMTVADIiAEGIDIHGLAKTRKERMAKvhELLETVGLNKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALD 182
Cdd:PRK13643 100 ETVLKDV-AFGPQNFGIPKEKAEKIAA--EKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 183 VSIQAQVVNLMKKLQrERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELA-PSD 236
Cdd:PRK13643 177 PKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGtPSD 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-230 |
2.48e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.13 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 23 KAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKKFNRKMQMIFQDPYASLNP 102
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 103 RmTVADIIAEGIDIHGLAKTRKERMAKvhELLETVGLNKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALD 182
Cdd:PRK13649 101 E-TVLKDVAFGPQNFGVSQEEAEALAR--EKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 654962578 183 VSIQAQVVNLMKKLQrERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:PRK13649 178 PKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-252 |
2.60e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.78 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 2 TDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYD-----ATSGEVLFNGENVHGr 76
Cdd:PRK14243 7 TETVLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 77 kSRSELKKFNRKMQMIFQDPyaslNP-RMTVADIIAEGIDIHGLAKTRKE------RMA----KVHELLETVGLNkehan 145
Cdd:PRK14243 82 -PDVDPVEVRRRIGMVFQKP----NPfPKSIYDNIAYGARINGYKGDMDElverslRQAalwdEVKDKLKQSGLS----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 146 rypheFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErgLTYLFIAHDLSMVKYISDRI---- 221
Cdd:PRK14243 152 -----LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTaffn 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 654962578 222 ------GVMYrGKIVELAPSDELYRNPVHPYTKALLS 252
Cdd:PRK14243 225 veltegGGRY-GYLVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-210 |
5.71e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 99.85 E-value: 5.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 2 TDKLLEIKGLKQHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVH--GRKSR 79
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmDEEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 80 SELKKfnRKMQMIFQDpyaslnpRMTVADIIA-EGIDIHGLAKTRKERMAKVH--ELLETVGLNKEhANRYPHEFSGGQR 156
Cdd:PRK10584 83 AKLRA--KHVGFVFQS-------FMLIPTLNAlENVELPALLRGESSRQSRNGakALLEQLGLGKR-LDHLPAQLSGGEQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 654962578 157 QRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHD 210
Cdd:PRK10584 153 QRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-224 |
6.41e-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: 104.29 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKqhfFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGEnvhgrksrsELKKF 85
Cdd:TIGR02857 322 LEFSGVS---VAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV---------PLADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKmQMIFQDPYASLNPRMtVADIIAEGIDIHGLAKTRKE-----RMAKVHELLETV--GLNKEhANRYPHEFSGGQRQR 158
Cdd:TIGR02857 390 DAD-SWRDQIAWVPQHPFL-FAGTIAENIRLARPDASDAEirealERAGLDEFVAALpqGLDTP-IGEGGAGLSGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654962578 159 IGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSmVKYISDRIGVM 224
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLA-LAALADRIVVL 529
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
23-231 |
6.50e-25 |
|
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: 98.54 E-value: 6.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 23 KAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrSELKKFNRK-MQMIFQDPYasln 101
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV------SDLEKALSSlISVLNQRPY---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 102 prmtvadiiaegidihgLAKTrkermakvhELLETVGLnkehanryphEFSGGQRQRIGIARALAVEPDFIIADEPISAL 181
Cdd:cd03247 86 -----------------LFDT---------TLRNNLGR----------RFSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 654962578 182 DVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKYIsDRIGVMYRGKIVE 231
Cdd:cd03247 130 DPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
24-231 |
8.57e-25 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 99.11 E-value: 8.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 24 AVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMIFQDPYaslnpr 103
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI----SKIGLHDLRSRISIIPQDPV------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 104 mTVADIIAEGIDIHGLAKTrkermAKVHELLETVGLnKEHANRYPHE-----------FSGGQRQRIGIARALAVEPDFI 172
Cdd:cd03244 89 -LFSGTIRSNLDPFGEYSD-----EELWQALERVGL-KEFVESLPGGldtvveeggenLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654962578 173 IADEPISALDVsiqaQVVNLMKKLQRE--RGLTYLFIAHDLSMVKYiSDRIGVMYRGKIVE 231
Cdd:cd03244 162 VLDEATASVDP----ETDALIQKTIREafKDCTVLTIAHRLDTIID-SDRILVLDKGRVVE 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-231 |
8.92e-25 |
|
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: 99.14 E-value: 8.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 17 TSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVlfngeNVHGRKSrSELkkfnrkmqmifqDP 96
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-----TVRGRVS-SLL------------GL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 97 YASLNPRMTVADIIAEGIDIHGLakTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADE 176
Cdd:cd03220 92 GGGFNPELTGRENIYLNGRLLGL--SRKEIDEKIDEIIEFSEL-GDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 177 PISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVE 231
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-230 |
1.02e-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: 99.33 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 8 IKGLKQHFFTSK-GTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGeNVHGRKSRSELKK-- 84
Cdd:cd03267 19 LIGSLKSLFKRKyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRig 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 --FNRKMQMIFQDPyaslnprmtVADIIAEGIDIHGLAKTR-KERMAKVHELLETVGLNKEHANRypheFSGGQRQRIGI 161
Cdd:cd03267 98 vvFGQKTQLWWDLP---------VIDSFYLLAAIYDLPPARfKKRLDELSELLDLEELLDTPVRQ----LSLGQRMRAEI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654962578 162 ARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
24-231 |
1.31e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 103.56 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 24 AVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKKFNRKMQMI--FQD------ 95
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVhlFNDtianni 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 96 PYASlNPRMTVADIIAEGIDIHGLaktrkERMAKVHELLETV-GLNKEhanryphEFSGGQRQRIGIARALAVEPDFIIA 174
Cdd:PRK11176 438 AYAR-TEQYSREQIEEAARMAYAM-----DFINKMDNGLDTViGENGV-------LLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654962578 175 DEPISALDV----SIQAQvvnlMKKLQRERglTYLFIAHDLSMVKYiSDRIGVMYRGKIVE 231
Cdd:PRK11176 505 DEATSALDTeserAIQAA----LDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVE 558
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-238 |
3.20e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.03 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 3 DKLLEIKGLkqhFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhGRKSRSEL 82
Cdd:COG3845 255 EVVLEVENL---SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-TGLSPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 kkfnRKMQM--IFQDPYAS-LNPRMTVAD-IIAEGIDIHGLAKTRKERMAKVHELleTVGLNKEHANRYPHE------FS 152
Cdd:COG3845 331 ----RRLGVayIPEDRLGRgLVPDMSVAEnLILGRYRRPPFSRGGFLDRKAIRAF--AEELIEEFDVRTPGPdtparsLS 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 153 GGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVEL 232
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGE 483
|
....*.
gi 654962578 233 APSDEL 238
Cdd:COG3845 484 VPAAEA 489
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
25-237 |
3.30e-24 |
|
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: 102.13 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgRKSRSELkkfnrkMQMIF---QDPyaSLN 101
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS-QWDREEL------GRHIGylpQDV--ELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 102 PRmTVADIIA--EGID---IHGLAktrkeRMAKVHELL-------ETV----GLNkehanrypheFSGGQRQRIGIARAL 165
Cdd:COG4618 419 DG-TIAENIArfGDADpekVVAAA-----KLAGVHEMIlrlpdgyDTRigegGAR----------LSGGQRQRIGLARAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKyISDRIGVMYRGKIVELAPSDE 237
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDE 552
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-242 |
3.33e-24 |
|
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: 97.61 E-value: 3.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 30 FDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENvhGRKSRSELKKFNRKMQMIFQDPyaslnprMTVADI 109
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS--PGKGWRHIGYVPQRHEFAWDFP-------ISVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 110 IAEGID--IHGLAKTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQA 187
Cdd:TIGR03771 72 VMSGRTghIGWLRRPCVADFAAVRDALRRVGL-TELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 188 QVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIgVMYRGKIVELAPSDELyRNP 242
Cdd:TIGR03771 151 LLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQL-QDP 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-236 |
3.42e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.02 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 3 DKLLEIKGLkqhffTSKGTIKAVDgltFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSEL 82
Cdd:COG1129 254 EVVLEVEGL-----SVGGVVRDVS---FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 KK---F---NRKMQMIFQDpyaslnprMTVADIIA----EGIDIHGLAKTRKERmAKVHELLETVGLnkehanRYPH--- 149
Cdd:COG1129 326 RAgiaYvpeDRKGEGLVLD--------LSIRENITlaslDRLSRGGLLDRRRER-ALAEEYIKRLRI------KTPSpeq 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 150 ---EFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYR 226
Cdd:COG1129 391 pvgNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMRE 469
|
250
....*....|.
gi 654962578 227 GKIV-ELAPSD 236
Cdd:COG1129 470 GRIVgELDREE 480
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-230 |
9.60e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.39 E-value: 9.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 13 QHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMI 92
Cdd:PRK11231 6 ENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI----SMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 93 FQDPyasLNPR-MTVADIIAEG----IDIHG-LAKTRKERMAKVHELLETVGLnkehANRYPHEFSGGQRQRIGIARALA 166
Cdd:PRK11231 82 PQHH---LTPEgITVRELVAYGrspwLSLWGrLSAEDNARVNQAMEQTRINHL----ADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654962578 167 VEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-244 |
1.20e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 96.69 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 10 GLKQHFF----TSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVlfngeNVHGRKSrselkkf 85
Cdd:COG1134 23 SLKELLLrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV-----EVNGRVS------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 nrkmQMIfqDPYASLNPRMTVAD-IIAEGIdIHGLakTRKERMAKVHELLETVGLnKEHAN----RYphefSGGQRQRIG 160
Cdd:COG1134 91 ----ALL--ELGAGFHPELTGREnIYLNGR-LLGL--SRKEIDEKFDEIVEFAEL-GDFIDqpvkTY----SSGMRARLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 161 IARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDE--- 237
Cdd:COG1134 157 FAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEvia 235
|
....*..
gi 654962578 238 LYRNPVH 244
Cdd:COG1134 236 AYEALLA 242
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-230 |
1.39e-23 |
|
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: 100.28 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLY--DATSGEVLFNGENVHGRKSRSEL 82
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 KKfnrKMQMIFQDpyASLNPRMTVADIIAEG--IDIHGLAKTRKERMAKVHELLETVGLNKEHANRYPHEFSGGQRQRIG 160
Cdd:TIGR02633 77 RA---GIVIIHQE--LTLVPELSVAENIFLGneITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 161 IARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQReRGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-230 |
3.13e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.08 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 22 IKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKKF---------------- 85
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVleklviqktrfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 ----NRKMQMIFQDPYASLNPRMTVADIIAEGIDIhGLAKTRKERMAKvhELLETVGLNKEHANRYPHEFSGGQRQRIGI 161
Cdd:PRK13651 100 ikeiRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSM-GVSKEEAKKRAA--KYIELVGLDESYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654962578 162 ARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-231 |
7.97e-23 |
|
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: 98.35 E-value: 7.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 26 DGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSelkkFNRKMQMIFQDpyaslnprmT 105
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS----LRAAIGIVPQD---------T 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 106 VA--DIIAEGIdIHG-LAKTRKE-----RMAKVHEL-------LETV----GLnkehanryphEFSGGQRQRIGIARALA 166
Cdd:COG5265 442 VLfnDTIAYNI-AYGrPDASEEEveaaaRAAQIHDFieslpdgYDTRvgerGL----------KLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654962578 167 VEPDFIIADEPISALDV----SIQAQvvnlMKKLQRERglTYLFIAHDLSMVKYiSDRIGVMYRGKIVE 231
Cdd:COG5265 511 KNPPILIFDEATSALDSrterAIQAA----LREVARGR--TTLVIAHRLSTIVD-ADEILVLEAGRIVE 572
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
27-229 |
9.62e-23 |
|
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: 94.07 E-value: 9.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 27 GLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMIFQDPyaSLNPRmTV 106
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI----SQYEHKYLHSKVSLVGQEP--VLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 107 ADIIAegidiHGLAKTRKERMAKVHELLETVGLNKEHANRYPHE-------FSGGQRQRIGIARALAVEPDFIIADEPIS 179
Cdd:cd03248 105 QDNIA-----YGLQSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 654962578 180 ALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKYiSDRIGVMYRGKI 229
Cdd:cd03248 180 ALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-241 |
2.74e-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: 91.82 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLkqHFFTSKGTIkaVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRL--YDATSGEVLFNGENVhgrKSRSELK 83
Cdd:cd03217 1 LEIKDL--HVSVGGKEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDI---TDLPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 84 KFNRKMQMIFQDPyaslnprmtvadiiaegIDIHGLaktrkermaKVHELLETVGLNkehanrypheFSGGQRQRIGIAR 163
Cdd:cd03217 74 RARLGIFLAFQYP-----------------PEIPGV---------KNADFLRYVNEG----------FSGGEKKRNEILQ 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 164 ALAVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYI-SDRIGVMYRGKIVELAPS---DELY 239
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKelaLEIE 196
|
..
gi 654962578 240 RN 241
Cdd:cd03217 197 KK 198
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
25-238 |
2.93e-22 |
|
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: 96.65 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgrksRSELKKFNRKMQMIFQDpyASLNPRm 104
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK----QWDRETFGKHIGYLPQD--VELFPG- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 105 TVADIIAEGIDIhglAKTRK----ERMAKVHELLEtvglnkehanRYPHEF-----------SGGQRQRIGIARALAVEP 169
Cdd:TIGR01842 407 TVAENIARFGEN---ADPEKiieaAKLAGVHELIL----------RLPDGYdtvigpggatlSGGQRQRIALARALYGDP 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654962578 170 DFIIADEPISALDVSIQAQVVNLMKKLQReRGLTYLFIAHDLSMVKYIsDRIGVMYRGKIVELAPSDEL 238
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEQALANAIKALKA-RGITVVVITHRPSLLGCV-DKILVLQDGRIARFGERDEV 540
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
25-229 |
3.53e-22 |
|
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: 91.12 E-value: 3.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgRKSRSELKKF-NRKMQ--MIFQDpyasln 101
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS-QWDPNELGDHvGYLPQddELFSG------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 102 prmTVADIIaegidihglaktrkermakvhelletvglnkehanrypheFSGGQRQRIGIARALAVEPDFIIADEPISAL 181
Cdd:cd03246 91 ---SIAENI----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 654962578 182 DVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKyISDRIGVMYRGKI 229
Cdd:cd03246 128 DVEGERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-238 |
6.09e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 93.61 E-value: 6.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 8 IKGLKQHFFTSKG-TIKAVDGLTFDIFRGETLGLVGESGCGKSTT-----GrtIIRlydATSGEVLFNGENVHGRKsrse 81
Cdd:COG4586 20 LKGALKGLFRREYrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTikmltG--ILV---PTSGEVRVLGYVPFKRR---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 82 lKKFNRKMQMIF----QdpyasLNPRMTVAD---IIAEgidIHGLAKTR-KERMAKVHELLEtVG--LNKehanryP-HE 150
Cdd:COG4586 91 -KEFARRIGVVFgqrsQ-----LWWDLPAIDsfrLLKA---IYRIPDAEyKKRLDELVELLD-LGelLDT------PvRQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 151 FSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
....*...
gi 654962578 231 ELAPSDEL 238
Cdd:COG4586 235 YDGSLEEL 242
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-230 |
1.18e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.97 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 24 AVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrKSRSELKKFNRKMQMIFQDPYASLNPR 103
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDT---GDFSKLQGIRKLVGIVFQNPETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 104 mTVADIIAEGIDIHGLAKTrkERMAKVHELLETVGLNKeHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDV 183
Cdd:PRK13644 94 -TVEEDLAFGPENLCLPPI--EIRKRVDRALAEIGLEK-YRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 654962578 184 SIQAQVVNLMKKLQrERGLTYLFIAHDLSMVkYISDRIGVMYRGKIV 230
Cdd:PRK13644 170 DSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKIV 214
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
27-239 |
1.70e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.61 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 27 GLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgrKSRSELKKFNRKMQMIFQDPyaslNPRMTV 106
Cdd:PRK13638 19 GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD--YSKRGLLALRQQVATVFQDP----EQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 107 ADIIAE-GIDIHGLAKTRKERMAKVHELLETVglNKEHANRYPHE-FSGGQRQRIGIARALAVEPDFIIADEPISALDVS 184
Cdd:PRK13638 93 TDIDSDiAFSLRNLGVPEAEITRRVDEALTLV--DAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 185 IQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELY 239
Cdd:PRK13638 171 GRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-238 |
2.00e-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: 94.42 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 23 KAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgRKSRSELKKFnrkMQMIFQDPYaslnp 102
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK-DIDRHTLRQF---INYLPQEPY----- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 103 rmTVADIIAEGIDIHGLAKTRKERMAKVHELLETvglnKEHANRYPHEF-----------SGGQRQRIGIARALAVEPDF 171
Cdd:TIGR01193 559 --IFSGSILENLLLGAKENVSQDEIWAACEIAEI----KDDIENMPLGYqtelseegssiSGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654962578 172 IIADEPISALDVSIQAQVVNLMKKLQRErglTYLFIAHDLSMVKYiSDRIGVMYRGKIVELAPSDEL 238
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
26-238 |
8.02e-21 |
|
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: 92.71 E-value: 8.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 26 DGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMIFQdpyaslNPRMT 105
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL----AGLDVQAVRRQLGVVLQ------NGRLM 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 106 VADI---IA-----------EGIDIHGLAKTRKERMAKVHELLETVGLNkehanrypheFSGGQRQRIGIARALAVEPDF 171
Cdd:TIGR03797 540 SGSIfenIAggapltldeawEAARMAGLAEDIRAMPMGMHTVISEGGGT----------LSGGQRQRLLIARALVRKPRI 609
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654962578 172 IIADEPISALDVSIQAQVVNLMKKLQrergLTYLFIAHDLSMVKYiSDRIGVMYRGKIVELAPSDEL 238
Cdd:TIGR03797 610 LLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDEL 671
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
23-233 |
1.31e-20 |
|
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: 87.85 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 23 KAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMIFQDPyaslnp 102
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI----STIPLEDLRSSLTIIPQDP------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 103 rMTVADIIAEGIDIHGLAKTRKERMA-KVHElletVGLNkehanrypheFSGGQRQRIGIARALAVEPDFIIADEPISAL 181
Cdd:cd03369 92 -TLFSGTIRSNLDPFDEYSDEEIYGAlRVSE----GGLN----------LSQGQRQLLCLARALLKRPRVLVLDEATASI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 182 DVSIQAqvvnLMKKLQRE--RGLTYLFIAHDL-SMVKYisDRIGVMYRGKIVELA 233
Cdd:cd03369 157 DYATDA----LIQKTIREefTNSTILTIAHRLrTIIDY--DKILVMDAGEVKEYD 205
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
25-238 |
1.75e-20 |
|
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: 88.22 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVL------FNGENVHgrksrsELKK----FNRKMQMIFQ 94
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVW------ELRKriglVSPALQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 95 dpyaslnPRMTVADIIAEGI-DIHGLAKTRKERM-AKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFI 172
Cdd:COG1119 93 -------RDETVLDVVLSGFfDSIGLYREPTDEQrERARELLELLGL-AHLADRPFGTLSQGEQRRVLIARALVKDPELL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654962578 173 IADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLS-MVKYISDRIgVMYRGKIVELAPSDEL 238
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITHVL-LLKDGRVVAAGPKEEV 230
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-238 |
2.84e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.65 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLkqHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgRKSRSELKk 84
Cdd:PRK11160 338 SLTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA-DYSEAALR- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 fnRKMQMIFQDPY---ASLNPRMTVADiiAEGIDihglaktrkermAKVHELLETVGLNKEHANRYP---------HEFS 152
Cdd:PRK11160 414 --QAISVVSQRVHlfsATLRDNLLLAA--PNASD------------EALIEVLQQVGLEKLLEDDKGlnawlgeggRQLS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 153 GGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERglTYLFIAHDL----SMvkyisDRIGVMYRGK 228
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLtgleQF-----DRICVMDNGQ 550
|
250
....*....|
gi 654962578 229 IVELAPSDEL 238
Cdd:PRK11160 551 IIEQGTHQEL 560
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-211 |
3.73e-20 |
|
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: 90.50 E-value: 3.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftsKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgRKSRSELKkf 85
Cdd:TIGR02868 335 LELRDLSAGY---PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS-SLDQDEVR-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 nRKMQMIFQDPY---ASL--NPRMTVADIIAEGIdihglakTRKERMAKVHELLETV--GLNK---EHANRypheFSGGQ 155
Cdd:TIGR02868 409 -RRVSVCAQDAHlfdTTVreNLRLARPDATDEEL-------WAALERVGLADWLRALpdGLDTvlgEGGAR----LSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 654962578 156 RQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMkkLQRERGLTYLFIAHDL 211
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-236 |
5.95e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.94 E-value: 5.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRS 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 elkkfnrKMQMIFQDPYASLNPRMTVadiiAEGIDIHG--LAKTRKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQR 158
Cdd:PRK13537 79 -------RQRVGVVPQFDNLDPDFTV----RENLLVFGryFGLSAAAARALVPPLLEFAKL-ENKADAKVGELSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 159 IGIARALAVEPDFIIADEPISALDvsiqAQVVNLMKKLQRE---RGLTYLFIAHDLSMVKYISDRIGVMYRG-KIVELAP 234
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLD----PQARHLMWERLRSllaRGKTILLTTHFMEEAERLCDRLCVIEEGrKIAEGAP 222
|
..
gi 654962578 235 SD 236
Cdd:PRK13537 223 HA 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-216 |
1.70e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 88.93 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 4 KLLEIKGLKQHFFTSKgTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNgeNVHGRKSRSeLK 83
Cdd:PTZ00265 381 KKIQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDIN-LK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 84 KFNRKMQMIFQDP-----------------------------------YASLNPRMTVA-------DIIAEGIDIHGLAK 121
Cdd:PTZ00265 457 WWRSKIGVVSQDPllfsnsiknnikyslyslkdlealsnyynedgndsQENKNKRNSCRakcagdlNDMSNTTDSNELIE 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 122 TRKE-------------RMAKVHELLET--------VGLNKEhanryphEFSGGQRQRIGIARALAVEPDFIIADEPISA 180
Cdd:PTZ00265 537 MRKNyqtikdsevvdvsKKVLIHDFVSAlpdkyetlVGSNAS-------KLSGGQKQRISIARAIIRNPKILILDEATSS 609
|
250 260 270
....*....|....*....|....*....|....*.
gi 654962578 181 LDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKY 216
Cdd:PTZ00265 610 LDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 645
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-230 |
3.12e-18 |
|
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: 81.55 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 21 TIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTI---IRLYDATSGEVLFNGEnvhgrksrsELKKfnRKMQMIF---- 93
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQ---------PRKP--DQFQKCVayvr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 94 QDPYasLNPRMTVADIIAEGIDIHGLAKTRKERMAKVhelLETVGLNKEHANRYPHEF----SGGQRQRIGIARALAVEP 169
Cdd:cd03234 88 QDDI--LLPGLTVRETLTYTAILRLPRKSSDAIRKKR---VEDVLLRDLALTRIGGNLvkgiSGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654962578 170 DFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-229 |
4.66e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.95 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 28 LTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKKF------NRKMQMIFQDPYASLN 101
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvylpeDRQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 102 prmtvadIIAEGIDIHGL-AKTRKERmAKVHELLETVGLNKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISA 180
Cdd:PRK15439 362 -------VCALTHNRRGFwIKPAREN-AVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 654962578 181 LDVSIQAQVVNLMKKLQrERGLTYLFIAHDLSMVKYISDRIGVMYRGKI 229
Cdd:PRK15439 434 VDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-242 |
5.63e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 83.99 E-value: 5.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 24 AVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgrksRSELKKFNRKMQMIFQDPYaslnpr 103
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT----KLQLDSWRSRLAVVSQTPF------ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 104 mTVADIIAEGIDIHGLAKTRKE-----RMAKVHE--LLETVGLNKEHANRYPHeFSGGQRQRIGIARALAVEPDFIIADE 176
Cdd:PRK10789 400 -LFSDTVANNIALGRPDATQQEiehvaRLASVHDdiLRLPQGYDTEVGERGVM-LSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654962578 177 PISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKYiSDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:PRK10789 478 ALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
25-209 |
7.72e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.70 E-value: 7.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNgenvhgrksrselkkfnRKMQMIF--QDPY---AS 99
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP-----------------AGARVLFlpQRPYlplGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 100 L-------NPRMTVADiiaegidihglaktrkermAKVHELLETVGLnkEH-------ANRYPHEFSGGQRQRIGIARAL 165
Cdd:COG4178 442 LreallypATAEAFSD-------------------AELREALEAVGL--GHlaerldeEADWDQVLSLGEQQRLAFARLL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQvvnLMKKLQRE-RGLTYLFIAH 209
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAA---LYQLLREElPGTTVISVGH 542
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-230 |
9.02e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 79.52 E-value: 9.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 16 FTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKST-----TGRTIirlYDATSGEVLFNGENVHgrksrseLKKFNRKMQ 90
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTllnalAGRRT---GLGVSGEVLINGRPLD-------KRSFRKIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 91 MIFQDPYasLNPRMTVAdiiaEGIDIHglAKTRkermakvhelletvGLnkehanryphefSGGQRQRIGIARALAVEPD 170
Cdd:cd03213 86 YVPQDDI--LHPTLTVR----ETLMFA--AKLR--------------GL------------SGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654962578 171 FIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYIS-DRIGVMYRGKIV 230
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPSSEIFELfDKLLLLSQGRVI 191
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
6-246 |
9.23e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 82.23 E-value: 9.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEI---KGLKQHFFTSKGTIKAVdGLTfDIFrgetlglvGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSEL 82
Cdd:PRK11144 2 LELnfkQQLGDLCLTVNLTLPAQ-GIT-AIF--------GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 KKFNRKMQMIFQDpyASLNPRMTVadiiaEGIDIHGLAKTRKERMAKVHELLetvGLnkEHA-NRYPHEFSGGQRQRIGI 161
Cdd:PRK11144 72 PPEKRRIGYVFQD--ARLFPHYKV-----RGNLRYGMAKSMVAQFDKIVALL---GI--EPLlDRYPGSLSGGEKQRVAI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 162 ARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRN 241
Cdd:PRK11144 140 GRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWAS 219
|
....*.
gi 654962578 242 PV-HPY 246
Cdd:PRK11144 220 SAmRPW 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
27-193 |
1.13e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 27 GLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSelkkfnrkmQMIFQDPYASLNPRMTV 106
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE---------ACHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 107 ADIIAEGIDIHGlaktrkERMAKVHELLETVGLNkEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQ 186
Cdd:PRK13539 91 AENLEFWAAFLG------GEELDIAAALEAVGLA-PLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
....*..
gi 654962578 187 AQVVNLM 193
Cdd:PRK13539 164 ALFAELI 170
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-231 |
1.42e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.53 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATS--GEVLFNGENVHGRKSR-SE 81
Cdd:NF040905 1 ILEMRGITKTF----PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRdSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 82 lkkfNRKMQMIFQDpyASLNPRMTVADIIAEG--------IDihglaktRKERMAKVHELLETVGLnKEHANRYPHEFSG 153
Cdd:NF040905 77 ----ALGIVIIHQE--LALIPYLSIAENIFLGnerakrgvID-------WNETNRRARELLAKVGL-DESPDTLVTDIGV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 154 GQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVE 231
Cdd:NF040905 143 GKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-214 |
1.56e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.81 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 24 AVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVlfngENVHGRK-----SRSELkkfnrkmqmifqdpya 98
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV----RRAGGARvayvpQRSEV---------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 99 slnPR---MTVADIIAEGIDIH-GLAK--TRKERMAkVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFI 172
Cdd:NF040873 67 ---PDslpLTVRDLVAMGRWARrGLWRrlTRDDRAA-VDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 654962578 173 IADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMV 214
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELV 182
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-193 |
1.67e-17 |
|
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: 78.94 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 18 SKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVH-GRKSRSElkkfnrkmQMIFQDP 96
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAeQRDEPHE--------NILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 97 YASLNPRMTVADIIAEGIDIHGLAktrkERMakVHELLETVGLNkEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADE 176
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGA----QRT--IEDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170
....*....|....*..
gi 654962578 177 PISALDVSIQAQVVNLM 193
Cdd:TIGR01189 154 PTTALDKAGVALLAGLL 170
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
29-236 |
1.73e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.31 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 29 TFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVlfngeNVHGRKSRSELKKfnRKMQMIFQDPYASLNPRMTVAD 108
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQK--NLVAYVPQSEEVDWSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 109 IIAEGIDIH-GLAKTRKER-MAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQ 186
Cdd:PRK15056 100 VVMMGRYGHmGWLRRAKKRdRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 654962578 187 AQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIgVMYRGKIVELAPSD 236
Cdd:PRK15056 179 ARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTE 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-231 |
3.50e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 22 IKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELkkfNRKMQMIFQDpyASLN 101
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAAL---AAGVAIIYQE--LHLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 102 PRMTVADIIAEG--------IDihglaktRKERMAKVHELLETVGLNKEHANRYPHeFSGGQRQRIGIARALAVEPDFII 173
Cdd:PRK11288 92 PEMTVAENLYLGqlphkggiVN-------RRLLNYEAREQLEHLGVDIDPDTPLKY-LSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 174 ADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVE 231
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-236 |
5.86e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 5.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLKQHFftsKGtIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVH--GRKSRSEl 82
Cdd:PRK10762 4 LLQLKGIDKAF---PG-VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 kkfnRKMQMIFQDpyasLN--PRMTVADIIAEGIDI-HGLAKTRKERM-AKVHELLETVGLnKEHANRYPHEFSGGQRQR 158
Cdd:PRK10762 79 ----AGIGIIHQE----LNliPQLTIAENIFLGREFvNRFGRIDWKKMyAEADKLLARLNL-RFSSDKLVGELSIGEQQM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 159 IGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRE-RGLTYlfIAHDLSMVKYISDRIGVMYRGK-IVELAPSD 236
Cdd:PRK10762 150 VEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQgRGIVY--ISHRLKEIFEICDDVTVFRDGQfIAEREVAD 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-238 |
6.25e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.00 E-value: 6.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTI--IRLYDATSGEVLFN-------------- 69
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 70 --GEN--VHGRK-----------SRSELKKFNRKMQMIFQDPYAsLNPRMTVADIIAEGIdiHGLAKTRKERMAKVHELL 134
Cdd:TIGR03269 77 kvGEPcpVCGGTlepeevdfwnlSDKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEAL--EEIGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 135 ETVGLnkEHanRYPH---EFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDL 211
Cdd:TIGR03269 154 EMVQL--SH--RITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260
....*....|....*....|....*..
gi 654962578 212 SMVKYISDRIGVMYRGKIVELAPSDEL 238
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-230 |
1.16e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.83 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGEnvhgrksrs 80
Cdd:PRK09700 1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 ELKKFNRKMQ------MIFQDpyASLNPRMTVADII---------AEGIDIHGLAKTRKermaKVHELLETVGLnKEHAN 145
Cdd:PRK09700 68 NYNKLDHKLAaqlgigIIYQE--LSVIDELTVLENLyigrhltkkVCGVNIIDWREMRV----RAAMMLLRVGL-KVDLD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 146 RYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMY 225
Cdd:PRK09700 141 EKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMK 219
|
....*
gi 654962578 226 RGKIV 230
Cdd:PRK09700 220 DGSSV 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-209 |
1.16e-16 |
|
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: 75.65 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 15 FFTSKGTIKaVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVlfngenvhgrksrselkKFNRKMQMIF- 93
Cdd:cd03223 8 LATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------------GMPEGEDLLFl 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 94 -QDPYAslnPRMTVADIIAegidihglaktrkermakvhelletvglnkehanrYP--HEFSGGQRQRIGIARALAVEPD 170
Cdd:cd03223 70 pQRPYL---PLGTLREQLI-----------------------------------YPwdDVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*....
gi 654962578 171 FIIADEPISALDVSIQAQVVNLMKklqrERGLTYLFIAH 209
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-231 |
1.47e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 77.37 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKqhffTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTII--RLYDATSGEVLFNGENVHGR-- 76
Cdd:CHL00131 3 KNKPILEIKNLH----ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLep 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 77 KSRSELKKFnrkmqMIFQDPYASlnPRMTVADIIAegidihgLAKTRKERMAKVHEL------------LETVGLNKEHA 144
Cdd:CHL00131 79 EERAHLGIF-----LAFQYPIEI--PGVSNADFLR-------LAYNSKRKFQGLPELdplefleiinekLKLVGMDPSFL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 145 NRYPHE-FSGGQRQRIGIARALAVEPDFIIADEPISALDVS---IQAQVVNLMKKLQRerglTYLFIAHDLSMVKYIS-D 219
Cdd:CHL00131 145 SRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSEN----SIILITHYQRLLDYIKpD 220
|
250
....*....|..
gi 654962578 220 RIGVMYRGKIVE 231
Cdd:CHL00131 221 YVHVMQNGKIIK 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-236 |
2.44e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 78.33 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRkSRSELKKFNRKMQmifqdpYASLNPRM 104
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR-ARLARARIGVVPQ------FDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 105 TVadiiAEGIDIHGL---AKTRkERMAKVHELLETVGLNKEhANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISAL 181
Cdd:PRK13536 130 TV----RENLLVFGRyfgMSTR-EIEAVIPSLLEFARLESK-ADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 654962578 182 DVSIQAQVVNLMKKLQrERGLTYLFIAHDLSMVKYISDRIGVMYRG-KIVELAPSD 236
Cdd:PRK13536 204 DPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGRPHA 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
26-210 |
2.54e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.95 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 26 DGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGenvhgrksrselkkfNRKMQMIFQDPYasLNPRMT 105
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---------------GLRIGYLPQEPP--LDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 106 VADIIAEG----------------------IDIHGLAK--TRKERM------AKVHELLETVGLNKEHANRYPHEFSGGQ 155
Cdd:COG0488 78 VLDTVLDGdaelraleaeleeleaklaepdEDLERLAElqEEFEALggweaeARAEEILSGLGFPEEDLDRPVSELSGGW 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 654962578 156 RQRIGIARALAVEPDFIIADEPISALDV-SIQAqvvnLMKKLQRERGlTYLFIAHD 210
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDLeSIEW----LEEFLKNYPG-TVLVVSHD 208
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
23-241 |
5.93e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.20 E-value: 5.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 23 KAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLY--DATSG---EVLFNGENVHGRKSRsELKKFNRKMQMIFQDpy 97
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGshiELLGRTVQREGRLAR-DIRKSRANTGYIFQQ-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 98 ASLNPRMTVAdiiaEGIDIHGLAKT----------RKERMAKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAV 167
Cdd:PRK09984 95 FNLVNRLSVL----ENVLIGALGSTpfwrtcfswfTREQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 168 EPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPS--------DELY 239
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSqqfdnerfDHLY 249
|
..
gi 654962578 240 RN 241
Cdd:PRK09984 250 RS 251
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
23-241 |
9.77e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.93 E-value: 9.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 23 KAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrSELKKFNRKMQMIFQDPY-ASLN 101
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI------SLLPLHARARRGIGYLPQeASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 102 PRMTVADIIAEGIDIHGlAKTRKERMAKVHELLETvgLNKEH-ANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISA 180
Cdd:PRK10895 91 RRLSVYDNLMAVLQIRD-DLSAEQREDRANELMEE--FHIEHlRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654962578 181 LDvsiQAQVVNLMKKLQ--RERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRN 241
Cdd:PRK10895 168 VD---PISVIDIKRIIEhlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-230 |
1.19e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.92 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 1 MTDKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRS 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI----TDW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 81 ELKKFNRKMQMIFQDPYASLNpRMTVADIIAEGidihGLAKTRK---ERMAKVHELLETVglnKEHANRYPHEFSGGQRQ 157
Cdd:PRK11614 73 QTAKIMREAVAIVPEGRRVFS-RMTVEENLAMG----GFFAERDqfqERIKWVYELFPRL---HERRIQRAGTMSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654962578 158 RIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:PRK11614 145 MLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-221 |
1.73e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.98 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGLkqHFFTskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksrSELK- 83
Cdd:PRK10247 7 LLQLQNV--GYLA--GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI------STLKp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 84 -KFNRKMQMIFQDPyaslnprMTVADIIAEGIDIHGLAKTRKERMAKVHELLETVGLNKEHANRYPHEFSGGQRQRIGIA 162
Cdd:PRK10247 77 eIYRQQVSYCAQTP-------TLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 654962578 163 RALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRI 221
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-223 |
3.64e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 75.59 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 31 DIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNgenvhgrksrselKKFNRKMQmifqdpYASLNPRMTVADIi 110
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-------------LKISYKPQ------YISPDYDGTVEEF- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 111 aegidihgLAKTRKERMAKV---HELLETVGLNKEHaNRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQA 187
Cdd:COG1245 422 --------LRSANTDDFGSSyykTEIIKPLGLEKLL-DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 492
|
170 180 190
....*....|....*....|....*....|....*.
gi 654962578 188 QVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGV 223
Cdd:COG1245 493 AVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-223 |
7.42e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.84 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 32 IFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNgenvhgrksrselKKFNRKMQmifqdpYASLNPRMTVADIia 111
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------------LKISYKPQ------YIKPDYDGTVEDL-- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 112 egidihgLAKTRKERMAKV--HELLETVGLNKEHaNRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQV 189
Cdd:PRK13409 421 -------LRSITDDLGSSYykSEIIKPLQLERLL-DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 492
|
170 180 190
....*....|....*....|....*....|....
gi 654962578 190 VNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGV 223
Cdd:PRK13409 493 AKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-242 |
7.43e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.88 E-value: 7.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 21 TIKAVDG------LTFDIFRGETLGLVGESGCGKSTtgrtiirLYDATSG------EVLFNGENVhgrkSRSELKKFNRK 88
Cdd:PRK11174 356 EILSPDGktlagpLNFTLPAGQRIALVGPSGAGKTS-------LLNALLGflpyqgSLKINGIEL----RELDPESWRKH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 89 MQMIFQDP---YASLNPRMTVADIIAEGIDIHGLAKtrkerMAKVHELLE--TVGLN---KEHANRypheFSGGQRQRIG 160
Cdd:PRK11174 425 LSWVGQNPqlpHGTLRDNVLLGNPDASDEQLQQALE-----NAWVSEFLPllPQGLDtpiGDQAAG----LSVGQAQRLA 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 161 IARALAVEPDFIIADEPISALDVSIQAQVvnlMKKLQRE-RGLTYLFIAHDLSMVKYIsDRIGVMYRGKIVELAPSDELY 239
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLV---MQALNAAsRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELS 571
|
...
gi 654962578 240 RNP 242
Cdd:PRK11174 572 QAG 574
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-238 |
8.38e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.44 E-value: 8.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 23 KAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrKSRSELKKFNRKMQMIFQD------- 95
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI---SPRSPLDAVKKGMAYITESrrdngff 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 96 PYASLNPRMTVADIIAEG--IDIHGLAKTRKER--MAKVHELLEtvgLNKEHANRYPHEFSGGQRQRIGIARALAVEPDF 171
Cdd:PRK09700 354 PNFSIAQNMAISRSLKDGgyKGAMGLFHEVDEQrtAENQRELLA---LKCHSVNQNITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 172 IIADEPISALDVSIQAQVVNLMKKLQrERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVE-LAPSDEL 238
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRLTQiLTNRDDM 497
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-223 |
8.61e-15 |
|
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: 72.44 E-value: 8.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 31 DIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLfngenvhgrksrSELKKFNRKMQMIFQDPyaslnpRMTVADII 110
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIE------------IELDTVSYKPQYIKADY------EGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 111 AEGIDIHGLAKTRKErmakvhELLETVGLNKEHANRYPhEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVV 190
Cdd:cd03237 83 SSITKDFYTHPYFKT------EIAKPLQIEQILDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180 190
....*....|....*....|....*....|...
gi 654962578 191 NLMKKLQRERGLTYLFIAHDLSMVKYISDRIGV 223
Cdd:cd03237 156 KVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-231 |
1.10e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.95 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 3 DKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFnGENVHgrksrsel 82
Cdd:COG0488 313 KKVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 kkfnrkmqmI--F-QDpYASLNPRMTVADIIAEGidihglAKTRKERmaKVHELLETVGLNKEHANRYPHEFSGGQRQRI 159
Cdd:COG0488 380 ---------IgyFdQH-QEELDPDKTVLDELRDG------APGGTEQ--EVRGYLGRFLFSGDDAFKPVGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654962578 160 GIARALAVEPDFIIADEPISALDV-SIQAqvvnLMKKLQRERGlTYLFIAHDLSMVKYISDRIGVMYRGKIVE 231
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIeTLEA----LEEALDDFPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
27-255 |
1.62e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.24 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 27 GLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMIFQDPYA-SLNPRMT 105
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV----AKFGLTDLRRVLSIIPQSPVLfSGTVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 106 VaDIIAEGIDIhGLAKTRKERMAKVHELLETVGLNKEhANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSI 185
Cdd:PLN03232 1330 I-DPFSEHNDA-DLWEALERAHIKDVIDRNPFGLDAE-VSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654962578 186 QAqvvnLMKKLQRE--RGLTYLFIAHDLSMVkYISDRIGVMYRGKIVELAPSDELYRNPVHPYTKALLSAIP 255
Cdd:PLN03232 1407 DS----LIQRTIREefKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGP 1473
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-229 |
2.67e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.24 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 7 EIKGLKQHF--FTskgtikAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSelkk 84
Cdd:NF033858 268 EARGLTMRFgdFT------AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIAT---- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 fnRK----MQMIFqdpyaSLNPRMTVadiiAEGIDIHglAK----TRKERMAKVHELLETVGLnKEHANRYPHEFSGGQR 156
Cdd:NF033858 338 --RRrvgyMSQAF-----SLYGELTV----RQNLELH--ARlfhlPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 157 QRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTylfIahdlsmvkYIS----------DRIGVMYR 226
Cdd:NF033858 404 QRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT---I--------FISthfmneaercDRISLMHA 472
|
...
gi 654962578 227 GKI 229
Cdd:NF033858 473 GRV 475
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-229 |
3.15e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.55 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 3 DKLLEIKGLKQHFFTSKgTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYD-ATSGEVLFNGENVhgrKSRSE 81
Cdd:TIGR02633 255 DVILEARNLTCWDVINP-HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPV---DIRNP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 82 LKKFNRKMQMIFQD-PYASLNPRMTVADIIAEGIDIHGLAKTRKERMAKVHELLETVG---LNKEHANRYPHEFSGGQRQ 157
Cdd:TIGR02633 331 AQAIRAGIAMVPEDrKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQrlkVKTASPFLPIGRLSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654962578 158 RIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKI 229
Cdd:TIGR02633 411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-242 |
3.73e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.89 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 27 GLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENV--HGrksrseLKKFNRKMQMIFQDPY------- 97
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIgaYG------LRELRRQFSMIPQDPVlfdgtvr 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 98 ASLNP--RMTVADIIAeGIDIHGLaktrKERMAKVHELLETVGLnkEHANRYphefSGGQRQRIGIARALAVE-PDFIIA 174
Cdd:PTZ00243 1402 QNVDPflEASSAEVWA-ALELVGL----RERVASESEGIDSRVL--EGGSNY----SVGQRQLMCMARALLKKgSGFILM 1470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654962578 175 DEPIS----ALDVSIQAQVVNLMKklqrerGLTYLFIAHDLSMV-KYisDRIGVMYRGKIVELAPSDELYRNP 242
Cdd:PTZ00243 1471 DEATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVaQY--DKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-241 |
4.47e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.85 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 27 GLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMIFQDPyaslnprmtv 106
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI----SKFGLMDLRKVLGIIPQAP---------- 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 107 adIIAEGIDIHGLAKTRKERMAKVHELLE-----------TVGLNKEHANRyPHEFSGGQRQRIGIARALAVEPDFIIAD 175
Cdd:PLN03130 1323 --VLFSGTVRFNLDPFNEHNDADLWESLErahlkdvirrnSLGLDAEVSEA-GENFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654962578 176 EPISALDVSIQAqvvnLMKKLQRE--RGLTYLFIAHDLSMVkyI-SDRIGVMYRGKIVELAPSDELYRN 241
Cdd:PLN03130 1400 EATAAVDVRTDA----LIQKTIREefKSCTMLIIAHRLNTI--IdCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
228-295 |
6.31e-14 |
|
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: 66.23 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 228 KIVELAPSDELYRNPVHPYTKALLSAIPLPdpdseKTRQRKIYD-----PSIHD------YNG-----------EEPELR 285
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTI-----KKRDRKLISipgevPSLINlpsgcrFYPrcpyaqdecrkEPPALV 75
|
90
....*....|
gi 654962578 286 EVSPGHYVSC 295
Cdd:TIGR01727 76 EIAEGHRVAC 85
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
26-219 |
1.70e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.45 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 26 DGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDatsgevlfngenvhgrksrselkkfNRKMQMIFQDPYASLNPRMT 105
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK-------------------------GTPVAGCVDVPDNQFGREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 106 VADIIAEGIDIHglaktrkermAKVhELLETVGLNKEHA-NRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVS 184
Cdd:COG2401 102 LIDAIGRKGDFK----------DAV-ELLNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 654962578 185 iQAQVVNL-MKKLQRERGLTYLFIAHDLSMVKYISD 219
Cdd:COG2401 171 -TAKRVARnLQKLARRAGITLVVATHHYDVIDDLQP 205
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-238 |
2.23e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 69.76 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTtGRTIIRLYDATSGEVLFNGENVHGrkSRSELKKF 85
Cdd:NF000106 14 VEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRF*TWCA--NRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKMQMIFQDPYASLNPRMTVAdIIAEGIDIhglakTRKERMAKVHELLETVGLNkEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:NF000106 87 IG*HRPVR*GRRESFSGRENLY-MIGR*LDL-----SRKDARARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDEL 238
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-229 |
5.69e-13 |
|
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: 69.66 E-value: 5.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 24 AVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrksRSELKKFNRKMQMIFQdpYASLNPR 103
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-----ETNLDAVRQSLGMCPQ--HNILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 104 MTVADIIAEGIDIHGlaKTRKERMAKVHELLETVGLNKEHaNRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDV 183
Cdd:TIGR01257 1018 LTVAEHILFYAQLKG--RSWEEAQLEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 654962578 184 SIQAQVVNLMkkLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKI 229
Cdd:TIGR01257 1095 YSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-223 |
1.10e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 16 FTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKKFNRKMQMIFQD 95
Cdd:PTZ00265 1175 YISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQGDEEQNVGMKN 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 96 --PYASLNPRMTVAD---------IIAEGIDI--HGLAKTR-------KERMAKVHELLETVGLNKEHANR--------- 146
Cdd:PTZ00265 1255 vnEFSLTKEGGSGEDstvfknsgkILLDGVDIcdYNLKDLRnlfsivsQEPMLFNMSIYENIKFGKEDATRedvkrackf 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 147 --------------------YPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVS----IQAQVVNLMKKLQRergl 202
Cdd:PTZ00265 1335 aaidefieslpnkydtnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADK---- 1410
|
250 260
....*....|....*....|.
gi 654962578 203 TYLFIAHDLSMVKYiSDRIGV 223
Cdd:PTZ00265 1411 TIITIAHRIASIKR-SDKIVV 1430
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
35-238 |
2.06e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.38 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 35 GETLGLVGESGCGKsTTGRTIIRLYDAT----SGEVLFNGENVhgrksrsELKKFNRKMQMIFQDpyaSLN-PRMTVAdi 109
Cdd:TIGR00955 51 GELLAVMGSSGAGK-TTLMNALAFRSPKgvkgSGSVLLNGMPI-------DAKEMRAISAYVQQD---DLFiPTLTVR-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 110 iaEGIDIHGLAK-----TRKERMAKVHELLETVGLNKEHANRYPHE-----FSGGQRQRIGIARALAVEPDFIIADEPIS 179
Cdd:TIGR00955 118 --EHLMFQAHLRmprrvTKKEKRERVDEVLQALGLRKCANTRIGVPgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 180 ALDVSIQAQVVNLMKKLQrERGLTYLFIAHDLSMVKY-ISDRIGVMYRGKIVELAPSDEL 238
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLA-QKGKTIICTIHQPSSELFeLFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-221 |
2.78e-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: 64.44 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 27 GLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHgrKSRSELKKfnrkmQMIFQDPYASLNPRMTV 106
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD--FQRDSIAR-----GLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 107 ADIIAEGIDIHGlaktrkerMAKVHELLETVGLNK-EHanRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSI 185
Cdd:cd03231 91 LENLRFWHADHS--------DEQVEEALARVGLNGfED--RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 654962578 186 QAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRI 221
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-225 |
3.77e-12 |
|
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: 65.08 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 29 TFDIFR------GETLGLVGESGCGKSTTGRTIirlydatSGEVLFNGENVHGRKS---------RSELKKF-----NRK 88
Cdd:cd03236 14 SFKLHRlpvpreGQVLGLVGPNGIGKSTALKIL-------AGKLKPNLGKFDDPPDwdeildefrGSELQNYftkllEGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 89 MQMIFQDPYASLNPRM---TVADIIaegidihglakTRKERMAKVHELLETVGLNKEhANRYPHEFSGGQRQRIGIARAL 165
Cdd:cd03236 87 VKVIVKPQYVDLIPKAvkgKVGELL-----------KKKDERGKLDELVDQLELRHV-LDRNIDQLSGGELQRVAIAAAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 166 AVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMY 225
Cdd:cd03236 155 ARDADFYFFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-229 |
3.90e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELK------KFNRK-----MQMif 93
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAngivyiSEDRKrdglvLGM-- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 94 qdpyaSLNPRMTVADIiAEGIDIHGLAKTRKERMAkVHELLETVGLNKEHANRYPHEFSGGQRQRIGIARALAVEPDFII 173
Cdd:PRK10762 346 -----SVKENMSLTAL-RYFSRAGGSLKHADEQQA-VSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 654962578 174 ADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKI 229
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-238 |
4.80e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.23 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 5 LLEIKGL-KQhfFTSKGTIKAVDgltFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRksrSELK 83
Cdd:PRK15439 11 LLCARSIsKQ--YSGVEVLKGID---FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL---TPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 84 KFNRKMQMIFQDPYasLNPRMTVADIIAegidiHGLAKTRkERMAKVHELLETVGLnkeHANryPHEFSG----GQRQRI 159
Cdd:PRK15439 83 AHQLGIYLVPQEPL--LFPNLSVKENIL-----FGLPKRQ-ASMQKMKQLLAALGC---QLD--LDSSAGslevADRQIV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 160 GIARALAVEPDFIIADEPISALdvsIQAQVVNLMKKLQ--RERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDE 237
Cdd:PRK15439 150 EILRGLMRDSRILILDEPTASL---TPAETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
.
gi 654962578 238 L 238
Cdd:PRK15439 227 L 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-193 |
6.56e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.28 E-value: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 26 DGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgRKSRSElkkFNRkmQMIFQDPYASLNPRMT 105
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--RRQRDE---YHQ--DLLYLGHQPGIKTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 106 VADIIAEGIDIHGLAKTrkermAKVHELLETVGL-NKEHAnryP-HEFSGGQRQRIGIARALAVEPDFIIADEPISALDV 183
Cdd:PRK13538 91 ALENLRFYQRLHGPGDD-----EALWEALAQVGLaGFEDV---PvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
170
....*....|
gi 654962578 184 SIQAQVVNLM 193
Cdd:PRK13538 163 QGVARLEALL 172
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-225 |
1.01e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.19 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 34 RGETLGLVGESGCGKSTtgrtIIRLYdatSGEVLFNGENVHGRKSRSE-LKKFNRK-MQMIFQDPY-----ASLNPRM-- 104
Cdd:COG1245 98 KGKVTGILGPNGIGKST----ALKIL---SGELKPNLGDYDEEPSWDEvLKRFRGTeLQDYFKKLAngeikVAHKPQYvd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 105 --------TVADIIaEGIDihglaktrkERMaKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADE 176
Cdd:COG1245 171 lipkvfkgTVRELL-EKVD---------ERG-KLDELAEKLGL-ENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 654962578 177 PISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMY 225
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-225 |
1.31e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 34 RGETLGLVGESGCGKSTtgrtIIRLYdatSGEVLFNGENVHGRKSRSE-LKKFNRK-MQMIFQDPY-----ASLNPRM-- 104
Cdd:PRK13409 98 EGKVTGILGPNGIGKTT----AVKIL---SGELIPNLGDYEEEPSWDEvLKRFRGTeLQNYFKKLYngeikVVHKPQYvd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 105 --------TVADIIaEGIDIHGlaktrkermaKVHELLETVGLnKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADE 176
Cdd:PRK13409 171 lipkvfkgKVRELL-KKVDERG----------KLDEVVERLGL-ENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 654962578 177 PISALDVSIQAQVVNLMKKLQRERglTYLFIAHDLSMVKYISDRIGVMY 225
Cdd:PRK13409 239 PTSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIAY 285
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
40-231 |
1.45e-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: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 40 LVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhGRKSRSELKKfnrKMQMIFQDPYASLNprmTVADIIAEGIDIhgl 119
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL-SSLSHSVLRQ---GVAMVQQDPVVLAD---TFLANVTLGRDI--- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 120 aktrkeRMAKVHELLETVGLNkEHANRYP-----------HEFSGGQRQRIGIARALAVEPDFIIADEPISALDvSIQAQ 188
Cdd:PRK10790 442 ------SEEQVWQALETVQLA-ELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANID-SGTEQ 513
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 654962578 189 VVNLMKKLQRERgLTYLFIAHDLSMVkYISDRIGVMYRGKIVE 231
Cdd:PRK10790 514 AIQQALAAVREH-TTLVVIAHRLSTI-VEADTILVLHRGQAVE 554
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-233 |
1.60e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.55 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 3 DKLLEIKGLKQHFFTSkgtikavdGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSEL 82
Cdd:PRK11288 255 EVRLRLDGLKGPGLRE--------PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 KKF------NRKMQMIFqdPYASlnprmtvadiIAEGIDIHglaktrkermAKVHELLETVGLN----KEHANRY----- 147
Cdd:PRK11288 327 RAGimlcpeDRKAEGII--PVHS----------VADNINIS----------ARRHHLRAGCLINnrweAENADRFirsln 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 148 ---PH------EFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQrERGLTYLFIAHDLSMVKYIS 218
Cdd:PRK11288 385 iktPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVA 463
|
250
....*....|....*.
gi 654962578 219 DRIGVMYRGKIV-ELA 233
Cdd:PRK11288 464 DRIVVMREGRIAgELA 479
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
14-230 |
1.77e-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: 62.28 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 14 HFFTSKG--TIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTI---IRLYDATSGEVLFNGENVHGRKSRSelkkfnrK 88
Cdd:cd03233 10 SFTTGKGrsKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEKY-------P 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 89 MQMIFQDPYASLNPRMTVAdiiaegidihglaktrkermakvhELLETVGLNKehANRYPHEFSGGQRQRIGIARALAVE 168
Cdd:cd03233 83 GEIIYVSEEDVHFPTLTVR------------------------ETLDFALRCK--GNEFVRGISGGERKRVSIAEALVSR 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654962578 169 PDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKY-ISDRIGVMYRGKIV 230
Cdd:cd03233 137 ASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYdLFDKVLVLYEGRQI 199
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-243 |
3.13e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 28 LTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDAtSGEVLFNGENVhGRKSRSELKKfnRKMQMIFQDPYASLnprMTVA 107
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPL-EAWSAAELAR--HRAYLSQQQTPPFA---MPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 108 DIIAegidIHGLAKTRKERMAK-VHELLETVGL-NKEHanRYPHEFSGGQRQRIGIARA-LAVEPD------FIIADEPI 178
Cdd:PRK03695 88 QYLT----LHQPDKTRTEAVASaLNEVAEALGLdDKLG--RSVNQLSGGEWQRVRLAAVvLQVWPDinpagqLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 179 SALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDELYRNPV 243
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
27-228 |
3.93e-11 |
|
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: 61.33 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 27 GLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVlfngeNVHGRKSrselkkfnrkmqmifqdpYASLNP---R 103
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-----SVPGSIA------------------YVSQEPwiqN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 104 MTVADIIAEGidihglAKTRKERMAKV-------------HELLETV----GLNkehanrypheFSGGQRQRIGIARALA 166
Cdd:cd03250 80 GTIRENILFG------KPFDEERYEKVikacalepdleilPDGDLTEigekGIN----------LSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654962578 167 VEPDFIIADEPISALDVSIQAQVVN--LMKKLQRERglTYLFIAHDLSMVKYiSDRIGVMYRGK 228
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-230 |
6.02e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 6.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 30 FDIFRGETLGLVGESGCGKSTTGRTIirlydatSGEVLFN-GENVHGRK---SRSElkkfnrkmqmifQDPyaslnPRM- 104
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQDlivARLQ------------QDP-----PRNv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 105 --TVADIIAEGI-----------DI-HGLAKTRKERM--------------------AKVHELLETVGLNkehANRYPHE 150
Cdd:PRK11147 80 egTVYDFVAEGIeeqaeylkryhDIsHLVETDPSEKNlnelaklqeqldhhnlwqleNRINEVLAQLGLD---PDAALSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 151 FSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQrerGlTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ---G-SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
28-215 |
7.80e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 28 LTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgRKSRSELKKfnrkmQMIFQDPYASLNPRMTVA 107
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--KKDLCTYQK-----QLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 108 DIIAegIDIHglakTRKERMaKVHELLETVGLnkEHANRYP-HEFSGGQRQRIGIARALAVEPDFIIADEPISALDvsiQ 186
Cdd:PRK13540 93 ENCL--YDIH----FSPGAV-GITELCRLFSL--EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---E 160
|
170 180 190
....*....|....*....|....*....|..
gi 654962578 187 AQVVNLMKKLQ--RERGLTYLFIAH-DLSMVK 215
Cdd:PRK13540 161 LSLLTIITKIQehRAKGGAVLLTSHqDLPLNK 192
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-229 |
1.25e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 22 IKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYD-ATSGEVLFNGENVhgrKSRSELKKFNRKMQMIFQDPYA-S 99
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPV---KIRNPQQAIAQGIAMVPEDRKRdG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 100 LNPRMTVADIIAegidihgLAKTRK-ERMAKVHELLETVGLNKEHAN---RYPHEF------SGGQRQRIGIARALAVEP 169
Cdd:PRK13549 352 IVPVMGVGKNIT-------LAALDRfTGGSRIDDAAELKTILESIQRlkvKTASPElaiarlSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 170 DFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKI 229
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-227 |
1.47e-10 |
|
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: 60.04 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 15 FFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENvHGRKSRSELKKFNRkmqmiFQ 94
Cdd:cd03290 7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKN-ESEPSFEATRSRNR-----YS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 95 DPYASLNPRM---TVADIIAEGIDIHglaKTRKERMAKVHELLETVGL----NKEHANRYPHEFSGGQRQRIGIARALAV 167
Cdd:cd03290 81 VAYAAQKPWLlnaTVEENITFGSPFN---KQRYKAVTDACSLQPDIDLlpfgDQTEIGERGINLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654962578 168 EPDFIIADEPISALDVSIQAQVVN--LMKKLQRERgLTYLFIAHDLSMVKYiSDRIGVMYRG 227
Cdd:cd03290 158 NTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
230-290 |
1.77e-10 |
|
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: 55.87 E-value: 1.77e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654962578 230 VELAPSDELYRNPVHPYTKALLSAIPLPDPdsektrqRKIYDPSIhdyNGEEPELREVSPG 290
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDP-------PKRPLYTI---PGNVPSLLELPEG 51
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-221 |
1.87e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.13 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 20 GTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLfngenvhgrksRSELKKFNRKMQMIFQDP--- 96
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGYVPQKLYLDTtlp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 97 -----YASLNPRMTVADIIAEgidihglaktrkermakvhelLETVglNKEHANRYP-HEFSGGQRQRIGIARALAVEPD 170
Cdd:PRK09544 84 ltvnrFLRLRPGTKKEDILPA---------------------LKRV--QAGHLIDAPmQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 654962578 171 FIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRI 221
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-238 |
2.06e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 22 IKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELKKfnrKMQMIFQDpyASLN 101
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALEN---GISMVHQE--LNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 102 PRMTVADIIAEG--------IDiHGlaKTRKERMAKVHELLETVGLNKEHANrypheFSGGQRQRIGIARALAVEPDFII 173
Cdd:PRK10982 86 LQRSVMDNMWLGryptkgmfVD-QD--KMYRDTKAIFDELDIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 174 ADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDEL 238
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-238 |
2.40e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.50 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 15 FFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGeNVHGRKSRSELKKFNRKMQMIFQ 94
Cdd:TIGR00957 644 FTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVPQQAWIQNDSLRENILFG 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 95 DPyasLNPRMTVADIIAEGI--DIHGLAKTRKERMAKVhelletvGLNkehanrypheFSGGQRQRIGIARALAVEPDFI 172
Cdd:TIGR00957 723 KA---LNEKYYQQVLEACALlpDLEILPSGDRTEIGEK-------GVN----------LSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654962578 173 IADEPISALDVSIQAQVV-NLMKKLQRERGLTYLFIAHDLSMVKYIsDRIGVMYRGKIVELAPSDEL 238
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 848
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-230 |
4.23e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.08 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTgrtIIRLYDATS--GEVLFNGENVhGRKSRSELKKFnRKM--QmifQDPYASL 100
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTL---LARMAGLLPgqGEILLNGRPL-SDWSAAELARH-RAYlsQ---QQSPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 101 nprMTVADIIAegidIHGLAKTRKERMAK-VHELLETVGLNKEhANRYPHEFSGGQRQRIGIARAL-----AVEPD--FI 172
Cdd:COG4138 84 ---MPVFQYLA----LHQPAGASSEAVEQlLAQLAEALGLEDK-LSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 173 IADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV 230
Cdd:COG4138 156 LLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
27-231 |
4.89e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.65 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 27 GLTFDIFRGETLGLVGESGCGKSTTGRTII--RLYDATSGEVLFNGENVhgrksrSELKKFNRKMQ---MIFQDP----- 96
Cdd:PRK09580 19 GLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDL------LELSPEDRAGEgifMAFQYPveipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 97 ----------------YASLNP--RMTVADIIAEGIdihglaktrkeRMAKVHELLETVGLNKEhanrypheFSGGQRQR 158
Cdd:PRK09580 93 vsnqfflqtalnavrsYRGQEPldRFDFQDLMEEKI-----------ALLKMPEDLLTRSVNVG--------FSGGEKKR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654962578 159 IGIARALAVEPDFIIADEPISALDV---SIQAQVVNLMKKLQRerglTYLFIAHDLSMVKYIS-DRIGVMYRGKIVE 231
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLDIdalKIVADGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLYQGRIVK 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-261 |
5.61e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 30 FDIFRGETLGLVGESGCGKSTTGRtiirlydATSGE-VLFNGENVHgRKSRSELKKFnRKMQMIFQDPYASLNPRM---- 104
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALAR-------ALAGElPLLSGERQS-QFSHITRLSF-EQLQKLVSDEWQRNNTDMlspg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 105 ------TVADIIAEGIDihglaktrkeRMAKVHELLETVGLNKEHANRYPHeFSGGQRQRIGIARALAVEPDFIIADEPI 178
Cdd:PRK10938 95 eddtgrTTAEIIQDEVK----------DPARCEQLAQQFGITALLDRRFKY-LSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 179 SALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAP-----SDELYRNPVHPYTkalLSA 253
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEreeilQQALVAQLAHSEQ---LEG 239
|
....*...
gi 654962578 254 IPLPDPDS 261
Cdd:PRK10938 240 VQLPEPDE 247
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
147-221 |
9.32e-10 |
|
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: 55.92 E-value: 9.32e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654962578 147 YPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRerglTYLFIAHDLSMVKYISDRI 221
Cdd:cd03221 67 YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKI 137
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-238 |
9.46e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.57 E-value: 9.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 28 LTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMIFQDPYA-SLNPRMtv 106
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI----AKIGLHDLRFKITIIPQDPVLfSGSLRM-- 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 107 adiiaegiDIHGLAKTRKERMAKVHELLETVGLNKEHANRYPHE-------FSGGQRQRIGIARALAVEPDFIIADEPIS 179
Cdd:TIGR00957 1379 --------NLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654962578 180 ALDVSIQaqvvNLMKKLQRER--GLTYLFIAHDLSMVKYISdRIGVMYRGKIVEL-APSDEL 238
Cdd:TIGR00957 1451 AVDLETD----NLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFgAPSNLL 1507
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
150-225 |
1.14e-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: 1.14e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654962578 150 EFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMY 225
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-227 |
1.23e-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: 59.26 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 24 AVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVlfngeNVHGRKSRSELKKFNRKMQMIFQdpYASLNPR 103
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDA-----TVAGKSILTNISDVHQNMGYCPQ--FDAIDDL 2026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 104 MTVADIIAEGIDIHGLAKTRKERMAKVHelLETVGLNKeHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDV 183
Cdd:TIGR01257 2027 LTGREHLYLYARLRGVPAEEIEKVANWS--IQSLGLSL-YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 654962578 184 SIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRG 227
Cdd:TIGR01257 2104 QARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
13-244 |
1.35e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.91 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 13 QHFFTSKGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTI-------IRLYDAT-SGEVLFNGENVHGRKSRsELKK 84
Cdd:PRK13547 5 DHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltggGAPRGARvTGDVTLNGEPLAAIDAP-RLAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 85 FNRKMQMIFQDPYAslnprMTVADIIAEGIDIH---GLAKTRKERMAKVHELlETVGLNKeHANRYPHEFSGGQRQRIGI 161
Cdd:PRK13547 84 LRAVLPQAAQPAFA-----FSAREIVLLGRYPHarrAGALTHRDGEIAWQAL-ALAGATA-LVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 162 ARALA---------VEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIV-E 231
Cdd:PRK13547 157 ARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVaH 236
|
250
....*....|...
gi 654962578 232 LAPSDELyrNPVH 244
Cdd:PRK13547 237 GAPADVL--TPAH 247
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
152-241 |
2.07e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 152 SGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNlmKKLQRE-RGLTYLFIAHDLSMVKYIsDRIGVMYRGKIV 230
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDElRGKTRVLVTNQLHFLSQV-DRIILVHEGMIK 818
|
90
....*....|.
gi 654962578 231 ELAPSDELYRN 241
Cdd:PLN03130 819 EEGTYEELSNN 829
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-221 |
2.54e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.87 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 19 KGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGenvhgrksrselkkfNRKMQMIFQDP-- 96
Cdd:PRK10636 11 RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG---------------NWQLAWVNQETpa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 97 ---------------YASLNPRMTVADIIAEGIDI---HGL-----AKTRKERMAkvhELLETVGLNKEHANRYPHEFSG 153
Cdd:PRK10636 76 lpqpaleyvidgdreYRQLEAQLHDANERNDGHAIatiHGKldaidAWTIRSRAA---SLLHGLGFSNEQLERPVSDFSG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 154 GQRQRIGIARALAVEPDFIIADEPISALDVSiqaQVVNLMKKLQRERGlTYLFIAHDLSMVKYISDRI 221
Cdd:PRK10636 153 GWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQG-TLILISHDRDFLDPIVDKI 216
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-238 |
2.92e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 56.75 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 21 TIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGEnvhgrksrselkkfnrkMQMIFQDpyASL 100
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------------VSVIAIS--AGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 101 NPRMTVADIIAEGIDIHGLakTRKERMAKVHELLETVGLNkEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISA 180
Cdd:PRK13546 97 SGQLTGIENIEFKMLCMGF--KRKEIKAMTPKIIEFSELG-EFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 181 LDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVELAPSDEL 238
Cdd:PRK13546 174 GDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-210 |
3.83e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVlfngenvhgrksrselkKFNRKMQMIFQDPY-ASLNPR 103
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----------------HCGTKLEVAYFDQHrAELDPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 104 MTVADIIAEGidihglaktRKERMakvhelletVGLNKEHANRYPHEF--------------SGGQRQRIGIARALAVEP 169
Cdd:PRK11147 398 KTVMDNLAEG---------KQEVM---------VNGRPRHVLGYLQDFlfhpkramtpvkalSGGERNRLLLARLFLKPS 459
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 654962578 170 DFIIADEPISALDVsiqaQVVNLMKKLQRERGLTYLFIAHD 210
Cdd:PRK11147 460 NLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-216 |
5.18e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.07 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 22 IKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDatsgevLFNGENVHGRKSrselkkfnrKMQMIFQDPYASLN 101
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP------VYGGRLTKPAKG---------KLFYVPQRPYMTLG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 102 --------PrMTVADIIAEGIDIHGLAKTRKErmAKVHELLE-TVGLnkEHANRYPHEFSGGQRQRIGIARALAVEPDFI 172
Cdd:TIGR00954 530 tlrdqiiyP-DSSEDMKRRGLSDKDLEQILDN--VQLTHILErEGGW--SAVQDWMDVLSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 654962578 173 IADEPISALDVSIQAQvvnlMKKLQRERGLTYLFIAHDLSMVKY 216
Cdd:TIGR00954 605 ILDECTSAVSVDVEGY----MYRLCREFGITLFSVSHRKSLWKY 644
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-232 |
6.25e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 4 KLLEIKGLKQHFFTSKGTIKAVDgltFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVHGRKSRSELK 83
Cdd:PRK10522 321 QTLELRNVTFAYQDNGFSVGPIN---LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 84 KFNrkmqMIFQDPY---ASLNPRMTVADIiaegidihglaktrkermAKVHELLETVGLN---KEHANRYPH-EFSGGQR 156
Cdd:PRK10522 398 LFS----AVFTDFHlfdQLLGPEGKPANP------------------ALVEKWLERLKMAhklELEDGRISNlKLSKGQK 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 157 QRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSmvkYI--SDRIGVMYRGKIVEL 232
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDH---YFihADRLLEMRNGQLSEL 530
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
35-231 |
6.78e-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: 55.69 E-value: 6.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 35 GETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhgrkSRSELKKFNRKMQMIFQDPYA-------SLNPRMTVA 107
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI----SKLPLHTLRSRLSIILQDPILfsgsirfNLDPECKCT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 108 D-IIAEGIDIHGLAKTRKERMAKVHELLETVGLNkehanrypheFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQ 186
Cdd:cd03288 123 DdRLWEALEIAQLKNMVKSLPGGLDAVVTEGGEN----------FSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 654962578 187 aqvvNLMKKLQR----ERglTYLFIAHDLSMVkYISDRIGVMYRGKIVE 231
Cdd:cd03288 193 ----NILQKVVMtafaDR--TVVTIAHRVSTI-LDADLVLVLSRGILVE 234
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-228 |
1.61e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.66 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 25 VDGLTFDIFRGETLGLVGESGCGKSTtgrtiirLYDATSGEVlfNGENVHGR---KSRSELKKFNRKMQMIFQDPYasLN 101
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKST-------LLNALAGRI--QGNNFTGTilaNNRKPTKQILKRTGFVTQDDI--LY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 102 PRMTVADIIAeGIDIHGLAK--TRKERMAKVHELLETVGLNKEH----ANRYPHEFSGGQRQRIGIARALAVEPDFIIAD 175
Cdd:PLN03211 153 PHLTVRETLV-FCSLLRLPKslTKQEKILVAESVISELGLTKCEntiiGNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 654962578 176 EPISALDVSIQAQVVNLMKKLQrERGLTYLFIAHDLSMVKY-ISDRIGVMYRGK 228
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLA-QKGKTIVTSMHQPSSRVYqMFDSVLVLSEGR 284
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-237 |
2.41e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 19 KGTIKAVDGLTFDIFR--------GETLGLVGESGCGKSTTGRTI-IRLYD---ATSGEVLFNGENVHgrksrsELKKFN 86
Cdd:TIGR00956 63 RKLKKFRDTKTFDILKpmdglikpGELTVVLGRPGSGCSTLLKTIaSNTDGfhiGVEGVITYDGITPE------EIKKHY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 87 RKMQMifqdpYASLN----PRMTVADII-----AEGIDIHGLAKTRKERMAKVHEL-LETVGL----NKEHANRYPHEFS 152
Cdd:TIGR00956 137 RGDVV-----YNAETdvhfPHLTVGETLdfaarCKTPQNRPDGVSREEYAKHIADVyMATYGLshtrNTKVGNDFVRGVS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 153 GGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRERGLTYLFIAHDLSMVKY-ISDRIGVMYRGKIVE 231
Cdd:TIGR00956 212 GGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYeLFDKVIVLYEGYQIY 291
|
....*.
gi 654962578 232 LAPSDE 237
Cdd:TIGR00956 292 FGPADK 297
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-210 |
3.30e-08 |
|
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: 51.99 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 34 RGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLfngenvhgrksrselkkfnrkmqmifqdpYASLNPRMTVADIIAEG 113
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI-----------------------------YIDGEDILEEVLDQLLL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 114 IDIhglaktrkermakvhelletvglnkehaNRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQV---- 189
Cdd:smart00382 52 IIV----------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllle 103
|
170 180
....*....|....*....|..
gi 654962578 190 -VNLMKKLQRERGLTYLFIAHD 210
Cdd:smart00382 104 eLRLLLLLKSEKNLTVILTTND 125
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
8-231 |
3.93e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 8 IKGLKQHFF-TSKGTIK-AVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVlfngeNVHGRKSRSELKkf 85
Cdd:PRK13545 21 FDKLKDLFFrSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAIS-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 nrkmqmifqdpyASLNPRMT-VADIIAEGIdIHGLAKTR-KERMAKVHELLEtVGlnkEHANRYPHEFSGGQRQRIGIAR 163
Cdd:PRK13545 94 ------------SGLNGQLTgIENIELKGL-MMGLTKEKiKEIIPEIIEFAD-IG---KFIYQPVKTYSSGMKSRLGFAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 164 ALAVEPDFIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYISDRIGVMYRGKIVE 231
Cdd:PRK13545 157 SVHINPDILVIDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKE 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
152-241 |
3.96e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 152 SGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKlQRERGLTYLFIAHDLSMVKYIsDRIGVMYRGKIVE 231
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKE 819
|
90
....*....|
gi 654962578 232 LAPSDELYRN 241
Cdd:PLN03232 820 EGTFAELSKS 829
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-210 |
8.58e-07 |
|
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: 49.93 E-value: 8.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 13 QHFFTSKGTIKAVDG---------LTFdiFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGenvhgrksrselk 83
Cdd:TIGR03719 2 QYIYTMNRVSKVVPPkkeilkdisLSF--FPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 84 kfNRKMQMIFQDPYasLNPRMTVADIIAEGI----------------------DIHGLAktrkERMAKVHELLETVG--- 138
Cdd:TIGR03719 67 --GIKVGYLPQEPQ--LDPTKTVRENVEEGVaeikdaldrfneisakyaepdaDFDKLA----AEQAELQEIIDAADawd 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 139 LNKE-----HANRYP------HEFSGGQRQRIGIARALAVEPDFIIADEPISALDvsiqAQVVN-LMKKLQRERGlTYLF 206
Cdd:TIGR03719 139 LDSQleiamDALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAwLERHLQEYPG-TVVA 213
|
....
gi 654962578 207 IAHD 210
Cdd:TIGR03719 214 VTHD 217
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-237 |
1.31e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 11 LKQHF----FTSKGTIKAVDGLT-----------FDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENVhg 75
Cdd:PRK10982 235 LTQRFpdkeNKPGEVILEVRNLTslrqpsirdvsFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 76 rKSRSELKKFNRKMQMIFQDP-----YASLNprMTVADIIAEgIDIH----GLAKTRKERmAKVHELLETVGLNKEHANR 146
Cdd:PRK10982 313 -NNHNANEAINHGFALVTEERrstgiYAYLD--IGFNSLISN-IRNYknkvGLLDNSRMK-SDTQWVIDSMRVKTPGHRT 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 147 YPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKL-QRERGLtyLFIAHDLSMVKYISDRIGVMY 225
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMS 465
|
250
....*....|....*
gi 654962578 226 RGK---IVELAPSDE 237
Cdd:PRK10982 466 NGLvagIVDTKTTTQ 480
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-183 |
1.45e-06 |
|
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: 49.55 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 3 DKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFnGENVH---GRKSR 79
Cdd:TIGR03719 320 DKVIEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKlayVDQSR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 80 SelkkfnrkmqmifqdpyaSLNPRMTVADIIAEGIDIHGLAKTRKERMA--------------KVHELletvglnkehan 145
Cdd:TIGR03719 395 D------------------ALDPNKTVWEEISGGLDIIKLGKREIPSRAyvgrfnfkgsdqqkKVGQL------------ 444
|
170 180 190
....*....|....*....|....*....|....*...
gi 654962578 146 ryphefSGGQRQRIGIARALAVEPDFIIADEPISALDV 183
Cdd:TIGR03719 445 ------SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
6-221 |
1.50e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.70 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 6 LEIKGLKQHfftskgtikAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIrlydATSGEVLFNgenvhgrksrSELKKF 85
Cdd:cd03238 1 LTVSGANVH---------NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLI----------SFLPKF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 86 NRKmQMIFQDPYASLnprmtvadiiaegIDihglaktrkermakvhelletVGLNKEHANRYPHEFSGGQRQRIGIARAL 165
Cdd:cd03238 58 SRN-KLIFIDQLQFL-------------ID---------------------VGLGYLTLGQKLSTLSGGELQRVKLASEL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 654962578 166 AVEPD--FIIADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYiSDRI 221
Cdd:cd03238 103 FSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSS-ADWI 158
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-73 |
2.38e-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: 2.38e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654962578 6 LEIKGLKQHFFTSKG----TIKAVDgLTFDifRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGENV 73
Cdd:COG4615 328 LELRGVTYRYPGEDGdegfTLGPID-LTIR--RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-177 |
2.71e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 7 EIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKST-----TGRTIIRlydatSGEVLFNGENVHGRKSRSE 81
Cdd:NF033858 3 RLEGVSHRY----GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSllsliAGARKIQ-----QGRVEVLGGDMADARHRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 82 LKKfnRKMQMifqdP-------YASLNprmtvadiIAEGIDIHG--LAKTRKERMAKVHELLETVGLnKEHANRYPHEFS 152
Cdd:NF033858 74 VCP--RIAYM----PqglgknlYPTLS--------VFENLDFFGrlFGQDAAERRRRIDELLRATGL-APFADRPAGKLS 138
|
170 180
....*....|....*....|....*
gi 654962578 153 GGQRQRIGIARALAVEPDFIIADEP 177
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEP 163
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
128-183 |
5.25e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 5.25e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 654962578 128 AKVHELLETVGLNKEHANRYPHEFSGGQRQRIGIARALAVEPDFIIADEPISALDV 183
Cdd:PLN03073 322 ARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
35-227 |
1.30e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 44.93 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 35 GETLGLVGESGCGKST-----TGRTIIRLydaTSGEVLFNGenvhgrksrSELKK-FNRkmqmifqdpyaslnprmTVAd 108
Cdd:cd03232 33 GTLTALMGESGAGKTTlldvlAGRKTAGV---ITGEILING---------RPLDKnFQR-----------------STG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 109 iIAEGIDIHglaktrkERMAKVHELLETvglnkeHAN-RyphEFSGGQRQRIGIARALAVEPDFIIADEPISALDVSIQA 187
Cdd:cd03232 83 -YVEQQDVH-------SPNLTVREALRF------SALlR---GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 654962578 188 QVVNLMKKLQRErGLTYLFIAHDLSMVKYIS-DRIGVMYRG 227
Cdd:cd03232 146 NIVRFLKKLADS-GQAILCTIHQPSASIFEKfDRLLLLKRG 185
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
152-243 |
3.55e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 152 SGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMkKLQRERGLTYLFIAHDLSMVKYiSDRIGVMYRGKIVE 231
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEC-FLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEF 861
|
90
....*....|..
gi 654962578 232 LAPSDELYRNPV 243
Cdd:PTZ00243 862 SGSSADFMRTSL 873
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-183 |
1.01e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 3 DKLLEIKGLKQHFftskGTIKAVDGLTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFnGENVhgrksrsel 82
Cdd:PRK11819 322 DKVIEAENLSKSF----GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 kkfnrkmQMIFQDPY-ASLNPRMTVADIIAEGIDIHglaktrkermakvhelleTVGlNKEHANR-YPHEF--------- 151
Cdd:PRK11819 388 -------KLAYVDQSrDALDPNKTVWEEISGGLDII------------------KVG-NREIPSRaYVGRFnfkggdqqk 441
|
170 180 190
....*....|....*....|....*....|....*..
gi 654962578 152 -----SGGQRQRIGIARALAVEPDFIIADEPISALDV 183
Cdd:PRK11819 442 kvgvlSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
28-189 |
1.22e-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: 43.75 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 28 LTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGenvhgRKSRSelkkfnrkmqmifqdPYASLNPRMTVA 107
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----RISFS---------------PQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 108 DIIaegidIHGLA--KTRKERMAKVHELLETVGLNKEHANRYPHE----FSGGQRQRIGIARALAVEPDFIIADEPISAL 181
Cdd:TIGR01271 505 DNI-----IFGLSydEYRYTSVIKACQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
....*...
gi 654962578 182 DVSIQAQV 189
Cdd:TIGR01271 580 DVVTEKEI 587
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-182 |
1.41e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 26 DGLTFDIFRGETLGLVGESGCGKST-----TGrtiirlyDATSGE----VLFngenvhGRKSRS-----ELKKfnrkmqm 91
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKSTllsliTG-------DHPQGYsndlTLF------GRRRGSgetiwDIKK------- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 92 ifQDPYAS----LNPRM--TVADIIAEG----IDIHGLAKTRKERMAKvhELLETVGLNKEHANRYPHEFSGGQRQRIGI 161
Cdd:PRK10938 337 --HIGYVSsslhLDYRVstSVRNVILSGffdsIGIYQAVSDRQQKLAQ--QWLDILGIDKRTADAPFHSLSWGQQRLALI 412
|
170 180
....*....|....*....|.
gi 654962578 162 ARALAVEPDFIIADEPISALD 182
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLD 433
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
35-196 |
1.73e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 35 GETLGLVGESGCGKST-----TGRT---IIrlydaTSGEVLFNGenvHGRKSrselkKFNRKMQMIFQDPYASlnPRMTV 106
Cdd:TIGR00956 789 GTLTALMGASGAGKTTllnvlAERVttgVI-----TGGDRLVNG---RPLDS-----SFQRSIGYVQQQDLHL--PTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 107 ADIIAEGIDIHGLAK-TRKERMA---KVHELLET------------VGLNKEhanryphefsggQRQRIGIARALAVEPD 170
Cdd:TIGR00956 854 RESLRFSAYLRQPKSvSKSEKMEyveEVIKLLEMesyadavvgvpgEGLNVE------------QRKRLTIGVELVAKPK 921
|
170 180
....*....|....*....|....*..
gi 654962578 171 FII-ADEPISALDVSIQAQVVNLMKKL 196
Cdd:TIGR00956 922 LLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
22-57 |
2.44e-04 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 41.57 E-value: 2.44e-04
10 20 30
....*....|....*....|....*....|....*.
gi 654962578 22 IKAVDGLtFDIFRGETLGLVGESGCGKSTTGRTIIR 57
Cdd:pfam00006 2 IRAIDGL-LPIGRGQRIGIFGGSGVGKTVLAGMIAR 36
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
83-221 |
2.50e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 83 KKFNRKMQMIFQDPYASLNPRMTVADIIAEGIDihGLaktrKERMAkvheLLETVGLNKEHANRYPHEFSGGQRQRIGIA 162
Cdd:PRK00635 419 KTFAEFQQMSLQELFIFLSQLPSKSLSIEEVLQ--GL----KSRLS----ILIDLGLPYLTPERALATLSGGEQERTALA 488
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654962578 163 RALAVEPDFI--IADEPISALDVSIQAQVVNLMKKLqRERGLTYLFIAHDLSMVKYiSDRI 221
Cdd:PRK00635 489 KHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQMISL-ADRI 547
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
28-189 |
4.17e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 41.38 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 28 LTFDIFRGETLGLVGESGCGKSTTGRTIIRLYDATSGEVLFNGenvhgrksrselkkfnrkmQMIFQDPYASLNPRmTVA 107
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------------RISFSSQFSWIMPG-TIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 108 DIIAEGIDIHglaKTRKERMAKVHELLETVGLNKEHANRYPHE----FSGGQRQRIGIARALAVEPDFIIADEPISALDV 183
Cdd:cd03291 116 ENIIFGVSYD---EYRYKSVVKACQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
....*.
gi 654962578 184 SIQAQV 189
Cdd:cd03291 193 FTEKEI 198
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
152-236 |
1.07e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 152 SGGQRQRIGIARALAVEPDFIIADEPISALDVSIQAQVVNLMKKLQRErGLTYLFIAHDLSMVKYISDRIGVMYRGKIV- 230
Cdd:NF040905 406 SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRITg 484
|
....*.
gi 654962578 231 ELAPSD 236
Cdd:NF040905 485 ELPREE 490
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
125-219 |
2.19e-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: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 125 ERMAKVHELLET---VGLNKEHANRYPHEFSGGQRQRIGIARAL---AVEPDFIIADEPISALDVSIQAQVVNLMKKLqR 198
Cdd:cd03271 141 ENIPKIARKLQTlcdVGLGYIKLGQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRL-V 219
|
90 100
....*....|....*....|....
gi 654962578 199 ERGLTYLFIAHDLSMVK---YISD 219
Cdd:cd03271 220 DKGNTVVVIEHNLDVIKcadWIID 243
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
152-226 |
2.70e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 38.36 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654962578 152 SGGQRQ------RIGIARALAVEPDFIIADEPISALDV-SIQAQVVNLMKKLQRERGLTYLFIAHDLSMVkyisDRIGVM 224
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELV----DAADHI 192
|
..
gi 654962578 225 YR 226
Cdd:cd03240 193 YR 194
|
|
| |
