|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-270 |
1.36e-123 |
|
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: 355.90 E-value: 1.36e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMR---EYLPTSGRILYKGRPVEAAKSAEI 81
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 82 ARYR-RSVQMIFQDPFASLNPAHTIAHHLRRPLKLHRPeIKGAEIDVAVRELLQRVRL-DPDLVAPKYPHELSGGQRQRV 159
Cdd:COG0444 81 RKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGG-LSKAEARERAIELLERVGLpDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 160 NIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVI 239
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260 270
....*....|....*....|....*....|.
gi 1586794399 240 DNPLHPYTRLLLSAVPDPdvrfDDPKARLRP 270
Cdd:COG0444 240 ENPRHPYTRALLSSIPRL----DPDGRRLIP 266
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-260 |
2.64e-121 |
|
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: 357.29 E-value: 2.64e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFG-HGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSA 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 80 EIARYRRSVQMIFQDPFASLNPAHTIAHHLRRPLKLHRpEIKGAEIDVAVRELLQRVRLDPDLvAPKYPHELSGGQRQRV 159
Cdd:COG1123 336 SLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHG-LLSRAERRERVAELLERVGLPPDL-ADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 160 NIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVI 239
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
250 260
....*....|....*....|.
gi 1586794399 240 DNPLHPYTRLLLSAVPDPDVR 260
Cdd:COG1123 494 ANPQHPYTRALLAAVPSLDPA 514
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-258 |
5.76e-120 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 347.10 E-value: 5.76e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTF-------GHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPV 73
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 74 EAAKSAEIARYRRSVQMIFQDPFASLNPAHTIAHHLRRPLKLHRPeIKGAEIDVAVRELLQRVRLDPDlVAPKYPHELSG 153
Cdd:COG4608 83 TGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGL-ASKAERRERVAELLELVGLRPE-HADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 154 GQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWG 233
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250 260
....*....|....*....|....*
gi 1586794399 234 SVAKVIDNPLHPYTRLLLSAVPDPD 258
Cdd:COG4608 241 PRDELYARPLHPYTQALLSAVPVPD 265
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-231 |
1.35e-105 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 306.74 E-value: 1.35e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARY 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 85 RRSVQMIFQDPFASLNPAHTIAHHLRRPLKLHRPEIKGAEIDVAVRELLQRVRLDPDlVAPKYPHELSGGQRQRVNIARA 164
Cdd:cd03257 81 RKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEE-VLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586794399 165 LAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVE 231
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-258 |
2.40e-101 |
|
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: 306.61 E-value: 2.40e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 15 FGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMReYLPTSGRILYKGRPVEAAKSAEIARYRRSVQMIFQD 94
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 95 PFASLNPAHTIAHHLRRPLKLHRPEIKGAEIDVAVRELLQRVRLDPDlVAPKYPHELSGGQRQRVNIARALAVKPEVIVA 174
Cdd:COG4172 371 PFGSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVAEALEEVGLDPA-ARHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 175 DEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPYTRLLLSAV 254
Cdd:COG4172 450 DEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAA 529
|
....
gi 1586794399 255 PDPD 258
Cdd:COG4172 530 PLLE 533
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-260 |
1.01e-98 |
|
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: 290.17 E-value: 1.01e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaKSAEIARYR 85
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV---TRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQDPFASLNPAHTIAHHLRRPLKLHRpeikGAEIDVAVRELLQRVRLDPDLvAPKYPHELSGGQRQRVNIARAL 165
Cdd:COG1124 79 RRVQMVFQDPYASLHPRHTVDRILAEPLRIHG----LPDREERIAELLEQVGLPPSF-LDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 166 AVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHP 245
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
250
....*....|....*
gi 1586794399 246 YTRLLLSAVPDPDVR 260
Cdd:COG1124 234 YTRELLAASLAFERA 248
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-279 |
1.51e-88 |
|
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: 273.87 E-value: 1.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMReYLP-----TSGRILYKGRPVEA 75
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILR-LLPdpaahPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 76 AKSAEIARYR-RSVQMIFQDPFASLNPAHTIAHHLRRPLKLHRPeIKGAEIDVAVRELLQRVRL-DPDLVAPKYPHELSG 153
Cdd:COG4172 81 LSERELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRG-LSGAAARARALELLERVGIpDPERRLDAYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 154 GQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWG 233
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQG 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1586794399 234 SVAKVIDNPLHPYTRLLLSAVPDPDVRFDDPKAR--LrpdEVEDIRRR 279
Cdd:COG4172 240 PTAELFAAPQHPYTRKLLAAEPRGDPRPVPPDAPplL---EARDLKVW 284
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
10-260 |
3.59e-85 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 258.36 E-value: 3.59e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 10 SVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARM-AMREYlPTSGRILYKGRPVEAAKSAEIARYRRSV 88
Cdd:PRK11308 16 PVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLlTMIET-PTGGELYYQGQDLLKADPEAQKLLRQKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 89 QMIFQDPFASLNPAHTIAHHLRRPLKLHrPEIKGAEIDVAVRELLQRVRLDPDLvAPKYPHELSGGQRQRVNIARALAVK 168
Cdd:PRK11308 95 QIVFQNPYGSLNPRKKVGQILEEPLLIN-TSLSAAERREKALAMMAKVGLRPEH-YDRYPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 169 PEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPYTR 248
Cdd:PRK11308 173 PDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQ 252
|
250
....*....|....
gi 1586794399 249 LLLSAVP--DPDVR 260
Cdd:PRK11308 253 ALLSATPrlNPDDR 266
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-258 |
3.65e-80 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 245.77 E-value: 3.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 24 AARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYRRSVQMIFQDPFASLNPAH 103
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLRRPLKLHRPEIKGAEIDVAVRELLQRVRLDPDLVApKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDV 183
Cdd:PRK15079 116 TIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLIN-RYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586794399 184 SVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPYTRLLLSAVPDPD 258
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVPIPD 269
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-296 |
2.15e-69 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 226.28 E-value: 2.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 22 VHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYRRSVQMIFQDPFASLNP 101
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 102 AHTIAHHLRRPLKLHRPeIKGAEIDVAVRELLQRVRLDPDLvAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSML 181
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGL-LPGKAAAARVAWLLERVGLLPEH-AWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 182 DVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPYTRLLLSAVPDPDVRF 261
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVADPSR 574
|
250 260 270
....*....|....*....|....*....|....*..
gi 1586794399 262 DDPKARLRPDEV-EDIRRR-SAMPQDDIVEFEQDHFM 296
Cdd:PRK10261 575 QRPQRVLLSDDLpSNIHLRgEEVAAVSLQCVGPGHYV 611
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-253 |
2.68e-67 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 210.85 E-value: 2.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 4 AILALDSVTKTFGHGSG-----AVHAARAISFSLHAGRALALVGESGSGKTTCARM--AMREylPTSGRILYKGRPVEAA 76
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMlaGIIE--PTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 77 KsaeiARYR-RSVQMIFQDPFASLNPAHTIAHHLRRPLKLHrPEIKGAEIDVAVRELLQRVRLDPDLvAPKYPHELSGGQ 155
Cdd:COG4167 81 D----YKYRcKHIRMIFQDPNTSLNPRLNIGQILEEPLRLN-TDLTAEEREERIFATLRLVGLLPEH-ANFYPHMLSSGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 156 RQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSV 235
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKT 234
|
250
....*....|....*...
gi 1586794399 236 AKVIDNPLHPYTRLLLSA 253
Cdd:COG4167 235 AEVFANPQHEVTKRLIES 252
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-279 |
1.41e-65 |
|
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: 213.61 E-value: 1.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 3 DAILALDSVTKTFGHGsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMReYLP----TSGRILYKGRPVEAAKS 78
Cdd:COG1123 2 TPLLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPhggrISGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 79 AEIARYrrsVQMIFQDPFASLNPAhTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDpdLVAPKYPHELSGGQRQR 158
Cdd:COG1123 79 ALRGRR---IGMVFQDPMTQLNPV-TVGDQIAEALENLG--LSRAEARARVLELLEAVGLE--RRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 159 VNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKV 238
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1586794399 239 IDNPlhpytrLLLSAVPDPDVRFDDPKARLRPD----EVEDIRRR 279
Cdd:COG1123 231 LAAP------QALAAVPRLGAARGRAAPAAAAAepllEVRNLSKR 269
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-258 |
1.08e-63 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 203.80 E-value: 1.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCArMAMREYLPTSGRI----LYKGRPVEAA 76
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTA-FALMGLLAANGRIggsaTFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 77 KSAEIARYR-RSVQMIFQDPFASLNPAHTIAHHLRRPLKLHRPEIKGAEIDVAVReLLQRVRLdPDlvAPK----YPHEL 151
Cdd:PRK09473 87 PEKELNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVR-MLDAVKM-PE--ARKrmkmYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 152 SGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVE 231
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
250 260
....*....|....*....|....*..
gi 1586794399 232 WGSVAKVIDNPLHPYTRLLLSAVPDPD 258
Cdd:PRK09473 243 YGNARDVFYQPSHPYSIGLLNAVPRLD 269
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-258 |
2.51e-62 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 205.71 E-value: 2.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMReYLPT------SGRILYKGRPVE 74
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILR-LLPSppvvypSGDIRFHGESLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 75 AAKSAEIARYR-RSVQMIFQDPFASLNPAHTIAHHLRRPLKLHR---PEIKGAEI-----DVAVRELLQRVRldpdlvap 145
Cdd:PRK15134 80 HASEQTLRGVRgNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRgmrREAARGEIlncldRVGIRQAAKRLT-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 146 KYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMY 225
Cdd:PRK15134 152 DYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQ 231
|
250 260 270
....*....|....*....|....*....|...
gi 1586794399 226 AGQIVEWGSVAKVIDNPLHPYTRLLLSAVPDPD 258
Cdd:PRK15134 232 NGRCVEQNRAATLFSAPTHPYTQKLLNSEPSGD 264
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-275 |
3.03e-61 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 197.61 E-value: 3.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARM-AMREyLPTSGRILYKGRPVEAAKSAEIAR 83
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCiNLLE-RPTSGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 84 YRRSVQMIFQDpFASLNpAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDpDLvAPKYPHELSGGQRQRVNIAR 163
Cdd:COG1135 80 ARRKIGMIFQH-FNLLS-SRTVAENVALPLEIAG--VPKAEIRKRVAELLELVGLS-DK-ADAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 164 ALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPL 243
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQ 233
|
250 260 270
....*....|....*....|....*....|..
gi 1586794399 244 HPYTRLLLSAVPDPDVrFDDPKARLRPDEVED 275
Cdd:COG1135 234 SELTRRFLPTVLNDEL-PEELLARLREAAGGG 264
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-254 |
1.32e-59 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 191.05 E-value: 1.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHGS-----GAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSA 79
Cdd:PRK10419 3 LLNVSGLSHHYAHGGlsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 80 EIARYRRSVQMIFQDPFASLNPAHTIAHHLRRPLKlHRPEIKGAEIDVAVRELLQRVRLDPDLvAPKYPHELSGGQRQRV 159
Cdd:PRK10419 83 QRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLR-HLLSLDKAERLARASEMLRAVDLDDSV-LDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 160 NIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVI 239
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKL 240
|
250
....*....|....*
gi 1586794399 240 DNPlHPYTRLLLSAV 254
Cdd:PRK10419 241 TFS-SPAGRVLQNAV 254
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-254 |
1.97e-59 |
|
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: 190.79 E-value: 1.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 4 AILALDSVTKTFGHGSGAVHAARA-----ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKS 78
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGGLFGAKQRApvltnVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 79 AEIARYRRSVQMIFQDPFASLNPAHTIAHHLRRPLKlHRPEIKGAEIDVAVRELLQRVRLDPDlVAPKYPHELSGGQRQR 158
Cdd:TIGR02769 81 KQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLR-HLTSLDESEQKARIAELLDMVGLRSE-DADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 159 VNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKv 238
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQ- 237
|
250
....*....|....*.
gi 1586794399 239 IDNPLHPYTRLLLSAV 254
Cdd:TIGR02769 238 LLSFKHPAGRNLQSAV 253
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
28-253 |
1.02e-58 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 187.58 E-value: 1.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCArMAMREYLP-----TSGRILYKGRPVeaaksAEIARYRRSVQMIFQDPFASLNPA 102
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLTC-LAILGLLPpgltqTSGEILLDGRPL-----LPLSIRGRHIATIMQNPRTAFNPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 103 HTIAHHLRRPLKLHRPEIKGAEIDVAvrELLQRVRL-DPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSML 181
Cdd:TIGR02770 79 FTMGNHAIETLRSLGKLSKQARALIL--EALEAVGLpDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586794399 182 DVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPYTRLLLSA 253
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
3-254 |
1.11e-57 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 185.79 E-value: 1.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 3 DAILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGR-----PVEAAK 77
Cdd:COG4107 6 QPLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDRdggprDLFALS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 78 SAEIARYRRSV-QMIFQDPFASLNPAHT----IAHHLrrplkLHRPEIKGAEIDVAVRELLQRVRLDPDLVApKYPHELS 152
Cdd:COG4107 86 EAERRRLRRTDwGMVYQNPRDGLRMDVSaggnIAERL-----MAAGERHYGDIRARALEWLERVEIPLERID-DLPRTFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 153 GGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEW 232
Cdd:COG4107 160 GGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVES 239
|
250 260
....*....|....*....|..
gi 1586794399 233 GSVAKVIDNPLHPYTRLLLSAV 254
Cdd:COG4107 240 GLTDQVLEDPQHPYTQLLVSSV 261
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-252 |
5.36e-57 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 191.46 E-value: 5.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 23 HAARAISFSLHAGRALALVGESGSGKTTCArMAMREYLPTSGRILYKGRPVEAAKSAEIARYRRSVQMIFQDPFASLNPA 102
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTG-LALLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 103 HTIAHHLRRPLKLHRPEIKGAEIDVAVRELLQRVRLDPDLvAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLD 182
Cdd:PRK15134 379 LNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPET-RHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 183 VSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPYTRLLLS 252
Cdd:PRK15134 458 KTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-242 |
1.52e-56 |
|
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: 182.01 E-value: 1.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMA-MREYlPTSGRILYKGRPVEAAKSAEIAR 83
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInGLER-PTSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 84 YRRSVQMIFQ--DPFASLNPAHTIAHhlrrPLKLHRpeIKGAEIDVAVRELLQRVRLDPDlvAPKYPHELSGGQRQRVNI 161
Cdd:cd03258 80 ARRRIGMIFQhfNLLSSRTVFENVAL----PLEIAG--VPKAEIEERVLELLELVGLEDK--ADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 162 ARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDN 241
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
.
gi 1586794399 242 P 242
Cdd:cd03258 232 P 232
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-268 |
3.15e-56 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 184.17 E-value: 3.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 4 AILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKT--TCARMAMREYlptSGRIL-----YKGRPVEAA 76
Cdd:PRK11022 2 ALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsSLAIMGLIDY---PGRVMaekleFNGQDLQRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 77 KSAEiaryRRS-----VQMIFQDPFASLNPAHTIAHHLRRPLKLHRPEIKGAEIDVAVrELLQRVRL-DPDLVAPKYPHE 150
Cdd:PRK11022 79 SEKE----RRNlvgaeVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAI-DLLNQVGIpDPASRLDVYPHQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 151 LSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIV 230
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 1586794399 231 EWGSVAKVIDNPLHPYTRLLLSAVPDpdvrFDDPKARL 268
Cdd:PRK11022 234 ETGKAHDIFRAPRHPYTQALLRALPE----FAQDKARL 267
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-248 |
7.03e-55 |
|
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: 177.86 E-value: 7.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGhgSGAVHaaRAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAE 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFG--DRVVL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 IARYRRSVQMIFQDP--FASLNPAHTIAHHLRRPLKLHRPEIKgaEIdvaVRELLQRVRLDPdlVAPKYPHELSGGQRQR 158
Cdd:COG1127 77 LYELRRRIGMLFQGGalFDSLTVFENVAFPLREHTDLSEAEIR--EL---VLEKLELVGLPG--AADKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 159 VNIARALAVKPEVIVADEPTSMLD-VSVRLgVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAK 237
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDpITSAV-IDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEE 228
|
250
....*....|.
gi 1586794399 238 VIDNPlHPYTR 248
Cdd:COG1127 229 LLASD-DPWVR 238
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-270 |
3.19e-54 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 179.61 E-value: 3.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 8 LDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYRRS 87
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 88 VQMIFQDpFASLNpAHTIAHHLRRPLKL-HRPEikgAEIDVAVRELLQRVRLDpDLvAPKYPHELSGGQRQRVNIARALA 166
Cdd:PRK11153 84 IGMIFQH-FNLLS-SRTVFDNVALPLELaGTPK---AEIKARVTELLELVGLS-DK-ADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 167 VKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPY 246
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPL 236
|
250 260
....*....|....*....|....
gi 1586794399 247 TRLLLSAVPDPDVRfDDPKARLRP 270
Cdd:PRK11153 237 TREFIQSTLHLDLP-EDYLARLQA 259
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-231 |
3.50e-53 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 173.31 E-value: 3.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 3 DAILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMA---MReylPTSGRILYKGRPVEAAKSA 79
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILgglDR---PTSGEVLIDGQDISSLSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 80 EIARYRR-SVQMIFQDPFasLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQR 158
Cdd:COG1136 79 ELARLRRrHIGFVFQFFN--LLPELTALENVALPLLLAG--VSRKERRERARELLERVGLGD--RLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586794399 159 VNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYvAEDIAVMYAGQIVE 231
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-253 |
3.66e-53 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 174.59 E-value: 3.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 3 DAILALDSVTKTFGHGSG-----AVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAK 77
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 78 SaeiaRYR-RSVQMIFQDPFASLNPAHTIAHHLRRPLKLHrPEIKGAEIDVAVRELLQRVRLDPDLvAPKYPHELSGGQR 156
Cdd:PRK15112 82 Y----SYRsQRIRMIFQDPSTSLNPRQRISQILDFPLRLN-TDLEPEQREKQIIETLRQVGLLPDH-ASYYPHMLAPGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 157 QRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVA 236
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTA 235
|
250
....*....|....*..
gi 1586794399 237 KVIDNPLHPYTRLLLSA 253
Cdd:PRK15112 236 DVLASPLHELTKRLIAG 252
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-246 |
3.83e-53 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 177.21 E-value: 3.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMamreyL-----PTSGRILYKGRPVea 75
Cdd:COG3842 1 MAMPALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRM-----IagfetPDSGRILLDGRDV-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 76 aksAEIARYRRSVQMIFQDpFAsLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQ 155
Cdd:COG3842 70 ---TGLPPEKRNVGMVFQD-YA-LFPHLTVAENVAFGLRMRG--VPKAEIRARVAELLELVGLEG--LADRYPHQLSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 156 RQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSV 235
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTP 220
|
250
....*....|.
gi 1586794399 236 AKVIDNPLHPY 246
Cdd:COG3842 221 EEIYERPATRF 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-248 |
9.71e-53 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 172.49 E-value: 9.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHGSGAVhaaRAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryR 85
Cdd:cd03295 1 IEFENVTKRYGGGKKAV---NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQDpfASLNPAHTIAHHLRRPLKL-HRPEikgAEIDVAVRELLQRVRLDPDLVAPKYPHELSGGQRQRVNIARA 164
Cdd:cd03295 75 RKIGYVIQQ--IGLFPHMTVEENIALVPKLlKWPK---EKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 165 LAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLH 244
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
|
....
gi 1586794399 245 PYTR 248
Cdd:cd03295 230 DFVA 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-255 |
1.05e-51 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 179.28 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRI-------LYKGRPVEAAK 77
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 78 SAEIARYRR----SVQMIFQDPFASLNPAHTIAHHLRRPLKLHRpEIKGAEIDVAVRELLQRVRL-DPDLVAPKYPHELS 152
Cdd:PRK10261 92 EQSAAQMRHvrgaDMAMIFQEPMTSLNPVFTVGEQIAESIRLHQ-GASREEAMVEAKRMLDQVRIpEAQTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 153 GGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEW 232
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
|
250 260
....*....|....*....|...
gi 1586794399 233 GSVAKVIDNPLHPYTRLLLSAVP 255
Cdd:PRK10261 251 GSVEQIFHAPQHPYTRALLAAVP 273
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-243 |
1.24e-51 |
|
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: 169.19 E-value: 1.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAksaeiaryR 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP--------G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQDPfaSLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARAL 165
Cdd:cd03293 73 PDRGYVFQQD--ALLPWLTVLDNVALGLELQG--VPKAEARERAEELLELVGLSG--FENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 166 AVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQivewGSVAKVIDNPL 243
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARP----GRIVAEVEVDL 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-242 |
3.62e-51 |
|
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: 168.28 E-value: 3.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 20 GAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryRRSVQMIFQDP---- 95
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL---RRKVGLVFQNPddql 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 96 FASlnpahTIAH-------HLRRPlklhrpeikGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVK 168
Cdd:COG1122 89 FAP-----TVEEdvafgpeNLGLP---------REEIRERVEEALELVGLEH--LADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 169 PEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNP 242
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-229 |
5.33e-51 |
|
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: 167.28 E-value: 5.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARM--AMREylPTSGRILYKGRPVEAAKSAEIAR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNIlgGLDR--PTSGEVRVDGTDISKLSEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 84 YRR-SVQMIFQDPfaSLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDpdLVAPKYPHELSGGQRQRVNIA 162
Cdd:cd03255 79 FRRrHIGFVFQSF--NLLPDLTALENVELPLLLAG--VPKKERRERAEELLERVGLG--DRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586794399 163 RALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYvAEDIAVMYAGQI 229
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-243 |
8.64e-51 |
|
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: 167.29 E-value: 8.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 8 LDSVTKTFGhgSGAVHaaRAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYRRS 87
Cdd:cd03261 3 LRGLTKSFG--GRTVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 88 VQMIFQDP--FASLNPAHTIAHHLRRPLKLHRPEIKgaEIdvaVRELLQRVRLDPDlvAPKYPHELSGGQRQRVNIARAL 165
Cdd:cd03261 79 MGMLFQSGalFDSLTVFENVAFPLREHTRLSEEEIR--EI---VLEKLEAVGLRGA--EDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 166 AVKPEVIVADEPTSMLDvSVRLGVLN-LLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKV--IDNP 242
Cdd:cd03261 152 ALDPELLLYDEPTAGLD-PIASGVIDdLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELraSDDP 230
|
.
gi 1586794399 243 L 243
Cdd:cd03261 231 L 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-233 |
3.53e-50 |
|
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: 165.00 E-value: 3.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaksAEIARYR 85
Cdd:cd03259 1 LELKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-----TGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQDPfaSLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPDLvaPKYPHELSGGQRQRVNIARAL 165
Cdd:cd03259 72 RNIGMVFQDY--ALFPHLTVAENIAFGLKLRG--VPKAEIRARVRELLELVGLEGLL--NRYPHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 166 AVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWG 233
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-254 |
5.85e-50 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 165.17 E-value: 5.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHgsgaVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeAAKSAEIARY 84
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 85 RRSVQMIFQDP--FASLNPAHTIAHHLRRPLKLHRPEikgAEiDVAvRELLQRVRLdPDLvAPKYPHELSGGQRQRVNIA 162
Cdd:COG1126 76 RRKVGMVFQQFnlFPHLTVLENVTLAPIKVKKMSKAE---AE-ERA-MELLERVGL-ADK-ADAYPAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 163 RALAVKPEVIVADEPTSMLD---VSvrlGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVI 239
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFF 224
|
250
....*....|....*
gi 1586794399 240 DNPLHPYTRLLLSAV 254
Cdd:COG1126 225 ENPQHERTRAFLSKV 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-269 |
9.66e-50 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 165.26 E-value: 9.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAkSAE 80
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-GPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 IAryrrsvqMIFQDPfaSLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVN 160
Cdd:COG1116 82 RG-------VVFQEP--ALLPWLTVLDNVALGLELRG--VPKAERRERARELLELVGLAG--FEDAYPHQLSGGMRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 161 IARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQivewGSVAKVID 240
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARP----GRIVEEID 224
|
250 260
....*....|....*....|....*....
gi 1586794399 241 NPLhPYTRlllsavpDPDVRFDDPKARLR 269
Cdd:COG1116 225 VDL-PRPR-------DRELRTSPEFAALR 245
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
15-238 |
8.47e-48 |
|
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: 159.27 E-value: 8.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 15 FGHGSGAVHAARAISFSLHAGRALALVGESGSGKTT----CARM-AMREYLPTSGRILYKGRPVeAAKSAEIARYRRSVQ 89
Cdd:cd03260 6 LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTllrlLNRLnDLIPGAPDEGEVLLDGKDI-YDLDVDVLELRRRVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 90 MIFQDPfaslNPAH-TIAHHLRRPLKLHRpEIKGAEIDVAVRELLQRVRLDPDLVAPKYPHELSGGQRQRVNIARALAVK 168
Cdd:cd03260 85 MVFQKP----NPFPgSIYDNVAYGLRLHG-IKLKEELDERVEEALRKAALWDEVKDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 169 PEVIVADEPTSMLDVSVRLGVLNLLNEMKRElnLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKV 238
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-254 |
9.11e-47 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 157.78 E-value: 9.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGHGsgavHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAE 80
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 IARYRRSVQM------IFQDPFASLNPAHTIAHHLRRPL----KLHRPEIKGAEIDvavreLLQRVRLDPDLVAPKyPHE 150
Cdd:PRK11701 78 LSEAERRRLLrtewgfVHQHPRDGLRMQVSAGGNIGERLmavgARHYGDIRATAGD-----WLERVEIDAARIDDL-PTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 151 LSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIV 230
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
250 260
....*....|....*....|....
gi 1586794399 231 EWGSVAKVIDNPLHPYTRLLLSAV 254
Cdd:PRK11701 232 ESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-242 |
3.40e-46 |
|
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: 155.47 E-value: 3.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHGsgavHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaksAEIARYR 85
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-----TNLPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQDpFAsLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARAL 165
Cdd:cd03300 72 RPVNTVFQN-YA-LFPHLTVFENIAFGLRLKK--LPKAEIKERVAEALDLVQLEG--YANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586794399 166 AVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNP 242
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-253 |
4.37e-46 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 156.01 E-value: 4.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKT-TCArmAMREYLP-----TSGRILYKGRPVEAAksaeiARYRRSVQMIFQDPFASL 99
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCA--AALGILPagvrqTAGRVLLDGKPVAPC-----ALRGRKIATIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 100 NPAHTIAHHLRRPLKlhrpEIKGAEIDVAVRELLQRVRL-DPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPT 178
Cdd:PRK10418 93 NPLHTMHTHARETCL----ALGKPADDATLTAALEAVGLeNAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586794399 179 SMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPYTRLLLSA 253
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-242 |
6.11e-46 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 156.79 E-value: 6.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 8 LDSVTKTFGHGSGAVhaaRAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaKSAEIARYRRS 87
Cdd:COG1125 4 FENVTKRYPDGTVAV---DDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDI---RDLDPVELRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 88 VQMIFQDpfASLNPAHTIAhhlrrplklhR-----PEIKG---AEIDVAVRELLQRVRLDPDLVAPKYPHELSGGQRQRV 159
Cdd:COG1125 78 IGYVIQQ--IGLFPHMTVA----------EniatvPRLLGwdkERIRARVDELLELVGLDPEEYRDRYPHELSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 160 NIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVI 239
Cdd:COG1125 146 GVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEIL 225
|
...
gi 1586794399 240 DNP 242
Cdd:COG1125 226 ANP 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-228 |
1.56e-45 |
|
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: 153.01 E-value: 1.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 14 TFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryRRSVQMIFQ 93
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL---RRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 DP---FASLNPAHTIAHHLRRplkLHRPEikgAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPE 170
Cdd:cd03225 83 NPddqFFGPTVEEEVAFGLEN---LGLPE---EEIEERVEEALELVGLEG--LRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 171 VIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQ 228
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-231 |
4.51e-45 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 152.13 E-value: 4.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHGsgaVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARY 84
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 85 RRSVQMIFQDpFaSLNPAHTIAHHLRRPLKLHrpEIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARA 164
Cdd:COG2884 78 RRRIGVVFQD-F-RLLPDRTVYENVALPLRVT--GKSRKEIRRRVREVLDLVGLSD--KAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 165 LAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRelnLG--LLYITHDIATARYVAEDIAVMYAGQIVE 231
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINR---RGttVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
28-229 |
3.98e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 149.20 E-value: 3.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKsaeIARYRRSVQMIFQDPFAslnPAHTIAH 107
Cdd:COG4619 19 VSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQVAYVPQEPAL---WGGTVRD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 108 HLRRPLKLHRPEIKGAEidvaVRELLQRVRLDPDLVApKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRL 187
Cdd:COG4619 93 NLPFPFQLRERKFDRER----ALELLERLGLPPDILD-KPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1586794399 188 GVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQI 229
Cdd:COG4619 168 RVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-268 |
6.06e-44 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 152.37 E-value: 6.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 19 SGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAM----REYLPTSGRILYKGRPVEAAKSAEIARY-RRSVQMIFQ 93
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICgitkDNWHVTADRFRWNGIDLLKLSPRERRKIiGREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 DPFASLNPAHTIAHHL-----RRPLKLHRPEIKGAEIDVAVrELLQRVRL-DPDLVAPKYPHELSGGQRQRVNIARALAV 167
Cdd:COG4170 97 EPSSCLDPSAKIGDQLieaipSWTFKGKWWQRFKWRKKRAI-ELLHRVGIkDHKDIMNSYPHELTEGECQKVMIAMAIAN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 168 KPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPYT 247
Cdd:COG4170 176 QPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYT 255
|
250 260
....*....|....*....|....
gi 1586794399 248 RLLLSAVPDpdvrFDDP---KARL 268
Cdd:COG4170 256 KALLRSMPD----FRQPlphKSRL 275
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-243 |
6.91e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.44 E-value: 6.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHgsgaVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAaksaEIARYR 85
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----DPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQDPfaSLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARAL 165
Cdd:COG1131 73 RRIGYVPQEP--ALYPDLTVRENLRFFARLYG--LPRKEARERIDELLELFGLTD--AADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 166 AVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPL 243
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-231 |
9.64e-43 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 146.34 E-value: 9.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARY 84
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 85 R-RSVQMIFQdpFASLNPAHTIAHHLRRPLKLHRPEIKgaEIDVAVRELLQRVRLDPDLvaPKYPHELSGGQRQRVNIAR 163
Cdd:TIGR02211 81 RnKKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKSVK--EAKERAYEMLEKVGLEHRI--NHRPSELSGGERQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 164 ALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYvAEDIAVMYAGQIVE 231
Cdd:TIGR02211 155 ALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKK-LDRVLEMKDGQLFN 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
14-243 |
2.86e-42 |
|
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: 145.96 E-value: 2.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 14 TFGHGSGAVhaARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARyRRSVqmIFQ 93
Cdd:COG1120 8 SVGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELAR-RIAY--VPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 DPFAS--LNPAHTIAH----HLRRplkLHRPeikGAEIDVAVRELLQRVRLDpDLvAPKYPHELSGGQRQRVNIARALAV 167
Cdd:COG1120 83 EPPAPfgLTVRELVALgrypHLGL---FGRP---SAEDREAVEEALERTGLE-HL-ADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586794399 168 KPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPL 243
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPEL 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-179 |
5.16e-42 |
|
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: 142.02 E-value: 5.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaKSAEIARYRRSVQMIFQDPFasLNPAHTIAH 107
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL---TDDERKSLRKEIGYVFQDPQ--LFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 108 HLRRPLKLhrPEIKGAEIDVAVRELLQRVRL--DPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTS 179
Cdd:pfam00005 79 NLRLGLLL--KGLSKREKDARAEEALEKLGLgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-242 |
7.89e-42 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 147.53 E-value: 7.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 4 AILALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMamreyL-----PTSGRILYKGRPVeaaks 78
Cdd:COG3839 2 ASLELENVSKSYG----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRM-----IagledPTSGEILIGGRDV----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 79 AEIARYRRSVQMIFQDpFAsLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQR 158
Cdd:COG3839 68 TDLPPKDRNIAMVFQS-YA-LYPHMTVYENIAFPLKLRK--VPKAEIDRRVREAAELLGLED--LLDRKPKQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 159 VNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKV 238
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
....
gi 1586794399 239 IDNP 242
Cdd:COG3839 222 YDRP 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-228 |
1.26e-41 |
|
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: 141.94 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHgsgaVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeAAKSAEIARYR 85
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL-TDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQDPfaSLNPahtiahHLrrplklhrpeikgaeidvAVRELLQrvrldpdlvapkYPheLSGGQRQRVNIARAL 165
Cdd:cd03229 76 RRIGMVFQDF--ALFP------HL------------------TVLENIA------------LG--LSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586794399 166 AVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQ 228
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-233 |
1.27e-41 |
|
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: 143.16 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEiaryr 85
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQDpFAsLNPAHTIAHHLRRPLKL-HRPEikgAEIDVAVRELLQRVRLDPDLvaPKYPHELSGGQRQRVNIARA 164
Cdd:cd03301 72 RDIAMVFQN-YA-LYPHMTVYDNIAFGLKLrKVPK---DEIDERVREVAELLQIEHLL--DRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 165 LAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWG 233
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-254 |
1.51e-41 |
|
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: 144.20 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 4 AILALDSVTKTFGHGSGAvhaaRAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGR---PVEAAKSAE 80
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGC----RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsgaELELYQLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 IAR---YRRSVQMIFQDPFASLNPAHTIAHHL-RRPLKL---HRPEIKGAEIDvavreLLQRVRLDPDLVAPKyPHELSG 153
Cdd:TIGR02323 78 AERrrlMRTEWGFVHQNPRDGLRMRVSAGANIgERLMAIgarHYGNIRATAQD-----WLEEVEIDPTRIDDL-PRAFSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 154 GQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWG 233
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
250 260
....*....|....*....|.
gi 1586794399 234 SVAKVIDNPLHPYTRLLLSAV 254
Cdd:TIGR02323 232 LTDQVLDDPQHPYTQLLVSSI 252
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
11-246 |
1.61e-41 |
|
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: 143.63 E-value: 1.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 11 VTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEiaryrRSVQM 90
Cdd:cd03296 8 VSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 91 IFQD--PFASLNPAHTIAHHLR-RPLKLHRPEikgAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAV 167
Cdd:cd03296 79 VFQHyaLFRHMTVFDNVAFGLRvKPRSERPPE---AEIRAKVHELLKLVQLDW--LADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 168 KPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPY 246
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-242 |
1.79e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 146.45 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARM-AMREYlPTSGRILYKGRPVEAAKSAEiary 84
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiAGLET-PDSGRIVLNGRDLFTNLPPR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 85 RRSVQMIFQDP--FASLNPAHTIAHHLRrplklHRPEIKgAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIA 162
Cdd:COG1118 74 ERRVGFVFQHYalFPHMTVAENIAFGLR-----VRPPSK-AEIRARVEELLELVQLEG--LADRYPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 163 RALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNP 242
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-230 |
1.96e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 143.66 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 4 AILALDSVTKTFGhgsGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIAR 83
Cdd:COG3638 1 PMLELRNLSKRYP---GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 84 YRRSVQMIFQDPfaSLNPAHT---------IAHH--LRRPLKLHRPEikgaEIDVAvRELLQRVRLDPdlVAPKYPHELS 152
Cdd:COG3638 78 LRRRIGMIFQQF--NLVPRLSvltnvlagrLGRTstWRSLLGLFPPE----DRERA-LEALERVGLAD--KAYQRADQLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 153 GGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIV 230
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-248 |
2.02e-40 |
|
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: 141.63 E-value: 2.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 19 SGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYRR-SVQMIFQDpFA 97
Cdd:cd03294 34 TGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQS-FA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 98 sLNPAHTIAHHLRRPLklhrpEIKG---AEIDVAVRELLQRVRLDPDlvAPKYPHELSGGQRQRVNIARALAVKPEVIVA 174
Cdd:cd03294 113 -LLPHRTVLENVAFGL-----EVQGvprAEREERAAEALELVGLEGW--EHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 175 DEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPYTR 248
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVR 258
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
11-229 |
1.32e-39 |
|
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: 137.66 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 11 VTKTFGHgsgaVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKsAEIARYRRSVQM 90
Cdd:cd03262 6 LHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDK-KNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 91 IFQ--DPFASLNPAHTIAHHLRRPLKLHRpeikgAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVK 168
Cdd:cd03262 81 VFQqfNLFPHLTVLENITLAPIKVKGMSK-----AEAEERALELLEKVGLAD--KADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586794399 169 PEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQI 229
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
11-254 |
3.59e-39 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 137.62 E-value: 3.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 11 VTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaakSAEIARyRRSVQM 90
Cdd:TIGR00968 6 ISKRFG----SFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDA----TRVHAR-DRKIGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 91 IFQDpfASLNPAHTIAHHLRRPLKLHRPEikGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPE 170
Cdd:TIGR00968 77 VFQH--YALFKHLTVRDNIAFGLEIRKHP--KAKIKARVEELLELVQLEG--LGDRYPNQLSGGQRQRVALARALAVEPQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 171 VIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPYTRLL 250
Cdd:TIGR00968 151 VLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSF 230
|
....
gi 1586794399 251 LSAV 254
Cdd:TIGR00968 231 LGEV 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-230 |
4.37e-39 |
|
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: 136.66 E-value: 4.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRaLALVGESGSGKTTCARMAMREYLPTSGRILYKGRP-VEAAKSAEIARYRRSVQMIFQDpfASLNPAHTIA 106
Cdd:cd03297 17 IDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlFDSRKKINLPPQQRKIGLVFQQ--YALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 107 HHLRRPLKLHRPeikgAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVR 186
Cdd:cd03297 94 ENLAFGLKRKRN----REDRISVDELLDLLGLDH--LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1586794399 187 LGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIV 230
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-242 |
1.31e-38 |
|
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: 136.32 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 2 TDAILALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEI 81
Cdd:COG0411 1 SDPLLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 82 ARY--RRSvqmiFQDP--FASLnpahT------IAHHLRRP-------LKLHRPEIKGAEIDVAVRELLQRVRLDPdlVA 144
Cdd:COG0411 77 ARLgiART----FQNPrlFPEL----TvlenvlVAAHARLGrgllaalLRLPRARREEREARERAEELLERVGLAD--RA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 145 PKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVM 224
Cdd:COG0411 147 DEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVL 226
|
250
....*....|....*...
gi 1586794399 225 YAGQIVEWGSVAKVIDNP 242
Cdd:COG0411 227 DFGRVIAEGTPAEVRADP 244
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-234 |
6.83e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 134.87 E-value: 6.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 14 TFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKG-RPVEAAKSAEIaryRRSVQMIF 92
Cdd:TIGR04520 7 SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEI---RKKVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 93 QDP---FASLNPAHTIAHHLRRpLKLHRPEIKgaEIdvaVRELLQRVRLDPDLVAPkyPHELSGGQRQRVNIARALAVKP 169
Cdd:TIGR04520 84 QNPdnqFVGATVEDDVAFGLEN-LGVPREEMR--KR---VDEALKLVGMEDFRDRE--PHLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586794399 170 EVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYvAEDIAVMYAGQIVEWGS 234
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGT 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-244 |
7.70e-38 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 133.85 E-value: 7.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHGsgaVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYR 85
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQDP-------------FASLNPAHTIAHHLRRplkLHRPEIKGAeidvavRELLQRVRLDPDlvAPKYPHELS 152
Cdd:cd03256 78 RQIGMIFQQFnlierlsvlenvlSGRLGRRSTWRSLFGL---FPKEEKQRA------LAALERVGLLDK--AYQRADQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 153 GGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEW 232
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFD 226
|
250
....*....|..
gi 1586794399 233 GSVAKVIDNPLH 244
Cdd:cd03256 227 GPPAELTDEVLD 238
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-242 |
2.89e-37 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 132.18 E-value: 2.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARY- 84
Cdd:cd03219 1 LEVRGLTKRFG----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 85 -RRSvqmiFQDP--FASL----NPAHTIAHHLRRPLKLHRPEIKGAEIDVAVRELLQRVRLDPDLVAPkyPHELSGGQRQ 157
Cdd:cd03219 77 iGRT----FQIPrlFPELtvleNVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRP--AGELSYGQQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 158 RVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAK 237
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
....*
gi 1586794399 238 VIDNP 242
Cdd:cd03219 230 VRNNP 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-248 |
3.54e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 132.85 E-value: 3.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 20 GAVHAARAISFSLHAGRALALVGESGSGKTT---C-ARM-AMREYLPTSGRILYKGRPVeAAKSAEIARYRRSVQMIFQD 94
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTllrClNRMnDLIPGARVEGEILLDGEDI-YDPDVDVVELRRRVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 95 PfaslNP-AHTIAHHLRRPLKLHrpEIKG-AEIDVAVRELLQRV--------RLDpdlvapKYPHELSGGQRQRVNIARA 164
Cdd:COG1117 101 P----NPfPKSIYDNVAYGLRLH--GIKSkSELDEIVEESLRKAalwdevkdRLK------KSALGLSGGQQQRLCIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 165 LAVKPEVIVADEPTSMLD-VSVrLGVLNLLNEMKRElnlgllY----ITHDIATARYVAEDIAVMYAGQIVEWGSVAKVI 239
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDpIST-AKIEELILELKKD------YtiviVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
....*....
gi 1586794399 240 DNPLHPYTR 248
Cdd:COG1117 242 TNPKDKRTE 250
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-238 |
2.98e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.91 E-value: 2.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTktFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAE 80
Cdd:PRK13635 1 MKEEIIRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 IaryRRSVQMIFQDP---FASLNPAHTIAHHLR-----RPLKLHRpeikgaeidvaVRELLQRVRLDPdlVAPKYPHELS 152
Cdd:PRK13635 79 V---RRQVGMVFQNPdnqFVGATVQDDVAFGLEnigvpREEMVER-----------VDQALRQVGMED--FLNREPHRLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 153 GGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYvAEDIAVMYAGQIVEW 232
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
....*.
gi 1586794399 233 GSVAKV 238
Cdd:PRK13635 222 GTPEEI 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-236 |
4.94e-36 |
|
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: 129.21 E-value: 4.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 8 LDSVTKTFGHgsgaVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAaksaEIARYRRS 87
Cdd:COG4555 4 VENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK----EPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 88 VQMIFQDPFasLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPDLVapKYPHELSGGQRQRVNIARALAV 167
Cdd:COG4555 76 IGVLPDERG--LYDRLTVRENIRYFAELYG--LFDEELKKRIEELIELLGLEEFLD--RRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 168 KPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVA 236
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLD 217
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-240 |
1.15e-35 |
|
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: 128.57 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHGsgaVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARY 84
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 85 RRSVQMIFQDpFASLNPAHTIAHHLRRPLKLHrPEIKG-------AEIDVAVrELLQRVRLDpDLvAPKYPHELSGGQRQ 157
Cdd:TIGR02315 78 RRRIGMIFQH-YNLIERLTVLENVLHGRLGYK-PTWRSllgrfseEDKERAL-SALERVGLA-DK-AYQRADQLSGGQQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 158 RVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAK 237
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSE 232
|
...
gi 1586794399 238 VID 240
Cdd:TIGR02315 233 LDD 235
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
26-242 |
3.11e-35 |
|
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: 127.07 E-value: 3.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaksAEIARYRRSVQMIFQDP--FASLNPAH 103
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-----TNLPPEKRDISYVPQNYalFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLRRpLKLHRPEIKGAEIDVA----VRELLQRvrldpdlvapkYPHELSGGQRQRVNIARALAVKPEVIVADEPTS 179
Cdd:cd03299 91 NIAYGLKK-RKVDKKEIERKVLEIAemlgIDHLLNR-----------KPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586794399 180 MLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNP 242
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-230 |
3.32e-35 |
|
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: 125.24 E-value: 3.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 14 TFGHGSGAVhaARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARyRRSVqmifq 93
Cdd:cd03214 6 SVGYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR-KIAY----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 dpfaslnpahtiahhlrrplklhrpeikgaeidvaVRELLQRVRLDpDLvAPKYPHELSGGQRQRVNIARALAVKPEVIV 173
Cdd:cd03214 78 -----------------------------------VPQALELLGLA-HL-ADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586794399 174 ADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIV 230
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-231 |
3.93e-35 |
|
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: 126.78 E-value: 3.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCAR-MAMREyLPTSGRILYKGRPVEAAKSA 79
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGlLAGLD-RPTSGTVRLAGQDLFALDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 80 EIARYR-RSVQMIFQDpFaSLNPAHTIAHHLRRPLKL--HRPEIKGAeidvavRELLQRV----RLDpdlvapKYPHELS 152
Cdd:COG4181 83 ARARLRaRHVGFVFQS-F-QLLPTLTALENVMLPLELagRRDARARA------RALLERVglghRLD------HYPAQLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 153 GGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYvAEDIAVMYAGQIVE 231
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-253 |
6.58e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.02 E-value: 6.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHgsgavHAARAiSFSLHAGRALALVGESGSGKTTcarmamreyL---------PTSGRILYKGRPVeaa 76
Cdd:COG3840 2 LRLDDLTYRYGD-----FPLRF-DLTIAAGERVAILGPSGAGKST---------LlnliagflpPDSGRILWNGQDL--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 77 ksAEIARYRRSVQMIFQDP--FASLNPAHTIAHHLRRPLKLHRPEIKgaeidvAVRELLQRVRLDpDLvAPKYPHELSGG 154
Cdd:COG3840 64 --TALPPAERPVSMLFQENnlFPHLTVAQNIGLGLRPGLKLTAEQRA------QVEQALERVGLA-GL-LDRLPGQLSGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 155 QRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGS 234
Cdd:COG3840 134 QRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGP 213
|
250
....*....|....*....
gi 1586794399 235 VAKVIDNPLHPYTRLLLSA 253
Cdd:COG3840 214 TAALLDGEPPPALAAYLGI 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-252 |
6.64e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 126.79 E-value: 6.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 8 LDSVTKTFgHGSGAVHAaraISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRI------LYKGRPVEAAKSAeI 81
Cdd:PRK11264 6 VKNLVKKF-HGQTVLHG---IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLSQQKGL-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 82 ARYRRSVQMIFQDpfASLNPAHTIAHHLRRPLKLHRPEIKGAEIDVAvRELLQRVRLDPDLVApkYPHELSGGQRQRVNI 161
Cdd:PRK11264 81 RQLRQHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARA-RELLAKVGLAGKETS--YPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 162 ARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDN 241
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
250
....*....|.
gi 1586794399 242 PLHPYTRLLLS 252
Cdd:PRK11264 235 PQQPRTRQFLE 245
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-247 |
2.22e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 125.41 E-value: 2.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 20 GAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMR--EYLP---TSGRILYKGRPVEAAKSAEIaryRRSVQMIFQD 94
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPearVSGEVYLDGQDIFKMDVIEL---RRRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 95 PfaslNPAHT--IAHHLRRPLKLHRPEIKGAEIDVAVRELLQRVRLDPD----LVAPKypHELSGGQRQRVNIARALAVK 168
Cdd:PRK14247 91 P----NPIPNlsIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEvkdrLDAPA--GKLSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 169 PEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLlyITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPYT 247
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKKDMTIVL--VTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
11-228 |
5.03e-34 |
|
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: 121.58 E-value: 5.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 11 VTKTFGHGsgavHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEiarYRRSVQM 90
Cdd:cd00267 5 LSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---LRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 91 IFQdpfaslnpahtiahhlrrplklhrpeikgaeidvavrellqrvrldpdlvapkypheLSGGQRQRVNIARALAVKPE 170
Cdd:cd00267 78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 171 VIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQ 228
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-246 |
5.68e-34 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 126.69 E-value: 5.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 3 DAILALDSVTKTFGHGSgavhAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAeia 82
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFT----ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 83 ryRRSVQMIFQD--PFASLNPAHTIAHhlrrplKLHRPEIKGAEIDVAVRELLQRVRLdPDlVAPKYPHELSGGQRQRVN 160
Cdd:TIGR03265 75 --KRDYGIVFQSyaLFPNLTVADNIAY------GLKNRGMGRAEVAERVAELLDLVGL-PG-SERKYPGQLSGGQQQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 161 IARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVID 240
Cdd:TIGR03265 145 LARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYR 224
|
....*.
gi 1586794399 241 NPLHPY 246
Cdd:TIGR03265 225 HPATPF 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-242 |
6.62e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 126.74 E-value: 6.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHgsgaVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaakSAEIARYR 85
Cdd:PRK10851 3 IEIANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV----SRLHARDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RsVQMIFQD--PFASLNPAHTIAHHLRRPLKLHRPEikGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIAR 163
Cdd:PRK10851 75 K-VGFVFQHyaLFRHMTVFDNIAFGLTVLPRRERPN--AAAIKAKVTQLLEMVQLAH--LADRYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 164 ALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNP 242
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-242 |
1.05e-33 |
|
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: 124.10 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 8 LDSVTKTFGHGSGAVHAA-RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYRR 86
Cdd:TIGR04521 3 LKNVSYIYQPGTPFEKKAlDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 87 SVQMIFQdpfaslNPAH-----TIAHHLR---RPLKLhrpeiKGAEIDVAVRELLQRVRLDPDLVApKYPHELSGGQRQR 158
Cdd:TIGR04521 83 KVGLVFQ------FPEHqlfeeTVYKDIAfgpKNLGL-----SEEEAEERVKEALELVGLDEEYLE-RSPFELSGGQMRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 159 VNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKV 238
Cdd:TIGR04521 151 VAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
....
gi 1586794399 239 IDNP 242
Cdd:TIGR04521 231 FSDV 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-249 |
2.13e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 122.51 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 10 SVTKTFGHgsgaVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKsAEIARYRRSVQ 89
Cdd:PRK09493 6 NVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPK-VDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 90 MIFQ--DPFASLNPAHTIAHHLRRPLKLHRpeikgAEIDVAVRELLQRVRLDPDlvAPKYPHELSGGQRQRVNIARALAV 167
Cdd:PRK09493 81 MVFQqfYLFPHLTALENVMFGPLRVRGASK-----EEAEKQARELLAKVGLAER--AHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 168 KPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPlhPYT 247
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP--PSQ 230
|
..
gi 1586794399 248 RL 249
Cdd:PRK09493 231 RL 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-229 |
2.20e-33 |
|
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: 120.20 E-value: 2.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHGsgavHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaakSAEIARYR 85
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQDPfaSLNPahtiahHLRrplklhrpeikgaeidvaVRELLqrvrldpdlvapkyphELSGGQRQRVNIARAL 165
Cdd:cd03230 73 RRIGYLPEEP--SLYE------NLT------------------VRENL----------------KLSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 166 AVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQI 229
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-214 |
2.39e-33 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 121.18 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 8 LDSVTKTFGHgsgaVHAARAISFSLHAGRALALVGESGSGKTTCARM-AMREYlPTSGRILYKGRPVEAAKSAEIARYRR 86
Cdd:TIGR03608 1 LKNISKKFGD----KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIiGLLEK-FDSGQVYLNGQETPPLNSKKASKFRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 87 S-VQMIFQDpFAsLNPAHTIAHHLRRPLKLHRPEIKgaEIDVAVRELLQRVRLDPDLvaPKYPHELSGGQRQRVNIARAL 165
Cdd:TIGR03608 76 EkLGYLFQN-FA-LIENETVEENLDLGLKYKKLSKK--EKREKKKEALEKVGLNLKL--KQKIYELSGGEQQRVALARAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1586794399 166 AVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATA 214
Cdd:TIGR03608 150 LKPPPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVA 197
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-242 |
3.86e-33 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 123.76 E-value: 3.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 40 LVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaksAEIARYRRSVQMIFQDpfASLNPAHTIAHHLRRPLKLHRpe 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-----TNVPPHLRHINMVFQS--YALFPHMTVEENVAFGLKMRK-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 120 IKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRE 199
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQLEE--FADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1586794399 200 LNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNP 242
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-256 |
5.63e-33 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 123.76 E-value: 5.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCAR----MAMREYLPTSGRILYKGrpVEAAKSAE 80
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKaicgVTKDNWRVTADRMRFDD--IDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 IARYR---RSVQMIFQDPFASLNPAHTIAHHLRRPL-----KLHRPEIKGAEIDVAVrELLQRVRL-DPDLVAPKYPHEL 151
Cdd:PRK15093 81 RERRKlvgHNVSMIFQEPQSCLDPSERVGRQLMQNIpgwtyKGRWWQRFGWRKRRAI-ELLHRVGIkDHKDAMRSFPYEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 152 SGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVE 231
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
250 260
....*....|....*....|....*
gi 1586794399 232 WGSVAKVIDNPLHPYTRLLLSAVPD 256
Cdd:PRK15093 240 TAPSKELVTTPHHPYTQALIRAIPD 264
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-231 |
1.78e-32 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 120.74 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 4 AILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAkSAEiar 83
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP-GAD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 84 yrRSVqmIFQDpfASLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIAR 163
Cdd:COG4525 78 --RGV--VFQK--DALLPWLNVLDNVAFGLRLRG--VPKAERRARAEELLALVGLAD--FARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 164 ALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVM--YAGQIVE 231
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-249 |
2.47e-32 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 126.10 E-value: 2.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 14 TFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaKSAEIARYRRSVQMIFQ 93
Cdd:COG2274 480 SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL---RQIDPASLRRQIGVVLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 DP--FASlnpahTIAHHLRrplkLHRPEIKgaeiDVAVRELLQRVRLDPDLVA-PK-YPHE-------LSGGQRQRVNIA 162
Cdd:COG2274 557 DVflFSG-----TIRENIT----LGDPDAT----DEEIIEAARLAGLHDFIEAlPMgYDTVvgeggsnLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 163 RALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRelNLGLLYITHDIATARYvAEDIAVMYAGQIVEWGSVAKVIDNP 242
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARK 700
|
....*..
gi 1586794399 243 LHpYTRL 249
Cdd:COG2274 701 GL-YAEL 706
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-224 |
2.64e-32 |
|
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: 119.08 E-value: 2.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTdAILALDSVTKTF---GHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYK--GRPVEA 75
Cdd:COG4778 1 MT-TLLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 76 AKSA--EIARYRRsvqmifqdpfaslnpaHTIAH---HLR------------RPLkLHRpeikGAEIDVA---VRELLQR 135
Cdd:COG4778 80 AQASprEILALRR----------------RTIGYvsqFLRviprvsaldvvaEPL-LER----GVDREEArarARELLAR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 136 VRLDPDLvAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATAR 215
Cdd:COG4778 139 LNLPERL-WDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVRE 216
|
....*....
gi 1586794399 216 YVAEDIAVM 224
Cdd:COG4778 217 AVADRVVDV 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-228 |
3.13e-32 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 117.10 E-value: 3.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 14 TFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaKSAEIARYRRSVQMIFQ 93
Cdd:cd03228 7 SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL---RDLDLESLRKNIAYVPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 DP--FASlnpahTIAHHLrrplklhrpeikgaeidvavrellqrvrldpdlvapkypheLSGGQRQRVNIARALAVKPEV 171
Cdd:cd03228 84 DPflFSG-----TIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586794399 172 IVADEPTSMLDVSVRLGVLNLLNEMKRelNLGLLYITHDIATARYvAEDIAVMYAGQ 228
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
11-194 |
4.30e-32 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 118.28 E-value: 4.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 11 VTKTFGHGSGAVHAaraISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYRRSVQM 90
Cdd:cd03292 6 VTKTYPNGTAALDG---INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 91 IFQDpfASLNPAHTIAHHLRRPLKLhrPEIKGAEIDVAVRELLQRVRLDPDlvAPKYPHELSGGQRQRVNIARALAVKPE 170
Cdd:cd03292 83 VFQD--FRLLPDRNVYENVAFALEV--TGVPPREIRKRVPAALELVGLSHK--HRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180
....*....|....*....|....
gi 1586794399 171 VIVADEPTSMLDVSVRLGVLNLLN 194
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLK 180
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-230 |
4.44e-32 |
|
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: 116.76 E-value: 4.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEiARyR 85
Cdd:cd03216 1 LELRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-AR-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQdpfaslnpahtiahhlrrplklhrpeikgaeidvavrellqrvrldpdlvapkypheLSGGQRQRVNIARAL 165
Cdd:cd03216 75 AGIAMVYQ---------------------------------------------------------LSVGERQMVEIARAL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586794399 166 AVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIV 230
Cdd:cd03216 98 ARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-230 |
9.32e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 123.21 E-value: 9.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAE 80
Cdd:COG3845 1 MMPPALELRGITKRFG----GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 iARyRRSVQMIFQDPfaSLNPAHTIAHHL---RRPLKLHRPEIKGAEidVAVRELLQR--VRLDPDlvapKYPHELSGGQ 155
Cdd:COG3845 77 -AI-ALGIGMVHQHF--MLVPNLTVAENIvlgLEPTKGGRLDRKAAR--ARIRELSERygLDVDPD----AKVEDLSVGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586794399 156 RQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIV 230
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-238 |
1.17e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.82 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 2 TDAILALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEi 81
Cdd:COG1129 1 AEPLLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 82 ARyRRSVQMIFQDPfaSLNPAHTIA------HHLRRPLKLHRPEIKgaeidVAVRELLQRV--RLDPD-LVApkyphELS 152
Cdd:COG1129 76 AQ-AAGIAIIHQEL--NLVPNLSVAeniflgREPRRGGLIDWRAMR-----RRARELLARLglDIDPDtPVG-----DLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 153 GGQRQRVNIARALAVKPEVIVADEPTSMLDVS--VRLgvLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIV 230
Cdd:COG1129 143 VAQQQLVEIARALSRDARVLILDEPTASLTERevERL--FRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
....*...
gi 1586794399 231 EWGSVAKV 238
Cdd:COG1129 220 GTGPVAEL 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
1.50e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 118.32 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTktFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAE 80
Cdd:PRK13648 3 DKNSIIVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 IaryRRSVQMIFQDP---FASLNPAHTIAHHLRRPL----KLHRpEIKGAEIDVavrELLQRvrldpdlvAPKYPHELSG 153
Cdd:PRK13648 81 L---RKHIGIVFQNPdnqFVGSIVKYDVAFGLENHAvpydEMHR-RVSEALKQV---DMLER--------ADYEPNALSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 154 GQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYvAEDIAVMYAGQIVEWG 233
Cdd:PRK13648 146 GQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEG 224
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-228 |
2.11e-31 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 116.58 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGhgsGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARY 84
Cdd:TIGR02673 1 MIEFHNVSKAYP---GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 85 RRSVQMIFQDpfASLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPDLVApkYPHELSGGQRQRVNIARA 164
Cdd:TIGR02673 78 RRRIGVVFQD--FRLLPDRTVYENVALPLEVRG--KKEREIQRRVGAALRQVGLEHKADA--FPEQLSGGEQQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 165 LAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKReLNLGLLYITHDIATARYVAEDIAVMYAGQ 228
Cdd:TIGR02673 152 IVNSPPLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
5-230 |
3.26e-31 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 116.27 E-value: 3.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARM--AMREylPTSGRILYKGRPVEAAKSAEIA 82
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLigGLRS--VQEGSLKVLGQELHGASKKQLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 83 RYRRSVQMIFQDpfASLNPAHTIAHHLRRPLKLHrPEIKGAEIDVAVRELLQRVRLDPDLvaPKYPHELSGGQRQRVNIA 162
Cdd:TIGR02982 79 QLRRRIGYIFQA--HNLLGFLTARQNVQMALELQ-PNLSYQEARERARAMLEAVGLGDHL--NYYPHNLSGGQKQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 163 RALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDiatARY--VAEDIAVMYAGQIV 230
Cdd:TIGR02982 154 RALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD---NRIldVADRILQMEDGKLL 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-215 |
3.96e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 116.45 E-value: 3.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARY 84
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 85 R-RSVQMIFQdpFASLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPDlvAPKYPHELSGGQRQRVNIAR 163
Cdd:PRK11629 85 RnQKLGFIYQ--FHHLLPDFTALENVAMPLLIGK--KKPAEINSRALEMLAAVGLEHR--ANHRPSELSGGERQRVAIAR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1586794399 164 ALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATAR 215
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAK 210
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-274 |
9.94e-31 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 117.90 E-value: 9.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGhgSGAVhaARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEaaksae 80
Cdd:PRK11432 2 TQKNFVVLKNITKRFG--SNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 iaryRRSVQ-----MIFQDpfASLNPAHTIAHHLRRPLK-LHRPEikgAEIDVAVRELLQRVRLDPdlVAPKYPHELSGG 154
Cdd:PRK11432 72 ----HRSIQqrdicMVFQS--YALFPHMSLGENVGYGLKmLGVPK---EERKQRVKEALELVDLAG--FEDRYVDQISGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 155 QRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGS 234
Cdd:PRK11432 141 QQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGS 220
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1586794399 235 VAKVIdnpLHPYTRLLLSAVPDPDVrFDdpkARLRPDEVE 274
Cdd:PRK11432 221 PQELY---RQPASRFMASFMGDANI-FP---ATLSGDYVD 253
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-242 |
1.00e-30 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 115.67 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCAR-MAMREyLPTSGRILYKGRPV----------E 74
Cdd:COG4598 9 LEVRDLHKSFG----DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRcINLLE-TPDSGEIRVGGEEIrlkpdrdgelV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 75 AAKSAEIARYRRSVQMIFQdpfaSLNP-AH-TI--------AHHLRRPlklhrpeiKGAEIDVAvRELLQRVRLDPdlVA 144
Cdd:COG4598 84 PADRRQLQRIRTRLGMVFQ----SFNLwSHmTVlenvieapVHVLGRP--------KAEAIERA-EALLAKVGLAD--KR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 145 PKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLD---VSVRLGVLNLLNEMKRElnlgLLYITHDIATARYVAEDI 221
Cdd:COG4598 149 DAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDpelVGEVLKVMRDLAEEGRT----MLVVTHEMGFARDVSSHV 224
|
250 260
....*....|....*....|.
gi 1586794399 222 AVMYAGQIVEWGSVAKVIDNP 242
Cdd:COG4598 225 VFLHQGRIEEQGPPAEVFGNP 245
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
28-242 |
1.28e-30 |
|
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: 117.89 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMA---MReylPTSGRILYKGRP-VEAAKSAEIARYRRSVQMIFQDpfASLNPAH 103
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEVlQDSARGIFLPPHRRRIGYVFQE--ARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLRRPLKLHRPEIKGAEIDVAVR-----ELLQRvrldpdlvapkYPHELSGGQRQRVNIARALAVKPEVIVADEPT 178
Cdd:COG4148 93 SVRGNLLYGRKRAPRAERRISFDEVVEllgigHLLDR-----------RPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 179 SMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNP 242
Cdd:COG4148 162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
28-234 |
3.23e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 119.50 E-value: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaKSAEIARYRRSVQMIFQDP--FASlnpahTI 105
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI---RDLTLESLRRQIGVVPQDTflFSG-----TI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 106 AHHLRrplkLHRPEIKGAEidvaVRELLQRVRLDpDLVApKYPH-----------ELSGGQRQRVNIARALAVKPEVIVA 174
Cdd:COG1132 431 RENIR----YGRPDATDEE----VEEAAKAAQAH-EFIE-ALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 175 DEPTSMLDVSVRLGVLNLLNEMKRelNLGLLYITHDIATARYvAEDIAVMYAGQIVEWGS 234
Cdd:COG1132 501 DEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-238 |
3.54e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.94 E-value: 3.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGHGSgavHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAe 80
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGT---HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 IARYRRSVQMIFQDPFASLNPAHTIAHHLRRPLKLHRPEikgAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVN 160
Cdd:PRK13636 77 LMKLRESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPE---DEVRKRVDNALKRTGIEH--LKDKPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 161 IARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKV 238
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-292 |
3.56e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 115.21 E-value: 3.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIA-- 82
Cdd:COG4152 1 MLELKGLTKRFG----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 83 ---R--YRR-SV--QMIFqdpFASLnpahtiaHHLRRplklhrpeikgAEIDVAVRELLQRVRLDP---DLVapkypHEL 151
Cdd:COG4152 77 peeRglYPKmKVgeQLVY---LARL-------KGLSK-----------AEAKRRADEWLERLGLGDranKKV-----EEL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 152 SGGQRQRVNIARALAVKPEVIVADEPTSMLD-VSVRLgVLNLLNEMKRElnlG--LLYITHDIATARYVAEDIAVMYAGQ 228
Cdd:COG4152 131 SKGNQQKVQLIAALLHDPELLILDEPFSGLDpVNVEL-LKDVIRELAAK---GttVIFSSHQMELVEELCDRIVIINKGR 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586794399 229 IVEWGSVAKVIDNplHPYTRLLLSAVPDP----------DVRFDDPKARLRPDEVEDIRR--RSAMPQDDIVEFEQ 292
Cdd:COG4152 207 KVLSGSVDEIRRQ--FGRNTLRLEADGDAgwlralpgvtVVEEDGDGAELKLEDGADAQEllRALLARGPVREFEE 280
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-236 |
4.24e-30 |
|
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: 119.09 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTktFGHGSGAVhAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryR 85
Cdd:COG4988 337 IELEDVS--FSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---R 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQDPFasLnPAHTIAHHLRrplkLHRPEIKGAEIdvavRELLQRVRLDpDLVApKYPHE-----------LSGG 154
Cdd:COG4988 411 RQIAWVPQNPY--L-FAGTIRENLR----LGRPDASDEEL----EAALEAAGLD-EFVA-ALPDGldtplgeggrgLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 155 QRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRelNLGLLYITHDIATARYvAEDIAVMYAGQIVEWGS 234
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGT 554
|
..
gi 1586794399 235 VA 236
Cdd:COG4988 555 HE 556
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-233 |
4.81e-30 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 113.57 E-value: 4.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 20 GAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPV---EAAKSAEIARYRRSVQMIFQDpf 96
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELRRNVGMVFQQ-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 97 ASLNPAHTIAHHL----RRPLKLHRPE-IKGAEidvavrELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEV 171
Cdd:PRK11124 91 YNLWPHLTVQQNLieapCRVLGLSKDQaLARAE------KLLERLRLKP--YADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586794399 172 IVADEPTSMLDVSVRLGVLNLLNEMkRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWG 233
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
24-242 |
6.28e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.02 E-value: 6.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 24 AARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIArYRRSVQMIFQDPFASLNpAH 103
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLE-VRKTVGIVFQNPDDQLF-AP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLR-RPLKLHRPEikgAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLD 182
Cdd:PRK13639 95 TVEEDVAfGPLNLGLSK---EEVEKRVKEALKAVGMEG--FENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586794399 183 VSVRLGVLNLLNEMKRElnlGLLYI--THDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNP 242
Cdd:PRK13639 170 PMGASQIMKLLYDLNKE---GITIIisTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-249 |
1.10e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 115.70 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaksAEIARY 84
Cdd:PRK11607 19 LLEIRNLTKSFD----GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-----SHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 85 RRSVQMIFQDpfASLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARA 164
Cdd:PRK11607 90 QRPINMMFQS--YALFPHMTVEQNIAFGLKQDK--LPKAEIASRVNEMLGLVHMQE--FAKRKPHQLSGGQRQRVALARS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 165 LAVKPEVIVADEPTSMLDVSVR----LGVLNLLnemkRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVID 240
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRdrmqLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
....*....
gi 1586794399 241 nplHPYTRL 249
Cdd:PRK11607 240 ---HPTTRY 245
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
28-243 |
1.30e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 112.90 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARyRRSV-----QMIFqdPFaslnPA 102
Cdd:COG4559 20 VSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELAR-RRAVlpqhsSLAF--PF----TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 103 HTIAHHLRRPlklHRPEikGAEIDVAVRELLQRVRLDpDLVAPKYPhELSGGQRQRVNIARALA-------VKPEVIVAD 175
Cdd:COG4559 93 EEVVALGRAP---HGSS--AAQDRQIVREALALVGLA-HLAGRSYQ-TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 176 EPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDI-ATARYvAEDIAVMYAGQIVEWGSVAKVIDNPL 243
Cdd:COG4559 166 EPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLnLAAQY-ADRILLLHQGRLVAQGTPEEVLTDEL 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-234 |
1.31e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.43 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGHGSgavhAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeAAKSAE 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 iaryRRSVQMIFQDpFAsLNPAHTIAHHLRRPLKLHR-PEikgAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRV 159
Cdd:PRK09452 85 ----NRHVNTVFQS-YA-LFPHMTVFENVAFGLRMQKtPA---AEITPRVMEALRMVQLEE--FAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586794399 160 NIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGS 234
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-240 |
1.46e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 112.49 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGHgsgaVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSaE 80
Cdd:COG1121 2 MMMPAIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 IArY---RRSVQMIFqdpfaslnPAH---TIAHHLRRPLKLHRPeiKGAEIDVAVRELLQRVRLDpDLvAPKYPHELSGG 154
Cdd:COG1121 77 IG-YvpqRAEVDWDF--------PITvrdVVLMGRYGRRGLFRR--PSRADREAVDEALERVGLE-DL-ADRPIGELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 155 QRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMyAGQIVEWGS 234
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGP 221
|
....*.
gi 1586794399 235 VAKVID 240
Cdd:COG1121 222 PEEVLT 227
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-234 |
1.85e-29 |
|
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: 117.17 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 2 TDAILALDSVTktFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEI 81
Cdd:COG4987 330 GGPSLELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 82 aryRRSVQMIFQDP--FASlnpahTIAHHLRrplkLHRPEIKgaeiDVAVRELLQRVRLDpDLVApKYPHEL-------- 151
Cdd:COG4987 408 ---RRRIAVVPQRPhlFDT-----TLRENLR----LARPDAT----DEELWAALERVGLG-DWLA-ALPDGLdtwlgegg 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 152 ---SGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRelNLGLLYITHDIATARYVAEdIAVMYAGQ 228
Cdd:COG4987 470 rrlSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDR-ILVLEDGR 546
|
....*.
gi 1586794399 229 IVEWGS 234
Cdd:COG4987 547 IVEQGT 552
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-247 |
3.51e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 111.68 E-value: 3.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMR------EYLPTSGRILYKGRPVEAAKSAEIaryRRSVQMIFQ--DPFA 97
Cdd:PRK14246 27 KDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiydSKIKVDGKVLYFGKDIFQIDAIKL---RKEVGMVFQqpNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 98 SLNPAHTIAHhlrrPLKLHRPEIKgAEIDVAVRELLQRVRLDPD----LVAPKypHELSGGQRQRVNIARALAVKPEVIV 173
Cdd:PRK14246 104 HLSIYDNIAY----PLKSHGIKEK-REIKKIVEECLRKVGLWKEvydrLNSPA--SQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 174 ADEPTSMLDVSVRLGVLNLLNEMKRELNLGLlyITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPYT 247
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVI--VSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-237 |
4.06e-29 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 110.67 E-value: 4.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGhgSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaakSAEIARYR 85
Cdd:cd03263 1 LQIRNLTKTYK--KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQdpFASLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARAL 165
Cdd:cd03263 75 QSLGYCPQ--FDALFDELTVREHLRFYARLKG--LPKSEIKEEVELLLRVLGLTD--KANKRARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586794399 166 AVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRelNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAK 237
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-247 |
9.98e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 110.32 E-value: 9.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 20 GAVHAARAISFSLHAGRALALVGESGSGKTTCAR-----MAMREYLPTSGRILYKGRPVEAAKSAEIaRYRRSVQMIFQ- 93
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPDVDPI-EVRREVGMVFQy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 -DPFaslnPAHTIAHHLRRPLKLHRPEIKGAEIDVAVRELLQRVRLdPDLVAPK---YPHELSGGQRQRVNIARALAVKP 169
Cdd:PRK14267 94 pNPF----PHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAAL-WDEVKDRlndYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 170 EVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLlyITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPYT 247
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKEYTIVL--VTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
28-239 |
1.27e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 110.25 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYR----RSVQMIFqdPFaslnPAH 103
Cdd:PRK13548 21 VSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRavlpQHSSLSF--PF----TVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLRRPLKLHRpeikgAEIDVAVRELLQRVRLDpDLVAPKYPhELSGGQRQRVNIARALA------VKPEVIVADEP 177
Cdd:PRK13548 95 EVVAMGRAPHGLSR-----AEDDALVAAALAQVDLA-HLAGRDYP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586794399 178 TSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIA-TARYvAEDIAVMYAGQIVEWGSVAKVI 239
Cdd:PRK13548 168 TSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNlAARY-ADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-235 |
2.03e-28 |
|
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: 108.61 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 20 GAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaakSAEIARYRRSVQMIFQDPfaSL 99
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV----VREPREVRRRIGIVFQDL--SV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 100 NPAHTIAHHLRRPLKLHrpEIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTS 179
Cdd:cd03265 85 DDELTGWENLYIHARLY--GVPGAERRERIDELLDFVGLLE--AADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586794399 180 MLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSV 235
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
28-242 |
2.22e-28 |
|
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: 112.01 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLP--TSGRILYKGRPVEAAKSaeiarYRRSVQMIFQDpfASLNPAHTI 105
Cdd:TIGR03258 24 LSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLTHAPP-----HKRGLALLFQN--YALFPHLKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 106 AHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSV 185
Cdd:TIGR03258 97 EDNVAFGLRAQK--MPKADIAERVADALKLVGLGD--AAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDANI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 186 RLGVLNLLNEMKREL-NLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNP 242
Cdd:TIGR03258 173 RANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAP 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-233 |
2.35e-28 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 108.14 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIAR-- 83
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYlp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 84 -----YR-RSV--QMIFqdpFASLnpahtiahhlrRPLKLHrpeikgaEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQ 155
Cdd:cd03269 77 eerglYPkMKVidQLVY---LAQL-----------KGLKKE-------EARRRIDEWLERLELSE--YANKRVEELSKGN 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 156 RQRVNIARALAVKPEVIVADEPTSMLD-VSVRLgVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVEWG 233
Cdd:cd03269 134 QQKVQFIAAVIHDPELLILDEPFSGLDpVNVEL-LKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-242 |
2.39e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 110.27 E-value: 2.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTktFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTS---GRILYKGRPVEAAK 77
Cdd:PRK13640 1 MKDNIVEFKHVS--FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 78 SAEIaryRRSVQMIFQDP---FASLNPAHTIAHHLRRPlKLHRPEIKGaeidvAVRELLQRV-RLDPDLVAPKYpheLSG 153
Cdd:PRK13640 79 VWDI---REKVGIVFQNPdnqFVGATVGDDVAFGLENR-AVPRPEMIK-----IVRDVLADVgMLDYIDSEPAN---LSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 154 GQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARyVAEDIAVMYAGQIVEWG 233
Cdd:PRK13640 147 GQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQG 225
|
....*....
gi 1586794399 234 SVAKVIDNP 242
Cdd:PRK13640 226 SPVEIFSKV 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-246 |
5.08e-28 |
|
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: 110.59 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPV-EAAKSAEIARYRRSVQMIFQDpfASLNPAHTIA 106
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfDSRKGIFLPPEKRRIGYVFQE--ARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 107 HHLRRPLKLHRPEIKGAEIDvAVRELLQrvrLDPDLVapKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVR 186
Cdd:TIGR02142 94 GNLRYGMKRARPSERRISFE-RVIELLG---IGHLLG--RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 187 LGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPY 246
Cdd:TIGR02142 168 YEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
26-234 |
8.48e-28 |
|
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: 107.63 E-value: 8.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaKSAEIARYRRSVQMIFQDP--FASlnpah 103
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI---RDLNLRWLRSQIGLVSQEPvlFDG----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLRrplkLHRPEIKGAEIDVAVR--ELLQRVRLDPD----LVAPKYPhELSGGQRQRVNIARALAVKPEVIVADEP 177
Cdd:cd03249 92 TIAENIR----YGKPDATDEEVEEAAKkaNIHDFIMSLPDgydtLVGERGS-QLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586794399 178 TSMLDVSVRLGVLNLLNEMKRelNLGLLYITHDIATARYvAEDIAVMYAGQIVEWGS 234
Cdd:cd03249 167 TSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-234 |
1.18e-27 |
|
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: 106.93 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 14 TFGHGSGaVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaKSAEIARYRRSVQMIFQ 93
Cdd:cd03254 9 NFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI---RDISRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 DPFASlnpAHTIAHHLRrplkLHRPEIKGAEidvaVRELLQRVRLDP---------DLVAPKYPHELSGGQRQRVNIARA 164
Cdd:cd03254 85 DTFLF---SGTIMENIR----LGRPNATDEE----VIEAAKEAGAHDfimklpngyDTVLGENGGNLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586794399 165 LAVKPEVIVADEPTSMLDVSVRlgvlNLLNEMKRELNLG--LLYITHDIATARYvAEDIAVMYAGQIVEWGS 234
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETE----KLIQEALEKLMKGrtSIIIAHRLSTIKN-ADKILVLDDGKIIEEGT 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
28-241 |
1.93e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.83 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeAAKSAEIARYRRSVQMIFQDPFASL---NPAHT 104
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDIRKKVGLVFQYPEYQLfeeTIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 105 IAHHLRRpLKLHRPEIKGAeidvaVRELLQRVRLDPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVS 184
Cdd:PRK13637 105 IAFGPIN-LGLSEEEIENR-----VKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586794399 185 VRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDN 241
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
6-233 |
2.91e-27 |
|
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: 105.65 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHgsgavhAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEiaryr 85
Cdd:cd03298 1 VRLDKIRFSYGE------QPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQDP--FASLNPAHTIAHHLRRPLKLH---RPEIKGAEIDVAVRELLQRVrldpdlvapkyPHELSGGQRQRVN 160
Cdd:cd03298 70 RPVSMLFQENnlFAHLTVEQNVGLGLSPGLKLTaedRQAIEVALARVGLAGLEKRL-----------PGELSGGERQRVA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586794399 161 IARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWG 233
Cdd:cd03298 139 LARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
29-290 |
3.16e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 109.35 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 29 SFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYRRS-VQMIFQDpFAsLNPAHTIAH 107
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQS-FA-LMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 108 HLRRPLKLhrPEIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRL 187
Cdd:PRK10070 126 NTAFGMEL--AGINAEERREKALDALRQVGLEN--YAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 188 GVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPYTRLLLSAVPDPDVRFDDPKAR 267
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIAR 281
|
250 260 270
....*....|....*....|....*....|.
gi 1586794399 268 LRPDEVedIRR------RSAMP--QDDIVEF 290
Cdd:PRK10070 282 RTPNGL--IRKtpgfgpRSALKllQDEDREY 310
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
14-241 |
3.30e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.00 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 14 TFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryRRSVQMIFQ 93
Cdd:PRK13632 14 SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI---RKKIGIIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 DP---FASLNPAHTIAHHLRRPlKLHRPEIKgAEIDvavrELLQRVRLDPDLvaPKYPHELSGGQRQRVNIARALAVKPE 170
Cdd:PRK13632 91 NPdnqFIGATVEDDIAFGLENK-KVPPKKMK-DIID----DLAKKVGMEDYL--DKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586794399 171 VIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATArYVAEDIAVMYAGQIVEWGSVAKVIDN 241
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-234 |
4.16e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.03 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTcarmaMREYL-----PTSGRILYKGRPVEAAKSA-EIARYRRSVQMIFQDPFASLNP 101
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKST-----LLQHLngllqPTSGTVTIGERVITAGKKNkKLKPLRKKVGIVFQFPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 102 AhTIAHHLR-RPLKLHRPEikgAEIDVAVRELLQRVRLDPDLVApKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSM 180
Cdd:PRK13634 101 E-TVEKDICfGPMNFGVSE---EDAKQKAREMIELVGLPEELLA-RSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 181 LDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGS 234
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
24-234 |
5.10e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 106.71 E-value: 5.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 24 AARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGrpVEAAKSAEIARYRRSVQMIFQdpfaslNPAH 103
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIRNKAGMVFQ------NPDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLRRPLKLHRPE---IKGAEIDVAVRELLQRVRLDpdlvapKY----PHELSGGQRQRVNIARALAVKPEVIVADE 176
Cdd:PRK13633 97 QIVATIVEEDVAFGPEnlgIPPEEIRERVDESLKKVGMY------EYrrhaPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 177 PTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATArYVAEDIAVMYAGQIVEWGS 234
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-233 |
1.82e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 104.32 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 20 GAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPV---EAAKSAEIARYRRSVQMIFQDpf 96
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQQ-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 97 ASLNPAHTIAHHLR----RPLKLHrpeiKGAEIDVAvRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVI 172
Cdd:COG4161 91 YNLWPHLTVMENLIeapcKVLGLS----KEQAREKA-MKLLARLRLTD--KADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586794399 173 VADEPTSMLDVSVRLGVLNLLNEMKrELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWG 233
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
26-233 |
2.13e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.95 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTC-ARMA--MREYLPTSGRILYKGRPVeAAKSAEiaryRRSVQMIFQDPFasLNPA 102
Cdd:COG4136 18 APLSLTVAPGEILTLMGPSGSGKSTLlAAIAgtLSPAFSASGEVLLNGRRL-TALPAE----QRRIGILFQDDL--LFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 103 HTIAHHLRRPLklhRPEIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLD 182
Cdd:COG4136 91 LSVGENLAFAL---PPTIGRAQRRARVEQALEEAGLAG--FADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586794399 183 VSVRLGVLNLLNEMKRELNLGLLYITHDiataryvAEDIAVmyAGQIVEWG 233
Cdd:COG4136 166 AALRAQFREFVFEQIRQRGIPALLVTHD-------EEDAPA--AGRVLDLG 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-233 |
2.77e-26 |
|
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: 103.00 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 20 GAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAaKSAEIArY---RRSVQMIFqdP- 95
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-ERKRIG-YvpqRRSIDRDF--Pi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 96 ----FASLNPAHTIAHhLRRPLKLHRPeikgaeidvAVRELLQRVRLDpdlvapKYPH----ELSGGQRQRVNIARALAV 167
Cdd:cd03235 86 svrdVVLMGLYGHKGL-FRRLSKADKA---------KVDEALERVGLS------ELADrqigELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586794399 168 KPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMyAGQIVEWG 233
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
26-210 |
3.43e-26 |
|
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: 102.56 E-value: 3.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAeiarYRRSVQMIFQDPfaSLNPAHTI 105
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED----YRRRLAYLGHAD--GLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 106 AHHLRRPLKLHRPEIKGAEIDvavrELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSv 185
Cdd:COG4133 93 RENLRFWAALYGLRADREAID----EALEAVGLAG--LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA- 165
|
170 180
....*....|....*....|....*..
gi 1586794399 186 rlGVLNLLNEMKRELNLG--LLYITHD 210
Cdd:COG4133 166 --GVALLAELIAAHLARGgaVLLTTHQ 190
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-240 |
6.02e-26 |
|
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: 102.69 E-value: 6.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 14 TFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaKSAEIARYRRSVQMIFQ 93
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDYTLASLRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 DPFA-SLNPAHTIAHHlrrplklhRPEIKGAEIDVAVR-----ELLQRVRLDPDLVAPKYPHELSGGQRQRVNIARALAV 167
Cdd:cd03251 84 DVFLfNDTVAENIAYG--------RPGATREEVEEAARaanahEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 168 KPEVIVADEPTSMLD-VSVRLgVLNLLNEMKRelNLGLLYITHDIATARYvAEDIAVMYAGQIVEWGSVAKVID 240
Cdd:cd03251 156 DPPILILDEATSALDtESERL-VQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-233 |
7.41e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 101.50 E-value: 7.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHGsgavHAARAISFSLHAGrALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAeiarYR 85
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQDPfaSLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARAL 165
Cdd:cd03264 72 RRIGYLPQEF--GVYPNFTVREFLDYIAWLKG--IPSKEVKARVDEVLELVNLGD--RAKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 166 AVKPEVIVADEPTSMLDVSVRLGVLNLLnemkRELNLGLLYI--THDIATARYVAEDIAVMYAGQIVEWG 233
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLL----SELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
28-242 |
9.35e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 107.12 E-value: 9.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEaakSAEIARYRRSVQMIFQDPFA-SLNPAHTIA 106
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV---QYDHHYLHRQVALVGQEPVLfSGSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 107 HHLRRPLKlhrPEIKGAEIDVAVRELLQRVRLDPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVR 186
Cdd:TIGR00958 577 YGLTDTPD---EEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586794399 187 lgvlNLLNEMKRELNLGLLYITHDIATARYvAEDIAVMYAGQIVEWGSVAKVIDNP 242
Cdd:TIGR00958 654 ----QLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-212 |
1.56e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 101.10 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 20 GAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYRRSVQMIFQDPFASL 99
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 100 NpaHTIAHHLRRPLKlhrpeIKGAEIDvavrELLQRVRLDPDLV-----APKYPHELSGGQRQRVNIARALAVKPEVIVA 174
Cdd:PRK10908 93 D--RTVYDNVAIPLI-----IAGASGD----DIRRRVSAALDKVglldkAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1586794399 175 DEPTSMLDVSVRLGVLNLLNEMKReLNLGLLYITHDIA 212
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIG 198
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-240 |
3.99e-25 |
|
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: 100.64 E-value: 3.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 14 TFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEiarYRRSVQMIFQ 93
Cdd:cd03252 7 RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW---LRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 DPFaslnpahTIAHHLRRPLKLHRPEIKGAEIDVAVR-----ELLQRVRLDPDLVAPKYPHELSGGQRQRVNIARALAVK 168
Cdd:cd03252 84 ENV-------LFNRSIRDNIALADPGMSMERVIEAAKlagahDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 169 PEVIVADEPTSMLDV-SVRlgvlNLLNEMKREL-NLGLLYITHDIATARyVAEDIAVMYAGQIVEWGSVAKVID 240
Cdd:cd03252 157 PRILIFDEATSALDYeSEH----AIMRNMHDICaGRTVIIIAHRLSTVK-NADRIIVMEKGRIVEQGSHDELLA 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-255 |
4.54e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.42 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 19 SGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryRRSVQMIFQDP--- 95
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV---RKFVGLVFQNPddq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 96 -----------FASLN---PAHTIAHHLRRPLKLhrpeikgaeidVAVRELLQRVrldpdlvapkyPHELSGGQRQRVNI 161
Cdd:PRK13652 91 ifsptveqdiaFGPINlglDEETVAHRVSSALHM-----------LGLEELRDRV-----------PHHLSGGEKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 162 ARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDN 241
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
250
....*....|....*
gi 1586794399 242 P-LHPYTRLLLSAVP 255
Cdd:PRK13652 229 PdLLARVHLDLPSLP 243
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
6-240 |
4.99e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.04 E-value: 4.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHgsgavhaaRAISFSLHAGRA--LALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAeiar 83
Cdd:PRK10771 2 LKLTDITWLYHH--------LPMRFDLTVERGerVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 84 yRRSVQMIFQDP--FASLNPAHTIAHHLRRPLKLHrpeikgAEIDVAVRELLQRVRLDPDLvaPKYPHELSGGQRQRVNI 161
Cdd:PRK10771 70 -RRPVSMLFQENnlFSHLTVAQNIGLGLNPGLKLN------AAQREKLHAIARQMGIEDLL--ARLPGQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 162 ARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVID 240
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
26-234 |
5.98e-25 |
|
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: 100.00 E-value: 5.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaKSAEIARYRRSVQMIFQDP--FASlnpah 103
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI---REVTLDSLRRAIGVVPQDTvlFND----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLRrplkLHRPEIKgaeiDVAVRELLQRVRLDPDLVAPKYPHE---------LSGGQRQRVNIARALAVKPEVIVA 174
Cdd:cd03253 90 TIGYNIR----YGRPDAT----DEEVIEAAKAAQIHDKIMRFPDGYDtivgerglkLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 175 DEPTSMLDVSVRLGVLNLLNEMKRelNLGLLYITHDIATArYVAEDIAVMYAGQIVEWGS 234
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGT 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
26-252 |
1.41e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 99.66 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPV----------EAAKSAEIARYRRSVQMIFQ-- 93
Cdd:PRK10619 22 KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlKVADKNQLRLLRTRLTMVFQhf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 DPFASLNPAHTIAHHLRRPLKLHRPEIKgaeiDVAVReLLQRVRLDpDLVAPKYPHELSGGQRQRVNIARALAVKPEVIV 173
Cdd:PRK10619 102 NLWSHMTVLENVMEAPIQVLGLSKQEAR----ERAVK-YLAKVGID-ERAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 174 ADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPYTRLLLS 252
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-246 |
1.55e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 101.64 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 8 LDSVTKTFGHgsgaVHAARAISFSLHAGRALALVGESGSGKTTCARM-AMREYLpTSGRILYKGRPVEaaksaEIARYRR 86
Cdd:PRK11000 6 LRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMiAGLEDI-TSGDLFIGEKRMN-----DVPPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 87 SVQMIFQDpfASLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPDLvaPKYPHELSGGQRQRVNIARALA 166
Cdd:PRK11000 76 GVGMVFQS--YALYPHLSVAENMSFGLKLAG--AKKEEINQRVNQVAEVLQLAHLL--DRKPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 167 VKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSvakvidnPLHPY 246
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK-------PLELY 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
28-230 |
1.57e-24 |
|
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: 98.10 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAksaeiaRYRRSVQMIFQDP----FASlnpah 103
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK------ERRKSIGYVMQDVdyqlFTD----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLRRPLKLhrpeikGAEIDVAVRELLQRvrLDPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDV 183
Cdd:cd03226 88 SVREELLLGLKE------LDAGNEQAETVLKD--LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1586794399 184 SVRLGVLNLLNEMKRELNLGLLyITHDIATARYVAEDIAVMYAGQIV 230
Cdd:cd03226 160 KNMERVGELIRELAAQGKAVIV-ITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
28-229 |
1.67e-24 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 98.70 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSaeiARYRRSVQMIFQDP-FASLNPAHTIA 106
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH---KYLHSKVSLVGQEPvLFARSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 107 HHLRR-PLKlhrpEIKGAEIDVAVRELLQRVRLDPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSV 185
Cdd:cd03248 110 YGLQScSFE----CVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1586794399 186 RLGVLNLLNEMKRelNLGLLYITHDIATARYvAEDIAVMYAGQI 229
Cdd:cd03248 186 EQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
23-240 |
1.69e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.81 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 23 HAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryRRSVQMIFQDP----FAS 98
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---RSKVGLVFQDPddqvFSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 99 lnpahTIAHHLR-RPLKLhrpEIKGAEIDVAVRELLQRVRLDpDLvAPKYPHELSGGQRQRVNIARALAVKPEVIVADEP 177
Cdd:PRK13647 96 -----TVWDDVAfGPVNM---GLDKDEVERRVEEALKAVRMW-DF-RDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586794399 178 TSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVID 240
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-234 |
3.06e-24 |
|
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: 102.10 E-value: 3.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 14 TFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryRRSVQMIFQ 93
Cdd:TIGR02203 337 TFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASL---RRQVALVSQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 DPFASLNpahTIAHHLR--RPLKLHRPEIKGAEIDVAVRELLQRVRLDPDLVAPKYPHELSGGQRQRVNIARALAVKPEV 171
Cdd:TIGR02203 414 DVVLFND---TIANNIAygRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPI 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586794399 172 IVADEPTSMLDVSVRLGVLNLLNEMKRelNLGLLYITHDIATARYvAEDIAVMYAGQIVEWGS 234
Cdd:TIGR02203 491 LILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGT 550
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
28-229 |
8.46e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.88 E-value: 8.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryRRSVQMIFQDP---FASLNPAHT 104
Cdd:PRK13650 26 VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI---RHKIGMVFQNPdnqFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 105 IAHHLrrplklhrpEIKGaeidVAVRELLQRVRLDPDLV-----APKYPHELSGGQRQRVNIARALAVKPEVIVADEPTS 179
Cdd:PRK13650 103 VAFGL---------ENKG----IPHEEMKERVNEALELVgmqdfKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1586794399 180 MLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARyVAEDIAVMYAGQI 229
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-230 |
9.49e-24 |
|
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: 96.12 E-value: 9.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 22 VHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryRRSVQMIFQDPfaslnp 101
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---RRNIGYVPQDV------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 102 aHTIAHHLRRPLKLHRPEIKGAEIDVAVR--ELLQRVRLDP---DLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADE 176
Cdd:cd03245 88 -TLFYGTLRDNITLGAPLADDERILRAAElaGVTDFVNKHPnglDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 177 PTSMLDvsvrlgvLNLLNEMKRELNLGLLYITHDIATARYVAEDIA----VMYAGQIV 230
Cdd:cd03245 167 PTSAMD-------MNSEERLKERLRQLLGDKTLIIITHRPSLLDLVdriiVMDSGRIV 217
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-229 |
9.64e-24 |
|
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: 96.08 E-value: 9.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 29 SFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaksAEIARYRRSVQMIFQDP--FASLNPAHTIA 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH-----TGLAPYQRPVSMLFQENnlFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 107 HHLRRPLKLHrpeikgAEIDVAVRELLQRVRLDpDLVApKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVR 186
Cdd:TIGR01277 93 LGLHPGLKLN------AEQQEKVVDAAQQVGIA-DYLD-RLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1586794399 187 LGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQI 229
Cdd:TIGR01277 165 EEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
28-242 |
2.60e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.82 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAE-IARYRRSVQMIFQDPFASLNPAHTIA 106
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnLKKLRKKVSLVFQFPEAQLFENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 107 HHLRRPLKLHRPEIKGAEidvAVRELLQRVRLDPDLvAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVR 186
Cdd:PRK13641 106 DVEFGPKNFGFSEDEAKE---KALKWLKKVGLSEDL-ISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586794399 187 LGVLNLLNEMKRELNLGLLyITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNP 242
Cdd:PRK13641 182 KEMMQLFKDYQKAGHTVIL-VTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-231 |
2.60e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.70 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 22 VHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGrpvEAAKSAEIARYRRSVQMIFQDP---FAS 98
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLRRKIGMVFQNPdnqFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 99 LNPAHTIAHHLrrplklhrpEIKGaeidVAVRELLQRVrlDPDLVA-------PKYPHELSGGQRQRVNIARALAVKPEV 171
Cdd:PRK13642 97 ATVEDDVAFGM---------ENQG----IPREEMIKRV--DEALLAvnmldfkTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 172 IVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARyVAEDIAVMYAGQIVE 231
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIK 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-247 |
2.97e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 95.61 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGHGSgavhAARAISFSLHAGRALALVGESGSGKTTCARMA--MREYLP---TSGRILYKGRPVEA 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 76 AKsAEIARYRRSVQMIFQDPfaslNP-AHTIAHHLRRPLKLHRPEIKgAEIDVAVRELLQ--------RVRLDPDLVApk 146
Cdd:PRK14239 77 PR-TDTVDLRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIKDK-QVLDEAVEKSLKgasiwdevKDRLHDSALG-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 147 ypheLSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNlgLLYITHDIATARYVAEDIAVMYA 226
Cdd:PRK14239 149 ----LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYT--MLLVTRSMQQASRISDRTGFFLD 222
|
250 260
....*....|....*....|.
gi 1586794399 227 GQIVEWGSVAKVIDNPLHPYT 247
Cdd:PRK14239 223 GDLIEYNDTKQMFMNPKHKET 243
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-233 |
3.99e-23 |
|
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: 94.74 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGrpVEAAKSAEIARY 84
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 85 RRSVqmiFQDPFAsLNPAHTIAHHLRRPLKLHrpEIKGAEIDVAVRELLQRVRLDPDLvaPKYPHELSGGQRQRVNIARA 164
Cdd:cd03266 79 RLGF---VSDSTG-LYDRLTARENLEYFAGLY--GLKGDELTARLEELADRLGMEELL--DRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 165 LAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMkRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWG 233
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-248 |
5.91e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.10 E-value: 5.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 27 AISFSLHAGRALALVGESGSGKTT----CARMAMRE-YLPTSGRILYKGRPVeAAKSAEIARYRRSVQMIFQDPfaSLNP 101
Cdd:PRK14258 25 GVSMEIYQSKVTAIIGPSGCGKSTflkcLNRMNELEsEVRVEGRVEFFNQNI-YERRVNLNRLRRQVSMVHPKP--NLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 102 AhTIAHHLRRPLKL--HRPEIkgaEIDVAVRELLQRVRLDPDLVAP--KYPHELSGGQRQRVNIARALAVKPEVIVADEP 177
Cdd:PRK14258 102 M-SVYDNVAYGVKIvgWRPKL---EIDDIVESALKDADLWDEIKHKihKSALDLSGGQQQRLCIARALAVKPKVLLMDEP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586794399 178 TSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYA-----GQIVEWGSVAKVIDNPLHPYTR 248
Cdd:PRK14258 178 CFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTR 253
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-231 |
6.10e-23 |
|
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: 94.45 E-value: 6.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryrrsvqMIFQDpfASLNPAHTIAH 107
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQN--YSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 108 HLRRPLKLHRPEIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRL 187
Cdd:TIGR01184 74 NIALAVDRVLPDLSKSERRAIVEEHIALVGLTE--AADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1586794399 188 GVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVM------YAGQIVE 231
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILE 201
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-224 |
6.22e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 98.51 E-value: 6.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGhgsGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEiarYR 85
Cdd:TIGR02857 322 LEFSGVSVAYP---GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS---WR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQDPFAslnPAHTIAHHLRrplkLHRPEIKGAEIDVAVR-----ELLQRVRLDPDLVAPKYPHELSGGQRQRVN 160
Cdd:TIGR02857 396 DQIAWVPQHPFL---FAGTIAENIR----LARPDASDAEIREALEragldEFVAALPQGLDTPIGEGGAGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 161 IARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRelNLGLLYITHDIATARyVAEDIAVM 224
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAA-LADRIVVL 529
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-242 |
6.30e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 96.84 E-value: 6.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 4 AILALDSVTKTFGHGSGAVHAaraISFSLHAGRALALVGESGSGKTTCARM-AMREYLpTSGRILYKGRPVEAAKSAEia 82
Cdd:PRK11650 2 AGLKLQAVRKSYDGKTQVIKG---IDLDVADGEFIVLVGPSGCGKSTLLRMvAGLERI-TSGEIWIGGRVVNELEPAD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 83 ryrRSVQMIFQDpFAsLNPAHTIAHHLRRPLKlhrpeIKG---AEIDVAVRELLQRVRLDPDLvaPKYPHELSGGQRQRV 159
Cdd:PRK11650 76 ---RDIAMVFQN-YA-LYPHMSVRENMAYGLK-----IRGmpkAEIEERVAEAARILELEPLL--DRKPRELSGGQRQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 160 NIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVI 239
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVY 223
|
...
gi 1586794399 240 DNP 242
Cdd:PRK11650 224 EKP 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
9-234 |
1.04e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.85 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 9 DSVTKTFGHGSGAVHAA-RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEA-AKSAEIARYRR 86
Cdd:PRK13646 6 DNVSYTYQKGTPYEHQAiHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDKYIRPVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 87 SVQMIFQDPFASLnpahtIAHHLRRPLkLHRPEIKGAEIDvAVRELLQRVRLD---PDLVAPKYPHELSGGQRQRVNIAR 163
Cdd:PRK13646 86 RIGMVFQFPESQL-----FEDTVEREI-IFGPKNFKMNLD-EVKNYAHRLLMDlgfSRDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586794399 164 ALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDI-ATARYvAEDIAVMYAGQIVEWGS 234
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMnEVARY-ADEVIVMKEGSIVSQTS 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
28-231 |
1.62e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.00 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAkSAEiaryrRSVqmIFQDpfASLNPAHTIAH 107
Cdd:PRK11248 20 INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP-GAE-----RGV--VFQN--EGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 108 HLRRPLKLhrPEIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRL 187
Cdd:PRK11248 90 NVAFGLQL--AGVEKMQRLEIAHQMLKKVGLEG--AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1586794399 188 GVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMY--AGQIVE 231
Cdd:PRK11248 166 QMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-239 |
2.75e-22 |
|
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: 96.41 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 20 GAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYK--GRPVEAAKSAEIARYR--RSVQMIFQDp 95
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgDEWVDMTKPGPDGRGRakRYIGILHQE- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 96 fASLNPAHTIAHHLRRPLKLHRPEikgaeiDVAVRE---LLQRVRLDPDL---VAPKYPHELSGGQRQRVNIARALAVKP 169
Cdd:TIGR03269 374 -YDLYPHRTVLDNLTEAIGLELPD------ELARMKaviTLKMVGFDEEKaeeILDKYPDELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 170 EVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVI 239
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-230 |
2.93e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.72 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTdAILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCarMAMREYL--PTSGRILYKGRPVEAAKS 78
Cdd:PRK10535 1 MT-ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTL--MNILGCLdkPTSGTYRVAGQDVATLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 79 AEIARYRRS-VQMIFQDpfASLNPAHTIAHHLRRPlKLHRPEIKGAEIDVAvRELLQRVRLDpDLVApKYPHELSGGQRQ 157
Cdd:PRK10535 78 DALAQLRREhFGFIFQR--YHLLSHLTAAQNVEVP-AVYAGLERKQRLLRA-QELLQRLGLE-DRVE-YQPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586794399 158 RVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMkRELNLGLLYITHDIATARYvAEDIAVMYAGQIV 230
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-241 |
3.06e-22 |
|
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: 92.11 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 20 GAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARyrRSVQMIFQDP--FA 97
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAR--AGIGYVPEGRriFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 98 SLnpahTIAHHLRRPLKLHRPEIKGAEIDvAVREL---LQRVRLDPDlvapkypHELSGGQRQRVNIARALAVKPEVIVA 174
Cdd:cd03224 89 EL----TVEENLLLGAYARRRAKRKARLE-RVYELfprLKERRKQLA-------GTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586794399 175 DEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDN 241
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-210 |
4.34e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.08 E-value: 4.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 3 DAILALDSVtktfGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeAAKSAEia 82
Cdd:PRK10247 5 SPLLQLQNV----GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI-STLKPE-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 83 RYRRSVQMIFQDP--FASlnpahTIAHHLRRPLKLH--RPEIKgaeidvAVRELLQRVRLdPDLVAPKYPHELSGGQRQR 158
Cdd:PRK10247 78 IYRQQVSYCAQTPtlFGD-----TVYDNLIFPWQIRnqQPDPA------IFLDDLERFAL-PDTILTKNIAELSGGEKQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1586794399 159 VNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHD 210
Cdd:PRK10247 146 ISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-229 |
1.02e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.66 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHGSgavhAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILykgrpveaAKSAEIARYR 85
Cdd:PRK11247 13 LLLNAVSKRYGERT----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL--------AGTAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQDpfASLNPAHTIAHHLRRPLKLH-RPeikgaeidvAVRELLQRVRLDPDlvAPKYPHELSGGQRQRVNIARA 164
Cdd:PRK11247 81 EDTRLMFQD--ARLLPWKKVIDNVGLGLKGQwRD---------AALQALAAVGLADR--ANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586794399 165 LAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQI 229
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
26-264 |
2.19e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.84 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYrrsvqmifqdpfASLNPahti 105
Cdd:PRK11231 19 NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR------------LALLP---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 106 AHHLrrplklhRPEikgaeiDVAVRELL-------------------QRV-----RLDPDLVAPKYPHELSGGQRQRVNI 161
Cdd:PRK11231 83 QHHL-------TPE------GITVRELVaygrspwlslwgrlsaednARVnqameQTRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 162 ARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElnlGLLYIT--HDIATA-RYvAEDIAVMYAGQIVEWGSVAKV 238
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ---GKTVVTvlHDLNQAsRY-CDHLVVLANGHVMAQGTPEEV 225
|
250 260
....*....|....*....|....*..
gi 1586794399 239 IdnplhpyTRLLLSAVPDPDVR-FDDP 264
Cdd:PRK11231 226 M-------TPGLLRTVFDVEAEiHPEP 245
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
9-234 |
3.26e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 93.49 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 9 DSVTKTFGHGSGAVHAaraISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaKSAEIARYRRSV 88
Cdd:PRK13657 338 DDVSFSYDNSRQGVED---VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI---RTVTRASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 89 QMIFQDPfasLNPAHTIAHHLRrplkLHRPEIKGAEIDVAVR-----ELLQRVRLDPDLVAPKYPHELSGGQRQRVNIAR 163
Cdd:PRK13657 412 AVVFQDA---GLFNRSIEDNIR----VGRPDATDEEMRAAAEraqahDFIERKPDGYDTVVGERGRQLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586794399 164 ALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRelNLGLLYITHDIATARYvAEDIAVMYAGQIVEWGS 234
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGS 552
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
14-250 |
8.24e-21 |
|
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: 92.31 E-value: 8.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 14 TFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARyrrSVQMIFQ 93
Cdd:TIGR03796 484 TFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLAN---SVAMVDQ 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 DPFASlnpAHTIahhlRRPLKLHRPEIKGAEIDVAVRE--LLQRVRLDPDlvapKYPHEL-------SGGQRQRVNIARA 164
Cdd:TIGR03796 561 DIFLF---EGTV----RDNLTLWDPTIPDADLVRACKDaaIHDVITSRPG----GYDAELaegganlSGGQRQRLEIARA 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 165 LAVKPEVIVADEPTSMLDVSVRLGVL-NLlnemkRELNLGLLYITHDIATARYVAEdIAVMYAGQIVEWGSVAKVIDNPl 243
Cdd:TIGR03796 630 LVRNPSILILDEATSALDPETEKIIDdNL-----RRRGCTCIIVAHRLSTIRDCDE-IIVLERGKVVQRGTHEELWAVG- 702
|
....*..
gi 1586794399 244 HPYTRLL 250
Cdd:TIGR03796 703 GAYARLI 709
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
24-248 |
1.17e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.07 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 24 AARAISFSLHAGRALALVGESGSGKTTCARM--AMREYLPT---SGRILYKGRPVEAaKSAEIARYRRSVQMIFQDPfas 98
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnRLNDLIPGfrvEGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKP--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 99 lNP-AHTIAHHLRrplklHRPEIKG--AEIDVAVRELLQRVRLdPDLVAPKYPHE---LSGGQRQRVNIARALAVKPEVI 172
Cdd:PRK14243 101 -NPfPKSIYDNIA-----YGARINGykGDMDELVERSLRQAAL-WDEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 173 VADEPTSMLDVSVRLGVLNLLNEMKRELNlgLLYITHDIATARYVAEDIAVMYA---------GQIVEWGSVAKVIDNPL 243
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQYT--IIIVTHNMQQAARVSDMTAFFNVeltegggryGYLVEFDRTEKIFNSPQ 251
|
....*
gi 1586794399 244 HPYTR 248
Cdd:PRK14243 252 QQATR 256
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-211 |
1.41e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 88.63 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAIlALDSVTKTFGHGSgavhAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRpveaaksae 80
Cdd:PRK09544 1 MTSLV-SLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 iARYRRSVQMIFQDPfaslnpahTIAHHLRRPLKLhRPEIKGAEIDVAvrelLQRVRLDPDLVAPKypHELSGGQRQRVN 160
Cdd:PRK09544 67 -LRIGYVPQKLYLDT--------TLPLTVNRFLRL-RPGTKKEDILPA----LKRVQAGHLIDAPM--QKLSGGETQRVL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586794399 161 IARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDI 211
Cdd:PRK09544 131 LARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-241 |
1.63e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.30 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 8 LDSVTKTFGHGSG-AVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRIL---YKgRPVEAAKSAEIAR 83
Cdd:PRK13645 9 LDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIvgdYA-IPANLKKIKEVKR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 84 YRRSVQMIFQDPFASLNpAHTIAHHLR-RPLKLHRPEikgAEIDVAVRELLQRVRLdPDLVAPKYPHELSGGQRQRVNIA 162
Cdd:PRK13645 88 LRKEIGLVFQFPEYQLF-QETIEKDIAfGPVNLGENK---QEAYKKVPELLKLVQL-PEDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 163 RALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDN 241
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-236 |
1.80e-20 |
|
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: 87.58 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 20 GAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEiaRYRRSV------QMIFq 93
Cdd:TIGR03410 11 GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE--RARAGIayvpqgREIF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 dpfaslnPAHTIAHHLR-----RPLKLHR--PEIkgAEIDVAVRELLQRVRLDpdlvapkypheLSGGQRQRVNIARALA 166
Cdd:TIGR03410 88 -------PRLTVEENLLtglaaLPRRSRKipDEI--YELFPVLKEMLGRRGGD-----------LSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 167 VKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVA 236
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGD 217
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-240 |
2.78e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.59 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 27 AISFSLHAGRALALVGESGSGKTTC-ARMA-MreyLPTSGRILYKGRPVEAAKSAEIARYRR--SVQmifQDPFASLnPA 102
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLlARMAgL---LPGQGEILLNGRPLSDWSAAELARHRAylSQQ---QSPPFAM-PV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 103 HtiaHHLRrplkLHRP-EIKGAEIDVAVRELLQRVRLDPDLvaPKYPHELSGGQRQRVNIARA-LAVKPEV------IVA 174
Cdd:COG4138 87 F---QYLA----LHQPaGASSEAVEQLLAQLAEALGLEDKL--SRPLTQLSGGEWQRVRLAAVlLQVWPTInpegqlLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 175 DEPTSMLDVSVRLGVLNLLNEMKRelnLGLLYIT--HDIA-TARYvAEDIAVMYAGQIVEWGSVAKVID 240
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELCQ---QGITVVMssHDLNhTLRH-ADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
28-264 |
2.97e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 87.90 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYRRSVQMIFQDP--FASLNPAHTI 105
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGalFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 106 AHHLRRPLKLHRPEIKGAeidvaVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDvSV 185
Cdd:PRK11831 106 AYPLREHTQLPAPLLHST-----VMMKLEAVGLRG--AAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD-PI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 186 RLGVL-NLLNEMKRELNLGLLYITHDIATARYVAeDIAVMYAGQ-IVEWGSVAKVIDNPlHPYTRLLLSAVPDPDVRFDD 263
Cdd:PRK11831 178 TMGVLvKLISELNSALGVTCVVVSHDVPEVLSIA-DHAYIVADKkIVAHGSAQALQANP-DPRVRQFLDGIADGPVPFRY 255
|
.
gi 1586794399 264 P 264
Cdd:PRK11831 256 P 256
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
24-239 |
3.03e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.46 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 24 AARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKsaeIARYRRSVQMIFQDpfaslnpAH 103
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT---LASLRNQVALVSQN-------VH 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 ----TIAHHLR--RPLKLHRPEIKGAEIDVAVRELLQRVRLDPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEP 177
Cdd:PRK11176 428 lfndTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586794399 178 TSMLDVSVRLGVLNLLNEMKRelNLGLLYITHDIATARYvAEDIAVMYAGQIVEWGSVAKVI 239
Cdd:PRK11176 508 TSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELL 566
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-247 |
3.27e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.23 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 7 ALDSVTKTFGHGSGAVHAARAISFSLHAgrALALVGESGSGKTTCARMAMR-----EYLPTSGRILYKGRPVEAAKsaEI 81
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARA--VTSLMGPTGSGKTTFLRTLNRmndkvSGYRYSGDVLLGGRSIFNYR--DV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 82 ARYRRSVQMIFQDPfaslNP-AHTIAHHLRRPLKLH----RPEIKG-AEIDVAVRELLQRVRldpDLVAPKyPHELSGGQ 155
Cdd:PRK14271 97 LEFRRRVGMLFQRP----NPfPMSIMDNVLAGVRAHklvpRKEFRGvAQARLTEVGLWDAVK---DRLSDS-PFRLSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 156 RQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNlgLLYITHDIATARYVAEDIAVMYAGQIVEWGSV 235
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLT--VIIVTHNLAQAARISDRAALFFDGRLVEEGPT 246
|
250
....*....|..
gi 1586794399 236 AKVIDNPLHPYT 247
Cdd:PRK14271 247 EQLFSSPKHAET 258
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-239 |
3.58e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 87.73 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGHGSGAVhaARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAE 80
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTV--AENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 IARyrrSVQMIFQDpfASLNPAHTIAHHLRRPLKLHRPEIKG--AEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQR 158
Cdd:PRK10253 79 VAR---RIGLLAQN--ATTPGDITVQELVARGRYPHQPLFTRwrKEDEEAVTKAMQATGITH--LADQSVDTLSGGQRQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 159 VNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATA-RYVAEDIAvMYAGQIVEWGSVAK 237
Cdd:PRK10253 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIA-LREGKIVAQGAPKE 230
|
..
gi 1586794399 238 VI 239
Cdd:PRK10253 231 IV 232
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
28-233 |
4.24e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 87.04 E-value: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAM--REYLPTSGRILYKGRPVEAAKSAEIARyrRSVQMIFQDPFASlnPAHTI 105
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSPDERAR--AGIFLAFQYPVEI--PGVSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 106 AHHLRRPLKLHR-PEIKGAEIDVAVRELLQRVRLDPDLVApKYPHE-LSGGQRQRVNIARALAVKPEVIVADEPTSMLDV 183
Cdd:COG0396 95 SNFLRTALNARRgEELSAREFLKLLKEKMKELGLDEDFLD-RYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1586794399 184 -SVRLgVLNLLNEMKRElNLGLLYITHDIATARYVAED-IAVMYAGQIVEWG 233
Cdd:COG0396 174 dALRI-VAEGVNKLRSP-DRGILIITHYQRILDYIKPDfVHVLVDGRIVKSG 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-229 |
5.17e-20 |
|
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: 85.18 E-value: 5.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCAR--MAMREylPTSGRILYKGRPVEAAKSAEiaRYRRSVQMIFQDPFAS-LNPAHT 104
Cdd:cd03215 19 VSFEVRAGEIVGIAGLVGNGQTELAEalFGLRP--PASGEITLDGKPVTRRSPRD--AIRAGIAYVPEDRKREgLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 105 IAHHLrrplklhrpeikgaeidvAVRELLqrvrldpdlvapkyphelSGGQRQRVNIARALAVKPEVIVADEPTSMLDVS 184
Cdd:cd03215 95 VAENI------------------ALSSLL------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1586794399 185 VRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQI 229
Cdd:cd03215 139 AKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-240 |
7.24e-20 |
|
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: 89.54 E-value: 7.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 14 TFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryRRSVQMIFQ 93
Cdd:TIGR03375 470 SFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL---RRNIGYVPQ 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 DP---FASLnpahtiahhlRRPLKLHRPEIKGAEIDVAVRE--LLQRVRLDP---DLVAPKYPHELSGGQRQRVNIARAL 165
Cdd:TIGR03375 547 DPrlfYGTL----------RDNIALGAPYADDEEILRAAELagVTEFVRRHPdglDMQIGERGRSLSGGQRQAVALARAL 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 166 AVKPEVIVADEPTSMLDVSvrlgvlnllNEM--KRELNLG-----LLYITHDIATARYVaEDIAVMYAGQIVEWGSVAKV 238
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMDNR---------SEErfKDRLKRWlagktLVLVTHRTSLLDLV-DRIIVMDNGRIVADGPKDQV 686
|
..
gi 1586794399 239 ID 240
Cdd:TIGR03375 687 LE 688
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
26-234 |
1.02e-19 |
|
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: 89.03 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryRRSVQMIFQDPFaslnpahTI 105
Cdd:TIGR01846 474 SNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWL---RRQMGVVLQENV-------LF 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 106 AHHLRRPLKLHRPEIKGAEIDVAVR-----ELLQRVRLDPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSM 180
Cdd:TIGR01846 544 SRSIRDNIALCNPGAPFEHVIHAAKlagahDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSA 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 181 LDVSVRLGVLNLLNEMKRelNLGLLYITHDIATARYvAEDIAVMYAGQIVEWGS 234
Cdd:TIGR01846 624 LDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGR 674
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-238 |
1.30e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.69 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRP---VEAAK 77
Cdd:PRK09700 1 MATPYISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 78 SAEIAryrrsVQMIFQDpfASLNPAHTIAHHL---RRPLK--LHRPEIKGAEIDVAVRELLQRVRLDPDL---VApkyph 149
Cdd:PRK09700 77 AAQLG-----IGIIYQE--LSVIDELTVLENLyigRHLTKkvCGVNIIDWREMRVRAAMMLLRVGLKVDLdekVA----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 150 ELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQI 229
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSS 223
|
....*....
gi 1586794399 230 VEWGSVAKV 238
Cdd:PRK09700 224 VCSGMVSDV 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-242 |
1.34e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.19 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHGSGAVhaaRAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGrpVEAAKSAEIARY 84
Cdd:PRK13644 1 MIRLENVSYSYPDGTPAL---ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 85 RRSVQMIFQDPFASLnPAHTIAHHLR-RPLKLHRPEIKgaeidvaVRELLQRVRLDPDLVAPKY--PHELSGGQRQRVNI 161
Cdd:PRK13644 76 RKLVGIVFQNPETQF-VGRTVEEDLAfGPENLCLPPIE-------IRKRVDRALAEIGLEKYRHrsPKTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 162 ARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATArYVAEDIAVMYAGQIVEWGSVAKVIDN 241
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSD 225
|
.
gi 1586794399 242 P 242
Cdd:PRK13644 226 V 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-210 |
1.49e-19 |
|
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: 88.57 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 2 TDAILALDSVTKTFGHGS----GAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAK 77
Cdd:TIGR02868 324 AAGAVGLGKPTLELRDLSagypGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 78 SAEIaryRRSVQMIFQDPfaslnpaHTIAHHLRRPLKLHRPEIKGAEidvaVRELLQRVRLDPDLVApkYPH-------- 149
Cdd:TIGR02868 404 QDEV---RRRVSVCAQDA-------HLFDTTVRENLRLARPDATDEE----LWAALERVGLADWLRA--LPDgldtvlge 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 150 ---ELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElnLGLLYITHD 210
Cdd:TIGR02868 468 ggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHH 529
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-209 |
1.59e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.43 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 2 TDAILALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVE-----AA 76
Cdd:PRK11288 1 SSPYLSFDGIGKTFP----GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfasttAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 77 KSAEIAryrrsvqMIFQDpfASLNPAHTIAHHL---RRPLKLHRpeIKGAEIDVAVRELLQRVRLDPDLVAP-KYpheLS 152
Cdd:PRK11288 77 LAAGVA-------IIYQE--LHLVPEMTVAENLylgQLPHKGGI--VNRRLLNYEAREQLEHLGVDIDPDTPlKY---LS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 153 GGQRQRVNIARALAVKPEVIVADEPTSMLdvSVR-LGVL-NLLNEMKRElNLGLLYITH 209
Cdd:PRK11288 143 IGQRQMVEIAKALARNARVIAFDEPTSSL--SAReIEQLfRVIRELRAE-GRVILYVSH 198
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-240 |
2.45e-19 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 84.52 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 30 FSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSaEIARYRRSVQMIFQDPfasLNPAHTI---- 105
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWR-HIGYVPQRHEFAWDFP---ISVAHTVmsgr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 106 AHH---LRRPlklhrpeikGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLD 182
Cdd:TIGR03771 77 TGHigwLRRP---------CVADFAAVRDALRRVGLTE--LADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 183 VSVRLGVLNLLNEMKRELNlGLLYITHDIATARYVAeDIAVMYAGQIVEWGSVAKVID 240
Cdd:TIGR03771 146 MPTQELLTELFIELAGAGT-AILMTTHDLAQAMATC-DRVVLLNGRVIADGTPQQLQD 201
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
28-199 |
2.69e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 84.24 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTT----CARMAMREYLpTSGRILYKGRPVEAAKSAEIARYRRsvqmifQDPFasLNPAH 103
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPRKPDQFQKCVAYVR------QDDI--LLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLR--RPLKLHRPEIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSML 181
Cdd:cd03234 97 TVRETLTytAILRLPRKSSDAIRKKRVEDVLLRDLALTR--IGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170
....*....|....*...
gi 1586794399 182 DVSVRLGVLNLLNEMKRE 199
Cdd:cd03234 175 DSFTALNLVSTLSQLARR 192
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-230 |
3.50e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 84.75 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHGSG-AVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPV----EAAKSA 79
Cdd:COG1101 1 MLELKNLSKTFNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 80 EIARyrrsvqmIFQDPFASLNPAHTIAHHL--------RRPLklhRPEIKGAEIDvAVRELLQRV------RLDpDLVAp 145
Cdd:COG1101 81 YIGR-------VFQDPMMGTAPSMTIEENLalayrrgkRRGL---RRGLTKKRRE-LFRELLATLglglenRLD-TKVG- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 146 kyphELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMY 225
Cdd:COG1101 148 ----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMH 223
|
....*
gi 1586794399 226 AGQIV 230
Cdd:COG1101 224 EGRII 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-239 |
4.02e-19 |
|
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: 87.17 E-value: 4.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARM--AMREYLPTSGRILYK----------GRPV 73
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVlrGMDQYEPTSGRIIYHvalcekcgyvERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 74 EAAKS--------------------AEIARYRRSVQMIFQDPFASLNPAHTIAHHLRrplKLHRPEIKGAE-IDVAVrEL 132
Cdd:TIGR03269 77 KVGEPcpvcggtlepeevdfwnlsdKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLE---ALEEIGYEGKEaVGRAV-DL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 133 LQRVRLDPDLVapKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIA 212
Cdd:TIGR03269 153 IEMVQLSHRIT--HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*..
gi 1586794399 213 TARYVAEDIAVMYAGQIVEWGSVAKVI 239
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEVV 257
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
26-229 |
4.63e-19 |
|
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: 82.26 E-value: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEiarYRRSVqmifqdpfaslnpahti 105
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE---LGDHV----------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 106 ahhlrrplklhrpeikGAeidvavreLLQRVRLDPDLVAPKYpheLSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSV 185
Cdd:cd03246 79 ----------------GY--------LPQDDELFSGSIAENI---LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1586794399 186 RLGVLNLLNEMKRELNLGLLyITHDIATARyVAEDIAVMYAGQI 229
Cdd:cd03246 132 ERALNQAIAALKAAGATRIV-IAHRPETLA-SADRILVLEDGRV 173
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
26-241 |
5.29e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 82.96 E-value: 5.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCAR--MAMREYLPTSGRILYKGRPVEAAKSAEIARyrRSVQMIFQDPfaslnpah 103
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKtiMGHPKYEVTEGEILFKGEDITDLPPEERAR--LGIFLAFQYP-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 tiahhlrrplklhrPEIKGaeidVAVRELLQRVRLDpdlvapkypheLSGGQRQRVNIARALAVKPEVIVADEPTSMLDV 183
Cdd:cd03217 87 --------------PEIPG----VKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586794399 184 -SVRLgVLNLLNEMKRElNLGLLYITHDIATARYVAED-IAVMYAGQIVEWG--SVAKVIDN 241
Cdd:cd03217 138 dALRL-VAEVINKLREE-GKSVLIITHYQRLLDYIKPDrVHVLYDGRIVKSGdkELALEIEK 197
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
39-246 |
5.81e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.70 E-value: 5.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 39 ALVGESGSGKTTCARMAMREYLPTSGRILYKGRP-VEAAKSAEIARYRRSVQMIFQDpfASLNPAHTIAHHLRRPLKLHR 117
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEKGICLPPEKRRIGYVFQD--ARLFPHYKVRGNLRYGMAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 118 PeikgAEIDVAVR-----ELLQRvrldpdlvapkYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNL 192
Cdd:PRK11144 106 V----AQFDKIVAllgiePLLDR-----------YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1586794399 193 LNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNP-LHPY 246
Cdd:PRK11144 171 LERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSaMRPW 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-228 |
1.32e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.44 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 2 TDAILALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPV--EAAKSA 79
Cdd:PRK10762 1 MQALLQLKGIDKAFP----GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfNGPKSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 80 EIAryrrSVQMIFQDpfasLN--PAHTIAHH--LRRPLKLHRPEIKGAEIDVAVRELLQR--VRLDPD-LVApkyphELS 152
Cdd:PRK10762 77 QEA----GIGIIHQE----LNliPQLTIAENifLGREFVNRFGRIDWKKMYAEADKLLARlnLRFSSDkLVG-----ELS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586794399 153 GGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQ 228
Cdd:PRK10762 144 IGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
6-233 |
1.44e-18 |
|
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: 85.48 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTktFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGrpveaaksAEIARYR 85
Cdd:TIGR01842 317 LSVENVT--IVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG--------ADLKQWD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 R-----SVQMIFQDpfASLNPAhTIAHHLRRPLKLHRPE--IKGAEIdVAVRELLQRVRLDPDLVAPKYPHELSGGQRQR 158
Cdd:TIGR01842 387 RetfgkHIGYLPQD--VELFPG-TVAENIARFGENADPEkiIEAAKL-AGVHELILRLPDGYDTVIGPGGATLSGGQRQR 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586794399 159 VNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIAtARYVAEDIAVMYAGQIVEWG 233
Cdd:TIGR01842 463 IALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPS-LLGCVDKILVLQDGRIARFG 535
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-228 |
1.48e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 85.37 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARM--AMREYLPTSGRILYKGRPVEAA-- 76
Cdd:PRK13549 1 MMEYLLEMKNITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVlsGVYPHGTYEGEIIFEGEELQASni 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 77 KSAEiaryRRSVQMIFQDpfASLNPAHTIAHHL---RRPLKLHRpeIKGAEIDVAVRELLQRVRLDPDLVAPKYphELSG 153
Cdd:PRK13549 77 RDTE----RAGIAIIHQE--LALVKELSVLENIflgNEITPGGI--MDYDAMYLRAQKLLAQLKLDINPATPVG--NLGL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586794399 154 GQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQ 228
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
6-238 |
1.58e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 83.26 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGhgSGAVHAARA---ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEA-AKSAEI 81
Cdd:PRK13649 3 INLQNVSYTYQ--AGTPFEGRAlfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 82 ARYRRSVQMIFQDPFASLNpAHTIahhlrrpLK--LHRPEIKGAEIDVAV---RELLQRVRLDPDLVApKYPHELSGGQR 156
Cdd:PRK13649 81 KQIRKKVGLVFQFPESQLF-EETV-------LKdvAFGPQNFGVSQEEAEalaREKLALVGISESLFE-KNPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 157 QRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMkRELNLGLLYITH---DIATaryVAEDIAVMYAGQIVEWG 233
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHlmdDVAN---YADFVYVLEKGKLVLSG 227
|
....*
gi 1586794399 234 SVAKV 238
Cdd:PRK13649 228 KPKDI 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-242 |
2.35e-18 |
|
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: 81.95 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 20 GAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIAR----Y---RRSVqmif 92
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARlgigYvpeGRRI---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 93 qdpFASLnpahTIAHHLRRPLKLHRPeikgaeiDVAVRELLQRV-RLDPDLvapkypHE--------LSGGQRQRVNIAR 163
Cdd:COG0410 90 ---FPSL----TVEENLLLGAYARRD-------RAEVRADLERVyELFPRL------KErrrqragtLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 164 ALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNP 242
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-234 |
2.60e-18 |
|
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: 84.87 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryRRSVQMIFQDP--FaslNpaH 103
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---RAAIGIVPQDTvlF---N--D 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLRRPlklhRPEIKGAEIDVAVR--ELLQRVRLDPD----LVApkyphE----LSGGQRQRVNIARALAVKPEVIV 173
Cdd:COG5265 447 TIAYNIAYG----RPDASEEEVEAAARaaQIHDFIESLPDgydtRVG-----ErglkLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586794399 174 ADEPTSMLDVSVRLGVLNLLNEMKRelNLGLLYITHDIATARYvAEDIAVMYAGQIVEWGS 234
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGT 575
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
11-231 |
2.81e-18 |
|
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: 81.11 E-value: 2.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 11 VTKTFGHGsgavHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAeiaryRRSVQM 90
Cdd:cd03268 6 LTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA-----LRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 91 IFQDPfaSLNPAHTIAHHLRRPLKLHRpeIKGAEIDvavrELLQRVRLD--PDLVAPKYphelSGGQRQRVNIARALAVK 168
Cdd:cd03268 77 LIEAP--GFYPNLTARENLRLLARLLG--IRKKRID----EVLDVVGLKdsAKKKVKGF----SLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586794399 169 PEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVE 231
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-239 |
3.95e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.14 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARyrRSVQMIFQDPFASLNPAHTIAH 107
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR--KVAYLPQQLPAAEGMTVRELVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 108 HLRRPLK--LHRpeiKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSV 185
Cdd:PRK10575 108 IGRYPWHgaLGR---FGAADREKVEEAISLVGLKP--LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 186 RLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVI 239
Cdd:PRK10575 183 QVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
28-242 |
4.37e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.74 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYRRSVQmifQDPFASLN-PAHTIA 106
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP---QDTSLSFEfDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 107 HHLRRPlklHRPEIKGAEI--DVAVRELLQRVrlDPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVS 184
Cdd:PRK09536 99 EMGRTP---HRSRFDTWTEtdRAAVERAMERT--GVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 185 VRLGVLNLLNEMKRELNLGLLYItHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNP 242
Cdd:PRK09536 174 HQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-230 |
5.80e-18 |
|
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: 83.72 E-value: 5.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARM--AMREYLPTSGRILYKGRPVEAAKSAEIA 82
Cdd:TIGR02633 1 LLEMKGIVKTFG----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIlsGVYPHGTWDGEIYWSGSPLKASNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 83 RyrRSVQMIFQDpfASLNPAHTIAHH--LRRPLKLHRPEIKGAEIDVAVRELLQRVRLDPDLVApKYPHELSGGQRQRVN 160
Cdd:TIGR02633 77 R--AGIVIIHQE--LTLVPELSVAENifLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVT-RPVGDYGGGQQQLVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 161 IARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIV 230
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
28-242 |
8.98e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.82 E-value: 8.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRI----LYKG------RPVEAAKSAEIARY---RRSVQMIFQD 94
Cdd:PRK13631 45 ISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGdkknnhELITNPYSKKIKNFkelRRRVSMVFQF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 95 PFASLNpAHTIAHHLR-RPLKLHRPEIKGAEIdvaVRELLQRVRLDPDLVApKYPHELSGGQRQRVNIARALAVKPEVIV 173
Cdd:PRK13631 125 PEYQLF-KDTIEKDIMfGPVALGVKKSEAKKL---AKFYLNKMGLDDSYLE-RSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 174 ADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNP 242
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-236 |
1.08e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.97 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARmAMREYLPTSGRILYKGRPVeaaKSAEIARYRRSVQMIFQDPfaslnpaHTIAH 107
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLN-ALLGFLPYQGSLKINGIEL---RELDPESWRKHLSWVGQNP-------QLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 108 HLRRPLKLHRPEIKGAEIDVAVR-----ELLQRVRLDPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLD 182
Cdd:PRK11174 438 TLRDNVLLGNPDASDEQLQQALEnawvsEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1586794399 183 VSVRLGVLNLLNEMKRELNlgLLYITHDI-ATARYvaEDIAVMYAGQIVEWGSVA 236
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQT--TLMVTHQLeDLAQW--DQIWVMQDGQIVQQGDYA 568
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
6-234 |
1.94e-17 |
|
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: 82.31 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHGSGAVhaARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaKSAEIARYR 85
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLI--LDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL---AGLDVQAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 RSVQMIFQDpfASLNPA---HTIAHHLRRPLKlhrpeikgaeidvAVRELLQRVRLDPDLVA-PKYPH--------ELSG 153
Cdd:TIGR03797 527 RQLGVVLQN--GRLMSGsifENIAGGAPLTLD-------------EAWEAARMAGLAEDIRAmPMGMHtvisegggTLSG 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 154 GQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNemkrELNLGLLYITHDIATARYvAEDIAVMYAGQIVEWG 233
Cdd:TIGR03797 592 GQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLE----RLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
.
gi 1586794399 234 S 234
Cdd:TIGR03797 667 T 667
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-238 |
2.79e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.16 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 24 AARA---ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEA-AKSAEIARYRRSVQMIFQDPFASL 99
Cdd:PRK13643 18 ASRAlfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStSKQKEIKPVRKKVGVVFQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 100 NPAHTIAHHLRRPLKLHrpeIKGAEIDVAVRELLQRVRLDPDLvAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTS 179
Cdd:PRK13643 98 FEETVLKDVAFGPQNFG---IPKEKAEKIAAEKLEMVGLADEF-WEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 180 MLDVSVRLGVLNLLnEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKV 238
Cdd:PRK13643 174 GLDPKARIEMMQLF-ESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-230 |
4.39e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.22 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVE-----AAKSAEIArY----RRSvqmifqdpf 96
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprDAIRAGIA-YvpedRKG--------- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 97 ASLNPAHTIAH-----HLRRPLKLHRpeIKGAEIDVAVRELLQRVRL---DPDLVApkypHELSGGQRQRVNIARALAVK 168
Cdd:COG1129 339 EGLVLDLSIREnitlaSLDRLSRGGL--LDRRRERALAEEYIKRLRIktpSPEQPV----GNLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586794399 169 PEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIV 230
Cdd:COG1129 413 PKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-234 |
5.37e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.02 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 14 TFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryRRSVQMIFQ 93
Cdd:PRK11160 345 SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---RQAISVVSQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 DPfaslnpaHTIAHHLRRPLKLHRPEIkgaeIDVAVRELLQRVRLDpDLVAPKYP---------HELSGGQRQRVNIARA 164
Cdd:PRK11160 422 RV-------HLFSATLRDNLLLAAPNA----SDEALIEVLQQVGLE-KLLEDDKGlnawlgeggRQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 165 LAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRelNLGLLYITHdiataRYVAED----IAVMYAGQIVEWGS 234
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH-----RLTGLEqfdrICVMDNGQIIEQGT 556
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-214 |
5.47e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.28 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 2 TDAILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEI 81
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 82 ARYR-RSVQMIFQDPFasLNPAHTIAHHLRRPlKLHRPEIKGAEIDVAVrELLQRVRLDPDLvaPKYPHELSGGQRQRVN 160
Cdd:PRK10584 83 AKLRaKHVGFVFQSFM--LIPTLNALENVELP-ALLRGESSRQSRNGAK-ALLEQLGLGKRL--DHLPAQLSGGEQQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 161 IARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATA 214
Cdd:PRK10584 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-260 |
5.67e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.59 E-value: 5.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 8 LDSVTKTFGhGSGAVHAaraISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARyRRS 87
Cdd:COG4604 4 IKNVSKRYG-GKVVLDD---VSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK-RLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 88 VqmIFQDPfaSLNPAHTIA---------HHLRRPlklhrpeikGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQR 158
Cdd:COG4604 79 I--LRQEN--HINSRLTVRelvafgrfpYSKGRL---------TAEDREIIDEAIAYLDLED--LADRYLDELSGGQRQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 159 VNIARALAVKPEVIVADEPTSMLDV--SVRLgvLNLLNEMKRELNLGLLYITHDI-ATARYvAEDIAVMYAGQIVEWGSV 235
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDMkhSVQM--MKLLRRLADELGKTVVIVLHDInFASCY-ADHIVAMKDGRVVAQGTP 220
|
250 260
....*....|....*....|....*
gi 1586794399 236 AKVIDNPlhpytrlLLSAVPDPDVR 260
Cdd:COG4604 221 EEIITPE-------VLSDIYDTDIE 238
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-233 |
5.68e-17 |
|
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: 76.97 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 14 TFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAeiarYRRSVQMIFQ 93
Cdd:cd03247 7 SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSLISVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 DPfaslnpahtiahHLrrplklhrpeikgaeIDVAVRELLQRvrldpdlvapkyphELSGGQRQRVNIARALAVKPEVIV 173
Cdd:cd03247 83 RP------------YL---------------FDTTLRNNLGR--------------RFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 174 ADEPTSMLDVSVRLGVLNLLNEMKRELNlgLLYITHDIATARYVAEdIAVMYAGQIVEWG 233
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKT--LIWITHHLTGIEHMDK-ILFLENGKIIMQG 178
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-242 |
7.15e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.49 E-value: 7.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGhGSGAVHAaraISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAE 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFG-GLLAVNN---VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 IARyrRSVQMIFQDP--FASLNPAHT--IAHHlrRPLK-------LHRPEIKGAEIDVAVREL--LQRVRLDPdlVAPKY 147
Cdd:PRK11300 77 IAR--MGVVRTFQHVrlFREMTVIENllVAQH--QQLKtglfsglLKTPAFRRAESEALDRAAtwLERVGLLE--HANRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 148 PHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAG 227
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
250
....*....|....*
gi 1586794399 228 QIVEWGSVAKVIDNP 242
Cdd:PRK11300 231 TPLANGTPEEIRNNP 245
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-240 |
8.03e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.08 E-value: 8.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGHGSgavhAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAksAE 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKL----VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR--AR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 IARYRrsVQMIFQdpFASLNPAHTIAHHLR---RPLKLhrpeiKGAEIDVAVRELLQRVRLDPDLVAPKypHELSGGQRQ 157
Cdd:PRK13537 77 HARQR--VGVVPQ--FDNLDPDFTVRENLLvfgRYFGL-----SAAAARALVPPLLEFAKLENKADAKV--GELSGGMKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 158 RVNIARALAVKPEVIVADEPTSMLDVSVRlgvlNLLNEMKREL---NLGLLYITHDIATARYVAEDIAVMYAGQIVEWGS 234
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQAR----HLMWERLRSLlarGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGA 221
|
....*.
gi 1586794399 235 VAKVID 240
Cdd:PRK13537 222 PHALIE 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-240 |
8.59e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.49 E-value: 8.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGhGSGAVHAaraISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAakSAE 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYG-DKAVVNG---LSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 IARYRrsVQMIFQdpFASLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPDLVAPKypHELSGGQRQRVN 160
Cdd:PRK13536 111 LARAR--IGVVPQ--FDNLDLEFTVRENLLVFGRYFG--MSTREIEAVIPSLLEFARLESKADARV--SDLSGGMKRRLT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 161 IARALAVKPEVIVADEPTSMLDVSVRlgvlNLLNEMKREL---NLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAK 237
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHAR----HLIWERLRSLlarGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHA 258
|
...
gi 1586794399 238 VID 240
Cdd:PRK13536 259 LID 261
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
26-243 |
9.08e-17 |
|
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: 77.58 E-value: 9.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEiaRYRRSVQMIFQDP--FASLnpah 103
Cdd:cd03218 17 NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK--RARLGIGYLPQEAsiFRKL---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLRRPLKLHrpEIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLD- 182
Cdd:cd03218 91 TVEENILAVLEIR--GLSKKEREEKLEELLEEFHITH--LRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586794399 183 VSVRLgVLNLLNEMKrELNLGLLyIT-HDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNPL 243
Cdd:cd03218 167 IAVQD-IQKIIKILK-DRGIGVL-ITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
11-250 |
6.00e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 76.66 E-value: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 11 VTKTFGHGSG-AVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILY-------KGRPVEAAKSAE-- 80
Cdd:PRK13651 8 IVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknKKKTKEKEKVLEkl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 ------------IARYRRSVQMIFQdpFASLNP-AHTIAHHLR-RPLKLHrpeIKGAEIDVAVRELLQRVRLDPDLVaPK 146
Cdd:PRK13651 88 viqktrfkkikkIKEIRRRVGVVFQ--FAEYQLfEQTIEKDIIfGPVSMG---VSKEEAKKRAAKYIELVGLDESYL-QR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 147 YPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYA 226
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250 260 270
....*....|....*....|....*....|.
gi 1586794399 227 GQIVEWGSVAKV-------IDNPLHPyTRLL 250
Cdd:PRK13651 241 GKIIKDGDTYDIlsdnkflIENNMEP-PKLL 270
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-238 |
6.63e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.81 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAgrALALVGESGSGKTTCArMAMREYL-PTSGRILYKGRPVEAAKSAEIArYRRSVQMIFQDPFASL---NPAH 103
Cdd:PRK13638 22 LDFSLSP--VTGLVGANGCGKSTLF-MNLSGLLrPQKGAVLWQGKPLDYSKRGLLA-LRQQVATVFQDPEQQIfytDIDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLRrplklhrpeikgaEIDVAVRELLQRVRLDPDLV-APKYPHE----LSGGQRQRVNIARALAVKPEVIVADEPT 178
Cdd:PRK13638 98 DIAFSLR-------------NLGVPEAEITRRVDEALTLVdAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 179 SMLDVSVRLGVLNLLNEMKRELNlGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKV 238
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-193 |
6.99e-16 |
|
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: 74.12 E-value: 6.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCAR--MAMREYLPTSGRILYKGRPVEAAksaeiaRYRRSVQMIFQDP--FASLNPAH 103
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNalAGRRTGLGVSGEVLINGRPLDKR------SFRKIIGYVPQDDilHPTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLrrplklhrpEIKGaeidvavrellqrvrldpdlvapkypheLSGGQRQRVNIARALAVKPEVIVADEPTSMLDV 183
Cdd:cd03213 102 TLMFAA---------KLRG----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170
....*....|
gi 1586794399 184 SVRLGVLNLL 193
Cdd:cd03213 145 SSALQVMSLL 154
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-232 |
1.22e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 8 LDSVTKTFGhgsgavhaARA----ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRilykgrpVEAAKSAEIAR 83
Cdd:COG0488 1 LENLSKSFG--------GRPllddVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGE-------VSIPKGLRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 84 YRrsvqmifQDPFasLNPAHTIAHHLRRPLK--------LHRPEIKGAEIDVA----------------------VRELL 133
Cdd:COG0488 66 LP-------QEPP--LDDDLTVLDTVLDGDAelraleaeLEELEAKLAEPDEDlerlaelqeefealggweaearAEEIL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 134 QRVRLDP-DLVAPkyPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDV-SVRlgvlnLLNEMKRELNLGLLYITHDi 211
Cdd:COG0488 137 SGLGFPEeDLDRP--VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIE-----WLEEFLKNYPGTVLVVSHD- 208
|
250 260
....*....|....*....|....*
gi 1586794399 212 ataRY----VAEDIAVMYAGQIVEW 232
Cdd:COG0488 209 ---RYfldrVATRILELDRGKLTLY 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-233 |
1.23e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.30 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGHGSGAVHAAraiSFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAE 80
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDA---SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 IARY-------RRSVQMIFQDPFASLNPAHTiaHHLRRPlKLHRPEIkgaeidvaVRELLQRVrldpDLVAPKYPH--EL 151
Cdd:PRK15056 79 LVAYvpqseevDWSFPVLVEDVVMMGRYGHM--GWLRRA-KKRDRQI--------VTAALARV----DMVEFRHRQigEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 152 SGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATaryVAE--DIAVMYAGQI 229
Cdd:PRK15056 144 SGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGS---VTEfcDYTVMVKGTV 219
|
....
gi 1586794399 230 VEWG 233
Cdd:PRK15056 220 LASG 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-232 |
2.21e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.87 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRilykgrpVEAAKSAEIARY 84
Cdd:COG0488 315 VLELEGLSKSYG----DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-------VKLGETVKIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 85 RrsvqmifQDpFASLNPAHTIAHHLRRplklHRPEIKgaeiDVAVRELLQRVRLDPDLVApKYPHELSGGQRQRVNIARA 164
Cdd:COG0488 384 D-------QH-QEELDPDKTVLDELRD----GAPGGT----EQEVRGYLGRFLFSGDDAF-KPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 165 LAVKPEVIVADEPTSMLDVsvrlgvlnllnEMKRELNLGL-------LYITHDiataRY----VAEDIAVMYAGQIVEW 232
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDI-----------ETLEALEEALddfpgtvLLVSHD----RYfldrVATRILEFEDGGVREY 510
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
28-234 |
2.35e-15 |
|
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: 73.30 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaksAEIAR--YRRSVQMIFQDP--FASlnpah 103
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI-----SKIGLhdLRSRISIIPQDPvlFSG----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLRrPLKLHRpeikgaeiDVAVRELLQRVRLDPDLVAPKYPHE---------LSGGQRQRVNIARALAVKPEVIVA 174
Cdd:cd03244 93 TIRSNLD-PFGEYS--------DEELWQALERVGLKEFVESLPGGLDtvveeggenLSVGQRQLLCLARALLRKSKILVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586794399 175 DEPTSMLDVSVRLGVLNLL-NEMKrelNLGLLYITHDIATaryVAE-D-IAVMYAGQIVEWGS 234
Cdd:cd03244 164 DEATASVDPETDALIQKTIrEAFK---DCTVLTIAHRLDT---IIDsDrILVLDKGRVVEFDS 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
26-239 |
3.40e-15 |
|
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: 75.55 E-value: 3.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGrpveaaksAEIARYRRSV--QMIF---QDPfaSLN 100
Cdd:COG4618 349 RGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG--------ADLSQWDREElgRHIGylpQDV--ELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 101 PAhTIAHHLRRpLKLHRPE--IKGAEIdVAVRELLQRV------RLDPDLVApkypheLSGGQRQRVNIARALAVKPEVI 172
Cdd:COG4618 419 DG-TIAENIAR-FGDADPEkvVAAAKL-AGVHEMILRLpdgydtRIGEGGAR------LSGGQRQRIGLARALYGDPRLV 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 173 VADEPTSMLDVSVRLGVLNLLNEMKRElnlG--LLYITHDIATARyVAEDIAVMYAGQIVEWGSVAKVI 239
Cdd:COG4618 490 VLDEPNSNLDDEGEAALAAAIRALKAR---GatVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
28-260 |
4.02e-15 |
|
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: 73.20 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSG---RIL---YKGRPVEAAK------SAEIA-RYRRSV---QMI 91
Cdd:COG1119 22 ISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVWELRkriglvSPALQlRFPRDEtvlDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 92 FQDPFASLNpahtiahhlrrplkLHRpEIKGAEIDVAvRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEV 171
Cdd:COG1119 102 LSGFFDSIG--------------LYR-EPTDEQRERA-RELLELLGLAH--LADRPFGTLSQGEQRRVLIARALVKDPEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 172 IVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIataryvaEDI-------AVMYAGQIVEWGSVAKVIdnplh 244
Cdd:COG1119 164 LILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHV-------EEIppgithvLLLKDGRVVAAGPKEEVL----- 231
|
250
....*....|....*.
gi 1586794399 245 pyTRLLLSAVPDPDVR 260
Cdd:COG1119 232 --TSENLSEAFGLPVE 245
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
26-239 |
7.44e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.94 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREY--------LPTSGRILYKGRPVEAAKSAEIARYRRSVQMIFQDPFA 97
Cdd:PRK13547 18 RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAFA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 98 SlnPAHTIAHHLRRPLKLHRPEIKGAEIDVAVRELlqrVRLDPDLVAPKYPHELSGGQRQRVNIARALA---------VK 168
Cdd:PRK13547 98 F--SAREIVLLGRYPHARRAGALTHRDGEIAWQAL---ALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586794399 169 PEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVI 239
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-215 |
9.53e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.11 E-value: 9.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 18 GSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEA---AKSAEI----ARYRRSVQM 90
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAyvpQRSEVPdslpLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 91 IFqdpFASLNPahtiahhLRRPLKLHRPEIKGAEIDVAVRELLQRvRLDpdlvapkyphELSGGQRQRVNIARALAVKPE 170
Cdd:NF040873 81 GR---WARRGL-------WRRLTRDDRAAVDDALERVGLADLAGR-QLG----------ELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1586794399 171 VIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATAR 215
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-230 |
1.59e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.52 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 3 DAILALDSVTKTFGHGSGAVhaaRAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEia 82
Cdd:COG3845 255 EVVLEVENLSVRDDRGVPAL---KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE-- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 83 RYRRSVQMIFQDPFAS-LNPAHTIAHHL-----RRPLKLHRPEIKGAEIDVAVRELLQR--VRL-DPDLVApkypHELSG 153
Cdd:COG3845 330 RRRLGVAYIPEDRLGRgLVPDMSVAENLilgryRRPPFSRGGFLDRKAIRAFAEELIEEfdVRTpGPDTPA----RSLSG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586794399 154 GQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIV 230
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
28-209 |
1.78e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYrrsvqMIFQDPfasLNPAHTIAH 107
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY-----LGHRNA---MKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 108 HLR--RplklhrpEIKGAEiDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDV-S 184
Cdd:PRK13539 93 NLEfwA-------AFLGGE-ELDIAAALEAVGLAP--LAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAaA 162
|
170 180
....*....|....*....|....*..
gi 1586794399 185 VRLgvlnLLNEMKRELNLGLLYI--TH 209
Cdd:PRK13539 163 VAL----FAELIRAHLAQGGIVIaaTH 185
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
28-234 |
1.82e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.60 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryRRSVQMIFQDPFaslnpahTIAH 107
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---RQGVAMVQQDPV-------VLAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 108 HLRRPLKLhrpeikGAEID-VAVRELLQRVRLDPdlVAPKYP-----------HELSGGQRQRVNIARALAVKPEVIVAD 175
Cdd:PRK10790 430 TFLANVTL------GRDISeEQVWQALETVQLAE--LARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 176 EPTSMLDVSVRLGVLNLLNEMKRELNlgLLYITHDIATArYVAEDIAVMYAGQIVEWGS 234
Cdd:PRK10790 502 EATANIDSGTEQAIQQALAAVREHTT--LVVIAHRLSTI-VEADTILVLHRGQAVEQGT 557
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-291 |
2.40e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.04 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 22 VHAARAISFSLHAGRALALVGESGSGKTTCARMamreyL-----PTSGRILYKGR-PVEaaksaEIARYRRSVQMIF--- 92
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKM-----LtgilvPTSGEVRVLGYvPFK-----RRKEFARRIGVVFgqr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 93 ----QDpfasLNPAHTiahhlrrpLKLHRP--EIKGAEIDVAVRELLQRVRLDPDLvapKYP-HELSGGQRQRVNIARAL 165
Cdd:COG4586 105 sqlwWD----LPAIDS--------FRLLKAiyRIPDAEYKKRLDELVELLDLGELL---DTPvRQLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 166 AVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDNpLHP 245
Cdd:COG4586 170 LHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKER-FGP 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 246 YTRL---LLSAVPDPD-------VRFDDPKARLRPDEVEDIRRRSA--MPQDDIVEFE 291
Cdd:COG4586 249 YKTIvleLAEPVPPLElprggevIEREGNRVRLEVDPRESLAEVLArlLARYPVRDLT 306
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
7-242 |
8.54e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 71.28 E-value: 8.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 7 ALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEiarYRR 86
Cdd:PRK10789 313 ELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS---WRS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 87 SVQMIFQDPFA-SLNPAHTIAhhlrrplkLHRPEIKGAEIDVAVRelLQRVRLDPDLVAPKYPHE-------LSGGQRQR 158
Cdd:PRK10789 390 RLAVVSQTPFLfSDTVANNIA--------LGRPDATQQEIEHVAR--LASVHDDILRLPQGYDTEvgergvmLSGGQKQR 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 159 VNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNlglLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKV 238
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRT---VIISAHRLSALTEASEILVMQHGHIAQRGNHDQL 536
|
....
gi 1586794399 239 IDNP 242
Cdd:PRK10789 537 AQQS 540
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-238 |
1.58e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.81 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTC-ARMAmrEYLPTSGRILYKGRPVEAAKSAEIARYRR--SVQmifQDPFASLNPAHT 104
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLlARMA--GLLPGSGSIQFAGQPLEAWSAAELARHRAylSQQ---QTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 105 iahhlrrpLKLHRPEikGAEIDV---AVRELLQRVRLDPDLvaPKYPHELSGGQRQRVNIARA-LAVKPEV------IVA 174
Cdd:PRK03695 90 --------LTLHQPD--KTRTEAvasALNEVAEALGLDDKL--GRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586794399 175 DEPTSMLDVSVRLGVLNLLNEMKReLNLGLLYITHDIA-TARYvAEDIAVMYAGQIVEWGSVAKV 238
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNhTLRH-ADRVWLLKQGKLLASGRRDEV 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
28-243 |
1.68e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 68.52 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRpveaaksaEIAR---YRRSVQMIF---QDP--FASL 99
Cdd:COG1137 22 VSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE--------DITHlpmHKRARLGIGylpQEAsiFRKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 100 npahTIAHHLRRPLKLHrpEIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTS 179
Cdd:COG1137 94 ----TVEDNILAVLELR--KLSKKEREERLEELLEEFGITH--LRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586794399 180 MLD-VSV----RLgVLNLlnemkRELNLGLLyIT-HDiataryVAE-----DIA-VMYAGQIVEWGSVAKVIDNPL 243
Cdd:COG1137 166 GVDpIAVadiqKI-IRHL-----KERGIGVL-ITdHN------VREtlgicDRAyIISEGKVLAEGTPEEILNNPL 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
26-234 |
2.01e-13 |
|
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: 67.82 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaKSAEIARYRRSVQMIFQDP--FASlnpah 103
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLRSSLTIIPQDPtlFSG----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLrrplklhrpEIKGAEIDVAVRELLqRVRLDPDlvapkyphELSGGQRQRVNIARALAVKPEVIVADEPTSMLDV 183
Cdd:cd03369 97 TIRSNL---------DPFDEYSDEEIYGAL-RVSEGGL--------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDY 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 184 SVRlgvlNLLNEMKREL--NLGLLYITHDIAT-ARYvaEDIAVMYAGQIVEWGS 234
Cdd:cd03369 159 ATD----ALIQKTIREEftNSTILTIAHRLRTiIDY--DKILVMDAGEVKEYDH 206
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-241 |
2.22e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.50 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGHGsgavHAARAISFSLHAGRALALVGESGSGKTTCAR----MAMREYLPTSgRILYKGRPVEAAK--S 78
Cdd:PRK09984 4 IIRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGS-HIELLGRTVQREGrlA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 79 AEIARYRRSVQMIFQDpFASLNPAHTIAHHL----------RRPLKLHRPEIKGaeidvavRELLQRVRLDPDLVAPKYP 148
Cdd:PRK09984 79 RDIRKSRANTGYIFQQ-FNLVNRLSVLENVLigalgstpfwRTCFSWFTREQKQ-------RALQALTRVGMVHFAHQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 149 HELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQ 228
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
250
....*....|...
gi 1586794399 229 IVEWGSvAKVIDN 241
Cdd:PRK09984 231 VFYDGS-SQQFDN 242
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
11-209 |
3.05e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 11 VTKTFGHGSGAV--HAARAISFSLHAGRALALVGESGSGKTTCARMAMREYlptsgrilyKGRPVEAAksaeiaryrrsv 88
Cdd:COG2401 30 VLEAFGVELRVVerYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL---------KGTPVAGC------------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 89 qmiFQDPFASLNPAHTIAHHLRRPlklhrpeikgAEIDVAVrELLQRVRL-DPDLVAPKYpHELSGGQRQRVNIARALAV 167
Cdd:COG2401 89 ---VDVPDNQFGREASLIDAIGRK----------GDFKDAV-ELLNAVGLsDAVLWLRRF-KELSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1586794399 168 KPEVIVADEPTSMLDVSV-RLGVLNLLnEMKRELNLGLLYITH 209
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTaKRVARNLQ-KLARRAGITLVVATH 195
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-223 |
3.79e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 29 SFSL-------HAGRALALVGESGSGKTTCARMAMREYLPTSG------RILYKGRPVEAAKSAEIARYRRSVQMIFQDP 95
Cdd:PRK13409 352 DFSLeveggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGevdpelKISYKPQYIKPDYDGTVEDLLRSITDDLGSS 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 96 FaslnpahtIAHHLRRPLKLHRpeikgaeidvavreLLQRvRLDpdlvapkyphELSGGQRQRVNIARALAVKPEVIVAD 175
Cdd:PRK13409 432 Y--------YKSEIIKPLQLER--------------LLDK-NVK----------DLSGGELQRVAIAACLSRDADLYLLD 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1586794399 176 EPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAV 223
Cdd:PRK13409 479 EPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-224 |
6.14e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.29 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 22 VHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRpvEAAKSAEIARYRRSVQMIFQDPFASLNp 101
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS--HNLKDINLKWWRSKIGVVSQDPLLFSN- 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 102 ahTIAHHLRRPL-----------------------------------------------------KLHRPEIKGAEI-DV 127
Cdd:PTZ00265 475 --SIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemRKNYQTIKDSEVvDV 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 128 AVRELLQR-VRLDPD----LVAPKyPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNL 202
Cdd:PTZ00265 553 SKKVLIHDfVSALPDkyetLVGSN-ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 631
|
250 260
....*....|....*....|..
gi 1586794399 203 GLLYITHDIATARYvAEDIAVM 224
Cdd:PTZ00265 632 ITIIIAHRLSTIRY-ANTIFVL 652
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
26-184 |
7.96e-13 |
|
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: 65.84 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAksaeiaRYRRSVQMIFQDPFASLNPAHTI 105
Cdd:TIGR01189 17 EGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ------RDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 106 AHHLRRPLKLHRPEikgaeiDVAVRELLQRVRLD--PDLVApkypHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDV 183
Cdd:TIGR01189 91 LENLHFWAAIHGGA------QRTIEDALAAVGLTgfEDLPA----AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
.
gi 1586794399 184 S 184
Cdd:TIGR01189 161 A 161
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-241 |
8.75e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 8.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARY 84
Cdd:PRK15439 11 LLCARSISKQYS----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 85 rrSVQMIFQDP--FASLNPAHTIAHHLRRPLKLHRpeikgaeidvAVRELLQR--VRLDPDLVAPKypheLSGGQRQRVN 160
Cdd:PRK15439 87 --GIYLVPQEPllFPNLSVKENILFGLPKRQASMQ----------KMKQLLAAlgCQLDLDSSAGS----LEVADRQIVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 161 IARALAVKPEVIVADEPTSMLD-VSVRlgvlNLLNEMK--RELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAK 237
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASLTpAETE----RLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
....
gi 1586794399 238 VIDN 241
Cdd:PRK15439 227 LSTD 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
28-224 |
1.02e-12 |
|
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: 64.39 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRIlykgrpveaaksaeiaryrrsvqmifqdpfaSLNPAHTIAH 107
Cdd:cd03221 19 ISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-------------------------------TWGSTVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 108 hlrrplklhrpeikgaeidvavrellqrvrldpdlvapkYPHeLSGGQRQRVNIARALAVKPEVIVADEPTSMLDV-SVr 186
Cdd:cd03221 68 ---------------------------------------FEQ-LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLeSI- 106
|
170 180 190
....*....|....*....|....*....|....*...
gi 1586794399 187 lgvlNLLNEMKRELNLGLLYITHDIATARYVAEDIAVM 224
Cdd:cd03221 107 ----EALEEALKEYPGTVILVSHDRYFLDQVATKIIEL 140
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
26-196 |
1.08e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.91 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARmAMREYLP-TSGRILykgRPVEAaksaeiaryrrsvQMIF--QDPFAslnPA 102
Cdd:COG4178 380 EDLSLSLKPGERLLITGPSGSGKSTLLR-AIAGLWPyGSGRIA---RPAGA-------------RVLFlpQRPYL---PL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 103 HTiahhLRRplKLHRPEIKGAEIDVAVRELLQRVRLDP-----DLVAPkYPHELSGGQRQRVNIARALAVKPEVIVADEP 177
Cdd:COG4178 440 GT----LRE--ALLYPATAEAFSDAELREALEAVGLGHlaerlDEEAD-WDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170
....*....|....*....
gi 1586794399 178 TSMLDVSVRLGVLNLLNEM 196
Cdd:COG4178 513 TSALDEENEAALYQLLREE 531
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-223 |
1.68e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 67.50 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGHGSGAVHAAraisfSLHAGRALALVGESGSGKTTCARMAMREYLPTSG------RILYKGRPVE 74
Cdd:COG1245 337 EEETLVEYPDLTKSYGGFSLEVEGG-----EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGevdedlKISYKPQYIS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 75 AAksaeiarYRRSVQMIFQDPFASLNPAHTIAHHLRRPLKLHRpeikgaeidvavreLLQRvRLDpdlvapkyphELSGG 154
Cdd:COG1245 412 PD-------YDGTVEEFLRSANTDDFGSSYYKTEIIKPLGLEK--------------LLDK-NVK----------DLSGG 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 155 QRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAV 223
Cdd:COG1245 460 ELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-240 |
2.37e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.49 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAIlALDSVTKTF------------------GHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPT 62
Cdd:COG1134 1 MSSMI-EVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 63 SGRILYKGR---PVEAAksaeiaryrrsvqmifqdpfASLNPAHT-------IAhhlrRPLKLHRPEIK----------- 121
Cdd:COG1134 80 SGRVEVNGRvsaLLELG--------------------AGFHPELTgreniylNG----RLLGLSRKEIDekfdeivefae 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 122 -GAEIDVAVRellqrvrldpdlvapKYphelSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKREl 200
Cdd:COG1134 136 lGDFIDQPVK---------------TY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES- 195
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1586794399 201 NLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVID 240
Cdd:COG1134 196 GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-225 |
2.61e-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: 65.47 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 22 VHAARAISFSLHA------GRALALVGESGSGKTTCARMAMREYLPTSGRilYKGRPveaaKSAEIARYRRSVQMifQDP 95
Cdd:cd03236 7 VHRYGPNSFKLHRlpvpreGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPP----DWDEILDEFRGSEL--QNY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 96 FASLnpahtIAHHLRRPLKLHRPEIKGAEIDVAVRELLQRV-----------RLDPDLVAPKYPHELSGGQRQRVNIARA 164
Cdd:cd03236 79 FTKL-----LEGDVKVIVKPQYVDLIPKAVKGKVGELLKKKdergkldelvdQLELRHVLDRNIDQLSGGELQRVAIAAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586794399 165 LAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNlGLLYITHDIATARYVAEDIAVMY 225
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-229 |
3.74e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.23 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTktfghGSGAVHaaraISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAeiARY 84
Cdd:PRK15439 268 VLTVEDLT-----GEGFRN----ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTA--QRL 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 85 R---------RSVQMIFQDPFASLNpAHTIAHHlRRPLKLHRPE-------------IKGAEIDVAVRELlqrvrldpdl 142
Cdd:PRK15439 337 ArglvylpedRQSSGLYLDAPLAWN-VCALTHN-RRGFWIKPARenavleryrralnIKFNHAEQAARTL---------- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 143 vapkyphelSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIA 222
Cdd:PRK15439 405 ---------SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVL 474
|
....*..
gi 1586794399 223 VMYAGQI 229
Cdd:PRK15439 475 VMHQGEI 481
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-233 |
4.22e-12 |
|
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: 64.48 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 18 GSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGR---PVEAAksaeiaryrrsvqmifqd 94
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssLLGLG------------------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 95 pfASLNPAHTIAHHLRRPLKLHRpeIKGAEIDVAVRELLQRVRLDPDLVAP-KyphELSGGQRQRVNIARALAVKPEVIV 173
Cdd:cd03220 93 --GGFNPELTGRENIYLNGRLLG--LSRKEIDEKIDEIIEFSELGDFIDLPvK---TYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 174 ADEPTSMLDVSVRLGVLNLLNEMKRELNlGLLYITHDIATARYVAEDIAVMYAGQIVEWG 233
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-233 |
4.50e-12 |
|
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: 63.82 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 4 AILALDSVTKTFGHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARM---AMREYLPTSGRILYKGRPVEAAKSae 80
Cdd:cd03233 2 STLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAlanRTEGNVSVEGDIHYNGIPYKEFAE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 iaRYRRSVQMIFQDpfaslnpahtiahhlrrplKLHRPEIkgaeidvAVRELLQ-RVRLDPDlvapKYPHELSGGQRQRV 159
Cdd:cd03233 80 --KYPGEIIYVSEE-------------------DVHFPTL-------TVRETLDfALRCKGN----EFVRGISGGERKRV 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586794399 160 NIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGL---LYITHDIATARYvaEDIAVMYAGQIVEWG 233
Cdd:cd03233 128 SIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTfvsLYQASDEIYDLF--DKVLVLYEGRQIYYG 202
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-230 |
5.49e-12 |
|
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: 64.28 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 22 VHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKG-RPVEAAKsaeiaRYRRSVQMIF---QDPFA 97
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWKRRK-----KFLRRIGVVFgqkTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 98 SLNPAHTIA--HHLRRplklhrpeIKGAEIDVAVRELLQRVRLDPDLVAPKypHELSGGQRQRVNIARALAVKPEVIVAD 175
Cdd:cd03267 109 DLPVIDSFYllAAIYD--------LPPARFKKRLDELSELLDLEELLDTPV--RQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1586794399 176 EPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIV 230
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
35-182 |
1.15e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.07 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 35 GRALALVGESGSGKTTCARmAMREYLPT----SGRILYKGRPVEAAKSAEIARYRRSVQMIFqdpfaslnPAHTIAHHL- 109
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMN-ALAFRSPKgvkgSGSVLLNGMPIDAKEMRAISAYVQQDDLFI--------PTLTVREHLm 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 110 -RRPLKLHRPEIKGAEIDvAVRELLQRVRLDP--DLV--APKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLD 182
Cdd:TIGR00955 122 fQAHLRMPRRVTKKEKRE-RVDEVLQALGLRKcaNTRigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-223 |
1.61e-11 |
|
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: 63.20 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 31 SLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeAAKSAEI-ARYRRSVqmifQDPFASLNPAHTIAHHL 109
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIkADYEGTV----RDLLSSITKDFYTHPYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 110 R----RPLKLhrpeikgaeIDVAVRELLqrvrldpdlvapkyphELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSV 185
Cdd:cd03237 96 KteiaKPLQI---------EQILDREVP----------------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 1586794399 186 RLGVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAV 223
Cdd:cd03237 151 RLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-225 |
1.69e-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: 64.42 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 35 GRALALVGESGSGKTTCARMAMREYLPTSGRIlykgrPVEAAKSAEIARYRRSvqmIFQDPFAslnpahtiahhlrrplK 114
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDY-----DEEPSWDEVLKRFRGT---ELQDYFK----------------K 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 115 LHRPEIKGAE----IDVA-------VRELLQRV-----------RLDPDLVAPKYPHELSGGQRQRVNIARALAVKPEVI 172
Cdd:COG1245 155 LANGEIKVAHkpqyVDLIpkvfkgtVRELLEKVdergkldelaeKLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586794399 173 VADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMY 225
Cdd:COG1245 235 FFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
26-235 |
3.01e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.35 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARM--AMREYLPTSGRILYKGRPVEAAKSAEiaRYRRSVQMIFQDPFASlnPAH 103
Cdd:CHL00131 24 KGLNLSINKGEIHAIMGPNGSGKSTLSKViaGHPAYKILEGDILFKGESILDLEPEE--RAHLGIFLAFQYPIEI--PGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLR-----RPLKLHRPEIKGAEIDVAVRELLQRVRLDPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPT 178
Cdd:CHL00131 100 SNADFLRlaynsKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEGFSGGEKKRNEILQMALLDSELAILDETD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 179 SMLDVSVRLGVLNLLNEMKRELNlGLLYITHDIATARYVAED-IAVMYAGQIVEWGSV 235
Cdd:CHL00131 180 SGLDIDALKIIAEGINKLMTSEN-SIILITHYQRLLDYIKPDyVHVMQNGKIIKTGDA 236
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-225 |
3.10e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 35 GRALALVGESGSGKTTCARMAMREYLPTSGRilYKGrpvEAAKSAEIARYRRSVqmiFQDPFASL-NPAHTIAHhlrrpl 113
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEE---EPSWDEVLKRFRGTE---LQNYFKKLyNGEIKVVH------ 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 114 klhrpeiKGAEIDVA-------VRELLQRV-----------RLDPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVAD 175
Cdd:PRK13409 165 -------KPQYVDLIpkvfkgkVRELLKKVdergkldevveRLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1586794399 176 EPTSMLDVSVRLGVLNLLNEMKRELNlgLLYITHDIATARYVAEDIAVMY 225
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAEGKY--VLVVEHDLAVLDYLADNVHIAY 285
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
28-184 |
7.89e-11 |
|
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: 60.20 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeAAKSAEIARyrrsvQMIFQDPFASLNPAHTIAH 107
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIAR-----GLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 108 HLRRPLKLHRpeikgaeiDVAVRELLQRVRLD--PDLVApkypHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVS 184
Cdd:cd03231 93 NLRFWHADHS--------DEQVEEALARVGLNgfEDRPV----AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
230-281 |
1.48e-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: 56.26 E-value: 1.48e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1586794399 230 VEWGSVAKVIDNPLHPYTRLLLSAVPDPDVRfdDPKARLRPDEVEDIRRRSA 281
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPP--KRPLYTIPGNVPSLLELPE 50
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
28-241 |
1.77e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.91 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEiaRYRRSVQMIFQDpfASLNPAHTIAH 107
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYLPQE--ASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 108 HLRRPLKLhRPEIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRL 187
Cdd:PRK10895 98 NLMAVLQI-RDDLSAEQREDRANELMEEFHIEH--LRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 188 GVLNLLNEMkRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDN 241
Cdd:PRK10895 175 DIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-231 |
2.05e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.96 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTFGhgsgAVHAARAISFSLHAGRALALVGESGSGKTTCarmaMR---------EYlptSGRILYKGRPVEA 75
Cdd:NF040905 1 ILEMRGITKTFP----GVKALDDVNLSVREGEIHALCGENGAGKSTL----MKvlsgvyphgSY---EGEILFDGEVCRF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 76 A--KSAEiaryRRSVQMIFQDpfASLNPAHTIAHHLRrplkLHRPEIKGAEID-----VAVRELLQRVRLDPDlvapkyP 148
Cdd:NF040905 70 KdiRDSE----ALGIVIIHQE--LALIPYLSIAENIF----LGNERAKRGVIDwnetnRRARELLAKVGLDES------P 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 149 HELSG----GQRQRVNIARALAVKPEVIVADEPTSML--DVSVRLgvLNLLNEMKRElnlGL--LYITHDIATARYVAED 220
Cdd:NF040905 134 DTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALneEDSAAL--LDLLLELKAQ---GItsIIISHKLNEIRRVADS 208
|
250
....*....|.
gi 1586794399 221 IAVMYAGQIVE 231
Cdd:NF040905 209 ITVLRDGRTIE 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-229 |
3.46e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.80 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 24 AARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAeiarYRRSVQMIfqdpfaslnPAH 103
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDA----VRQSLGMC---------PQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIA-HHLRRPLK-LHRPEIKGAEIDVAVRELlqRVRLDPDLVAPKYPHE---LSGGQRQRVNIARALAVKPEVIVADEPT 178
Cdd:TIGR01257 1012 NILfHHLTVAEHiLFYAQLKGRSWEEAQLEM--EAMLEDTGLHHKRNEEaqdLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586794399 179 SMLDVSVRLGVLNLLneMKRELNLGLLYITHDIATARYVAEDIAVMYAGQI 229
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-183 |
4.44e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.28 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMA---MReylPTSGRILYKGRPVEAAKSAeiarYRRsvQMIFQDPFASLNPA 102
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILaglAR---PDAGEVLWQGEPIRRQRDE----YHQ--DLLYLGHQPGIKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 103 HTIAHHLRRPLKLHRPEikGAEidvAVRELLQRVRLD--PDLVApkypHELSGGQRQRVNIARALAVKPEVIVADEPTSM 180
Cdd:PRK13538 89 LTALENLRFYQRLHGPG--DDE---ALWEALAQVGLAgfEDVPV----RQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
...
gi 1586794399 181 LDV 183
Cdd:PRK13538 160 IDK 162
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-176 |
5.61e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 59.81 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAaksAEIARYRR--SVqmIFQDpfaslnpahti 105
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA---DNREAYRQlfSA--VFSD----------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 106 aHHL-RRPLKLHrpeikGAEIDVAVRELLQRVRLDpdlvapkypH------------ELSGGQRQRVniarALAV----- 167
Cdd:COG4615 415 -FHLfDRLLGLD-----GEADPARARELLERLELD---------HkvsvedgrfsttDLSQGQRKRL----ALLValled 475
|
....*....
gi 1586794399 168 KPeVIVADE 176
Cdd:COG4615 476 RP-ILVFDE 483
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
28-229 |
1.12e-09 |
|
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: 58.68 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPT-SGRILYKGRPVEAAKSAEiaRYRRSVQMIFQD-------PFASL 99
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQ--AIRAGIAMVPEDrkrhgivPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 100 NPAHTIAHhLRRPLKLHRPEiKGAEIDvAVRELLQRVRL---DPDLVAPKypheLSGGQRQRVNIARALAVKPEVIVADE 176
Cdd:TIGR02633 357 GKNITLSV-LKSFCFKMRID-AAAELQ-IIGSAIQRLKVktaSPFLPIGR----LSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586794399 177 PTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQI 229
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
28-209 |
1.19e-09 |
|
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: 57.34 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGR-PVEAAKSAEIARYRRSVQMIFQDPFAsLNPAHTIA 106
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnESEPSFEATRSRNRYSVAYAAQKPWL-LNATVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 107 HHLRRPLKLHRpeikgaeidvaVRELLQRVRLDPDLvaPKYPH-----------ELSGGQRQRVNIARALAVKPEVIVAD 175
Cdd:cd03290 99 ITFGSPFNKQR-----------YKAVTDACSLQPDI--DLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1586794399 176 EPTSMLDVSV-----RLGVLNLLNEMKRELNL---GLLYITH 209
Cdd:cd03290 166 DPFSALDIHLsdhlmQEGILKFLQDDKRTLVLvthKLQYLPH 207
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
26-233 |
1.47e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.49 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTT-CARMAMRE-YLPTSGRILYKGRPVEAAKSAEiaRYRRSVQMIFQDPFASlnPAH 103
Cdd:PRK09580 18 RGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLELSPED--RAGEGIFMAFQYPVEI--PGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLRRPLKLHRPEIKGAEIDV-----AVRELLQRVRLDPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPT 178
Cdd:PRK09580 94 SNQFFLQTALNAVRSYRGQEPLDRfdfqdLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586794399 179 SMLDVSVRLGVLNLLNEMkRELNLGLLYITHDIATARYVAED-IAVMYAGQIVEWG 233
Cdd:PRK09580 174 SGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIKPDyVHVLYQGRIVKSG 228
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-215 |
4.21e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREY-LPTSGRILYKGRPVEAAKSAEIAR--YRRSVQMIFQDPFAS---- 98
Cdd:PTZ00265 1185 KDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdLKNDHHIVFKNEHTNDMTNEQDYQgdEEQNVGMKNVNEFSLtkeg 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 99 ----------------LNPAHTIAHHLR-----------RPLKLH---------------RPEIKGAEIDVAVRELLQRV 136
Cdd:PTZ00265 1265 gsgedstvfknsgkilLDGVDICDYNLKdlrnlfsivsqEPMLFNmsiyenikfgkedatREDVKRACKFAAIDEFIESL 1344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 137 RLDPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATAR 215
Cdd:PTZ00265 1345 PNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIK 1423
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-229 |
4.30e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 18 GSGaVHAaraISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAE--------IARYRR--- 86
Cdd:PRK10762 265 GPG-VND---VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDRKrdg 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 87 -----SVQ--MifqdPFASLNPAHTIAHHLRrplklHRPE-------IKGAEIDVAVREllQRVRLdpdlvapkypheLS 152
Cdd:PRK10762 341 lvlgmSVKenM----SLTALRYFSRAGGSLK-----HADEqqavsdfIRLFNIKTPSME--QAIGL------------LS 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586794399 153 GGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQI 229
Cdd:PRK10762 398 GGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-231 |
5.67e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.72 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 25 ARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGR------PVEAAKS--AEIARYRRSVQMifqdpF 96
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprsPLDAVKKgmAYITESRRDNGF-----F 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 97 ASLNPAHTIAhhLRRPLKL-----------HRPEIKGAEidvAVRELLQR--VRLDPDLVapkyphELSGGQRQRVNIAR 163
Cdd:PRK09700 354 PNFSIAQNMA--ISRSLKDggykgamglfhEVDEQRTAE---NQRELLALkcHSVNQNIT------ELSGGNQQKVLISK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 164 ALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVE 231
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
28-231 |
7.50e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKsaeIARYRRSVQMIFQDpfaslnpahtiaH 107
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ---PEDYRKLFSAVFTD------------F 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 108 HLRRplKLHRPEIKGAEiDVAVRELLQRVRLdpdlvAPKYPHE--------LSGGQRQRVNIARALAVKPEVIVADEPTS 179
Cdd:PRK10522 407 HLFD--QLLGPEGKPAN-PALVEKWLERLKM-----AHKLELEdgrisnlkLSKGQKKRLALLLALAEERDILLLDEWAA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 180 MLDVSVR----LGVLNLLNEMKRElnlgLLYITHDIAtarYV--AEDIAVMYAGQIVE 231
Cdd:PRK10522 479 DQDPHFRrefyQVLLPLLQEMGKT----IFAISHDDH---YFihADRLLEMRNGQLSE 529
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-255 |
8.30e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 8.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGrpVEAAKSAeIARYRRSVQMIFQ-------------D 94
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD--CDVAKFG-LTDLRRVLSIIPQspvlfsgtvrfniD 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 95 PFASLNPAHTIAhhlrrplKLHRPEIKgaeidvavrELLQRVRLDPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVA 174
Cdd:PLN03232 1332 PFSEHNDADLWE-------ALERAHIK---------DVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 175 DEPTSMLDVSVRLGVLNLLNEMKRELNlgLLYITHDIATArYVAEDIAVMYAGQIVEWGSVAKVIDNPLHPYTRLLLSAV 254
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRTIREEFKSCT--MLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTG 1472
|
.
gi 1586794399 255 P 255
Cdd:PLN03232 1473 P 1473
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
147-209 |
9.44e-09 |
|
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: 53.70 E-value: 9.44e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586794399 147 YP--HELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKrelnLGLLYITH 209
Cdd:cd03223 86 YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
39-230 |
1.17e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 39 ALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIarYRRSVQMIFQDpfasLNpaHTIAHHLRRPLKLHRP 118
Cdd:PRK10982 28 ALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA--LENGISMVHQE----LN--LVLQRSVMDNMWLGRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 119 EIKGAEID--------VAVRELLQrVRLDP-DLVApkyphELSGGQRQRVNIARALAVKPEVIVADEPTSML---DVSVR 186
Cdd:PRK10982 100 PTKGMFVDqdkmyrdtKAIFDELD-IDIDPrAKVA-----TLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekEVNHL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1586794399 187 LGVLNLLnemkRELNLGLLYITHDIATARYVAEDIAVMYAGQIV 230
Cdd:PRK10982 174 FTIIRKL----KERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-232 |
1.24e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 30 FSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKG------------RPVE-------AAKSAEIA----RYRR 86
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdppRNVEgtvydfvAEGIEEQAeylkRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 87 SVQMIFQDPFASlnpahtiahHLRRPLKL-----HRpeiKGAEIDVAVRELLQRVRLDPDlvapKYPHELSGGQRQRVNI 161
Cdd:PRK11147 104 ISHLVETDPSEK---------NLNELAKLqeqldHH---NLWQLENRINEVLAQLGLDPD----AALSSLSGGWLRKAAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586794399 162 ARALAVKPEVIVADEPTSMLDVSvrlgVLNLLNEMKRELNLGLLYITHDIATARYVAEDIAVMYAGQIVEW 232
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIE----TIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSY 234
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
26-183 |
1.79e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 54.48 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRpveaaksaeiaryrrsvqMIFQDPFASLNPAhTI 105
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR------------------ISFSSQFSWIMPG-TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 106 AHHLrrplklhrpeIKGAEID-VAVRELLQRVRLDPDLVapKYPHE-----------LSGGQRQRVNIARALAVKPEVIV 173
Cdd:cd03291 115 KENI----------IFGVSYDeYRYKSVVKACQLEEDIT--KFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYL 182
|
170
....*....|
gi 1586794399 174 ADEPTSMLDV 183
Cdd:cd03291 183 LDSPFGYLDV 192
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
28-183 |
2.74e-08 |
|
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: 54.92 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRpveaaksaeiaryrrsvqMIFQDPFASLNPAhTIAH 107
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR------------------ISFSPQTSWIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 108 HLrrplklhrpeIKGAEID-VAVRELLQRVRLDPDLVapKYPHE-----------LSGGQRQRVNIARALAVKPEVIVAD 175
Cdd:TIGR01271 506 NI----------IFGLSYDeYRYTSVIKACQLEEDIA--LFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLD 573
|
....*...
gi 1586794399 176 EPTSMLDV 183
Cdd:TIGR01271 574 SPFTHLDV 581
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-280 |
8.30e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 32 LHAGRALALVGESGSGKTTCAR-MAMREY---LPTSGRILYKGRPVEAAKSaeiaRYRRSVQMIFQDP--FASLNPAHTI 105
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKtIASNTDgfhIGVEGVITYDGITPEEIKK----HYRGDVVYNAETDvhFPHLTVGETL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 106 --AHHLR----RPLKLHRPEIKGAEIDVAVRELLQRVRLDPDlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTS 179
Cdd:TIGR00956 160 dfAARCKtpqnRPDGVSREEYAKHIADVYMATYGLSHTRNTK-VGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 180 MLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARY-VAEDIAVMYAGQIVEWGSVAKV--------IDNPLHPYTRLL 250
Cdd:TIGR00956 239 GLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYeLFDKVIVLYEGYQIYFGPADKAkqyfekmgFKCPDRQTTADF 318
|
250 260 270
....*....|....*....|....*....|....
gi 1586794399 251 LSAVPDPDVRFDDP----KARLRPDEVEDIRRRS 280
Cdd:TIGR00956 319 LTSLTSPAERQIKPgyekKVPRTPQEFETYWRNS 352
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-215 |
9.36e-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: 50.45 E-value: 9.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 35 GRALALVGESGSGKTTCARMAMREYLPTSGRILYkgrpveaaksaeiaryrrsvqmifqdpfaslnpahtiahhlrrplk 114
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 115 lhrpeIKGAEIDVAVRELLQRVRLDPDlvapkyPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVS-----VRLGV 189
Cdd:smart00382 36 -----IDGEDILEEVLDQLLLIIVGGK------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqeallLLLEE 104
|
170 180
....*....|....*....|....*.
gi 1586794399 190 LNLLNEMKRELNLGLLYITHDIATAR 215
Cdd:smart00382 105 LRLLLLLKSEKNLTVILTTNDEKDLG 130
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
141-225 |
1.50e-07 |
|
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: 50.65 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 141 DLVAPKYPHE---LSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITHDIATARYV 217
Cdd:cd03222 59 DGITPVYKPQyidLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYL 138
|
....*...
gi 1586794399 218 AEDIAVMY 225
Cdd:cd03222 139 SDRIHVFE 146
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-239 |
1.50e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 16 GHGSGAVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYRRSVQMIfqdP 95
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGIENI---E 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 96 FASLNPAHTiahhlRRPLKLHRPEIkgaeidVAVREL----LQRVRldpdlvapKYphelSGGQRQRVNIARALAVKPEV 171
Cdd:PRK13546 108 FKMLCMGFK-----RKEIKAMTPKI------IEFSELgefiYQPVK--------KY----SSGMRAKLGFSINITVNPDI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586794399 172 IVADEPTSMLDVSVRLGVLNLLNEMKrELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVI 239
Cdd:PRK13546 165 LVIDEALSVGDQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-240 |
1.64e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.64 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 27 AISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARYRRSVQMIFQDPfasLNPAHtia 106
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKA---LNEKY--- 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 107 hhlrrplklhrpeikgaeidvaVRELLQRVRLDPDL-VAPKYPH--------ELSGGQRQRVNIARALAVKPEVIVADEP 177
Cdd:TIGR00957 730 ----------------------YQQVLEACALLPDLeILPSGDRteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 178 TSMLDVSVRLGVL-NLLNEMKRELNLGLLYITHDIATARYVaEDIAVMYAGQIVEWGSVAKVID 240
Cdd:TIGR00957 788 LSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
228-278 |
1.73e-07 |
|
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: 48.13 E-value: 1.73e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1586794399 228 QIVEWGSVAKVIDNPLHPYTRLLLSAVPDPdVRFDDPKARLrPDEVEDIRR 278
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTI-KKRDRKLISI-PGEVPSLIN 49
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
20-235 |
2.91e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.27 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 20 GAVHAARAISFSLHAGRALALVGESGSGKTtcaRMAMREYL--PTSGRILYKGRPVEAAKSA--EIARYRRSVQMIFQDP 95
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**---RGALPAHV*gPDAGRRPWRF*TWCANRRAlrRTIG*HRPVR*GRRES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 96 FASLNPAHTIAhhlrRPLKLHRPEIKgAEIDvavrELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVAD 175
Cdd:NF000106 101 FSGRENLYMIG----R*LDLSRKDAR-ARAD----ELLERFSLTE--AAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 176 EPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSV 235
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-183 |
3.57e-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: 51.09 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRIlykgrpveaaksaeiaRYRRSVQMIFQDPF-ASLNPAHTIA 106
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI----------------EIGETVKLAYVDQSrDALDPNKTVW 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 107 HhlrrplklhrpEIKGA--EIDVAVRELLQRVRLD------PDlvAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPT 178
Cdd:TIGR03719 405 E-----------EISGGldIIKLGKREIPSRAYVGrfnfkgSD--QQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
....*
gi 1586794399 179 SMLDV 183
Cdd:TIGR03719 472 NDLDV 476
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-228 |
5.40e-07 |
|
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: 49.39 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 14 TFGHGSGAVHAARA---ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIarYRRSVQ- 89
Cdd:cd03250 7 SFTWDSGEQETSFTlkdINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWI--QNGTIRe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 90 -MIFqdpfaslnpahtiahhlrrplklhrpeikGAEIDvavRELLQRV----RLDPDLVApkYPH-------E----LSG 153
Cdd:cd03250 85 nILF-----------------------------GKPFD---EERYEKVikacALEPDLEI--LPDgdlteigEkginLSG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586794399 154 GQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVL-NLLNEMKRELNLGLLyITHDIATARYvAEDIAVMYAGQ 228
Cdd:cd03250 131 GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRIL-VTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
28-229 |
6.41e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYlP--TSGRILYKGRPVEAAKSAEIARYrrSVQMIFQD-------PFAS 98
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PgrWEGEIFIDGKPVKIRNPQQAIAQ--GIAMVPEDrkrdgivPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 99 LNPAHTIAHhLRRPLKLHRPEiKGAEIDVAVRELlQRVRL---DPDL-VApkyphELSGGQRQRVNIARALAVKPEVIVA 174
Cdd:PRK13549 358 VGKNITLAA-LDRFTGGSRID-DAAELKTILESI-QRLKVktaSPELaIA-----RLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1586794399 175 DEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQI 229
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
28-182 |
7.53e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEaaksAEIARYRRsvQMIFQDPFASLNPAHTIAH 107
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTYQK--QLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586794399 108 HLRRplklhrpEIKGAEIDVAVRELLQRVRLDPDLvapKYP-HELSGGQRQRVNIARALAVKPEVIVADEPTSMLD 182
Cdd:PRK13540 94 NCLY-------DIHFSPGAVGITELCRLFSLEHLI---DYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-235 |
7.69e-07 |
|
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: 50.40 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 5 ILALDSVTKTF-GHGSGAVHAaraISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaakSAEIAR 83
Cdd:TIGR01257 1937 ILRLNELTKVYsGTSSPAVDR---LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI----LTNISD 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 84 YRRSvqMIFQDPFASLNPAHTIAHHLRRPLKLHrpEIKGAEIDVAVRELLQRVRLDpdLVAPKYPHELSGGQRQRVNIAR 163
Cdd:TIGR01257 2010 VHQN--MGYCPQFDAIDDLLTGREHLYLYARLR--GVPAEEIEKVANWSIQSLGLS--LYADRLAGTYSGGNKRKLSTAI 2083
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586794399 164 ALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSV 235
Cdd:TIGR01257 2084 ALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI 2154
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
15-241 |
8.87e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.89 E-value: 8.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 15 FGHGSGAVH-AARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAeiaryrrsvqmifq 93
Cdd:PRK13545 29 FRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISS-------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 94 dpfaSLNPAHTiahhlrrplKLHRPEIKGAEIDVA---VRELLQRVRLDPDLvaPKYPHE----LSGGQRQRVNIARALA 166
Cdd:PRK13545 95 ----GLNGQLT---------GIENIELKGLMMGLTkekIKEIIPEIIEFADI--GKFIYQpvktYSSGMKSRLGFAISVH 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586794399 167 VKPEVIVADEPTSMLDVSVRLGVLNLLNEMKrELNLGLLYITHDIATARYVAEDIAVMYAGQIVEWGSVAKVIDN 241
Cdd:PRK13545 160 INPDILVIDEALSVGDQTFTKKCLDKMNEFK-EQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
28-182 |
9.40e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCarMAMREYL--PTSGRILYKGRPVEAaKSAEIaryRRSVQMIFQdPFaSLNPAHTI 105
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTT--MKMLTGLlpASEGEAWLFGQPVDA-GDIAT---RRRVGYMSQ-AF-SLYGELTV 356
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 106 ahhlRRPLKLHRP--EIKGAEIDVAVRELLQRVRLDPdlVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLD 182
Cdd:NF033858 357 ----RQNLELHARlfHLPAAEIAARVAEMLERFDLAD--VADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
151-231 |
1.08e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 151 LSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRElNLGLLYITHDIATARYVAEDIAVMYAGQ-- 228
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLva 470
|
....
gi 1586794399 229 -IVE 231
Cdd:PRK10982 471 gIVD 474
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
28-182 |
1.37e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.91 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMReYLPTSGRILYKGRpveAAKSAEIARYRRSVQMIFQDPFaslnpahTIAH 107
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLR-LLSTEGEIQIDGV---SWNSVTLQTWRKAFGVIPQKVF-------IFSG 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 108 HLRRPLKLHR----PEIKGAEIDVAVRELLQRV--RLDPDLVAPKYPheLSGGQRQRVNIARALAVKPEVIVADEPTSML 181
Cdd:TIGR01271 1307 TFRKNLDPYEqwsdEEIWKVAEEVGLKSVIEQFpdKLDFVLVDGGYV--LSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
.
gi 1586794399 182 D 182
Cdd:TIGR01271 1385 D 1385
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-237 |
1.53e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.14 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIARyrRSVQMIFQD-PFASLNPAHTIA 106
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIR--AGIMLCPEDrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 107 ---------HHLRRPLKLHRpeikGAEIDVAvRELLQRVRLdpdlvapKYPH------ELSGGQRQRVNIARALAVKPEV 171
Cdd:PRK11288 350 dninisarrHHLRAGCLINN----RWEAENA-DRFIRSLNI-------KTPSreqlimNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586794399 172 IVADEPTSMLDVSVRLGVLNLLNEMKrELNLGLLYITHDIATARYVAEDIAVMYAGQIVewGSVAK 237
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRIA--GELAR 480
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-230 |
3.69e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.18 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 1 MTDAILALDSVTKTFGHgsgaVHAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAE 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 81 IARYRRSVQMIFQDPFASLNPAHTIAhhlrrplklhrpeIKGAEIDvaVRELLQRVRLDPDLVAPKYPHE------LSGG 154
Cdd:PRK11614 77 IMREAVAIVPEGRRVFSRMTVEENLA-------------MGGFFAE--RDQFQERIKWVYELFPRLHERRiqragtMSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586794399 155 QRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMkRELNLGLLYITHDIATARYVAEDIAVMYAGQIV 230
Cdd:PRK11614 142 EQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
35-182 |
5.96e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 35 GRALALVGESGSGKTT-----CARMAMReyLPTSGRILYKGRPVEAAksaeiarYRRS---VQMifQD---PFASLNPAH 103
Cdd:TIGR00956 789 GTLTALMGASGAGKTTllnvlAERVTTG--VITGGDRLVNGRPLDSS-------FQRSigyVQQ--QDlhlPTSTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLRRPLKLHRPEiKGAEIDvAVRELLQRVRLDPDLVApkYPHE-LSGGQRQRVNIARALAVKPEVIV-ADEPTSML 181
Cdd:TIGR00956 858 RFSAYLRQPKSVSKSE-KMEYVE-EVIKLLEMESYADAVVG--VPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGL 933
|
.
gi 1586794399 182 D 182
Cdd:TIGR00956 934 D 934
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
28-209 |
6.02e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 47.44 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMaMREYLPTSGRILYKGRPveaaksaeiaryrrsvQMIF---QDPFASLNpahT 104
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRI-LGELWPVYGGRLTKPAK----------------GKLFyvpQRPYMTLG---T 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 105 IAHHLRRPLKLHRPEIKGAEiDVAVRELLQRVRLDP--------DLVApKYPHELSGGQRQRVNIARALAVKPEVIVADE 176
Cdd:TIGR00954 531 LRDQIIYPDSSEDMKRRGLS-DKDLEQILDNVQLTHilereggwSAVQ-DWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|...
gi 1586794399 177 PTSMLDVSVRLGVLNLLnemkRELNLGLLYITH 209
Cdd:TIGR00954 609 CTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
35-193 |
6.29e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.57 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 35 GRALALVGESGSGKTT-----CARMAMREYlptSGRILYKGRPVEAaksaeiaRYRRSVQMIFQD----PFASLNPAHTI 105
Cdd:PLN03211 94 GEILAVLGPSGSGKSTllnalAGRIQGNNF---TGTILANNRKPTK-------QILKRTGFVTQDdilyPHLTVRETLVF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 106 AHHLRRPLKLHRPE-IKGAEidvAVRELLQRVRLDPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVS 184
Cdd:PLN03211 164 CSLLRLPKSLTKQEkILVAE---SVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
....*....
gi 1586794399 185 VRLGVLNLL 193
Cdd:PLN03211 241 AAYRLVLTL 249
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-210 |
9.23e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 29 SFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRIlYKGRPVEAAKsaeIARYRrsvqmifqdpfASLNPAHTIAHH 108
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTKLEVAY---FDQHR-----------AELDPEKTVMDN 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 109 LrrplklhrPEIKgAEIDVAVRE-----LLQrvrldpD-LVAPK---YP-HELSGGQRQRVNIARaLAVKP-EVIVADEP 177
Cdd:PRK11147 404 L--------AEGK-QEVMVNGRPrhvlgYLQ------DfLFHPKramTPvKALSGGERNRLLLAR-LFLKPsNLLILDEP 467
|
170 180 190
....*....|....*....|....*....|...
gi 1586794399 178 TSMLDVSvrlgVLNLLNEMKRELNLGLLYITHD 210
Cdd:PRK11147 468 TNDLDVE----TLELLEELLDSYQGTVLLVSHD 496
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
29-183 |
1.00e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 29 SFSLHAGRALALVGESGSGKTTCAR-MAMR--EYLPTSGRILYKGRPV--------EAAKSAEIARyrrsVQMIFQDpfa 97
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRyMAMHaiDGIPKNCQILHVEQEVvgddttalQCVLNTDIER----TQLLEEE--- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 98 slnpAHTIAHHLRRPLKLHRPEIKGAEIDV----AVRELLQRV--RLD---------------------PDLvAPKYPHE 150
Cdd:PLN03073 270 ----AQLVAQQRELEFETETGKGKGANKDGvdkdAVSQRLEEIykRLElidaytaearaasilaglsftPEM-QVKATKT 344
|
170 180 190
....*....|....*....|....*....|...
gi 1586794399 151 LSGGQRQRVNIARALAVKPEVIVADEPTSMLDV 183
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-241 |
1.44e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGrpVEAAKSAeIARYRRSVQMIFQDP--FASlnpahTI 105
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG--CDISKFG-LMDLRKVLGIIPQAPvlFSG-----TV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 106 AHHLRrPLKLHRpeikgaeiDVAVRELLQR------VRLDP---DLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADE 176
Cdd:PLN03130 1330 RFNLD-PFNEHN--------DADLWESLERahlkdvIRRNSlglDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586794399 177 PTSMLDVsvrlGVLNLLNEMKRE--LNLGLLYITHDIATArYVAEDIAVMYAGQIVEWGSVAKVIDN 241
Cdd:PLN03130 1401 ATAAVDV----RTDALIQKTIREefKSCTMLIIAHRLNTI-IDCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-239 |
1.74e-05 |
|
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: 46.48 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVeaaksAEIARY--RRSVQMIFQDPFaslnpah 103
Cdd:TIGR00957 1303 RHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI-----AKIGLHdlRFKITIIPQDPV------- 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLRRPLKlhrPEIKGAEIDV----AVRELLQRVRLDPDlvapKYPHE-------LSGGQRQRVNIARALAVKPEVI 172
Cdd:TIGR00957 1371 LFSGSLRMNLD---PFSQYSDEEVwwalELAHLKTFVSALPD----KLDHEcaeggenLSVGQRQLVCLARALLRKTKIL 1443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586794399 173 VADEPTSMLDVSVRlgvlNLLNEMKREL--NLGLLYITHDIATARYVAEdIAVMYAGQIVEWGSVAKVI 239
Cdd:TIGR00957 1444 VLDEATAAVDLETD----NLIQSTIRTQfeDCTVLTIAHRLNTIMDYTR-VIVLDKGEVAEFGAPSNLL 1507
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
26-182 |
1.87e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCAR-MAMRE---YLptSGRILYKGRPVEAAKSAEIARYrrSVQMIFQDPFASLNP 101
Cdd:PLN03140 897 REVTGAFRPGVLTALMGVSGAGKTTLMDvLAGRKtggYI--EGDIRISGFPKKQETFARISGY--CEQNDIHSPQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 102 AHTIAHHLRRPLKLHRPEiKGAEIDvAVRELLQRVRLDPDLVAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTSML 181
Cdd:PLN03140 973 SLIYSAFLRLPKEVSKEE-KMMFVD-EVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
.
gi 1586794399 182 D 182
Cdd:PLN03140 1051 D 1051
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-216 |
2.76e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.85 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 22 VHAARAISFSLHAGRALALVGESGSGKTTCARmamrEYLPTSGRILYKGRPVEAAKSaeiaryrrsvQMIFQDPFASLnp 101
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN----EGLYASGKARLISFLPKFSRN----------KLIFIDQLQFL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 102 ahtiahhlrrplklhrpeikgaeIDVAvrelLQRVRLDPDLvapkypHELSGGQRQRVNIARALAVKPE--VIVADEPTS 179
Cdd:cd03238 72 -----------------------IDVG----LGYLTLGQKL------STLSGGELQRVKLASELFSEPPgtLFILDEPST 118
|
170 180 190
....*....|....*....|....*....|....*....
gi 1586794399 180 MLDVSVrlgVLNLLNEMKRELNLG--LLYITHDIATARY 216
Cdd:cd03238 119 GLHQQD---INQLLEVIKGLIDLGntVILIEHNLDVLSS 154
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-200 |
3.43e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPTS-GRILYKGRPVEAAKSAEI--ARYRRSVqmIFQDPFaslnpaht 104
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQVSWIfnATVRDNI--LFGSPF-------- 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 105 iahhlrRPLKLHRPeikgaeIDVAVrelLQRvrlDPDLVAPKYPHE-------LSGGQRQRVNIARALAVKPEVIVADEP 177
Cdd:PLN03130 706 ------DPERYERA------IDVTA---LQH---DLDLLPGGDLTEigergvnISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180
....*....|....*....|...
gi 1586794399 178 TSMLDVSVRLGVLNllNEMKREL 200
Cdd:PLN03130 768 LSALDAHVGRQVFD--KCIKDEL 788
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
151-210 |
3.73e-05 |
|
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: 43.75 E-value: 3.73e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586794399 151 LSGGQRQ------RVNIARALAVKPEVIVADEPTSMLDV-SVRLGVLNLLNEMKRELNLGLLYITHD 210
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
28-182 |
6.72e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 43.69 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMReYLPTSGRILYKGrpvEAAKSAEIARYRRSVQMIFQDPFASlnpAHTIAH 107
Cdd:cd03289 23 ISFSISPGQRVGLLGRTGSGKSTLLSAFLR-LLNTEGDIQIDG---VSWNSVPLQKWRKAFGVIPQKVFIF---SGTFRK 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586794399 108 HLRRPLKLHRPEIKGAEIDVAVRELLQRV--RLDPDLVAPKYPheLSGGQRQRVNIARALAVKPEVIVADEPTSMLD 182
Cdd:cd03289 96 NLDPYGKWSDEEIWKVAEEVGLKSVIEQFpgQLDFVLVDGGCV--LSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-242 |
6.86e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.38 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYKGRPVEAAKSAEIaryRRSVQMIFQDP--FASlnpah 103
Cdd:PTZ00243 1327 RGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL---RRQFSMIPQDPvlFDG----- 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 104 TIAHHLRRPLKLHRPEIKGAEIDVAVREllqRVRLDPDLVAPKYPH---ELSGGQRQRVNIARALAVKPE-VIVADEPTS 179
Cdd:PTZ00243 1399 TVRQNVDPFLEASSAEVWAALELVGLRE---RVASESEGIDSRVLEggsNYSVGQRQLMCMARALLKKGSgFILMDEATA 1475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586794399 180 MLDVSVRLGVLNLLneMKRELNLGLLYITHDIAT-ARYvaEDIAVMYAGQIVEWGSVAKVIDNP 242
Cdd:PTZ00243 1476 NIDPALDRQIQATV--MSAFSAYTVITIAHRLHTvAQY--DKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-182 |
9.65e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 6 LALDSVTKTFGHGSgavhAARAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILYkgrpveaAKSAEIARYR 85
Cdd:PRK15064 320 LEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-------SENANIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 86 rsvqmifQDP---FAS-LNPAHTIAHHlRRPlklhrpeikgAEIDVAVRELLQRVRLDPDLVaPKYPHELSGGQRQRVNI 161
Cdd:PRK15064 389 -------QDHaydFENdLTLFDWMSQW-RQE----------GDDEQAVRGTLGRLLFSQDDI-KKSVKVLSGGEKGRMLF 449
|
170 180
....*....|....*....|.
gi 1586794399 162 ARALAVKPEVIVADEPTSMLD 182
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMD 470
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
29-183 |
2.44e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 29 SFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRIlykgrpveaaksaeiaRYRRSVQMIFQDPF-ASLNPAHTIAH 107
Cdd:PRK11819 344 SFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI----------------KIGETVKLAYVDQSrDALDPNKTVWE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 108 hlrrplklhrpEIKGA--EIDVAVRELLQRVRLD------PDlvAPKYPHELSGGQRQRVNIARALAVKPEVIVADEPTS 179
Cdd:PRK11819 408 -----------EISGGldIIKVGNREIPSRAYVGrfnfkgGD--QQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTN 474
|
....
gi 1586794399 180 MLDV 183
Cdd:PRK11819 475 DLDV 478
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
149-209 |
3.15e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 3.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586794399 149 HELSGGQRQRVNIARALAVKPEVIVADEPTSMLDVSVRLGVLNLLNEMKRELNLGLLYITH 209
Cdd:PRK10938 400 HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
151-182 |
3.41e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 41.84 E-value: 3.41e-04
10 20 30
....*....|....*....|....*....|..
gi 1586794399 151 LSGGQRQRVNIARALAVKPEVIVADEPTSMLD 182
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
36-117 |
3.42e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 39.63 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 36 RALALVGESGSGKTTCARMAMREYLPTSGRILYkgrpVEAAKSAEIARYRRSVQMIFQDPFASLNPAHTIAHHLRRPLKL 115
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVF----VDLPSGTSPKDLLRALLRALGLPLSGRLSKEELLAALQQLLLA 81
|
..
gi 1586794399 116 HR 117
Cdd:pfam13401 82 LA 83
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-200 |
3.60e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.27 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 28 ISFSLHAGRALALVGESGSGKTTCARMAMREYLPT-SGRILYKGRPVEAAKSAEIARYRRSVQMIFQDPFaslnpahtia 106
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVPQVSWIFNATVRENILFGSDF---------- 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 107 hhlrrplklhRPEIKGAEIDVAVrelLQRvrlDPDLVAPKYPHEL-------SGGQRQRVNIARALAVKPEVIVADEPTS 179
Cdd:PLN03232 706 ----------ESERYWRAIDVTA---LQH---DLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180
....*....|....*....|.
gi 1586794399 180 MLDVSVRLGVLNllNEMKREL 200
Cdd:PLN03232 770 ALDAHVAHQVFD--SCMKDEL 788
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
151-182 |
1.79e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.72 E-value: 1.79e-03
10 20 30
....*....|....*....|....*....|..
gi 1586794399 151 LSGGQRQRVNIARALAVKPEVIVADEPTSMLD 182
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-185 |
4.20e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.61 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 26 RAISFSLHAGRALALVGESGSGKTTCARMAMREYLPTSGRILykgrpveaaksAEiaryrRSVQMIFQDPFaslnpahtI 105
Cdd:PTZ00243 677 RDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AE-----RSIAYVPQQAW--------I 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 106 AHHLRRPLKLHRPEIKGAEIDVAVRellqRVRLDPDLVAPKYPHE---------LSGGQRQRVNIARALAVKPEVIVADE 176
Cdd:PTZ00243 733 MNATVRGNILFFDEEDAARLADAVR----VSQLEADLAQLGGGLEteigekgvnLSGGQKARVSLARAVYANRDVYLLDD 808
|
....*....
gi 1586794399 177 PTSMLDVSV 185
Cdd:PTZ00243 809 PLSALDAHV 817
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
17-210 |
8.92e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 36.18 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 17 HGSGAVHAARAISFSLHAGRALALVGESGSGKTTcarmamreylptsgrILykgrpvEAAKSAEIARyrrsvqmifqdpf 96
Cdd:cd03227 3 VLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKST---------------IL------DAIGLALGGA------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586794399 97 aslnpahtiAHHLRRPLKLHRPEIKGAEIDVAVRELLQrvrldpdlvapkypheLSGGQRQRVNIARALA---VKPEVIV 173
Cdd:cd03227 49 ---------QSATRRRSGVKAGCIVAAVSAELIFTRLQ----------------LSGGEKELSALALILAlasLKPRPLY 103
|
170 180 190
....*....|....*....|....*....|....*...
gi 1586794399 174 A-DEPTSMLDVSVRLGVLNLLNEMKRELNLGLLyITHD 210
Cdd:cd03227 104 IlDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHL 140
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
40-74 |
9.06e-03 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 37.66 E-value: 9.06e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1586794399 40 LV-GESGSGKTTCARMAMReYLP-TSGRILYKGRPVE 74
Cdd:cd01384 78 LVsGESGAGKTETTKMLMQ-YLAyMGGRAVTEGRSVE 113
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
18-68 |
9.44e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.07 E-value: 9.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1586794399 18 GSGAVHAARA-ISFSLHAGRALALV-GESGSGKTTCARMAMREyLPTSGRILY 68
Cdd:COG3267 24 LSPSHREALArLEYALAQGGGFVVLtGEVGTGKTTLLRRLLER-LPDDVKVAY 75
|
|
| |
