|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-644 |
0e+00 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 766.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 2 SLIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAA 81
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 82 LRRERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNG 161
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 162 GEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDGEIISDtskNPEIPTSNVGRIREK 241
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRN---PPAQEKVNVAGGTEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 242 A-----SWSFYYDQFVEAFRMSVQAVLAHKMRSLLTMLGIIIGIASVVSVVALGNGSQKKILEDISSMGTNTISIFPGRG 316
Cdd:PRK10535 240 VvntasGWRQFVSGFREALTMAWRAMAANKMRTLLTMLGIIIGIASVVSIVVVGDAAKQMVLADIRAIGTNTIDIYPGKD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 317 FGDRRSGKIKTLTIDDAKIIAKQSYVASATPMTSSGGTLTYRNTDLTASLYGVGEQYFDVRGLKLESGRLFDENDVKEDA 396
Cdd:PRK10535 320 FGDDDPQYQQALKYDDLIAIQKQPWVASATPAVSQSLRLRYGNIDVAASANGVSGDYFNVYGMTFSEGNTFNQEQLNGRA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 397 QVVVIDQNVKDKLFAD-SDPLGKTILFRKRPLTVIGVMKKDENAFGNSDVLMLWSPYTTVMHQITGEGHTNSITVKIKDN 475
Cdd:PRK10535 400 QVVVLDSNTRRQLFPHkADVVGEVILVGNMPATVIGVAEEKQSMFGSSKVLRVWLPYSTMSGRVMGQSWLNSITVRVKEG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 476 ANIQVAEKGLTELLKARHGTEDFFMNNSDSIRQMVESTTGTMKLLISSIALISLVVGGIGVMNIMLVSVTERTKEIGIRM 555
Cdd:PRK10535 480 YDSAEAEQQLTRLLTLRHGKKDFFTWNMDSVLKTAEKTTRTLQLFLTLVAVISLVVGGIGVMNIMLVSVTERTREIGIRM 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 556 AIGARRGNILQQFLIEAVLICVIGGLVGVGLSAAVSLVFNHFVTDFPMDISAMSVIGAVACSTGIGIAFGFMPANKAAKL 635
Cdd:PRK10535 560 AVGARASDVLQQFLIEAVLVCLVGGALGITLSLLIAFTLQLFLPGWEIGFSPLALLSAFLCSTVTGILFGWLPARNAARL 639
|
....*....
gi 2559317375 636 NPIDALAQD 644
Cdd:PRK10535 640 DPVDALARE 648
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-225 |
5.34e-124 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 366.29 E-value: 5.34e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 2 SLIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAA 81
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 82 LRRERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNG 161
Cdd:COG1136 83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 162 GEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIAANANRIIEIRDGEIISDTS 225
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-220 |
3.83e-110 |
|
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: 330.22 E-value: 3.83e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHK-AGHTVIMVTHDPGIAANANRIIEIRDGEI 220
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| SalY |
COG0577 |
ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms]; |
253-641 |
1.24e-107 |
|
ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms];
Pssm-ID: 440342 [Multi-domain] Cd Length: 339 Bit Score: 328.40 E-value: 1.24e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 253 EAFRMSVQAVLAHKMRSLLTMLGIIIGIASVVSVVALGNGSQKKILEDISSMGTNTISIFPGRGfgdrrsGKIKTLTIDD 332
Cdd:COG0577 1 EYLRLALRSLRRNKLRSLLTVLGIAIGIALVIAILALGRGLRRSLLRDLDSLGFDLLTVSRTPG------GSRATLSYED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 333 A-KIIAKQSYVASATPMTSSGGTLTY-RNTDLTASLYGVGEQYFDVRGLKLESGRLFDENDVKEDAQVVVIDQNVKDKLF 410
Cdd:COG0577 75 LrEALRALPGVESVAPSSSGSATVRYgGGEPPSVRVLGVDPDYFRVLGIPLLAGRFFTAADDLGAPPVVVIGEALARRLF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 411 ADSDPLGKTILFRKRPLTVIGVMKKDenafgnsdvlmlwspyttvmhqitgeghtnsitvkikdnaniqvaekgLTELLK 490
Cdd:COG0577 155 GGEDPVGKTIRLNGRPFTVVGVVEAE------------------------------------------------LRALLR 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 491 ARHGTEDFFMNNSDSIRQMVESTTGTMKLLISSIALISLVVGGIGVMNIMLVSVTERTKEIGIRMAIGARRGNILQQFLI 570
Cdd:COG0577 187 RRDPGDDFEVQTLDEILAALYGVLRTLTLLLGAIAGLALLVACIGIMNLMLASVTERTREIGIRKALGASRRDILRQFLT 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 571 EAVLICVIGGLVGVGLSAAVSLVFNHFvTDFPMDISAMSVIGAVACSTGIGIAFGFMPANKAAKLNPIDAL 641
Cdd:COG0577 267 EALLLALLGGLLGLLLALLLLRLLAAL-LGLPVSLDPWVLLLALALSLLVGLLAGLYPARRAARLDPVEAL 336
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-224 |
1.20e-81 |
|
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: 257.36 E-value: 1.20e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 2 SLIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAA 81
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 82 LRRERFGFIFQRYNLLSSLTARDNVALPAVYMGMggKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNG 161
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 162 GEIIFADEPTGALDTASGKNVMEIIRRLHK-AGHTVIMVTHDPGIAANANRIIEIRDGEIISDT 224
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAARCDRVLRLRAGRLVEDT 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-226 |
6.21e-74 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 236.87 E-value: 6.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALR 83
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 ReRFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:COG2884 79 R-RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANAN-RIIEIRDGEIISDTSK 226
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPkRVLELEDGRLVRDEAR 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-223 |
5.98e-66 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 216.85 E-value: 5.98e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 2 SLIECKNINRYFGSGenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAA 81
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 82 LRReRFGFIFQRYNLLSSLTARDNV---ALPAV-----YMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVS 153
Cdd:COG3638 78 LRR-RIGMIFQQFNLVPRLSVLTNVlagRLGRTstwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 154 IARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIA-ANANRIIEIRDGEIISD 223
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLArRYADRIIGLRDGRVVFD 228
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
3-220 |
1.35e-65 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 214.58 E-value: 1.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAAL 82
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RRERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGG 162
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 163 EIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDGEI 220
Cdd:NF038007 161 ALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-213 |
1.53e-65 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 216.11 E-value: 1.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDela 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 alrrerFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMN 160
Cdd:COG1116 82 ------RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 161 GGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIAAN-ANRII 213
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHDVDEAVFlADRVV 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-221 |
2.03e-65 |
|
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: 214.75 E-value: 2.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAAL 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RReRFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGG 162
Cdd:cd03258 81 RR-RIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 163 EIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPG-IAANANRIIEIRDGEII 221
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEvVKRICDRVAVMEKGEVV 220
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-215 |
3.66e-64 |
|
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: 210.55 E-value: 3.66e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 7 KNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALRRER 86
Cdd:TIGR03608 2 KNISKKFGD----KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 87 FGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIF 166
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2559317375 167 ADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEI 215
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-221 |
1.40e-63 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 213.40 E-value: 1.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALR 83
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 ReRFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:COG1135 82 R-KIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLH-KAGHTVIMVTHDPG-IAANANRIIEIRDGEII 221
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINrELGLTIVLITHEMDvVRRICDRVAVLENGRIV 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-202 |
3.05e-62 |
|
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: 205.78 E-value: 3.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGietakmqpDELAALR 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--------EPVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERfGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:cd03293 73 PDR-GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2559317375 164 IIFADEPTGALDTASgKNVM--EIIRRLHKAGHTVIMVTHD 202
Cdd:cd03293 152 VLLLDEPFSALDALT-REQLqeELLDIWRETGKTVLLVTHD 191
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-221 |
5.81e-62 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 205.61 E-value: 5.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIE-TAKmqPDELAA 81
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDlTDS--KKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 82 LRReRFGFIFQRYNLLSSLTARDNVALPAVY-MGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMN 160
Cdd:COG1126 75 LRR-KVGMVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 161 GGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIV 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-223 |
4.00e-60 |
|
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: 200.87 E-value: 4.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALR 83
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 ReRFGFIFQRYNLLSSLTARDNVALPAV-YM-------GMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIA 155
Cdd:cd03256 78 R-QIGMIFQQFNLIERLSVLENVLSGRLgRRstwrslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 156 RALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIA-ANANRIIEIRDGEIISD 223
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLArEYADRIVGLKDGRIVFD 226
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-219 |
3.35e-59 |
|
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: 197.47 E-value: 3.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSGenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAAL 82
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RReRFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGG 162
Cdd:TIGR02673 78 RR-RIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 163 EIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPG-IAANANRIIEIRDGE 219
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSlVDRVAHRVIILDDGR 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-220 |
2.88e-57 |
|
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: 192.36 E-value: 2.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKmQPDELAALR 83
Cdd:cd03262 1 IEIKNLHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 ReRFGFIFQRYNLLSSLTARDNVALPAVYM-GMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGG 162
Cdd:cd03262 76 Q-KVGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 163 EIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEI 220
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-225 |
3.01e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 192.97 E-value: 3.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGsgenRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKmQPDELaalr 83
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEV---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:COG1131 72 RRRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEIISDTS 225
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGT 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-223 |
5.96e-57 |
|
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: 192.16 E-value: 5.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNIN-RYfgsgENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaal 82
Cdd:COG1122 1 IELENLSfSY----PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 rRERFGFIFQRY-NLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNG 161
Cdd:COG1122 74 -RRKVGLVFQNPdDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 162 GEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPG-IAANANRIIEIRDGEIISD 223
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDlVAELADRVIVLDDGRIVAD 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-230 |
1.66e-56 |
|
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: 191.35 E-value: 1.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAAL 82
Cdd:COG1127 5 MIEVRNLTKSFGD----RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RReRFGFIFQRYNLLSSLTARDNVALP-AVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNG 161
Cdd:COG1127 81 RR-RIGMLFQGGALFDSLTVFENVAFPlREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 162 GEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHD-PGIAANANRIIEIRDGEIISD-------TSKNPEI 230
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDlDSAFAIADRVAVLADGKIIAEgtpeellASDDPWV 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-240 |
1.51e-55 |
|
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: 188.48 E-value: 1.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGenrvHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALR 83
Cdd:cd03261 1 IELRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 ReRFGFIFQRYNLLSSLTARDNVALPAVYMG-MGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGG 162
Cdd:cd03261 77 R-RMGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 163 EIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHD-PGIAANANRIIEIRDGEIISDTSKnPEIPTSNVGRIRE 240
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDlDTAFAIADRIAVLYDGKIVAEGTP-EELRASDDPLVRQ 234
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-221 |
5.57e-55 |
|
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: 186.94 E-value: 5.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMqPDELAAL 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKL-SRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RRERFGFIFQryNLLSSLTARDNV------ALPAVYMGMGGKERSARADKLLQDLGLASKEGNK-PGELSGGQQQRVSIA 155
Cdd:cd03257 80 RRKEIQMVFQ--DPMSSLNPRMTIgeqiaePLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRyPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 156 RALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKiADRVAVMYAGKIV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-221 |
6.66e-55 |
|
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: 195.12 E-value: 6.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGS-GENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAA 81
Cdd:COG1123 260 LLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 82 LRReRFGFIFQryNLLSSL----TARDNVALPAVYMGMG-GKERSARADKLLQDLGLASKEGNK-PGELSGGQQQRVSIA 155
Cdd:COG1123 340 LRR-RVQMVFQ--DPYSSLnprmTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 156 RALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-220 |
1.80e-54 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 185.37 E-value: 1.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 2 SLIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAA 81
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 82 LRRERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNG 161
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 162 GEIIFADEPTGALDTASGKNVMEIIRRL-HKAGHTVIMVTHDPGIAANANRIIEIRDGEI 220
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-220 |
3.20e-54 |
|
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: 184.15 E-value: 3.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALR 83
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 ReRFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:cd03292 78 R-KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEI 220
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtRHRVIALERGKL 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-219 |
3.89e-54 |
|
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: 183.82 E-value: 3.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 5 ECKNINRYFGSGENRVhiLKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalrR 84
Cdd:cd03225 1 ELKNLSFSYPDGARPA--LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 85 ERFGFIFQRYNL-LSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:cd03225 75 RKVGLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDP-GIAANANRIIEIRDGE 219
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLdLLLELADRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-221 |
1.84e-53 |
|
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: 182.33 E-value: 1.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdelaalR 83
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP------E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIA-ANANRIIEIRDGEII 221
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEAlALADRIAVMNEGRIV 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-221 |
1.55e-52 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 184.53 E-value: 1.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDela 80
Cdd:COG3842 3 MPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 alRReRFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMN 160
Cdd:COG3842 76 --KR-NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 161 GGEIIFADEPTGALDtASGKNVMEI-IRRLHKA-GHTVIMVTHDPGIA-ANANRIIEIRDGEII 221
Cdd:COG3842 153 EPRVLLLDEPLSALD-AKLREEMREeLRRLQRElGITFIYVTHDQEEAlALADRIAVMNDGRIE 215
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-221 |
7.46e-52 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 179.05 E-value: 7.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSlIECKNINRYFGSGEnrvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIE---TAKMQPD 77
Cdd:COG4161 1 MS-IQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 78 ELAALRRErFGFIFQRYNLLSSLTARDN-VALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIAR 156
Cdd:COG4161 76 AIRLLRQK-VGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2559317375 157 ALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRII 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-220 |
1.70e-51 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 177.70 E-value: 1.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 2 SLIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAA 81
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 82 LRRERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNG 161
Cdd:PRK11629 84 LRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 162 GEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIAANANRIIEIRDGEI 220
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-223 |
1.83e-51 |
|
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: 177.88 E-value: 1.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSGenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAAL 82
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RReRFGFIFQRYNLLSSLTARDNVALPAV-YM-------GMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSI 154
Cdd:TIGR02315 78 RR-RIGMIFQHYNLIERLTVLENVLHGRLgYKptwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 155 ARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIA-ANANRIIEIRDGEIISD 223
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAkKYADRIVGLKAGEIVFD 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-221 |
2.90e-49 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 172.12 E-value: 2.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSlIECKNINRYFGSGEnrvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIE---TAKMQPD 77
Cdd:PRK11124 1 MS-IQLNGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfSKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 78 ELAALRRErFGFIFQRYNLLSSLTARDN-VALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIAR 156
Cdd:PRK11124 76 AIRELRRN-VGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2559317375 157 ALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIV 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-240 |
3.52e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 171.81 E-value: 3.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDElAAL 82
Cdd:PRK09493 1 MIEFKNVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-RLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RRERfGFIFQRYNLLSSLTARDNVAL-PAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNG 161
Cdd:PRK09493 76 RQEA-GMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 162 GEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEIISDTSKNPEIPTSNVGRIRE 240
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-219 |
6.25e-49 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 168.90 E-value: 6.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGsgenRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQpDELAALR 83
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE-DELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 ReRFGFIFQRYNLLSSLTARDNVALPavymgmggkersaradkllqdlglaskegnkpgeLSGGQQQRVSIARALMNGGE 163
Cdd:cd03229 76 R-RIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHK-AGHTVIMVTHDPGIAAN-ANRIIEIRDGE 219
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-223 |
1.51e-48 |
|
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: 177.79 E-value: 1.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MS-LIECKNINRYFGSGenRVHILKDISLSIEKGDFVAIIGQSGSGKSTL-MNILGCLDTAG--SGSYRIDGIETAKMQP 76
Cdd:COG1123 1 MTpLLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLaLALMGLLPHGGriSGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 77 delaALRRERFGFIFQRY-NLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIA 155
Cdd:COG1123 79 ----ALRGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 156 RALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIAAN-ANRIIEIRDGEIISD 223
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEiADRVVVMDDGRIVED 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-223 |
2.81e-48 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 169.45 E-value: 2.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINryFGSGENRvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAal 82
Cdd:COG1120 1 MLEAENLS--VGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 rrERFGFIFQRYNLLSSLTARDNVAL---PavYMGMGGKERS---ARADKLLQDLGLASKEGNKPGELSGGQQQRVSIAR 156
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRELVALgryP--HLGLFGRPSAedrEAVEEALERTGLEHLADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 157 ALMNGGEIIFADEPTGALDTASGKNVMEIIRRL-HKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEIISD 223
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQ 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-220 |
5.22e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 168.73 E-value: 5.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGsgenRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGcLDTAGSGSYRIDGietakmqpdEL 79
Cdd:COG1121 4 MPAIELENLTVSYG----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILG-LLPPTSGTVRLFG---------KP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 80 AALRRERFGFIFQRYNLLSS--LTARDNVALpAVYMGMG-----GKERSARADKLLQDLGLASKEgNKP-GELSGGQQQR 151
Cdd:COG1121 70 PRRARRRIGYVPQRAEVDWDfpITVRDVVLM-GRYGRRGlfrrpSRADREAVDEALERVGLEDLA-DRPiGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 152 VSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPG-IAANANRIIEIRDGEI 220
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGaVREYFDRVLLLNRGLV 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-201 |
6.11e-48 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 171.52 E-value: 6.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALR 83
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 ReRFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:PRK11153 82 R-QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTH 201
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRElGLTIVLITH 199
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-225 |
1.92e-47 |
|
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: 167.29 E-value: 1.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdelAAL 82
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRR---KAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RReRFGFIFQRYnlLSSL----TARDNVALPAVYMGMGgkERSARADKLLQDLGLASKEGNK-PGELSGGQQQRVSIARA 157
Cdd:COG1124 78 RR-RVQMVFQDP--YASLhprhTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 158 LMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPG-IAANANRIIEIRDGEIISDTS 225
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAvVAHLCDRVAVMQNGRIVEELT 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-221 |
2.59e-47 |
|
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: 166.20 E-value: 2.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGenrvHILKDISLSIEKGDFVAIIGQSGSGKSTLMNIL-GCLDTAG----SGSYRIDGIETAKMQPDE 78
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLnRLNDLIPgapdEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 79 LAaLRReRFGFIFQRYNLLSsLTARDNVALPAVYMGM-GGKERSARADKLLQDLGLASKEGNK--PGELSGGQQQRVSIA 155
Cdd:cd03260 77 LE-LRR-RVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2559317375 156 RALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAgHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARvADRTAFLLNGRLV 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-213 |
2.77e-47 |
|
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: 169.08 E-value: 2.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCLDTAG--SGSYRIDGIETAKMQPDEL 79
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPGitSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 80 AALRRERFGFIFQryNLLSSL----TARDNVALP-AVYMGMGGKERSARADKLLQDLGLASKE---GNKPGELSGGQQQR 151
Cdd:COG0444 81 RKIRGREIQMIFQ--DPMTSLnpvmTVGDQIAEPlRIHGGLSKAEARERAIELLERVGLPDPErrlDRYPHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 152 VSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIAAN-ANRII 213
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEiADRVA 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-220 |
6.38e-46 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 166.40 E-value: 6.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdela 80
Cdd:COG3839 1 MASLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 alrRER-FGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALM 159
Cdd:COG3839 73 ---KDRnIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 160 NGGEIIFADEPTGALDtASGKNVMEI-IRRLHKA-GHTVIMVTHDPGIA-ANANRIIEIRDGEI 220
Cdd:COG3839 150 REPKVFLLDEPLSNLD-AKLRVEMRAeIKRLHRRlGTTTIYVTHDQVEAmTLADRIAVMNDGRI 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-221 |
1.28e-45 |
|
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: 162.81 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGS-----------GENRVHILK---------DISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGS 63
Cdd:cd03294 1 IKIKGLYKIFGKnpqkafkllakGKSKEEILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 64 YRIDGIETAKMQPDELAALRRERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGE 143
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 144 LSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLH-KAGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQaELQKTIVFITHDLDEALRlGDRIAIMKDGRLV 240
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-220 |
1.35e-45 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 162.66 E-value: 1.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGEnrvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGiETAKMQPDELAALR 83
Cdd:COG4598 9 LEVRDLHKSFGDLE----VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGG-EEIRLKPDRDGELV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 ----------RERFGFIFQRYNLLSSLTARDNVALPAVY-MGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRV 152
Cdd:COG4598 84 padrrqlqriRTRLGMVFQSFNLWSHMTVLENVIEAPVHvLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 153 SIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEI 220
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDvSSHVVFLHQGRI 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-221 |
1.53e-45 |
|
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: 160.78 E-value: 1.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 5 ECKNIN-RYfgsgeNRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCLDTAgSGSYRIDGIETAKMqpdelaal 82
Cdd:cd03235 1 EVEDLTvSY-----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLKPT-SGSIRVFGKPLEKE-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 rRERFGFIFQRYNLLSS--LTARDNVALPAV-YMGMGG---KERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIAR 156
Cdd:cd03235 67 -RKRIGYVPQRRSIDRDfpISVRDVVLMGLYgHKGLFRrlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2559317375 157 ALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPG-IAANANRIIEIrDGEII 221
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDRVLLL-NRTVV 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-221 |
2.52e-45 |
|
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: 161.31 E-value: 2.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGENRVhilKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalr 83
Cdd:cd03295 1 IEFENVTKRYGGGKKAV---NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKE--GNKPGELSGGQQQRVSIARALMNG 161
Cdd:cd03295 74 RRKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 162 GEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRlADRIAIMKNGEIV 215
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-219 |
8.23e-45 |
|
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: 157.16 E-value: 8.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINryFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalr 83
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSlTARDNValpavymgmggkersaradkllqdlglaskegnkpgeLSGGQQQRVSIARALMNGGE 163
Cdd:cd03228 75 RKNIAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHKaGHTVIMVTHDPGIAANANRIIEIRDGE 219
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
22-220 |
8.54e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 158.44 E-value: 8.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalrRERFGFIFQRynllSSL- 100
Cdd:COG4619 15 ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW----RRQVAYVPQE----PALw 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 101 --TARDNvaLPAVYMGMGGKERSARADKLLQDLGLASKEGNKP-GELSGGQQQRVSIARALMNGGEIIFADEPTGALDTA 177
Cdd:COG4619 87 ggTVRDN--LPFPFQLRERKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2559317375 178 SGKNVMEIIRRL-HKAGHTVIMVTHDPG-IAANANRIIEIRDGEI 220
Cdd:COG4619 165 NTRRVEELLREYlAEEGRAVLWVSHDPEqIERVADRVLTLEAGRL 209
|
|
| MacB_PCD |
pfam12704 |
MacB-like periplasmic core domain; This family represents the periplasmic core domain found in ... |
269-488 |
9.56e-45 |
|
MacB-like periplasmic core domain; This family represents the periplasmic core domain found in a variety of ABC transporters. The structure of this family has been solved for the MacB protein. Some structural similarity was found to the periplasmic domain of the AcrB multidrug efflux transporter.
Pssm-ID: 463676 [Multi-domain] Cd Length: 211 Bit Score: 158.46 E-value: 9.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 269 SLLTMLGIIIGIASVVSVVALGNGSQKKILEDISSMGtNTISIFPGRGFGDRRSGkikTLTIDDAKIIAKQSYVASATPM 348
Cdd:pfam12704 1 TALTVLGIAIGVAAVIAILSLGDGLLSAVPEQISDSD-NLVVVQPGAAGGGGTRP---PLSDPDAEALRRAVPVEAVAPV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 349 tSSGGTLTYRNTDLTASLYGVGEQYFDVRGLKLESGRLFDENDVKEDAQVVVIDQNVKDKLFADSDPLGKTILFRKRPLT 428
Cdd:pfam12704 77 -VSTVRYGNSTTERLVTVVGVDPDFFKVFGLPLAEGRFFTEADVLGGPNVVVLGESLAEKLFGGDDPVGKTIRLNGQPFT 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 429 VIGVMKKDENAFGNSDVLMLwsPYTTVMHQITgeGHTNSITVKIKDNANIQVAEKGLTEL 488
Cdd:pfam12704 156 VVGVLPDFPGSDGGGDLVYV--PLTTLQRRLG--DSVSTILVRLKDGADLAAAAAELRAL 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-220 |
1.55e-44 |
|
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: 158.55 E-value: 1.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGenrvHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDelaalr 83
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIA-ANANRIIEIRDGEI 220
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEAlTMSDRIAVMNKGKI 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-221 |
4.79e-44 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 161.08 E-value: 4.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSlIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGiETAKMQpdeLA 80
Cdd:COG1118 1 MS-IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG-RDLFTN---LP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 ALRReRFGFIFQRYNLLSSLTARDNVA--LPAvyMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARAL 158
Cdd:COG1118 72 PRER-RVGFVFQHYALFPHMTVAENIAfgLRV--RPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 159 MNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIA-ANANRIIEIRDGEII 221
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEAlELADRVVVMNQGRIE 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-202 |
5.01e-44 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 158.49 E-value: 5.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKmqPDEla 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 alrrERfGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMN 160
Cdd:COG4525 77 ----DR-GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2559317375 161 GGEIIFADEPTGALDTASGKNVMEIIRRL-HKAGHTVIMVTHD 202
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHS 194
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
8-220 |
1.50e-43 |
|
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: 159.82 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 8 NINRYFGsgenRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDelaalRRErF 87
Cdd:TIGR03265 9 NIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ-----KRD-Y 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 88 GFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFA 167
Cdd:TIGR03265 79 GIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 168 DEPTGALDTASGKNVMEIIRRLH-KAGHTVIMVTHDPGIA-ANANRIIEIRDGEI 220
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQrRLGVTTIMVTHDQEEAlSMADRIVVMNHGVI 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-221 |
3.07e-43 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 155.68 E-value: 3.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFgsgeNRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIE--TAKMQPDE 78
Cdd:PRK11264 1 MSAIEVKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidTARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 79 LAALR--RERFGFIFQRYNLLSSLTARDNVAL-PAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIA 155
Cdd:PRK11264 77 KGLIRqlRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2559317375 156 RALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIV 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-221 |
6.07e-43 |
|
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: 154.63 E-value: 6.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKmQPDELaal 82
Cdd:COG4555 1 MIEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 rRERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGG 162
Cdd:COG4555 73 -RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 163 EIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDP-GIAANANRIIEIRDGEII 221
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMqEVEALCDRVVILHKGKVV 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-225 |
2.26e-42 |
|
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: 154.13 E-value: 2.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNInrYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKmqPDELAALR 83
Cdd:TIGR04520 1 IEVENV--SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD--EENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 ReRFGFIFQR-YNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARAL-MNG 161
Cdd:TIGR04520 77 K-KVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLaMRP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 162 GEIIFaDEPTGALDTASGKNVMEIIRRLHK-AGHTVIMVTHDPGIAANANRIIEIRDGEIISDTS 225
Cdd:TIGR04520 156 DIIIL-DEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-223 |
1.36e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 150.68 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGsgenrvHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDelaalr 83
Cdd:COG3840 2 LRLDDLTYRYG------DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 rER-FGFIFQRYNLLSSLTARDNVALpavymGM--GGK---ERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARA 157
Cdd:COG3840 70 -ERpVSMLFQENNLFPHLTVAQNIGL-----GLrpGLKltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 158 LMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPG-IAANANRIIEIRDGEIISD 223
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEdAARIADRVLLVADGRIAAD 211
|
|
| LolE |
COG4591 |
ABC-type transport system involved in lipoprotein release, permease component LolC [Cell wall ... |
394-641 |
1.73e-41 |
|
ABC-type transport system involved in lipoprotein release, permease component LolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443648 [Multi-domain] Cd Length: 283 Bit Score: 152.00 E-value: 1.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 394 EDAQVVVIDQNVKDKLfadSDPLGKTILF-------RKRPLTVIGVMKKDENAFGNSDVLMlwsPYTTVMHQITGEGHTN 466
Cdd:COG4591 31 KASDEVVLGEGLAKKL---GLKVGDTITLispdgspKTRRFTVVGIFESGGYELDGSLVYV---PLETAQELLGLGDQVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 467 SITVKIKDNANIQVAEKGLTELLKarhgteDFFMNNSDSIRQMVESTTGTMKLLISSIALISLVVGGIGVMNIMLVSVTE 546
Cdd:COG4591 105 GILVKLKDGADAEAVAAALEAALP------GLEVKTWRELNAALFSALKTEKLILLLILLLILLVAAFNIVNTLLMSVLE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 547 RTKEIGIRMAIGARRGNILQQFLIEAVLICVIGGLVGVGLSAAVSLVFNH-------FVTDFPMDISAMSVIGAVACSTG 619
Cdd:COG4591 179 RTREIGILKALGASRRQIRRIFLLEGLLLGLIGGLLGLLLGLLLALLLNAllgillpFIFALPVSLSPSDVLLALLLALL 258
|
250 260
....*....|....*....|..
gi 2559317375 620 IGIAFGFMPANKAAKLNPIDAL 641
Cdd:COG4591 259 ISLLASLYPARRAARLDPVEAL 280
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-219 |
2.43e-41 |
|
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: 147.39 E-value: 2.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 5 ECKNINRYFGSGenrvHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalrR 84
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 85 ERFGFIFQrynllssltardnvalpavymgmggkersaradkllqdlglaskegnkpgeLSGGQQQRVSIARALMNGGEI 164
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2559317375 165 IFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANA-NRIIEIRDGE 219
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-223 |
2.63e-41 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 149.89 E-value: 2.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAalr 83
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 reRFGFI--FQRYNLLSSLTARDNVALPAVYMGMGG----------KERSARADKLLQDLGLASKEGNKPGELSGGQQQR 151
Cdd:cd03219 74 --RLGIGrtFQIPRLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 152 VSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEIISD 223
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAE 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-221 |
3.29e-41 |
|
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: 158.00 E-value: 3.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNIN-RYfgsgENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaal 82
Cdd:COG4988 337 IELEDVSfSY----PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW--- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 rRERFGFIFQRyNLLSSLTARDNVALpavymgmGGKE----------RSARADKLLQDL--GLASK--EGNKPgeLSGGQ 148
Cdd:COG4988 410 -RRQIAWVPQN-PYLFAGTIRENLRL-------GRPDasdeeleaalEAAGLDEFVAALpdGLDTPlgEGGRG--LSGGQ 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 149 QQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLhKAGHTVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQADRILVLDDGRIV 550
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-226 |
3.40e-41 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 159.61 E-value: 3.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINryFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalr 83
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSlTARDNVAlpavymgMGGKERS-ARADKLLQDLGLASKEGNKP-------GE----LSGGQQQR 151
Cdd:COG2274 548 RRQIGVVLQDVFLFSG-TIRENIT-------LGDPDATdEEIIEAARLAGLHDFIEALPmgydtvvGEggsnLSGGQRQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 152 VSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLhKAGHTVIMVTHDPGIAANANRIIEIRDGEIISDTSK 226
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTH 693
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-223 |
3.08e-40 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 145.27 E-value: 3.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 5 ECKNINryFGSGENRvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAalrr 84
Cdd:cd03214 1 EVENLS--VGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 85 ERFGFIFQrynllssltardnvalpavymgmggkersaradkLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEI 164
Cdd:cd03214 73 RKIAYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 165 IFADEPTGALDTASGKNVMEIIRRL-HKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEIISD 223
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQ 179
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-220 |
1.22e-39 |
|
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: 143.31 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGEnrvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIEtakmqPDELAALR 83
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD-----IKKEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSLTARDNValpavymgmggkersaradkllqdlglaskegnkpgELSGGQQQRVSIARALMNGGE 163
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEI 220
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-240 |
3.71e-39 |
|
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: 143.76 E-value: 3.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAalrrerfgfIFQRYNLLSSLTA 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 103 RDNVALP--AVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGK 180
Cdd:TIGR01184 72 RENIALAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 181 NVME-IIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGeiisdtsknpeiPTSNVGRIRE 240
Cdd:TIGR01184 152 NLQEeLMQIWEEHRVTVLMVTHDVDEALLlSDRVVMLTNG------------PAANIGQILE 201
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-223 |
4.37e-39 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 144.41 E-value: 4.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELA 80
Cdd:COG0411 2 DPLLEVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 AL---RrerfgfIFQRYNLLSSLTARDNVALpAVYMGMGG----------------KERSARADKLLQDLGLASKEGNKP 141
Cdd:COG0411 78 RLgiaR------TFQNPRLFPELTVLENVLV-AAHARLGRgllaallrlprarreeREARERAEELLERVGLADRADEPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 142 GELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPG-IAANANRIIEIRDGE 219
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDlVMGLADRIVVLDFGR 230
|
....
gi 2559317375 220 IISD 223
Cdd:COG0411 231 VIAE 234
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-228 |
1.02e-38 |
|
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: 142.86 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSlIECKNINRYFGsgenRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdela 80
Cdd:cd03296 1 MS-IEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 alrRER-FGFIFQRYNLLSSLTARDNVALpavymGMGGKERS---------ARADKLLQDLGLASKEGNKPGELSGGQQQ 150
Cdd:cd03296 72 ---QERnVGFVFQHYALFRHMTVFDNVAF-----GLRVKPRSerppeaeirAKVHELLKLVQLDWLADRYPAQLSGGQRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 151 RVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLH-KAGHTVIMVTHDPGIAAN-ANRIIEIRDGEI-------- 220
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEvADRVVVMNKGRIeqvgtpde 223
|
....*...
gi 2559317375 221 ISDTSKNP 228
Cdd:cd03296 224 VYDHPASP 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-220 |
2.63e-38 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 145.23 E-value: 2.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSlIECKNINRYFGsgenRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdela 80
Cdd:PRK10851 1 MS-IEIANIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 alRRERFGFIFQRYNLLSSLTARDNVA-----LPAvymgmggKERSARAD------KLLQDLGLASKEGNKPGELSGGQQ 149
Cdd:PRK10851 72 --RDRKVGFVFQHYALFRHMTVFDNIAfgltvLPR-------RERPNAAAikakvtQLLEMVQLAHLADRYPAQLSGGQK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 150 QRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIAAN-ANRIIEIRDGEI 220
Cdd:PRK10851 143 QRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-221 |
3.56e-38 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 143.31 E-value: 3.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalR 83
Cdd:COG1125 2 IEFENVTKRYPDG---TVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 ReRFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKE-GNK-PGELSGGQQQRVSIARALMNG 161
Cdd:COG1125 76 R-RIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEyRDRyPHELSGGQQQRVGVARALAAD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 162 GEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIA-ANANRIIEIRDGEII 221
Cdd:COG1125 155 PPILLMDEPFGALDPITREQLQDELLRLQRElGKTIVFVTHDIDEAlKLGDRIAVMREGRIV 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-221 |
5.75e-38 |
|
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: 148.76 E-value: 5.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNIN-RYFGSGENrvhILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCLDTAgSGSYRIDGIETAKMQPDELaa 81
Cdd:COG4987 334 LELEDVSfRYPGAGRP---VLDGLSLTLPPGERVAIVGPSGSGKSTLLAlLLRFLDPQ-SGSITLGGVDLRDLDEDDL-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 82 lrRERFGFIFQRYNLLSSlTARDNVALpavymgmgGKE-----------RSARADKLLQDL--GLASKEGNKPGELSGGQ 148
Cdd:COG4987 408 --RRRIAVVPQRPHLFDT-TLRENLRL--------ARPdatdeelwaalERVGLGDWLAALpdGLDTWLGEGGRRLSGGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 149 QQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRlHKAGHTVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-221 |
7.68e-38 |
|
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: 147.52 E-value: 7.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKS-TLMNILGCLDTAG---SGSYRIDGIETAKMQP 76
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 77 DELAALRRERFGFIFQryNLLSSL----TARDNVALP-AVYMGMGGKERSARADKLLQDLGLASKE---GNKPGELSGGQ 148
Cdd:COG4172 84 RELRRIRGNRIAMIFQ--EPMTSLnplhTIGKQIAEVlRLHRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 149 QQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRL-HKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRfADRVAVMRQGEIV 236
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-171 |
1.90e-37 |
|
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: 136.24 E-value: 1.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIEtakMQPDELAALRReRFGFIFQRYNLLSSLTA 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRK-EIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 103 RDNVALPAVYMGMGGKERSARADKLLQDLGLASKE----GNKPGELSGGQQQRVSIARALMNGGEIIFADEPT 171
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-221 |
3.95e-37 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 137.39 E-value: 3.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 7 KNINRYFGSGENrvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGietakmqPDELAALRRER 86
Cdd:cd03226 3 ENISFSYKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-------KPIKAKERRKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 87 FGFIFQ--RYNLLSSlTARDNVALPAvymgMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEI 164
Cdd:cd03226 73 IGYVMQdvDYQLFTD-SVREELLLGL----KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 165 IFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-221 |
5.15e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 146.08 E-value: 5.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINryFGSGENRvHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalr 83
Cdd:COG1132 340 IEFENVS--FSYPGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLsSLTARDNVALpavymgmgGKE-----------RSARADKLLQDL--GLASKEGNKPGELSGGQQQ 150
Cdd:COG1132 413 RRQIGVVPQDTFLF-SGTIRENIRY--------GRPdatdeeveeaaKAAQAHEFIEALpdGYDTVVGERGVNLSGGQRQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 151 RVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKaGHTVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-223 |
7.54e-37 |
|
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: 136.95 E-value: 7.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGENrvHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalr 83
Cdd:cd03245 3 IEFRNVSFSYPNQEI--PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSlTARDNVALPAVYMGMGGKERSAR---ADKLLQDL--GLASKEGNKPGELSGGQQQRVSIARAL 158
Cdd:cd03245 77 RRNIGYVPQDVTLFYG-TLRDNITLGAPLADDERILRAAElagVTDFVNKHpnGLDLQIGERGRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 159 MNGGEIIFADEPTGALDTASGKNVMEIIRRLhKAGHTVIMVTHDPGIAANANRIIEIRDGEIISD 223
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
22-217 |
1.04e-36 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 136.07 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIEtakmqPDELAALRRERFGFIFQRYNLLSSLT 101
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP-----IRDAREDYRRRLAYLGHADGLKPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNVALpavYMGMGGKERS-ARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGK 180
Cdd:COG4133 92 VRENLRF---WAALYGLRADrEAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVA 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 2559317375 181 NVMEIIRRLHKAGHTVIMVTHDPgIAANANRIIEIRD 217
Cdd:COG4133 169 LLAELIAAHLARGGAVLLTTHQP-LELAAARVLDLGD 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-221 |
2.14e-36 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 136.31 E-value: 2.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDelaalrRERFGFIFQRYNLLSSLTA 102
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------KRDISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 103 RDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNV 182
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2559317375 183 MEIIRRLHKA-GHTVIMVTHD-PGIAANANRIIEIRDGEII 221
Cdd:cd03299 169 REELKKIRKEfGVTVLHVTHDfEEAWALADKVAIMLNGKLI 209
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-220 |
2.18e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 137.12 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 7 KNINRYFGSGEnrvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRidgietAKMQPdeLAALRrER 86
Cdd:PRK11247 16 NAVSKRYGERT----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL------AGTAP--LAEAR-ED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 87 FGFIFQRYNLLSSLTARDNVALpavymGMGGKERsARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIF 166
Cdd:PRK11247 83 TRLMFQDARLLPWKKVIDNVGL-----GLKGQWR-DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2559317375 167 ADEPTGALDTASGKNVMEIIRRL-HKAGHTVIMVTHDPGIA-ANANRIIEIRDGEI 220
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-223 |
4.58e-36 |
|
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: 134.54 E-value: 4.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 25 DISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDElaalrrERFGFIFQRYNLLSSLTARD 104
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQENNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 105 NVAL---PAVYMGmggKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKN 181
Cdd:cd03298 90 NVGLglsPGLKLT---AEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2559317375 182 VMEIIRRLHK-AGHTVIMVTHDPG-IAANANRIIEIRDGEIISD 223
Cdd:cd03298 167 MLDLVLDLHAeTKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQ 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-218 |
7.42e-36 |
|
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: 134.48 E-value: 7.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 19 RVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNIL--GCLDTAGSGSYRIDG--IETAKMQPDELAALRRERFGFIFQRY 94
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYLPDSGSILVRHDGgwVDLAQASPREILALRRRTIGYVSQFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 95 NLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLaskegnkPGEL--------SGGQQQRVSIARALMNGGEIIF 166
Cdd:COG4778 103 RVIPRVSALDVVAEPLLERGVDREEARARARELLARLNL-------PERLwdlppatfSGGEQQRVNIARGFIADPPLLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 167 ADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPG-IAANANRIIEIRDG 218
Cdd:COG4778 176 LDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEvREAVADRVVDVTPF 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-220 |
9.94e-36 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 134.23 E-value: 9.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALRRErFGFIFQRYNLLSSLTA 102
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 103 RDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNV 182
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 2559317375 183 MEIIRRLHKAGHTVIMVTHDPGIAANAN-RIIEIRDGEI 220
Cdd:PRK10908 177 LRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-221 |
3.31e-35 |
|
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: 130.63 E-value: 3.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDElaALR 83
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--ARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 ReRFGFIFQrynllssltardnvalpavymgmggkersaradkllqdlglaskegnkpgeLSGGQQQRVSIARALMNGGE 163
Cdd:cd03216 75 A-GIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPG-IAANANRIIEIRDGEII 221
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDeVFEIADRVTVLRDGRVV 161
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-221 |
4.73e-35 |
|
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: 131.93 E-value: 4.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGenrvHILKDISLSIEKGDFvAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMqPDELaalr 83
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:cd03264 71 RRRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLhKAGHTVIMVTHDPG-IAANANRIIEIRDGEII 221
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-233 |
5.41e-35 |
|
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: 132.90 E-value: 5.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSG-SYRIDGIETAKMQPDEL 79
Cdd:COG1119 1 DPLLELRNVTVRRGG----KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 80 aalrRERFGF----IFQRYNllSSLTARDnVALPAVYMGMG-----GKERSARADKLLQDLGLASKEGNKPGELSGGQQQ 150
Cdd:COG1119 77 ----RKRIGLvspaLQLRFP--RDETVLD-VVLSGFFDSIGlyrepTDEQRERARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 151 RVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGH-TVIMVTHD-----PGIaanaNRIIEIRDGEIISDT 224
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHveeipPGI----THVLLLKDGRVVAAG 225
|
....*....
gi 2559317375 225 SKNpEIPTS 233
Cdd:COG1119 226 PKE-EVLTS 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
16-220 |
1.45e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 132.01 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 16 GENRVhiLKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGiETAKMQPDELAALR----------RE 85
Cdd:PRK10619 16 GEHEV--LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNG-QTINLVRDKDGQLKvadknqlrllRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 86 RFGFIFQRYNLLSSLTARDNV-ALPAVYMGMGGKERSARADKLLQDLGLASK-EGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:PRK10619 93 RLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEI 220
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKI 230
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-220 |
1.53e-34 |
|
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: 128.87 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINryFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalr 83
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSlTARDNValpavymgmggkersaradkllqdlglaskegnkpgeLSGGQQQRVSIARALMNGGE 163
Cdd:cd03246 75 GDHVGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDGEI 220
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-223 |
1.79e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 131.78 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGsgenRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNIL-GCLdTAGSGSYRIDGIETAKMQPDELAA 81
Cdd:COG4559 1 MLEAENLSVRLG----GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGEL-TPSSGEVRLNGRPLAAWSPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 82 LRrerfGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARAL--- 158
Cdd:COG4559 76 RR----AVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaql 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 159 ---MNGGE-IIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEIISD 223
Cdd:COG4559 152 wepVDGGPrWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQyADRILLLHQGRLVAQ 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-220 |
2.33e-34 |
|
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: 130.07 E-value: 2.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdelaalr 83
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RER-FGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGG 162
Cdd:cd03301 70 KDRdIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 163 EIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIA-ANANRIIEIRDGEI 220
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-223 |
2.42e-34 |
|
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: 130.18 E-value: 2.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKmQPDELaal 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 rRERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGG 162
Cdd:cd03266 77 -RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 163 EIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPG-IAANANRIIEIRDGEIISD 223
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQeVERLCDRVVVLHRGRVVYE 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-213 |
4.11e-34 |
|
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: 136.65 E-value: 4.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 17 ENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAkmqpDELAALRRERFGFIFQRYNL 96
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA----DADADSWRDQIAWVPQHPFL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 97 LSSlTARDNVALPAVYMGMGGKERSAR---ADKLLQDL--GLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPT 171
Cdd:TIGR02857 408 FAG-TIAENIRLARPDASDAEIREALEragLDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2559317375 172 GALDTASGKNVMEIIRRLHKaGHTVIMVTHDPGIAANANRII 213
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRIV 527
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-222 |
5.04e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.91 E-value: 5.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 2 SLIECKNIN-RYfgsGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIEtakMQPDELA 80
Cdd:PRK13635 4 EIIRVEHISfRY---PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 ALRReRFGFIFQRY-NLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALM 159
Cdd:PRK13635 78 DVRR-QVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 160 NGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGH-TVIMVTHDPGIAANANRIIEIRDGEIIS 222
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-223 |
7.17e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 135.53 E-value: 7.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdeLAAL 82
Cdd:COG1129 4 LLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSP--RDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RReRFGFIFQRYNLLSSLTARDNVALPAVYMGMGG---KERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALM 159
Cdd:COG1129 78 AA-GIAIIHQELNLVPNLSVAENIFLGREPRRGGLidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 160 NGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRDGEIISD 223
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRlDEVFEIADRVTVLRDGRLVGT 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
18-217 |
9.13e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 127.98 E-value: 9.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 18 NRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCLDTA--GSGSYRIDGIETakmqpDELAALRReRFGFIFQRY 94
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRL-----TALPAEQR-RIGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 95 NLLSSLTARDNV--ALPAvymGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTG 172
Cdd:COG4136 86 LLFPHLSVGENLafALPP---TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2559317375 173 ALDTASGKNVMEIIR-RLHKAGHTVIMVTHDPGIAANANRIIEIRD 217
Cdd:COG4136 163 KLDAALRAQFREFVFeQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-202 |
1.15e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 131.39 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYF-------GSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQ 75
Cdd:COG4608 7 LLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 76 PDELAALRReRFGFIFQryNLLSSL----TARDNVALPAVYMGMG-GKERSARADKLLQDLGLASKEGNK-PGELSGGQQ 149
Cdd:COG4608 87 GRELRPLRR-RMQMVFQ--DPYASLnprmTVGDIIAEPLRIHGLAsKAERRERVAELLELVGLRPEHADRyPHEFSGGQR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 150 QRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHD 202
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHD 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-201 |
1.61e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 129.00 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTL------MN--ILGCldtAGSGSYRIDG--IETAK 73
Cdd:COG1117 12 IEVRNLNVYYGD----KQALKDINLDIPENKVTALIGPSGCGKSTLlrclnrMNdlIPGA---RVEGEILLDGedIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 74 MQPDELaalrRERFGFIFQRYNLLsSLTARDNVALPAVYMGMGGK-------ERSARA--------DKLlqdlglaskeg 138
Cdd:COG1117 85 VDVVEL----RRRVGMVFQKPNPF-PKSIYDNVAYGLRLHGIKSKseldeivEESLRKaalwdevkDRL----------- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 139 NKPG-ELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLhKAGHTVIMVTH 201
Cdd:COG1117 149 KKSAlGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYTIVIVTH 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-222 |
2.07e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 129.09 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalr 83
Cdd:PRK13647 5 IEVEDLHFRYKDG---TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYN-LLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGG 162
Cdd:PRK13647 78 RSKVGLVFQDPDdQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 163 EIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEIIS 222
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLA 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
21-223 |
2.77e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 128.35 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 21 HILKDISLSIEKGDFVAIIGQSGSGKSTLMNIL-GCLdTAGSGSYRIDGIETAKMQPDELAALRrerfGFIFQRYNLLSS 99
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGEL-SPDSGEVRLNGRPLADWSPAELARRR----AVLPQHSSLSFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 100 LTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALM------NGGEIIFADEPTGA 173
Cdd:PRK13548 91 FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 174 LDTASGKNVMEIIRRL-HKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEIISD 223
Cdd:PRK13548 171 LDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVAD 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-221 |
3.12e-33 |
|
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: 127.35 E-value: 3.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 13 FGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMqpdELAALRRErFGFIFQ 92
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY---TLASLRRQ-IGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 93 RYNLLSSlTARDNVALPAVYMGMGGKERSARADKLLQ-----DLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFA 167
Cdd:cd03251 84 DVFLFND-TVAENIAYGRPGATREEVEEAARAANAHEfimelPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 168 DEPTGALDTASGKNVMEIIRRLHKaGHTVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:cd03251 163 DEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIENADRIVVLEDGKIV 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-223 |
4.38e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 129.05 E-value: 4.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSG-ENRVHILKDISLSIEKGDFVAIIGQSGSGKSTL---MNILgCLDTAGSGSYRIDGIETAK------ 73
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNAL-LLPDTGTIEWIFKDEKNKKktkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 74 -------MQPDELAALR-----RERFGFIFQ--RYNLLSSlTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGN 139
Cdd:PRK13651 82 kvleklvIQKTRFKKIKkikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 140 K-PGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRD 217
Cdd:PRK13651 161 RsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDlDNVLEWTKRTIFFKD 240
|
....*.
gi 2559317375 218 GEIISD 223
Cdd:PRK13651 241 GKIIKD 246
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-223 |
1.49e-32 |
|
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: 124.71 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIE---KGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGI---ETAK---MQPdelaalRRERFGFIFQR 93
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkinLPP------QQRKIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 94 YNLLSSLTARDNVALpaVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGA 173
Cdd:cd03297 84 YALFPHLNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 174 LDTASGKNVMEIIRRLHKAGH-TVIMVTHDPGIAAN-ANRIIEIRDGEIISD 223
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNLNiPVIFVTHDLSEAEYlADRIVVMEDGRLQYI 213
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-223 |
1.94e-32 |
|
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: 128.00 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 38 IIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDelaalrRERFGFIFQRYNLLSSLTARDNVALPAVYMGMGG 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH------LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 118 KERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNV-MEIIRRLHKAGHTV 196
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMqLELKTIQEQLGITF 154
|
170 180
....*....|....*....|....*...
gi 2559317375 197 IMVTHDPGIA-ANANRIIEIRDGEIISD 223
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGKIAQI 182
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-221 |
2.58e-32 |
|
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: 131.35 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYF-------GSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTL-MNILGCLDTagSGSYRIDGIETAKM 74
Cdd:COG4172 275 LLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLIPS--EGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 75 QPDELAALRReRFGFIFQryNLLSSLTARDNVA------LPAVYMGMGGKERSARADKLLQDLGLASKEGNK-PGELSGG 147
Cdd:COG4172 353 SRRALRPLRR-RMQVVFQ--DPFGSLSPRMTVGqiiaegLRVHGPGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGG 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2559317375 148 QQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRL-HKAGHTVIMVTHDPG-IAANANRIIEIRDGEII 221
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAvVRALAHRVMVMKDGKVV 505
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
5.76e-32 |
|
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: 123.38 E-value: 5.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGENrvHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKmQPDELaalr 83
Cdd:cd03263 1 LQIRNLTKTYKKGTK--PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLhKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-221 |
6.43e-32 |
|
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: 123.25 E-value: 6.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGEnrvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKmQPDELaalr 83
Cdd:cd03265 1 IEVENLVKKYGDFE----AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREV---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:cd03265 72 RRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIA-ANANRIIEIRDGEII 221
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAeQLCDRVAIIDHGRII 211
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
12-225 |
7.28e-32 |
|
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: 123.75 E-value: 7.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 12 YFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdelAALRRErFGFIF 91
Cdd:cd03252 7 RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP---AWLRRQ-VGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 92 QRyNLLSSLTARDNVALPAVYMGMGGKERSAR---ADKLLQDL--GLASKEGNKPGELSGGQQQRVSIARALMNGGEIIF 166
Cdd:cd03252 83 QE-NVLFNRSIRDNIALADPGMSMERVIEAAKlagAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 167 ADEPTGALDTASGKNVMEIIRRLhKAGHTVIMVTHDPGIAANANRIIEIRDGEIISDTS 225
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGS 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-223 |
8.47e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 124.81 E-value: 8.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNIN-RYFGSGENRVHI-LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQpdELA 80
Cdd:PRK13633 4 MIKCKNVSyKYESNEESTEKLaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE--NLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 ALRReRFGFIFQRY-NLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALM 159
Cdd:PRK13633 82 DIRN-KAGMVFQNPdNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 160 NGGEIIFADEPTGALDTASGKNVMEIIRRLHK-AGHTVIMVTHDPGIAANANRIIEIRDGEIISD 223
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKkYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| ADOP |
TIGR03434 |
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, ... |
344-641 |
9.23e-32 |
|
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, only in three species of Acidobacteria, namely Acidobacteria bacterium Ellin345, Acidobacterium capsulatum ATCC 51196, and Solibacter usitatus Ellin6076, where they form large paralogous families. Each protein contains two copies of a domain called the efflux ABC transporter permease protein (pfam02687). However, unlike other members of that family (including LolC, FtsX, and MacB), genes for these proteins are essentially never found fused or adjacent to ABC transporter ATP-binding protein (pfam00005) genes. We name this family ADOP, for Acidobacterial Duplicated Orphan Permease, to reflect the restricted lineage, internal duplication, lack of associated ATP-binding cassette proteins, and permease homology. The function is unknown.
Pssm-ID: 274576 [Multi-domain] Cd Length: 803 Bit Score: 131.48 E-value: 9.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 344 SATPMTSSGGTLTYRNTDLTASLYGVGEQYFDVRGLKLESGRLFDENDVKEDAQVVVIDQNVKDKLFADSDPLGKTILF- 422
Cdd:TIGR03434 507 WSGGVTIEGRPPPPPGEEPLADYRRVSPGYFETMGIPLLRGRDFTERDTAGSPPVAIVNEAFARRYFPGEDPIGKRIRLg 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 423 --RKRPLTVIGVMKkD--ENAFGNSDVLMLWSPYTtvmhqitgEGHTNSITVKIKDNANIQVAEKGLTELLKARHGteDF 498
Cdd:TIGR03434 587 gdDGPWFEIVGVVG-DvrYAGLDEPPRPEVYLPYA--------QSPDRGMTLVVRTAGDPAALAAAVRRAVRAIDP--NL 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 499 FMNNSDSIRQMVESTTGT---MKLLISSIALISLVVGGIGVMNIMLVSVTERTKEIGIRMAIGARRGNILQQFLIEAVLI 575
Cdd:TIGR03434 656 PVYDVRTMEEQVDRSLAQerfLALLLGLFAALALLLAAIGLYGVLAYSVAQRTREIGIRMALGAQRGDVLRLVLRQGLRL 735
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 576 CVIGGLVGVGLSAAV-----SLVFNhfVTdfPMDisAMSVIGAVACSTGIGIAFGFMPANKAAKLNPIDAL 641
Cdd:TIGR03434 736 AAAGLAIGLAAALALarllaSLLFG--VS--PTD--PLTFAAVAALLLAVALLACYLPARRAARVDPMIAL 800
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-223 |
9.32e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 124.04 E-value: 9.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSG-ENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILgcldtAG-----SGSYRIDGIETAKMqPD 77
Cdd:COG1101 2 LELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAI-----AGslppdSGSILIDGKDVTKL-PE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 78 ElaalRRERF-GFIFQryNLL----SSLTARDNVALPA-------VYMGMGGKERSARADKLLQ-DLGLASKEGNKPGEL 144
Cdd:COG1101 76 Y----KRAKYiGRVFQ--DPMmgtaPSMTIEENLALAYrrgkrrgLRRGLTKKRRELFRELLATlGLGLENRLDTKVGLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 145 SGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGH-TVIMVTHDPGIAAN-ANRIIEIRDGEIIS 222
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDyGNRLIMMHEGRIIL 229
|
.
gi 2559317375 223 D 223
Cdd:COG1101 230 D 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-222 |
9.72e-32 |
|
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: 123.10 E-value: 9.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINryFGSGENRvHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalr 83
Cdd:cd03254 3 IEFENVN--FSYDEKK-PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSlTARDNVALpavymgmgGKERS-----------ARADKLLQDL--GLASKEGNKPGELSGGQQQ 150
Cdd:cd03254 76 RSMIGVVLQDTFLFSG-TIMENIRL--------GRPNAtdeevieaakeAGAHDFIMKLpnGYDTVLGENGGNLSQGERQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 151 RVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKaGHTVIMVTHDPGIAANANRIIEIRDGEIIS 222
Cdd:cd03254 147 LLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-225 |
2.22e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 123.79 E-value: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSlIECKNINRYFGSGENRVHI-LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIE-TAKMQPDE 78
Cdd:PRK13641 1 MS-IKFENVDYIYSPGTPMEKKgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHiTPETGNKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 79 LAALRReRFGFIFQ-RYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNK-PGELSGGQQQRVSIAR 156
Cdd:PRK13641 80 LKKLRK-KVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKsPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 157 ALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRDGEIISDTS 225
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNmDDVAEYADDVLVLEHGKLIKHAS 228
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-221 |
2.47e-31 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 122.40 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGsgENrvHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGsYRIDG--------IETAKM 74
Cdd:TIGR00972 1 AIEIENLNLFYG--EK--EALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPG-VRIEGkvlfdgqdIYDKKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 75 QPDELaalrRERFGFIFQRYNLLSsLTARDNVAL-PAVYMGMGGKERSARADKLLQDLGLASKEGNK----PGELSGGQQ 149
Cdd:TIGR00972 76 DVVEL----RRRVGMVFQKPNPFP-MSIYDNIAYgPRLHGIKDKKELDEIVEESLKKAALWDEVKDRlhdsALGLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 150 QRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLhKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:TIGR00972 151 QRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQEL-KKKYTIVIVTHNMQQAARiSDRTAFFYDGELV 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-220 |
2.84e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 125.83 E-value: 2.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSGEnrvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDela 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 alrRERFGFIFQRYNLLSSLTARDNVA-------LPAVYMgmggKERSARADKLLQDLGLASKegnKPGELSGGQQQRVS 153
Cdd:PRK09452 85 ---NRHVNTVFQSYALFPHMTVFENVAfglrmqkTPAAEI----TPRVMEALRMVQLEEFAQR---KPHQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 154 IARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLH-KAGHTVIMVTHDPGIA-ANANRIIEIRDGEI 220
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEAlTMSDRIVVMRDGRI 223
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-227 |
4.07e-31 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 129.22 E-value: 4.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINryFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalr 83
Cdd:TIGR03375 464 IEFRNVS--FAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL---- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSlTARDNVALPAVYMGmggKERSARADKL--LQDL------GLASKEGNKPGELSGGQQQRVSIA 155
Cdd:TIGR03375 538 RRNIGYVPQDPRLFYG-TLRDNIALGAPYAD---DEEILRAAELagVTEFvrrhpdGLDMQIGERGRSLSGGQRQAVALA 613
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 156 RALMNGGEIIFADEPTGALDTASGKNVMEIIRRLhKAGHTVIMVTHDPGIAANANRIIEIRDGEIISDTSKN 227
Cdd:TIGR03375 614 RALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKD 684
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
22-203 |
1.13e-30 |
|
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: 118.81 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNIL-GCLDTAG-SGSYRIDGIetakmqPDELAALRReRFGFIFQRYNLLSS 99
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLGvSGEVLINGR------PLDKRSFRK-IIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 100 LTARDNVALPAvymgmggKERSaradkllqdlglaskegnkpgeLSGGQQQRVSIARALMNGGEIIFADEPTGALDTASG 179
Cdd:cd03213 97 LTVRETLMFAA-------KLRG----------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180
....*....|....*....|....
gi 2559317375 180 KNVMEIIRRLHKAGHTVIMVTHDP 203
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIHQP 171
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-217 |
1.41e-30 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 119.46 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGsgenRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCLDTAgSGSYRIDGIETAKMQPDELAal 82
Cdd:cd03224 1 LEVENLNAGYG----KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMGLLPPR-SGSIRFDGRDITGLPPHERA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 rRERFGFIFQRYNLLSSLTARDNVAlpavyMGMGGKERSARADKLLQDLG----LASKEGNKPGELSGGQQQRVSIARAL 158
Cdd:cd03224 74 -RAGIGYVPEGRRIFPELTVEENLL-----LGAYARRRAKRKARLERVYElfprLKERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 159 MNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHdpgiaaNANRIIEIRD 217
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQ------NARFALEIAD 200
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-221 |
1.61e-30 |
|
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: 118.86 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGenrvHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDelaalr 83
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSLTARDNVALPAVYMGMggkeRSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPG-IAANANRIIEIRDGEII 221
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSeIQKVADRIGIINKGKLI 205
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-213 |
1.74e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 118.11 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILgcldtAG-----SGSYRIDGietakmqpdelaalrRERFGFIFQRYNLL 97
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVL-----AGvlrptSGTVRRAG---------------GARVAYVPQRSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 98 SSL--TARDNVAL----PAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPT 171
Cdd:NF040873 68 DSLplTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2559317375 172 GALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRII 213
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-199 |
2.21e-30 |
|
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: 119.32 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGsgenRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGcLDTAGSGSYRIDGIETAKMQPDEL 79
Cdd:COG0410 1 MPMLEVENLHAGYG----GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISG-LLPPRSGSIRFDGEDITGLPPHRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 80 AAL--------RRerfgfIFqrynllSSLTARDNVALPAvYMGMGGKERSARADKLLqDL--GLASKEGNKPGELSGGQQ 149
Cdd:COG0410 76 ARLgigyvpegRR-----IF------PSLTVEENLLLGA-YARRDRAEVRADLERVY-ELfpRLKERRRQRAGTLSGGEQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2559317375 150 QRVSIARALMNGGEIIFADEPTgaldtaSG------KNVMEIIRRLHKAGHTVIMV 199
Cdd:COG0410 143 QMLAIGRALMSRPKLLLLDEPS------LGlaplivEEIFEIIRRLNREGVTILLV 192
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-221 |
2.22e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 120.90 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRI-DGIETAKMQPDELAALRReRFGFIFQ--RYNLLSS 99
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKLKPLRK-KVGIVFQfpEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 100 LTARDnVALPAVYMGMGGKERSARADKLLQDLGLASKEGNK-PGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTAS 178
Cdd:PRK13634 102 TVEKD-ICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2559317375 179 GKNVMEIIRRLHK-AGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:PRK13634 181 RKEMMEMFYKLHKeKGLTTVLVTHSMEDAARyADQIVVMHKGTVF 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-202 |
2.58e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 119.80 E-value: 2.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKmqPDElaalrrERfGFIFQRYNLLSSLT 101
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG--PGA------ER-GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKN 181
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|..
gi 2559317375 182 VMEIIRRL-HKAGHTVIMVTHD 202
Cdd:PRK11248 167 MQTLLLKLwQETGKQVLLITHD 188
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
23-225 |
3.98e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 119.35 E-value: 3.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGS-YRIDGIETAKMQPDELAA-LRRER--FGFIFQRYNLLS 98
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgSHIELLGRTVQREGRLARdIRKSRanTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 99 SLTARDNVALPAV-----------YMGMGGKERSARAdklLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFA 167
Cdd:PRK09984 100 RLSVLENVLIGALgstpfwrtcfsWFTREQKQRALQA---LTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 168 DEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIAAN-ANRIIEIRDGEIISDTS 225
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRyCERIVALRQGHVFYDGS 236
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-220 |
4.60e-30 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 117.65 E-value: 4.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 21 HILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdelaalRRERFGFIFQRYNLLSSL 100
Cdd:TIGR01277 12 HLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP------YQRPVSMLFQENNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 101 TARDNVAL---PAVYMGMGGKERSARAdklLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTA 177
Cdd:TIGR01277 86 TVRQNIGLglhPGLKLNAEQQEKVVDA---AQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2559317375 178 SGKNVMEIIRRL-HKAGHTVIMVTHDPG-IAANANRIIEIRDGEI 220
Cdd:TIGR01277 163 LREEMLALVKQLcSERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-221 |
6.29e-30 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 118.10 E-value: 6.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNInrYFGSGENRVhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalr 83
Cdd:cd03253 1 IEFENV--TFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQ---------RYNLLsslTARDNVALPAVYmgmggkeRSARADKLlQDLGLASKEG--NKPGE----LSGGQ 148
Cdd:cd03253 74 RRAIGVVPQdtvlfndtiGYNIR---YGRPDATDEEVI-------EAAKAAQI-HDKIMRFPDGydTIVGErglkLSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 149 QQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKaGHTVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVNADKIIVLKDGRIV 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
7.96e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.94 E-value: 7.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 2 SLIECKNInrYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaa 81
Cdd:PRK13632 6 VMIKVENV--SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 82 lrRERFGFIFQRY-NLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMN 160
Cdd:PRK13632 82 --RKKIGIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 161 GGEIIFADEPTGALDTASGKNVMEIIRRLHKAGH-TVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-203 |
9.34e-30 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 124.77 E-value: 9.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 18 NRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAG---SGSYRIDG--IETAKMqpdelaalrRERFGFIFQ 92
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGmpIDAKEM---------RAISAYVQQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 93 RYNLLSSLTARDNVALPA-VYMG--MGGKERSARADKLLQDLGLAS-------KEGNKPGeLSGGQQQRVSIARALMNGG 162
Cdd:TIGR00955 107 DDLFIPTLTVREHLMFQAhLRMPrrVTKKEKRERVDEVLQALGLRKcantrigVPGRVKG-LSGGERKRLAFASELLTDP 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2559317375 163 EIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDP 203
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQP 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-226 |
1.09e-29 |
|
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: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdeLAAL 82
Cdd:COG3845 5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSP--RDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RReRFGFIFQRYNLLSSLTARDNVAL---PAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALM 159
Cdd:COG3845 79 AL-GIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 160 NGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRDGEII-----SDTSK 226
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKlREVMAIADRVTVLRRGKVVgtvdtAETSE 230
|
|
| ADOP |
TIGR03434 |
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, ... |
373-641 |
5.26e-29 |
|
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, only in three species of Acidobacteria, namely Acidobacteria bacterium Ellin345, Acidobacterium capsulatum ATCC 51196, and Solibacter usitatus Ellin6076, where they form large paralogous families. Each protein contains two copies of a domain called the efflux ABC transporter permease protein (pfam02687). However, unlike other members of that family (including LolC, FtsX, and MacB), genes for these proteins are essentially never found fused or adjacent to ABC transporter ATP-binding protein (pfam00005) genes. We name this family ADOP, for Acidobacterial Duplicated Orphan Permease, to reflect the restricted lineage, internal duplication, lack of associated ATP-binding cassette proteins, and permease homology. The function is unknown.
Pssm-ID: 274576 [Multi-domain] Cd Length: 803 Bit Score: 123.01 E-value: 5.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 373 YFDVRGLKLESGRLF-DENDVKEDAQVVVIDqnvkDKLF-----ADSDPLGKTILFRKRPLTVIGVMKKD-ENAFGNSDV 445
Cdd:TIGR03434 119 FFPVLGVQPALGRLFtPEDDRPGAPPVVVLS----YALWqrrfgGDPAVVGRTIRLNGRPYTVVGVMPPGfTFPGRDPDV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 446 LMLWSPYTTVMHQITGEGHTNSITVKIKD-------NANIQVAEKGLTELLKARHGTEDFFMNNSDsiRQMVESTTGTMK 518
Cdd:TIGR03434 195 WVPLAMDPALAGSANRGSRWLRVIGRLKPgvtlaqaQAELDAIAARLAAAYPDTNAGRGLAVTPLR--ESLVGDVRPPLL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 519 LLISSIALIsLVVGGIGVMNIMLVSVTERTKEIGIRMAIGARRGNILQQFLIEAVLICVIGGLVGVGLSAAVSLVFNHFV 598
Cdd:TIGR03434 273 VLLGAVGLV-LLIACANVANLLLARAAARQREIAVRLALGAGRGRLVRQLLTESLLLALAGGALGLLLAYWGLRLLLALL 351
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2559317375 599 -TDFPMDISA---MSVIG-AVACSTGIGIAFGFMPANKAAKLNPIDAL 641
Cdd:TIGR03434 352 pASLPRLLEIsldGRVLLfALALSLLTGLLFGLAPALQATRSDLAEAL 399
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-221 |
5.63e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 115.95 E-value: 5.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGEnrvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAA-- 81
Cdd:COG4604 2 IEIKNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 82 --LRrerfgfifQRYNLLSSLTARDNVAL---PavY-MGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIA 155
Cdd:COG4604 78 aiLR--------QENHINSRLTVRELVAFgrfP--YsKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 156 RALMNGGEIIFADEPTGALDTASGKNVMEIIRRL-HKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDINFASCyADHIVAMKDGRVV 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-221 |
3.61e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 117.06 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALRRERFGFIFQRYNLLSSLTA 102
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 103 RDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNV 182
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2559317375 183 M-EIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:PRK10070 204 QdELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVV 244
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
23-221 |
3.92e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.37 E-value: 3.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAkmqpDELAALR--RERFGFIFQ--RYNLLS 98
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT----DKKVKLSdiRKKVGLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 99 SLTARDnVALPAVYMGMGGKERSARADKLLQDLGLaSKEGNK---PGELSGGQQQRVSIARALMNGGEIIFADEPTGALD 175
Cdd:PRK13637 99 ETIEKD-IAFGPINLGLSEEEIENRVKRAMNIVGL-DYEDYKdksPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2559317375 176 TASGKNVMEIIRRLHKA-GHTVIMVTHD-PGIAANANRIIEIRDGEII 221
Cdd:PRK13637 177 PKGRDEILNKIKELHKEyNMTIILVSHSmEDVAKLADRIIVMNKGKCE 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-220 |
4.52e-28 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 116.28 E-value: 4.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDEla 80
Cdd:PRK11000 1 MASVTLRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 alrRErFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMN 160
Cdd:PRK11000 75 ---RG-VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 161 GGEIIFADEPTGALDtASGKNVMEI-IRRLHKA-GHTVIMVTHDPGIAAN-ANRIIEIRDGEI 220
Cdd:PRK11000 151 EPSVFLLDEPLSNLD-AALRVQMRIeISRLHKRlGRTMIYVTHDQVEAMTlADKIVVLDAGRV 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-221 |
5.33e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 116.09 E-value: 5.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFgSGEnrvHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdelaal 82
Cdd:PRK11607 19 LLEIRNLTKSF-DGQ---HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RRERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGG 162
Cdd:PRK11607 89 YQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 163 EIIFADEPTGALDTA-SGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:PRK11607 169 KLLLLDEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFV 229
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-206 |
6.07e-28 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 110.98 E-value: 6.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 17 ENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAalRRERFGFIFQRY-N 95
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLE--RRQRVGLVFQDPdD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 96 LLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALD 175
Cdd:TIGR01166 80 QLFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|.
gi 2559317375 176 TASGKNVMEIIRRLHKAGHTVIMVTHDPGIA 206
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
7-204 |
8.14e-28 |
|
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: 111.59 E-value: 8.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 7 KNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAG---SGSYRIDGIEtakMQPDELaalr 83
Cdd:cd03234 7 WDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQP---RKPDQF---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSLTARDNVALPAVYMG---MGGKERSAR-ADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALM 159
Cdd:cd03234 80 QKCVAYVRQDDILLPGLTVRETLTYTAILRLprkSSDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2559317375 160 NGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPG 204
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPR 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-201 |
9.96e-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: 110.83 E-value: 9.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGsgenRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGietakmqpDELAALR 83
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--------KPLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTH 201
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTH 186
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-233 |
1.10e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.88 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 17 ENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGietAKMQPDELAALRReRFGFIFQRY-N 95
Cdd:PRK13642 17 ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLRR-KIGMVFQNPdN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 96 LLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALD 175
Cdd:PRK13642 93 QFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 176 TASGKNVMEIIRRLHKAGH-TVIMVTHDPGIAANANRIIEIRDGEIISDTSKNPEIPTS 233
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-201 |
1.17e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 112.92 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSG---ENRVhiLKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIE-TAKMQPDEL 79
Cdd:PRK13649 3 INLQNVSYTYQAGtpfEGRA--LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 80 AALRReRFGFIFQ-RYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNK-PGELSGGQQQRVSIARA 157
Cdd:PRK13649 81 KQIRK-KVGLVFQfPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2559317375 158 LMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTH 201
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-225 |
1.34e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.59 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKST---LMNILGCLDTAGSGSYRIDGIE-TAKMQPDelaalRRERFGFIFQRY-NL 96
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITlTAKTVWD-----IREKVGIVFQNPdNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 97 LSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDT 176
Cdd:PRK13640 97 FVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2559317375 177 ASGKNVMEIIRRLHKA-GHTVIMVTHDPGIAANANRIIEIRDGEIISDTS 225
Cdd:PRK13640 177 AGKEQILKLIRKLKKKnNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-225 |
1.91e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 112.57 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIE-TAKMQPDELAALRReRFGFIFQrynLLSSLT 101
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITiTHKTKDKYIRPVRK-RIGMVFQ---FPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNVALPAVY----MGMGGKERSARADKLLQDLGLASKEGNK-PGELSGGQQQRVSIARALMNGGEIIFADEPTGALDT 176
Cdd:PRK13646 99 FEDTVEREIIFgpknFKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 177 ASGKNVMEIIRRLH-KAGHTVIMVTHDPG-IAANANRIIEIRDGEIISDTS 225
Cdd:PRK13646 179 QSKRQVMRLLKSLQtDENKTIILVSHDMNeVARYADEVIVMKEGSIVSQTS 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-221 |
1.98e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 117.23 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNInrYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaal 82
Cdd:PRK11160 338 SLTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL--- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 rRERFGFIFQRYNLLSSlTARDNVALPAvymgmggkeRSARADKL---LQDLGLAS-KEGNKP-----GE----LSGGQQ 149
Cdd:PRK11160 413 -RQAISVVSQRVHLFSA-TLRDNLLLAA---------PNASDEALievLQQVGLEKlLEDDKGlnawlGEggrqLSGGEQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 150 QRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRlHKAGHTVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE-HAQNKTVLMITHRLTGLEQFDRICVMDNGQII 552
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-221 |
3.75e-27 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 113.27 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 25 DISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDG---IETAKMQpdELAALRReRFGFIFQRYNLLSSLT 101
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGI--FLPPHRR-RIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNVAlpavYmGM---GGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTAS 178
Cdd:COG4148 94 VRGNLL----Y-GRkraPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2559317375 179 GKNVMEIIRRLHKAGHT-VIMVTHDPG-IAANANRIIEIRDGEII 221
Cdd:COG4148 169 KAEILPYLERLRDELDIpILYVSHSLDeVARLADHVVLLEQGRVV 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-221 |
8.62e-27 |
|
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: 109.17 E-value: 8.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 20 VHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalrRERFGFIFQRYNLLSS 99
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----RSQIGLVSQEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 100 lTARDNVALpavymgmgGKE-----------RSARADKLLQDL--GLASKEGNKPGELSGGQQQRVSIARALMNGGEIIF 166
Cdd:cd03249 92 -TIAENIRY--------GKPdatdeeveeaaKKANIHDFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 167 ADEPTGALDTASGKNVMEIIRRLHKaGHTVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRAMK-GRTTIVIAHRLSTIRNADLIAVLQNGQVV 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-221 |
1.05e-26 |
|
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: 107.01 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINryFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCLDtAGSGSYRIDGIETAKMQpdelaAL 82
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQlLTGDLK-PQQGEITLDGVPVSDLE-----KA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RRERFGFIFQRYNLLSSlTARDNVALPavymgmggkersaradkllqdlglaskegnkpgeLSGGQQQRVSIARALMNGG 162
Cdd:cd03247 73 LSSLISVLNQRPYLFDT-TLRNNLGRR----------------------------------FSGGERQRLALARILLQDA 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 163 EIIFADEPTGALDTASGKNVMEIIRRLHKaGHTVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-222 |
1.14e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.39 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 6 CKNINRYFGSgenRVhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDG----------------- 68
Cdd:COG0488 1 LENLSKSFGG---RP-LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpqeppldddl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 69 --IETAKMQPDELAALRRE------RFGFIFQRYNLLSSLTARdnvalpavYMGMGGKERSARADKLLQDLGLASKEGNK 140
Cdd:COG0488 77 tvLDTVLDGDAELRALEAEleeleaKLAEPDEDLERLAELQEE--------FEALGGWEAEARAEEILSGLGFPEEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 141 P-GELSGGQQQRVSIARALMNGGEIIFADEPTGALDtasgknvMEIIR----RLHKAGHTVIMVTHDPG-IAANANRIIE 214
Cdd:COG0488 149 PvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEwleeFLKNYPGTVLVVSHDRYfLDRVATRILE 221
|
....*...
gi 2559317375 215 IRDGEIIS 222
Cdd:COG0488 222 LDRGKLTL 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-207 |
1.20e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 109.16 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGenrvHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCL-----DTAGSGSYRIDG--IETAKMQP 76
Cdd:PRK14267 5 IETVNLRVYYGSN----HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGrnIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 77 DELaalrRERFGFIFQRYNLLSSLTARDNVALPAVYMGM--GGKERSARADKLLQDLGL----ASKEGNKPGELSGGQQQ 150
Cdd:PRK14267 81 IEV----RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2559317375 151 RVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLhKAGHTVIMVTHDPGIAA 207
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAA 212
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-221 |
1.29e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 109.25 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSGenrvHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILG--CLDTAGSGSYRI-DG--IETAKMQPD 77
Cdd:PRK11701 6 LLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSarLAPDAGEVHYRMrDGqlRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 78 ELAALRRERFGFIFQ--RYNLLSSLTARDNVALPavYMGMG----GKERSARADkLLQDLGL-ASKEGNKPGELSGGQQQ 150
Cdd:PRK11701 82 ERRRLLRTEWGFVHQhpRDGLRMQVSAGGNIGER--LMAVGarhyGDIRATAGD-WLERVEIdAARIDDLPTTFSGGMQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 151 RVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRL-HKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLlAHRLLVMKQGRVV 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-220 |
1.59e-26 |
|
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: 111.36 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 25 DISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALRRERFGFIFQRYNLLSSLTARD 104
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 105 NValpaVYmGMG---GKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKN 181
Cdd:TIGR02142 95 NL----RY-GMKrarPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2559317375 182 VMEIIRRLHKA-GHTVIMVTHDPG-IAANANRIIEIRDGEI 220
Cdd:TIGR02142 170 ILPYLERLHAEfGIPILYVSHSLQeVLRLADRVVVLEDGRV 210
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-223 |
1.80e-26 |
|
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: 108.19 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 20 VHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAalrreRFGFIF-QRYNLLS 98
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-----RIGVVFgQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 99 SLTARDNVALPAVYMGMGGKERSARADKLLQDLGLAsKEGNKP-GELSGGQQQRVSIARALMNGGEIIFADEPTGALDTA 177
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLE-ELLDTPvRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2559317375 178 SGKNVMEIIRRLHKA-GHTVIMVTHDPG-IAANANRIIEIRDGEIISD 223
Cdd:cd03267 188 AQENIRNFLKEYNRErGTTVLLTSHYMKdIEALARRVLVIDKGRLLYD 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
9-175 |
2.31e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 110.44 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 9 INRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALRReRFG 88
Cdd:PRK11308 17 VKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQ-KIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 89 FIFQryNLLSSLTARDNV----ALP-AVYMGMGGKERSARADKLLQDLGLASKEGNK-PGELSGGQQQRVSIARALMNGG 162
Cdd:PRK11308 96 IVFQ--NPYGSLNPRKKVgqilEEPlLINTSLSAAERREKALAMMAKVGLRPEHYDRyPHMFSGGQRQRIAIARALMLDP 173
|
170
....*....|...
gi 2559317375 163 EIIFADEPTGALD 175
Cdd:PRK11308 174 DVVVADEPVSALD 186
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-202 |
3.22e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 109.04 E-value: 3.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLM-NILGCLDtAGSGSYRIDGietakmQPDELAAL 82
Cdd:COG4152 2 LELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIrIILGILA-PDSGEVLWDG------EPLDPEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RR------ERfGfifqrynLLSSLTARDNvalpAVYM----GMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRV 152
Cdd:COG4152 71 RRigylpeER-G-------LYPKMKVGEQ----LVYLarlkGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2559317375 153 SIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD 202
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQ 188
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-221 |
3.30e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 108.54 E-value: 3.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAkmQPDELAALRReRFGFIFQryNLLSSLTA 102
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG--DFSKLQGIRK-LVGIVFQ--NPETQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 103 R----------DNVALPAVymgmggkERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTG 172
Cdd:PRK13644 93 RtveedlafgpENLCLPPI-------EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2559317375 173 ALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-207 |
3.50e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 109.81 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKS-TLMNILGCLDTAG--SGSYRIDGIETAKMQPD 77
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 78 ELAALRRERFGFIFQryNLLSSLTARDNVA--LPAVYM---GMGGKERSARADKLLQdlglASK--EGNK-----PGELS 145
Cdd:PRK09473 90 ELNKLRAEQISMIFQ--DPMTSLNPYMRVGeqLMEVLMlhkGMSKAEAFEESVRMLD----AVKmpEARKrmkmyPHEFS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 146 GGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHT-VIMVTHDPGIAA 207
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVA 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-221 |
3.80e-26 |
|
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: 113.27 E-value: 3.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNIN-RYFGSGenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQpdeLAA 81
Cdd:TIGR02203 330 DVEFRNVTfRYPGRD---RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LAS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 82 LRRErFGFIFQRYNLLSSlTARDNVALPAVYMGMGGKERSARADKLLQD------LGLASKEGNKPGELSGGQQQRVSIA 155
Cdd:TIGR02203 404 LRRQ-VALVSQDVVLFND-TIANNIAYGRTEQADRAEIERALAAAYAQDfvdklpLGLDTPIGENGVLLSGGQRQRLAIA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2559317375 156 RALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKaGHTVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-207 |
4.15e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 107.69 E-value: 4.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCL-----DTAGSGSYRIDGIETAKMQ 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 76 PDELaalrRERFGFIFQRYNLLSSLTARDNVALPAVY--MGMGGKERSARADKLLQDLGLASKEGNK----PGELSGGQQ 149
Cdd:PRK14247 77 VIEL----RRRVQMVFQIPNPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 150 QRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAgHTVIMVTHDPGIAA 207
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAA 209
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-222 |
6.80e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.47 E-value: 6.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSGenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGiETAKMQPDELAAL 82
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG-EPIKYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RReRFGFIFQRY-NLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNG 161
Cdd:PRK13639 77 RK-TVGIVFQNPdDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 162 GEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAA-NANRIIEIRDGEIIS 222
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIK 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-225 |
8.07e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 107.51 E-value: 8.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSGENRvHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGietAKMQPDELA 80
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEK-YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 ALRReRFGFIFQRY-NLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALM 159
Cdd:PRK13650 78 DIRH-KIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2559317375 160 NGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIAANANRIIEIRDGEIISDTS 225
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQVESTST 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-223 |
1.36e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 105.43 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 27 SLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDelaalrRERFGFIFQRYNLLSSLTARDNV 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS------RRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 107 ALpavymGM--GGKERSARADKL---LQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKN 181
Cdd:PRK10771 93 GL-----GLnpGLKLNAAQREKLhaiARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2559317375 182 VMEII------RRLhkaghTVIMVTHDPGIAAN-ANRIIEIRDGEIISD 223
Cdd:PRK10771 168 MLTLVsqvcqeRQL-----TLLMVSHSLEDAARiAPRSLVVADGRIAWD 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-220 |
1.89e-25 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 110.99 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 16 GENRVhILKDISLSIEKGDFVAIIGQSGSGKSTLMNIL-GCLDTAgSGSYRIDGIETAKMQPDELAalrrERFGFIFQRY 94
Cdd:COG4618 342 GSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVWPPT-AGSVRLDGADLSQWDREELG----RHIGYLPQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 95 NLLSSlTARDNVALpavyMGMGGKE------RSARADKLLQDL--GLASKEGNKPGELSGGQQQRVSIARALMNGGEIIF 166
Cdd:COG4618 416 ELFDG-TIAENIAR----FGDADPEkvvaaaKLAGVHEMILRLpdGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 167 ADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDGEI 220
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-224 |
4.14e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 105.15 E-value: 4.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNI-NRYFGSGENRVH----ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQ 75
Cdd:PRK10419 1 MTLLNVSGLsHHYAHGGLSGKHqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 76 PDELAALRRErFGFIFQryNLLSSLTARDNV----ALPAVYM-GMGGKERSARADKLLQDLGLASKEGNK-PGELSGGQQ 149
Cdd:PRK10419 81 RAQRKAFRRD-IQMVFQ--DSISAVNPRKTVreiiREPLRHLlSLDKAERLARASEMLRAVDLDDSVLDKrPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2559317375 150 QRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRL-HKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEIISDT 224
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQ 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-202 |
5.17e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 104.86 E-value: 5.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSgenrvHI-LKDISLSIEKGDFVAIIGQSGSGKSTlmnILGCLDTAGS--GSYRIDG--------IET 71
Cdd:PRK14243 10 VLRTENLNVYYGS-----FLaVKNVWLDIPKNQITAFIGPSGCGKST---ILRCFNRLNDliPGFRVEGkvtfhgknLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 72 AKMQPDELaalrRERFGFIFQRYNLLSSlTARDNVALPAVYMGMGGK-----ERSAR--------ADKLLQDlGLAskeg 138
Cdd:PRK14243 82 PDVDPVEV----RRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGDmdelvERSLRqaalwdevKDKLKQS-GLS---- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 139 nkpgeLSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLhKAGHTVIMVTHD 202
Cdd:PRK14243 152 -----LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHN 209
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-221 |
9.50e-25 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 102.96 E-value: 9.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNIN-RYfgsGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaal 82
Cdd:cd03244 3 IEFKNVSlRY---RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 rRERFGFIFQRYNLLSSlTARDNV-------------ALPAVYMgmggKERSARADKLLqDLGLASKEGNkpgeLSGGQQ 149
Cdd:cd03244 77 -RSRISIIPQDPVLFSG-TIRSNLdpfgeysdeelwqALERVGL----KEFVESLPGGL-DTVVEEGGEN----LSVGQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 150 QRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRlHKAGHTVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-222 |
1.02e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.43 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRI-DGIETAKMQPDELAALRReRFGFIFQ--RYNLLSS 99
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEIKPVRK-KVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 100 LTARDnVALPAVYMGMGGKERSARADKLLQDLGLASKEGNK-PGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTAS 178
Cdd:PRK13643 101 TVLKD-VAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKsPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2559317375 179 GKNVMEIIRRLHKAGHTVIMVTH-DPGIAANANRIIEIRDGEIIS 222
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIIS 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-221 |
1.04e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.78 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCLdtAGSGSYRIDGIETAKMQPDELaalrRERFGFIFQRYNLLSSl 100
Cdd:PRK11174 365 LAGPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIELRELDPESW----RKHLSWVGQNPQLPHG- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 101 TARDNVALPAVYMGmggkerSARADKLLQD-----------LGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADE 169
Cdd:PRK11174 438 TLRDNVLLGNPDAS------DEQLQQALENawvseflpllpQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 170 PTGALDTASGKNVMEIIRRLHkAGHTVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-237 |
1.76e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 107.56 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAAL 82
Cdd:PRK09700 5 YISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RrerFGFIFQRYNLLSSLTARDNValpavYMG-------MG-----GKERSARADKLLQDLGLASKEGNKPGELSGGQQQ 150
Cdd:PRK09700 81 G---IGIIYQELSVIDELTVLENL-----YIGrhltkkvCGvniidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 151 RVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRDGE-----IISDT 224
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDGSsvcsgMVSDV 232
|
250
....*....|...
gi 2559317375 225 SkNPEIPTSNVGR 237
Cdd:PRK09700 233 S-NDDIVRLMVGR 244
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-221 |
2.34e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 104.80 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 2 SLIECKNINRYFGSgeNRVhiLKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKmqpdelAA 81
Cdd:PRK11432 5 NFVVLKNITKRFGS--NTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 82 LRRERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNG 161
Cdd:PRK11432 75 IQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 162 GEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIA-ANANRIIEIRDGEII 221
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAfAVSDTVIVMNKGKIM 216
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-221 |
4.07e-24 |
|
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: 101.83 E-value: 4.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSGENrvhiLKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDG-----IETAKMQPD 77
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKG----CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaeLELYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 78 ELAALRRERFGFIFQ--RYNLLSSLTARDNVA--LPAVYMGMGGKERsARADKLLQDLGL-ASKEGNKPGELSGGQQQRV 152
Cdd:TIGR02323 79 ERRRLMRTEWGFVHQnpRDGLRMRVSAGANIGerLMAIGARHYGNIR-ATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 153 SIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRL-HKAGHTVIMVTHDPGIAA-NANRIIEIRDGEII 221
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLvRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVV 228
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
10-220 |
5.36e-24 |
|
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: 106.28 E-value: 5.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 10 NRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAalrrERFGF 89
Cdd:TIGR01842 321 NVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG----KHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 90 IFQRYNLLSSLTA------RDNVALPAVYMGmggkERSARADKLLQDL--GLASKEGNKPGELSGGQQQRVSIARALMNG 161
Cdd:TIGR01842 397 LPQDVELFPGTVAeniarfGENADPEKIIEA----AKLAGVHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGD 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 162 GEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDGEI 220
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-225 |
1.01e-23 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 100.31 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGsgenRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDelaalR 83
Cdd:cd03218 1 LRAENLSKRYG----KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH-----K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIF--QRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNG 161
Cdd:cd03218 72 RARLGIGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 162 GEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHdpgiaaNANRIIEIRD-GEIISDTS 225
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH------NVRETLSITDrAYIIYEGK 210
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-226 |
1.01e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 102.24 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 17 ENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALR------------R 84
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkelR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 85 ERFGFIFQ--RYNLLSSLTARDnVALPAVYMGMGGKERSARADKLLQDLGLASK--EGNkPGELSGGQQQRVSIARALMN 160
Cdd:PRK13631 116 RRVSMVFQfpEYQLFKDTIEKD-IMFGPVALGVKKSEAKKLAKFYLNKMGLDDSylERS-PFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2559317375 161 GGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHdpgiaaNANRIIEIRDGEIISDTSK 226
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITH------TMEHVLEVADEVIVMDKGK 253
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
7-223 |
1.74e-23 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 99.14 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 7 KNINRYFGSGENR-VHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMqpdELAAlrre 85
Cdd:cd03220 21 KKLGILGRKGEVGeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL---GLGG---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 86 rfGFifqrynlLSSLTARDNVALPAVYMGMGGKERSARADKLLQ--DLGlasKEGNKP-GELSGGQQQRVSIARALMNGG 162
Cdd:cd03220 94 --GF-------NPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEfsELG---DFIDLPvKTYSSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 163 EIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPG-IAANANRIIEIRDGEIISD 223
Cdd:cd03220 162 DILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSsIKRLCDRALVLEKGKIRFD 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-241 |
2.21e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 99.74 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 8 NINRYFGSGENRVhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGiETAKMQPD--ELAALR-R 84
Cdd:PRK14246 12 NISRLYLYINDKA-ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG-KVLYFGKDifQIDAIKlR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 85 ERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSAR-ADKLLQDLGLASK---EGNKPG-ELSGGQQQRVSIARALM 159
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGLWKEvydRLNSPAsQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 160 NGGEIIFADEPTGALDTASGKNVMEIIRRLHKAgHTVIMVTHDPGIAAN-ANRIIEIRDGEIISDTSKNpEIPTSNVGRI 238
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSN-EIFTSPKNEL 247
|
...
gi 2559317375 239 REK 241
Cdd:PRK14246 248 TEK 250
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-237 |
2.47e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 103.86 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGS--GSYRIDGietakmQPDELA 80
Cdd:PRK13549 5 LLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEG------EELQAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 ALR-RERFG--FIFQRYNLLSSLTARDNVAL------------PAVYmgmggkersARADKLLQDLGLASKEGNKPGELS 145
Cdd:PRK13549 75 NIRdTERAGiaIIHQELALVKELSVLENIFLgneitpggimdyDAMY---------LRAQKLLAQLKLDINPATPVGNLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 146 GGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPG-IAANANRIIEIRDGEIISDT 224
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNeVKAISDTICVIRDGRHIGTR 225
|
250
....*....|....*..
gi 2559317375 225 SKN----PEIPTSNVGR 237
Cdd:PRK13549 226 PAAgmteDDIITMMVGR 242
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-220 |
4.29e-23 |
|
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: 96.73 E-value: 4.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalRRERFGFI---FQRYNLLSS 99
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA---IRAGIAYVpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 100 LTARDNVALPAVymgmggkersaradkllqdlglaskegnkpgeLSGGQQQRVSIARALMNGGEIIFADEPTGALDTASG 179
Cdd:cd03215 93 LSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2559317375 180 KNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRDGEI 220
Cdd:cd03215 141 AEIYRLIRELADAGKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
22-203 |
4.30e-23 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 103.59 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTL-MNILGCLDTAGsGSYRIDGIETAKMQPDELAAlrreRFGFIFQRYNLLSSl 100
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLlATLAGLLDPLQ-GEVTLDGVPVSSLDQDEVRR----RVSVCAQDAHLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 101 TARDNVALP---AVYMGMGGKERSARADKLLQDL--GLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALD 175
Cdd:TIGR02868 424 TVRENLRLArpdATDEELWAALERVGLADWLRALpdGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180 190
....*....|....*....|....*....|
gi 2559317375 176 TASGKnvmEIIRRLHKA--GHTVIMVTHDP 203
Cdd:TIGR02868 504 AETAD---ELLEDLLAAlsGRTVVLITHHL 530
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-221 |
5.64e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 98.76 E-value: 5.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGS-----GENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQ 75
Cdd:COG4167 2 SALLEVRNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 76 PDELAALRRerfgFIFQRYNllSSLTARDNValpavymG------------MGGKERSARADKLLQDLGLASKEGN-KPG 142
Cdd:COG4167 82 YKYRCKHIR----MIFQDPN--TSLNPRLNI-------GqileeplrlntdLTAEEREERIFATLRLVGLLPEHANfYPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 143 ELSGGQQQRVSIARALMNGGEIIFADEPTGALDtASGK----NVM-EIIRRLhkaGHTVIMVTHDPGIAAN-ANRIIEIR 216
Cdd:COG4167 149 MLSSGQKQRVALARALILQPKIIIADEALAALD-MSVRsqiiNLMlELQEKL---GISYIYVSQHLGIVKHiSDKVLVMH 224
|
....*
gi 2559317375 217 DGEII 221
Cdd:COG4167 225 QGEVV 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-221 |
6.35e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 103.17 E-value: 6.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGENRVhiLKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIEtakMQPDELAALR 83
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPA--LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 rERFGFIFQRYNLLSSlTARDNVALPAvymgmGGK------ERSARA-------DKLlqDLGLASKEGNKPGELSGGQQQ 150
Cdd:PRK11176 417 -NQVALVSQNVHLFND-TIANNIAYAR-----TEQysreqiEEAARMayamdfiNKM--DNGLDTVIGENGVLLSGGQRQ 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 151 RVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKaGHTVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTIEKADEILVVEDGEIV 557
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
9.41e-23 |
|
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: 102.19 E-value: 9.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGEnrvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLD----TAGSGSYRIDGIET-------- 71
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyepTSGRIIYHVALCEKcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 72 ----------AKMQPDEL----------AALRReRFGFIFQR-YNLLSSLTARDNV--ALPAVymGMGGKERSARADKLL 128
Cdd:TIGR03269 77 kvgepcpvcgGTLEPEEVdfwnlsdklrRRIRK-RIAIMLQRtFALYGDDTVLDNVleALEEI--GYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 129 QDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIAA 207
Cdd:TIGR03269 154 EMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEVIE 233
|
250
....*....|....*
gi 2559317375 208 N-ANRIIEIRDGEII 221
Cdd:TIGR03269 234 DlSDKAIWLENGEIK 248
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-213 |
1.20e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.71 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalrRERFGFIFQRYNLLSSlT 101
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY----RQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNVALPAVYMGMGGKERSARADklLQDLGLASKEGNKP-GELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGK 180
Cdd:PRK10247 97 VYDNLIFPWQIRNQQPDPAIFLDD--LERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180 190
....*....|....*....|....*....|....
gi 2559317375 181 NVMEIIRRLHK-AGHTVIMVTHDPGIAANANRII 213
Cdd:PRK10247 175 NVNEIIHRYVReQNIAVLWVTHDKDEINHADKVI 208
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-219 |
3.21e-22 |
|
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: 94.84 E-value: 3.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCLdTAGSGSYRIDGietakmqpdelaalrreRFGFIFQRYNLLSSl 100
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPG-----------------SIAYVSQEPWIQNG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 101 TARDNVALPAVYmgmgGKERSARADK---LLQDL-----GLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTG 172
Cdd:cd03250 81 TIRENILFGKPF----DEERYEKVIKacaLEPDLeilpdGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2559317375 173 ALDTASGKNVME-IIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDGE 219
Cdd:cd03250 157 AVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-221 |
3.89e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.52 E-value: 3.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILgcldtAG-----SGSYRIdGiETAKmqpd 77
Cdd:COG0488 315 VLELEGLSKSYGD----KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL-----AGelepdSGTVKL-G-ETVK---- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 78 elaalrrerFGFIFQRYNLL-SSLTARDNVAlpavYMGMGGKERSARAdkLLQDLGLASKEGNKP-GELSGGQQQRVSIA 155
Cdd:COG0488 380 ---------IGYFDQHQEELdPDKTVLDELR----DGAPGGTEQEVRG--YLGRFLFSGDDAFKPvGVLSGGEKARLALA 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 156 RALMNGGEIIFADEPTGALDTASgKNVMEiirrlhKA-----GhTVIMVTHDPG-IAANANRIIEIRDGEII 221
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIET-LEALE------EAlddfpG-TVLLVSHDRYfLDRVATRILEFEDGGVR 508
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-218 |
4.08e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.65 E-value: 4.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGsyRIDgietakmQPDELAALrrerfgFIFQR-YNLLSSL 100
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG--RIA-------RPAGARVL------FLPQRpYLPLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 101 taRDNVALPAvymgmGGKERS-ARADKLLQDLGLA------SKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGA 173
Cdd:COG4178 443 --REALLYPA-----TAEAFSdAELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2559317375 174 LDTASGKNVMEIIR-RLHKAghTVIMVTHDPGIAANANRIIEIRDG 218
Cdd:COG4178 516 LDEENEAALYQLLReELPGT--TVISVGHRSTLAAFHDRVLELTGD 559
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
9-223 |
4.50e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.53 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 9 INRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAkmqPDELAAlrrerfG 88
Cdd:COG1134 28 LLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSA---LLELGA------G 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 89 FIfqrynllSSLTARDNVALPAVYMGMGGKERSARADKLLQ--DLGlasKEGNKP-GELSGGQQQRVSIARALMNGGEII 165
Cdd:COG1134 99 FH-------PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEfaELG---DFIDQPvKTYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 166 FADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPG-IAANANRIIEIRDGEIISD 223
Cdd:COG1134 169 LVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGaVRRLCDRAIWLEKGRLVMD 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-227 |
5.37e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.47 E-value: 5.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 20 VHILKDISLSIEKGDFVAIIGQSGSGKSTLMNIL-GCLdTAGSGSYRIDGIETAKmqpdELAALRReRFGFIF-QRYNLL 97
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL-VPTSGEVRVLGYVPFK----RRKEFAR-RIGVVFgQRSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 98 SSLTARDNVAL-PAVYmGMGGKERSARADKLLQDLGLASKEgNKP-GELSGGQQQRVSIARALMNGGEIIFADEPTGALD 175
Cdd:COG4586 109 WDLPAIDSFRLlKAIY-RIPDAEYKKRLDELVELLDLGELL-DTPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 176 TASGKNVMEIIRRLHKA-GHTVIMVTHDPG-IAANANRIIEIRDGEIISDTSKN 227
Cdd:COG4586 187 VVSKEAIREFLKEYNRErGTTILLTSHDMDdIEALCDRVIVIDHGRIIYDGSLE 240
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-225 |
6.74e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 96.23 E-value: 6.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCL---DTAGS--GSYRID-GIETAKmqpdELAALRRErFGFIFQ--RY 94
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisETGQTivGDYAIPaNLKKIK----EVKRLRKE-IGLVFQfpEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 95 NLLSSLTARDnVALPAVYMGMGGKERSARADKLLQDLGLASKEGNK-PGELSGGQQQRVSIARALMNGGEIIFADEPTGA 173
Cdd:PRK13645 102 QLFQETIEKD-IAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 174 LDTASGKNVMEIIRRLHKA-GHTVIMVTHD-PGIAANANRIIEIRDGEIISDTS 225
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEyKKRIIMVTHNmDQVLRIADEVIVMHEGKVISIGS 234
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-230 |
8.08e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 96.73 E-value: 8.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKS-TLMNILGCLDTAG---SGSYRIDGIETAKMQP 76
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGrvmAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 77 DELAALRRERFGFIFQryNLLSSLTARDNVA---LPAVYMGMGG--KERSARADKLLQDLGL---ASKEGNKPGELSGGQ 148
Cdd:PRK11022 81 KERRNLVGAEVAMIFQ--DPMTSLNPCYTVGfqiMEAIKVHQGGnkKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 149 QQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLH-KAGHTVIMVTHDPGIAAN-ANRIIEIRDGEIIsDTSK 226
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEaAHKIIVMYAGQVV-ETGK 237
|
....
gi 2559317375 227 NPEI 230
Cdd:PRK11022 238 AHDI 241
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-202 |
1.16e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.70 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 10 NRYFGSGENRvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAalrrERFGF 89
Cdd:PRK11231 7 NLTVGYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 90 IFQRYNLLSSLTARDNVAL---PAV-YMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEII 165
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYgrsPWLsLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 2559317375 166 FADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD 202
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD 197
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
28-223 |
1.36e-21 |
|
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: 93.76 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 28 LSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALRRERFGFIFQ---RYNLLSSLTARd 104
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQRHEFAWDFPisvAHTVMSGRTGH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 105 nvalpavymgMGGKERSARAD-----KLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASG 179
Cdd:TIGR03771 80 ----------IGWLRRPCVADfaavrDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2559317375 180 KNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIeIRDGEIISD 223
Cdd:TIGR03771 150 ELLTELFIELAGAGTAILMTTHDlAQAMATCDRVV-LLNGRVIAD 193
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-201 |
1.37e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 95.64 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGEnrvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGietakmQP-DELAAL 82
Cdd:PRK13537 8 IDFRNVEKRYGDKL----VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG------EPvPSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RRERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGG 162
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 2559317375 163 EIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTH 201
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-201 |
1.87e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.05 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGsgeNRVhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETakmqPDElAALR 83
Cdd:PRK13536 42 IDLAGVSKSYG---DKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PAR-ARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGE 163
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190
....*....|....*....|....*....|....*...
gi 2559317375 164 IIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTH 201
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-237 |
2.02e-21 |
|
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: 97.97 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDgIETAKMQPDELAAL 82
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIY-WSGSPLKASNIRDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RRERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGK----ERSARADKLLQDLGLASKEGNKP-GELSGGQQQRVSIARA 157
Cdd:TIGR02633 76 ERAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRmaynAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 158 LMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRDGEIISDTS----KNPEIPT 232
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKlNEVKAVCDTICVIRDGQHVATKDmstmSEDDIIT 235
|
....*
gi 2559317375 233 SNVGR 237
Cdd:TIGR02633 236 MMVGR 240
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-220 |
2.55e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.05 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 2 SLIECKNINRYFGSGEnrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIdgiETAKMQPDELAA 81
Cdd:PRK13648 6 SIIVFKNVSFQYQSDA--SFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY---NNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 82 LRrERFGFIFQR-YNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMN 160
Cdd:PRK13648 81 LR-KHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 161 GGEIIFADEPTGALDTASGKNVMEIIRRLHKAGH-TVIMVTHDPGIAANANRIIEIRDGEI 220
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-222 |
3.52e-21 |
|
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: 92.59 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 5 ECKNINRYFGsgenRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAalrR 84
Cdd:TIGR03410 2 EVSNLNVYYG----QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 85 ERFGFIFQRYNLLSSLTARDNVAlpavyMGMGG-KERSARADKLLQDLGLASKE--GNKPGELSGGQQQRVSIARALMNG 161
Cdd:TIGR03410 75 AGIAYVPQGREIFPRLTVEENLL-----TGLAAlPRRSRKIPDEIYELFPVLKEmlGRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 162 GEIIFADEPTGALDTASGKNVMEIIRRLHK-AGHTVIMVTHDPGIA-ANANRIIEIRDGEIIS 222
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAeGGMAILLVEQYLDFArELADRYYVMERGRVVA 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-201 |
4.21e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.90 E-value: 4.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 20 VHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETA-KMQPDELAAlrreRFGFIFQRYNLLS 98
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAA----GVAIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 99 SLTARDNV---ALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALD 175
Cdd:PRK11288 93 EMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180
....*....|....*....|....*.
gi 2559317375 176 TASGKNVMEIIRRLHKAGHTVIMVTH 201
Cdd:PRK11288 173 AREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-219 |
7.82e-21 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 89.04 E-value: 7.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGEnrvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDgietakmqpdelaalR 83
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------S 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQrynllssltardnvalpavymgmggkersaradkllqdlglaskegnkpgeLSGGQQQRVSIARALMNGGE 163
Cdd:cd03221 62 TVKIGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2559317375 164 IIFADEPTGALDTASgknVMEIIRRLHKAGHTVIMVTHDPG-IAANANRIIEIRDGE 219
Cdd:cd03221 91 LLLLDEPTNHLDLES---IEALEEALKEYPGTVILVSHDRYfLDQVATKIIELEDGK 144
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-220 |
9.06e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.27 E-value: 9.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdelaaL 82
Cdd:PRK15439 11 LLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP-----A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RRERFG--FIFQRYNLLSSLTARDNVALpavymGMGGKERS-ARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALM 159
Cdd:PRK15439 82 KAHQLGiyLVPQEPLLFPNLSVKENILF-----GLPKRQASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 160 NGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRDGEI 220
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKlPEIRQLADRISVMRDGTI 218
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-223 |
1.37e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 92.20 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAG--------SGSYRIDGIETAKMQPDELAALR-----RERFG 88
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRavlpqAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 89 FIFqrynllsslTARDNVALPAVYMGMGGKERSAR----ADKLLQDLGLASKEGNKPGELSGGQQQRVSIARAL------ 158
Cdd:PRK13547 96 FAF---------SAREIVLLGRYPHARRAGALTHRdgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 159 ---MNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHT-VIMVTHDPGIAA-NANRIIEIRDGEIISD 223
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAArHADRIAMLADGAIVAH 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-223 |
1.58e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.59 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAalrrERFGFIFQRYNLLSSLT 101
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNVA---LPAVYM-GMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTA 177
Cdd:PRK10253 98 VQELVArgrYPHQPLfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2559317375 178 SGKNVMEIIRRLHKA-GHTVIMVTHDPGIAAN-ANRIIEIRDGEIISD 223
Cdd:PRK10253 178 HQIDLLELLSELNREkGYTLAAVLHDLNQACRyASHLIALREGKIVAQ 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-221 |
3.28e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.39 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 21 HILKDISLSIEKGDFVAIIGQSGSGKST----LMNILgcldtAGSGSYRIDGIETAKMQPDELAALRReRFGFIFQRYNl 96
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRH-RIQVVFQDPN- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 97 lSSLTARDNVA------LPAVYMGMGGKERSARADKLLQDLGLASKEGNK-PGELSGGQQQRVSIARALMNGGEIIFADE 169
Cdd:PRK15134 373 -SSLNPRLNVLqiieegLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 170 PTGALDTASGKNVMEIIRRLHKAGH-TVIMVTHDPGIA-ANANRIIEIRDGEII 221
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVrALCHQVIVLRQGEVV 505
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-215 |
3.68e-20 |
|
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: 87.98 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIdgietakmqpdelaaLRRERFGFIFQR-YnlLSSL 100
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------------PEGEDLLFLPQRpY--LPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 101 TARDNVALPavymgmggkersaradklLQDlglaskegnkpgELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGK 180
Cdd:cd03223 79 TLREQLIYP------------------WDD------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180 190
....*....|....*....|....*....|....*
gi 2559317375 181 NVMEIirrLHKAGHTVIMVTHDPGIAANANRIIEI 215
Cdd:cd03223 129 RLYQL---LKELGITVISVGHRPSLWKFHDRVLDL 160
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-221 |
4.38e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.93 E-value: 4.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 18 NRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDElaALRReRFGFI---FQRY 94
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD--AIRA-GIAYVpedRKGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 95 NLLSSLTARDNVALPAV--YMGMG----GKERsARADKLLQDLGLASKEGNKP-GELSGGQQQRVSIARALMNGGEIIFA 167
Cdd:COG1129 340 GLVLDLSIRENITLASLdrLSRGGlldrRRER-ALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 168 DEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRDGEII 221
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSElPELLGLSDRILVMREGRIV 473
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-202 |
4.55e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 92.21 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRyfgSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdela 80
Cdd:PRK11650 1 MAGLKLQAVRK---SYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 alrRER-FGFIFQRYNLLSSLTARDNVAlpavY----MGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIA 155
Cdd:PRK11650 74 ---ADRdIAMVFQNYALYPHMSVRENMA----YglkiRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMG 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2559317375 156 RALMNGGEIIFADEPTGALDtASGKNVMEI-IRRLHKA-GHTVIMVTHD 202
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLD-AKLRVQMRLeIQRLHRRlKTTSLYVTHD 194
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-220 |
6.28e-20 |
|
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: 89.07 E-value: 6.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalrRERFGFIFQRyNLLSSLT 101
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL----HSKVSLVGQE-PVLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNVA--LPAVYMGM-GGKERSARADKLLQDL--GLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDT 176
Cdd:cd03248 104 LQDNIAygLQSCSFECvKEAAQKAHAHSFISELasGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2559317375 177 ASGKNVMEIIRRLHKAgHTVIMVTHDPGIAANANRIIEIRDGEI 220
Cdd:cd03248 184 ESEQQVQQALYDWPER-RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-221 |
9.31e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 89.37 E-value: 9.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKStlMNILGCLDTAGSGSYRIDGIETAKMQPDELAALRRERFGFIFQR----YNLL 97
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQNprsaFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 98 SSLTARDNVALPAVymgmGGKERSARADKLLQDLGLASKE---GNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGAL 174
Cdd:PRK10418 96 HTMHTHARETCLAL----GKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2559317375 175 DTASGKNVMEIIRRL-HKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:PRK10418 172 DVVAQARILDLLESIvQKRALGMLLVTHDMGVVARlADDVAVMSHGRIV 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-221 |
1.03e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.91 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSGenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDG--IETAKMQPDELa 80
Cdd:PRK13636 5 ILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 alrRERFGFIFQRY-NLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEgNKPGE-LSGGQQQRVSIARAL 158
Cdd:PRK13636 81 ---RESVGMVFQDPdNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLK-DKPTHcLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 159 MNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIAA-NANRIIEIRDGEII 221
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPlYCDNVFVMKEGRVI 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-221 |
1.29e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 92.72 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQpdeLAALRRErFGFIFQRYNLLSSlTA 102
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLRRN-IAVVFQDAGLFNR-SI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 103 RDNVALpavymgmgGK------------ERSARADKLL-QDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADE 169
Cdd:PRK13657 426 EDNIRV--------GRpdatdeemraaaERAQAHDFIErKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 170 PTGALDTASGKNVMEIIRRLHKaGHTVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-225 |
2.25e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 92.23 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 7 KNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKS-TLMNILGCLDTAGsGSYRIDG----------IETAKMQ 75
Cdd:PRK10261 16 ENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAG-GLVQCDKmllrrrsrqvIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 76 PDELAALRRERFGFIFQR--YNLLSSLTARDNVALPA-VYMGMGGKERSARADKLLQDLGLASKE---GNKPGELSGGQQ 149
Cdd:PRK10261 95 AAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIrLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 150 QRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHK-AGHTVIMVTHDPGIAAN-ANRIIEIRDGEIISDTS 225
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKeMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-193 |
3.39e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.01 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSgenRvHILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGcLDTAGSGSYRIDGIETAKMQPDel 79
Cdd:COG1137 1 MMTLEAENLVKSYGK---R-TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYmIVG-LVKPDSGRIFLDGEDITHLPMH-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 80 aalRRERFGF--------IFQRynllssLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQR 151
Cdd:COG1137 74 ---KRARLGIgylpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2559317375 152 VSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAG 193
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERG 186
|
|
| YbbP |
COG3127 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ... |
504-644 |
7.65e-19 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442361 [Multi-domain] Cd Length: 830 Bit Score: 91.02 E-value: 7.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 504 DSIRQMVESTTGTMKLLISSIALISLVVGGIGVMNIMLVSVTERTKEIGIRMAIGARRGNILQQFLIEAVLICVIGGLVG 583
Cdd:COG3127 690 DAILDQVRDILDQVSLAVEFLAGFALLAGLLVLAAALAASRDERTREAALLRTLGASRRQLRRALALEFALLGLLAGLLA 769
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 584 VGLSAAVSLVFNHFVTDFPMDISAMSVIGAVACSTGIGIAFGFMPANKAAKLNPIDALAQD 644
Cdd:COG3127 770 ALLAELAGWALARFVFDLPFSPPWWLWLAGLLGGALLVLLAGLLGARRVLRQPPLEVLREE 830
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-221 |
8.13e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.06 E-value: 8.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQP--DELA 80
Cdd:PRK10762 4 LLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPksSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 ALrrerfGFIFQRYNLLSSLTARDNVALPAVYMG-MGG---KERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIAR 156
Cdd:PRK10762 80 GI-----GIIHQELNLIPQLTIAENIFLGREFVNrFGRidwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 157 ALMNGGEIIFADEPTGAL---DTASGKNVmeiIRRLHKAGHTVIMVTHdpgiaananRIIEI----------RDGEII 221
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALtdtETESLFRV---IRELKSQGRGIVYISH---------RLKEIfeicddvtvfRDGQFI 220
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
9-218 |
8.78e-19 |
|
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: 85.46 E-value: 8.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 9 INRYFGSGENrVHILKDISLSIEKGDFVAIIGQSGSGKSTLM-NILGCLDTAgSGSYRIDGIETAKMQPDELAALRRERF 87
Cdd:cd03290 4 TNGYFSWGSG-LATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL-EGKVHWSNKNESEPSFEATRSRNRYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 88 GFIFQRYNLLSSlTARDNVALPAVYmgmgGKER--------SARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALM 159
Cdd:cd03290 82 AYAAQKPWLLNA-TVEENITFGSPF----NKQRykavtdacSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 160 NGGEIIFADEPTGALDTASGKNVME--IIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDG 218
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-240 |
9.64e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 86.74 E-value: 9.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNInrYFGSGeNRVhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELA 80
Cdd:PRK11831 5 ANLVDMRGV--SFTRG-NRC-IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 ALRReRFGFIFQRYNLLSSLTARDNVALPAvymgmggKERSARADKLLQD--------LGLASKEGNKPGELSGGQQQRV 152
Cdd:PRK11831 81 TVRK-RMSMLFQSGALFTDMNVFDNVAYPL-------REHTQLPAPLLHStvmmkleaVGLRGAAKLMPSELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 153 SIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHD-PGIAANANRIIEIRDGEIISDTSKnPEI 230
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDvPEVLSIADHAYIVADKKIVAHGSA-QAL 231
|
250
....*....|
gi 2559317375 231 PTSNVGRIRE 240
Cdd:PRK11831 232 QANPDPRVRQ 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-207 |
1.69e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.97 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELA 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGD----TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 alrrERFGFIFQRYNLLSSLTARDNVAL---P--AVYMGMGGKERSArADKLLQDLGLASKEGNKPGELSGGQQQRVSIA 155
Cdd:PRK09536 77 ----RRVASVPQDTSLSFEFDVRQVVEMgrtPhrSRFDTWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 156 RALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAA 207
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAA 203
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
22-222 |
2.31e-18 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 84.00 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMqpdELAALRReRFGFIFQRYNLLSSlT 101
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLRS-SLTIIPQDPTLFSG-T 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNVALPAVYmgmggkersarADKLLQDlGLASKEGNKpgELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKN 181
Cdd:cd03369 98 IRSNLDPFDEY-----------SDEEIYG-ALRVSEGGL--NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2559317375 182 VMEIIRRLHKaGHTVIMVTHDPGIAANANRIIEIRDGEIIS 222
Cdd:cd03369 164 IQKTIREEFT-NSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
7-206 |
2.36e-18 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 83.45 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 7 KNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAG--SGSYRIDGIETAKmqpdelaALRR 84
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK-------NFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 85 eRFGFIFQRYNLLSSLTARdnVALpavymgmggkERSAradkLLQDLGLAskegnkpgelsggQQQRVSIARALMNGGEI 164
Cdd:cd03232 80 -STGYVEQQDVHSPNLTVR--EAL----------RFSA----LLRGLSVE-------------QRKRLTIGVELAAKPSI 129
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2559317375 165 IFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIA 206
Cdd:cd03232 130 LFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSAS 171
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-202 |
2.54e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.89 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLdTAGSGSYRIDGIETAKMQPDELAALR-----RERFGFIFQRYNLL 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRaylsqQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 98 SsLTARDNVALPAVymgmggkerSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMN-------GGEIIFADEP 170
Cdd:COG4138 91 A-LHQPAGASSEAV---------EQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEP 160
|
170 180 190
....*....|....*....|....*....|..
gi 2559317375 171 TGALDTASGKNVMEIIRRLHKAGHTVIMVTHD 202
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCQQGITVVMSSHD 192
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-218 |
3.15e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.22 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKS-TLMNILGCLDTAG----SGSYRIDGIETAKMQ 75
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 76 PDELAALRRERFGFIFQR----YNLLSSLTARDNVALpAVYMGMGGKerSARADKL--LQDLGL---ASKEGNKPGELSG 146
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEpmvsLNPLHTLEKQLYEVL-SLHRGMRRE--AARGEILncLDRVGIrqaAKRLTDYPHQLSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 147 GQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPGIAAN-ANRIIEIRDG 218
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-221 |
3.24e-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: 88.72 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 13 FGSGENRVhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalrRERFGFIFQ 92
Cdd:COG5265 365 FGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL----RAAIGIVPQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 93 ---------RYNLLsslTARDNVALPAVymgmggkERSARADKLLqDLGLASKEG--NKPGE----LSGGQQQRVSIARA 157
Cdd:COG5265 440 dtvlfndtiAYNIA---YGRPDASEEEV-------EAAARAAQIH-DFIESLPDGydTRVGErglkLSGGEKQRVAIART 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 158 LMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKaGHTVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHRLSTIVDADEILVLEAGRIV 571
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-222 |
4.52e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.45 E-value: 4.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGietakmQPdeLAALRRERFG----FIFQRYNLL 97
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA------QP--LESWSSKAFArkvaYLPQQLPAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 98 SSLTARDNVALpAVY-----MGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTG 172
Cdd:PRK10575 98 EGMTVRELVAI-GRYpwhgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 173 ALDTASGKNVMEIIRRL-HKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEIIS 222
Cdd:PRK10575 177 ALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARyCDYLVALRGGEMIA 228
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-217 |
5.36e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.77 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGsgenRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdelA 80
Cdd:PRK11614 3 KVMLSFDKVSAHYG----KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT---A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 ALRRERFGFIFQRYNLLSSLTARDNVAlpavymgMGG--------KERSARADKLLQDLglASKEGNKPGELSGGQQQRV 152
Cdd:PRK11614 76 KIMREAVAIVPEGRRVFSRMTVEENLA-------MGGffaerdqfQERIKWVYELFPRL--HERRIQRAGTMSGGEQQML 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 153 SIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHdpgiaaNANRIIEIRD 217
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQ------NANQALKLAD 205
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-221 |
5.93e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.58 E-value: 5.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILgcldtAGSGSYRI-------DGIETAKMQPDELAalrRERFGFIFQR- 93
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL-----MGHPKYEVtsgsillDGEDILELSPDERA---RAGIFLAFQYp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 94 --------YNLL-SSLTARDNVALPAvymgmggKERSARADKLLQDLGLASK-------EGnkpgeLSGGQQQRVSIARA 157
Cdd:COG0396 87 veipgvsvSNFLrTALNARRGEELSA-------REFLKLLKEKMKELGLDEDfldryvnEG-----FSGGEKKRNEILQM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2559317375 158 LMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGI--AANANRIIEIRDGEII 221
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRIldYIKPDFVHVLVDGRIV 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-220 |
7.99e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.47 E-value: 7.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 20 VHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMqpdELAALRRERFgfIFQRYNLLSS 99
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY---DHHYLHRQVA--LVGQEPVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 100 LTARDNVALPAVYMGMGGKERSAR---ADKLLQDL--GLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGAL 174
Cdd:TIGR00958 569 GSVRENIAYGLTDTPDEEIMAAAKaanAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2559317375 175 DTASGKNVMEIIRRlhkAGHTVIMVTHDPGIAANANRIIEIRDGEI 220
Cdd:TIGR00958 649 DAECEQLLQESRSR---ASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-221 |
1.00e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.29 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSGEnrvhILKDISLSIEKGDFVAIIGQSGSGKSTLM---NILGCLD----TAGSGSYRIDGIETAKMQ 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLNpevtITGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 76 PDELaalrRERFGFIFQRYNLLSsLTARDNVALPAVYMGMGGK-------ERSARADKL-------LQDLGLAskegnkp 141
Cdd:PRK14239 81 TVDL----RKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKqvldeavEKSLKGASIwdevkdrLHDSALG------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 142 geLSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLhKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEI 220
Cdd:PRK14239 149 --LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRiSDRTGFFLDGDL 225
|
.
gi 2559317375 221 I 221
Cdd:PRK14239 226 I 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-203 |
1.54e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGietakmQPDELAALRrERFGFIFQRYNLLSSLT 101
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG------GDIDDPDVA-EACHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNVALPAVYMGmgGKERSARAdkLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKN 181
Cdd:PRK13539 90 VAENLEFWAAFLG--GEELDIAA--ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|..
gi 2559317375 182 VMEIIRRLHKAGHTVIMVTHDP 203
Cdd:PRK13539 166 FAELIRAHLAQGGIVIAATHIP 187
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
3.17e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.16 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNI-NRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDEL 79
Cdd:PRK13652 1 MHLIETRDLcYSYSGS----KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 80 aalrRERFGFIFQRYN-LLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARAL 158
Cdd:PRK13652 77 ----RKFVGLVFQNPDdQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2559317375 159 MNGGEIIFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHDPG-IAANANRIIEIRDGEIIS 222
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDlVPEMADYIYVMDKGRIVA 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-203 |
3.54e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 80.10 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdelaaLRRERFGFIFQRYNLLSSLT 101
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-----EPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNVALpavYMGMGGKERSArADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKN 181
Cdd:TIGR01189 90 ALENLHF---WAAIHGGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|..
gi 2559317375 182 VMEIIRRLHKAGHTVIMVTHDP 203
Cdd:TIGR01189 166 LAGLLRAHLARGGIVLLTTHQD 187
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-212 |
4.86e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 82.65 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCLD-----TAgsGSYRIDGIETAKM 74
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKdnwhvTA--DRFRWNGIDLLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 75 QPDELAALRRERFGFIFQryNLLSSLTARDNV------ALPA-VYMGM---GGKERSARADKLLQDLGLasKEGNK---- 140
Cdd:COG4170 79 SPRERRKIIGREIAMIFQ--EPSSCLDPSAKIgdqlieAIPSwTFKGKwwqRFKWRKKRAIELLHRVGI--KDHKDimns 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 141 -PGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIM-VTHDPG-IAANANRI 212
Cdd:COG4170 155 yPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILlISHDLEsISQWADTI 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-202 |
5.90e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.45 E-value: 5.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 24 KDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGcLDTAGSGSYRIDGIETAKMQPDELAALRRErFGFIFQryNLLSSLTA 102
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARaIIG-LVKATDGEVAWLGKDLLGMKDDEWRAVRSD-IQMIFQ--DPLASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 103 RDNVA------LPAVYMGMGGKERSARADKLLQDLGLASKEGNK-PGELSGGQQQRVSIARALMNGGEIIFADEPTGALD 175
Cdd:PRK15079 114 RMTIGeiiaepLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180
....*....|....*....|....*...
gi 2559317375 176 TASGKNVMEIIRRLHKA-GHTVIMVTHD 202
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREmGLSLIFIAHD 221
|
|
| FtsX |
pfam02687 |
FtsX-like permease family; This is a family of predicted permeases and hypothetical ... |
522-637 |
1.11e-16 |
|
FtsX-like permease family; This is a family of predicted permeases and hypothetical transmembrane proteins. Swiss:P57382 has been shown to transport lipids targeted to the outer membrane across the inner membrane. Both Swiss:P57382 and Swiss:O54500 have been shown to require ATP. This region contains three transmembrane helices.
Pssm-ID: 460652 [Multi-domain] Cd Length: 120 Bit Score: 76.52 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 522 SSIALISLVVGGIGVMNIMLVSVTERTKEIGIRMAIGARRGNILQQFLIEAVLICVIGGLVGVGLSAAVSLVFN----HF 597
Cdd:pfam02687 1 ILFSLLILLLAVLIILLLLSISISERRREIGILRALGASRKQIFKLLLLEALLIGLIGLVIGLLLGLLLAKLIAillySS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2559317375 598 VTDFPMDISAMSVIGAVACSTGIGIAFGFMPANKAAKLNP 637
Cdd:pfam02687 81 GISLPILVPPLSILIALLLALLIALLASLLPALRIRKINP 120
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-241 |
1.15e-16 |
|
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: 78.72 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILgcldtAGSGSYRI-------DGIETAKMQPDElaalrRERFGfIFqry 94
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI-----MGHPKYEVtegeilfKGEDITDLPPEE-----RARLG-IF--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 95 nllssLTARDNVALPAVYMGMggkersaradkLLQDLGlaskEGnkpgeLSGGQQQRVSIARALMNGGEIIFADEPTGAL 174
Cdd:cd03217 81 -----LAFQYPPEIPGVKNAD-----------FLRYVN----EG-----FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 175 DTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAA--NANRIIEIRDGEIIsdTSKNPEIptsnVGRIREK 241
Cdd:cd03217 136 DIDALRLVAEVINKLREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIV--KSGDKEL----ALEIEKK 198
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-224 |
1.33e-16 |
|
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: 83.31 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNIN-RYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIEtakMQPDELAAL 82
Cdd:COG4615 328 LELRGVTyRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 rRERFGFIFQRYNLLSSLtardnvalpavyMGMGGKERSARADKLLQDLGLASK---EGNK--PGELSGGQQQRVSIARA 157
Cdd:COG4615 405 -RQLFSAVFSDFHLFDRL------------LGLDGEADPARARELLERLELDHKvsvEDGRfsTTDLSQGQRKRLALLVA 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 158 LMNGGEIIFADE------PTgaldtasGKNV--MEIIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDGEIISDT 224
Cdd:COG4615 472 LLEDRPILVFDEwaadqdPE-------FRRVfyTELLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVELT 539
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-222 |
1.76e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.53 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGS--GSYRIDGietakmQPDELA 80
Cdd:NF040905 1 ILEMRGITKTFPG----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG------EVCRFK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 ALR-RERFGF--IFQRYNLLSSLTARDNVAL---PAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSI 154
Cdd:NF040905 71 DIRdSEALGIviIHQELALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 155 ARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPG-IAANANRIIEIRDGEIIS 222
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNeIRRVADSITVLRDGRTIE 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-202 |
2.10e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.98 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 20 VHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALRRErFGFIFQryNLLSS 99
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQ--DPYAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 100 LTARDNVAL----PAVYMGMG-GKERSARADKLLQDLGLASKEGNK-PGELSGGQQQRVSIARALMNGGEIIFADEPTGA 173
Cdd:PRK10261 414 LDPRQTVGDsimePLRVHGLLpGKAAAARVAWLLERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190
....*....|....*....|....*....|
gi 2559317375 174 LDTASGKNVMEIIRRLHKA-GHTVIMVTHD 202
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDfGIAYLFISHD 523
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-221 |
2.25e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 82.68 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 21 HILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSyridgietAKMQPDelaalrrERFGFIFQRYNLLSSL 100
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------ARPQPG-------IKVGYLPQEPQLDPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 101 TARDNVA------------LPAVYMGMGgkERSARADKL------LQDL-------GLASK-----------EGNKP-GE 143
Cdd:TIGR03719 84 TVRENVEegvaeikdaldrFNEISAKYA--EPDADFDKLaaeqaeLQEIidaadawDLDSQleiamdalrcpPWDADvTK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 144 LSGGQQQRVSIARALMNGGEIIFADEPTGALDTASgknVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEYPGTVVAVTHDRYFLDNvAGWILELDRGRGI 237
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-243 |
2.74e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 82.33 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalrRERFGFIFQRYNLLSSLta 102
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY----RKLFSAVFTDFHLFDQL-- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 103 rdnvalpavyMGMGGKE-RSARADKLLQDLGLASK---EGNKPG--ELSGGQQQRVSIARALMNGGEIIFADEptgaldT 176
Cdd:PRK10522 413 ----------LGPEGKPaNPALVEKWLERLKMAHKlelEDGRISnlKLSKGQKKRLALLLALAEERDILLLDE------W 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 177 ASGKNVM-------EIIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDGEIISDTsknpeiptsnvGRIREKAS 243
Cdd:PRK10522 477 AADQDPHfrrefyqVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELT-----------GEERDAAS 539
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-204 |
2.76e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.54 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKmqpdelaALRRERFGFIFQRYNLLSSLTA 102
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-------ALQKNLVAYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 103 R-DNVALPAVYMGMGGKERSARADKLLQDLGLASKE-----GNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDT 176
Cdd:PRK15056 96 LvEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDmvefrHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180
....*....|....*....|....*...
gi 2559317375 177 ASGKNVMEIIRRLHKAGHTVIMVTHDPG 204
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVSTHNLG 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-220 |
2.89e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 5 ECKNINRYfgsGENRVhilKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdeLAALRR 84
Cdd:PRK09700 267 EVRNVTSR---DRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 85 ErFGFIFQ--RYN-LLSSLTARDNVALP-----AVYMGMGG------KERSARADKLLQDLGLASKEGNKpGELSGGQQQ 150
Cdd:PRK09700 339 G-MAYITEsrRDNgFFPNFSIAQNMAISrslkdGGYKGAMGlfhevdEQRTAENQRELLALKCHSVNQNI-TELSGGNQQ 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 151 RVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRDGEI 220
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRL 487
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
22-202 |
3.66e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.40 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGiETAKMQPdeLAALRRERFGFIFQRYNLLSSLT 101
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD-EDISLLP--LHARARRGIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNV-ALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGK 180
Cdd:PRK10895 95 VYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170 180
....*....|....*....|..
gi 2559317375 181 NVMEIIRRLHKAGHTVIMVTHD 202
Cdd:PRK10895 175 DIKRIIEHLRDSGLGVLITDHN 196
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-230 |
7.19e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.00 E-value: 7.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 3 LIECKNINRYFGSGENRV-HILKDISLSIEKGDFVAIIGQSGSGKSTLMNIL-GCLD-TAGSGSYRI--DGIETAKMQPD 77
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIaGVLEpTSGEVNVRVgdEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 78 ELAalRRERF-GFIFQRYNL------LSSLTARDNVALPAVYMGMggkersaRADKLLQDLGLASKEGNK-----PGELS 145
Cdd:TIGR03269 359 GRG--RAKRYiGILHQEYDLyphrtvLDNLTEAIGLELPDELARM-------KAVITLKMVGFDEEKAEEildkyPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 146 GGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIrrlHKA----GHTVIMVTHDPGIAAN-ANRIIEIRDGEI 220
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSI---LKAreemEQTFIIVSHDMDFVLDvCDRAALMRDGKI 506
|
250
....*....|
gi 2559317375 221 IsDTSKNPEI 230
Cdd:TIGR03269 507 V-KIGDPEEI 515
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-201 |
1.08e-15 |
|
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: 81.60 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 26 ISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDG--IETakmqpdELAALRrERFGFIFQRYNLLSSLTAR 103
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdIET------NLDAVR-QSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 104 DNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVM 183
Cdd:TIGR01257 1022 EHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170
....*....|....*...
gi 2559317375 184 EIIRRlHKAGHTVIMVTH 201
Cdd:TIGR01257 1102 DLLLK-YRSGRTIIMSTH 1118
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-202 |
1.45e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.00 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGEnrvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAgSGSYRIDG-IETAKMQPDE---- 78
Cdd:PRK14258 8 IKVNNLSFYYDTQK----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrVEFFNQNIYErrvn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 79 LAALRRErFGFIFQRYNLLSsLTARDNVALPAVYMGMGGK-ERSARADKLLQDLGLASKEGNK----PGELSGGQQQRVS 153
Cdd:PRK14258 83 LNRLRRQ-VSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLWDEIKHKihksALDLSGGQQQRLC 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2559317375 154 IARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLH-KAGHTVIMVTHD 202
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHN 210
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
11-221 |
1.94e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 79.76 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 11 RYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalrRERFGFI 90
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 91 FQRYNLLSSLTARdNVALPAVYMGMGGKERSARADKLLQDL-----GLASKEGNKPGELSGGQQQRVSIARALMNGGEII 165
Cdd:PRK10789 395 SQTPFLFSDTVAN-NIALGRPDATQQEIEHVARLASVHDDIlrlpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 166 FADEPTGALDtasGKNVMEIIRRLHKAGH--TVIMVTHDPGIAANANRIIEIRDGEII 221
Cdd:PRK10789 474 ILDDALSAVD---GRTEHQILHNLRQWGEgrTVIISAHRLSALTEASEILVMQHGHIA 528
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-215 |
2.59e-15 |
|
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: 74.84 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKmQPDELAalrrERFGFIFQRYNLLSSLT 101
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF-QRDSIA----RGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNVALpavYMGMGGKERSARAdklLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKN 181
Cdd:cd03231 90 VLENLRF---WHADHSDEQVEEA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|....*
gi 2559317375 182 VMEIIRRLHKAGHTVIMVTHDP-GIAANANRIIEI 215
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHQDlGLSEAGARELDL 198
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-213 |
3.08e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.84 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 25 DISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMqpdelaalrRERFgfifqRYNLL------- 97
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ---------RDEY-----HQDLLylghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 98 --SSLTARDNVALpavYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALD 175
Cdd:PRK13538 85 ikTELTALENLRF---YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2559317375 176 TASgknVMEIIRRL--H-KAGHTVIMVTHDP-GIAANANRII 213
Cdd:PRK13538 162 KQG---VARLEALLaqHaEQGGMVILTTHQDlPVASDKVRKL 200
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-215 |
4.59e-15 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 74.99 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 19 RVHILKDISLSIEKGDFVAIIGQSGSGKSTLmnilgCLDT---AGSGSY----------RIDGIETAKMqpDELAALR-- 83
Cdd:cd03270 7 REHNLKNVDVDIPRNKLVVITGVSGSGKSSL-----AFDTiyaEGQRRYveslsayarqFLGQMDKPDV--DSIEGLSpa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 ------------RERFGFIFQRYNLLSSLTARdnvalpavymgMGGKERSaradKLLQDLGLA----SKEGNKpgeLSGG 147
Cdd:cd03270 80 iaidqkttsrnpRSTVGTVTEIYDYLRLLFAR-----------VGIRERL----GFLVDVGLGyltlSRSAPT---LSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 148 QQQRVSIARALMNG--GEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEI 215
Cdd:cd03270 142 EAQRIRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-223 |
4.80e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.90 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGsYRIDGietakmqpDELAALR-----------RERFGFI 90
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSG--------DVLLGGRsifnyrdvlefRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 91 FQRYNLLSsLTARDNV-ALPAVYMGMGGKERSARADKLLQDLGL----ASKEGNKPGELSGGQQQRVSIARALMNGGEII 165
Cdd:PRK14271 107 FQRPNPFP-MSIMDNVlAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 166 FADEPTGALDTASGKNVMEIIRRLHKAgHTVIMVTHDPGIAAN-ANRIIEIRDGEIISD 223
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARiSDRAALFFDGRLVEE 243
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
5-205 |
7.01e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.22 E-value: 7.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 5 ECKNINRYFGSGENRV--HILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCL-DTAGSGSYRIDGIEtakmqpdela 80
Cdd:COG2401 26 RVAIVLEAFGVELRVVerYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRlLAGALkGTPVAGCVDVPDNQ---------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 alrrerfgfIFQRYNLLSSLTARDNVALpavymgmggkersarADKLLQDLGLASKEG--NKPGELSGGQQQRVSIARAL 158
Cdd:COG2401 96 ---------FGREASLIDAIGRKGDFKD---------------AVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2559317375 159 MNGGEIIFADEPTGALDTASGKNVMEIIRRL-HKAGHTVIMVTHDPGI 205
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHHYDV 199
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-220 |
7.19e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 78.67 E-value: 7.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILgcldtagSGSYRIdgietakmQPDELAALRRerFGFIFQRYNLLSSlT 101
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSL-------LSQFEI--------SEGRVWAERS--IAYVPQQAWIMNA-T 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNVALpavymgmGGKERSAR-AD-----KLLQDL-----GLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEP 170
Cdd:PTZ00243 737 VRGNILF-------FDEEDAARlADavrvsQLEADLaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2559317375 171 TGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDGEI 220
Cdd:PTZ00243 810 LSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-221 |
8.23e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.83 E-value: 8.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 2 SLIECKNIN---RYFGSGENRVHI--LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGietakmQP 76
Cdd:PRK15112 3 TLLEVRNLSktfRYRTGWFRRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD------HP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 77 DELA--ALRRERFGFIFQryNLLSSLTARDNVA----LP-AVYMGMGGKERSARADKLLQDLGLASKEGN-KPGELSGGQ 148
Cdd:PRK15112 77 LHFGdySYRSQRIRMIFQ--DPSTSLNPRQRISqildFPlRLNTDLEPEQREKQIIETLRQVGLLPDHASyYPHMLAPGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 149 QQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLH-KAGHTVIMVTHDPGIAAN-ANRIIEIRDGEII 221
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVV 229
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-221 |
9.56e-15 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 74.57 E-value: 9.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 19 RVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNilgclDTAGSGSYRIdgIETAKMQPDELAALrrERFGFIFQRYNLLS 98
Cdd:cd03271 7 RENNLKNIDVDIPLGVLTCVTGVSGSGKSSLIN-----DTLYPALARR--LHLKKEQPGNHDRI--EGLEHIDKVIVIDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 99 SLTARDNVALPAVYMGM------------GGKE----------------------------------RSARADKLLQDLG 132
Cdd:cd03271 78 SPIGRTPRSNPATYTGVfdeirelfcevcKGKRynretlevrykgksiadvldmtveealeffenipKIARKLQTLCDVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 133 LAS-KEGNKPGELSGGQQQRVSIARALMN---GGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN 208
Cdd:cd03271 158 LGYiKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKC 237
|
250
....*....|....*....
gi 2559317375 209 ANRIIEI------RDGEII 221
Cdd:cd03271 238 ADWIIDLgpeggdGGGQVV 256
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-237 |
1.40e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.60 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 16 GENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdelAALRRERFGFI---FQ 92
Cdd:COG3845 267 DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP---RERRRLGVAYIpedRL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 93 RYNLLSSLTARDNVALPAVY---MGMGG----KERSARADKLLQDLGL-ASKEGNKPGELSGGQQQRVSIARALMNGGEI 164
Cdd:COG3845 344 GRGLVPDMSVAENLILGRYRrppFSRGGfldrKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKL 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559317375 165 IFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPG-IAANANRIIEIRDGEIIsdtsknPEIPTSNVGR 237
Cdd:COG3845 424 LIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDeILALSDRIAVMYEGRIV------GEVPAAEATR 491
|
|
| YbbP |
COG3127 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ... |
474-644 |
1.81e-14 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442361 [Multi-domain] Cd Length: 830 Bit Score: 77.15 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 474 DNANIQVAEKGLTELLKARHGTEDFfMNNSDSIRQMVESTTGTMKLlissIALISLVVGGIGVMNIMLVSVTERTKEIGI 553
Cdd:COG3127 214 PDADLEALRAWLEPALPAGQRVRTV-EDARPELGRALDRAEQFLLL----VALLALLLAGVAVANAARRYVARRLDTIAL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 554 RMAIGARRGNILQQFLIEAVLICVIGGLVGVGLSAAVSLVFNHFVTDF-PMD----ISAMSVIGAVAcsTGIGIAFGF-- 626
Cdd:COG3127 289 LRCLGASRRQIFRIYLLQLLLLGLLGSLLGLLLGALLQALLAALLADLlPVPlepaLSPLPLLLGLL--VGLLVLLLFal 366
|
170
....*....|....*...
gi 2559317375 627 MPANKAAKLNPIDALAQD 644
Cdd:COG3127 367 PPLLRLRRVPPLRVLRRD 384
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-201 |
2.96e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.53 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 37 AIIGQSGSGKSTLMNILGCLDTAGSGSYRIDG-----IETAKMQPDElaalrRERFGFIFQRYNLLSSLTARDNVAlpav 111
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdAEKGICLPPE-----KRRIGYVFQDARLFPHYKVRGNLR---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 112 YmGMGgKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHK 191
Cdd:PRK11144 99 Y-GMA-KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAR 176
|
170
....*....|.
gi 2559317375 192 AGHTVIM-VTH 201
Cdd:PRK11144 177 EINIPILyVSH 187
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-202 |
4.30e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 73.68 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCLD-----TAGSgsYRIDGIETAKM 74
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKaICGVTKdnwrvTADR--MRFDDIDLLRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 75 QPDELAALRRERFGFIFQRYNllSSLTARDNV------ALPA-VYMGMGGKE---RSARADKLLQDLGLASKE---GNKP 141
Cdd:PRK15093 79 SPRERRKLVGHNVSMIFQEPQ--SCLDPSERVgrqlmqNIPGwTYKGRWWQRfgwRKRRAIELLHRVGIKDHKdamRSFP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 142 GELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVI-MVTHD 202
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIlLISHD 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-220 |
6.00e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.54 E-value: 6.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 10 NRYFG-SGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCLDTAGSGSYRIDGieTAKMQPdelaalrreRF 87
Cdd:PLN03130 619 NGYFSwDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG--TVAYVP---------QV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 88 GFIFqrynllsSLTARDNVAL-----PAVYmgmggkERSARADKLLQDLGL-----ASKEGNKPGELSGGQQQRVSIARA 157
Cdd:PLN03130 688 SWIF-------NATVRDNILFgspfdPERY------ERAIDVTALQHDLDLlpggdLTEIGERGVNISGGQKQRVSMARA 754
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 158 LMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDGEI 220
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-220 |
6.93e-14 |
|
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: 72.19 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGENRVhiLKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCLDTagSGSYRIDGIETAKMQPDELaal 82
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLNT--EGDIQIDGVSWNSVPLQKW--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 rRERFGFIFQRYNLLSSlTARDNvalpavyMGMGGKERSARADKLLQDLGLASKEGNKPGE-----------LSGGQQQR 151
Cdd:cd03289 76 -RKAFGVIPQKVFIFSG-TFRKN-------LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 152 VSIARALMNGGEIIFADEPTGALDTASgknvMEIIRRLHK---AGHTVIMVTHDPGIAANANRIIEIRDGEI 220
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPIT----YQVIRKTLKqafADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-203 |
8.14e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.53 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNIL-GCLDTAG-SGSYRIDGIETAKMqpdelaALRRErfGFIFQRYNLLSS 99
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALaGRIQGNNfTGTILANNRKPTKQ------ILKRT--GFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 100 LTARDN---VALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGE-----LSGGQQQRVSIARALMNGGEIIFADEPT 171
Cdd:PLN03211 155 LTVRETlvfCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190
....*....|....*....|....*....|..
gi 2559317375 172 GALDTASGKNVMEIIRRLHKAGHTVIMVTHDP 203
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMHQP 266
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-221 |
1.10e-13 |
|
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: 70.37 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILgCLDTAG----SGSYRIDGIEtakmqP 76
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL-ANRTEGnvsvEGDIHYNGIP-----Y 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 77 DELAALRRERFGFIFQRYNLLSSLTARDNVALPAvymgmggkerSARADKLLQDLglaskegnkpgelSGGQQQRVSIAR 156
Cdd:cd03233 75 KEFAEKYPGEIIYVSEEDVHFPTLTVRETLDFAL----------RCKGNEFVRGI-------------SGGERKRVSIAE 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 157 ALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVT---HDPGIAANANRIIEIRDGEII 221
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSlyqASDEIYDLFDKVLVLYEGRQI 199
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
25-171 |
1.74e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.01 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 25 DISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGietAKMQPDELAAlrRERFGFIFQRYNLLSSLTARD 104
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG---QPVDAGDIAT--RRRVGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2559317375 105 NVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPT 171
Cdd:NF033858 359 NLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
26-202 |
2.38e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.40 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 26 ISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMqPDELAAlrreRFGFI--FQRYNLLSSLTAR 103
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQIA----RMGVVrtFQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 104 DNV-----------------ALPAVYMgmggKERSA--RADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEI 164
Cdd:PRK11300 99 ENLlvaqhqqlktglfsgllKTPAFRR----AESEAldRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 2559317375 165 IFADEPTGALDTASGKNVMEIIRRLHKA-GHTVIMVTHD 202
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHD 213
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-215 |
3.22e-13 |
|
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: 68.12 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 19 RVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNilgcldtagsgsyriDGIETAKMQPDELAALRRERFGFIFqrynlLS 98
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------------EGLYASGKARLISFLPKFSRNKLIF-----ID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 99 SLtardnvalpavymgmggkersaradKLLQDLGLAS-KEGNKPGELSGGQQQRVSIARALMNG--GEIIFADEPTGALD 175
Cdd:cd03238 67 QL-------------------------QFLIDVGLGYlTLGQKLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLH 121
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2559317375 176 TASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEI 215
Cdd:cd03238 122 QQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-202 |
7.60e-13 |
|
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: 71.35 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 31 EKGDFVAIIGQSGSGKSTLMNILgcldtAGS-----GSYridgietaKMQPDELAALRRERfGFIFQRYnlLSSLTARD- 104
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKIL-----SGElkpnlGDY--------DEEPSWDEVLKRFR-GTELQDY--FKKLANGEi 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 105 NVA--------LPAVYMGMGGK------ERSArADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEP 170
Cdd:COG1245 161 KVAhkpqyvdlIPKVFKGTVREllekvdERGK-LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|..
gi 2559317375 171 TGALDTASGKNVMEIIRRLHKAGHTVIMVTHD 202
Cdd:COG1245 240 SSYLDIYQRLNVARLIRELAEEGKYVLVVEHD 271
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-220 |
9.03e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.93 E-value: 9.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCLDTAGSGSYRIDGieTAKMQPdelaalrreRFGFIFqrynllsSLT 101
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG--SVAYVP---------QVSWIF-------NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNVALPAVYMgmggKERSARA---DKLLQDLGL-ASKEGNKPGE----LSGGQQQRVSIARALMNGGEIIFADEPTGA 173
Cdd:PLN03232 695 VRENILFGSDFE----SERYWRAidvTALQHDLDLlPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2559317375 174 LDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDGEI 220
Cdd:PLN03232 771 LDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMI 817
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-222 |
9.17e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.88 E-value: 9.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTL-MNILGCL-DTAGSGSYRIDGIETAKMQpdeLAALRRErFGFIFQRYNLLSS 99
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLLrPQKGAVLWQGKPLDYSKRG---LLALRQQ-VATVFQDPEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 100 LTARD-NVALPAVYMGMGGKERSARADKLLQdLGLASKEGNKPGE-LSGGQQQRVSIARALMNGGEIIFADEPTGALDTA 177
Cdd:PRK13638 92 YTDIDsDIAFSLRNLGVPEAEITRRVDEALT-LVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2559317375 178 SGKNVMEIIRRLHKAGHTVIMVTHDPG-IAANANRIIEIRDGEIIS 222
Cdd:PRK13638 171 GRTQMIAIIRRIVAQGNHVIISSHDIDlIYEISDAVYVLRQGQILT 216
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-205 |
9.51e-13 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 71.80 E-value: 9.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 14 GSGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAG--SGSYRIDGIETakmqpdelaalRRERFGFI- 90
Cdd:PLN03140 887 GVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPK-----------KQETFARIs 955
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 91 -FQRYNLLSS--LTARDNVALPAVY---MGMGGKERSARADKL--------LQD--LGLASKEGnkpgeLSGGQQQRVSI 154
Cdd:PLN03140 956 gYCEQNDIHSpqVTVRESLIYSAFLrlpKEVSKEEKMMFVDEVmelveldnLKDaiVGLPGVTG-----LSTEQRKRLTI 1030
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 155 ARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGI 205
Cdd:PLN03140 1031 AVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-230 |
1.12e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 71.52 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNIL--------GCLDTAGSGSYRIdgiETAKMQPDELaalrRER--FGFIFQ 92
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALlaemdkveGHVHMKGSVAYVP---QQAWIQNDSL----RENilFGKALN 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 93 RYNLLSSLTArdNVALPAVYMGMGGKErsaradkllqdlglaSKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTG 172
Cdd:TIGR00957 727 EKYYQQVLEA--CALLPDLEILPSGDR---------------TEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 173 ALDTASGKNVME--IIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDGEiISDTSKNPEI 230
Cdd:TIGR00957 790 AVDAHVGKHIFEhvIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGK-ISEMGSYQEL 848
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-202 |
1.31e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.22 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSGEnrvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRidgietakmQPDELa 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKL- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 81 alrreRFGFIFQRYNLLSSL--------TARDNVA----LPAVymgmggkeRSARADKLLQdlglaskegnKPGE-LSGG 147
Cdd:PRK09544 68 -----RIGYVPQKLYLDTTLpltvnrflRLRPGTKkediLPAL--------KRVQAGHLID----------APMQkLSGG 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2559317375 148 QQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRL-HKAGHTVIMVTHD 202
Cdd:PRK09544 125 ETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHD 180
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-202 |
1.46e-12 |
|
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: 70.35 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSgenRVhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDgiETAKMqpdelaalr 83
Cdd:TIGR03719 323 IEAENLTKAFGD---KL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETVKL--------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 rerfGFIFQ-RYNLLSSLTARDNVALPAVYMGMGGKERSARADkllqdLGLASKEGN----KPGELSGGQQQRVSIARAL 158
Cdd:TIGR03719 388 ----AYVDQsRDALDPNKTVWEEISGGLDIIKLGKREIPSRAY-----VGRFNFKGSdqqkKVGQLSGGERNRVHLAKTL 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2559317375 159 MNGGEIIFADEPTGALDTasgknvmEIIRRLHKA----GHTVIMVTHD 202
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDV-------ETLRALEEAllnfAGCAVVISHD 499
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-220 |
1.66e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 71.13 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalrRERFGFIFQRYNLLSSlT 101
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL----RFKITIIPQDPVLFSG-S 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNV------ALPAVYMGMGGKERSARADKLLQDLGLASKEGnkpGE-LSGGQQQRVSIARALMNGGEIIFADEPTGAL 174
Cdd:TIGR00957 1376 LRMNLdpfsqySDEEVWWALELAHLKTFVSALPDKLDHECAEG---GEnLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2559317375 175 DTASgKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDGEI 220
Cdd:TIGR00957 1453 DLET-DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-219 |
3.99e-12 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 67.19 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTL-MNILGCLDtAGSGSYRIDGietakmqpdelaalrreRFGFIFQrYNLLSSL 100
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLlMLILGELE-PSEGKIKHSG-----------------RISFSSQ-FSWIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 101 TARDNVALPAVYMGMGGKErSARADKLLQDLG-LASKEGNKPGE----LSGGQQQRVSIARALMNGGEIIFADEPTGALD 175
Cdd:cd03291 113 TIKENIIFGVSYDEYRYKS-VVKACQLEEDITkFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2559317375 176 TASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDGE 219
Cdd:cd03291 192 VFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-202 |
4.68e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.99 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 21 HILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGsyridgieTAKMQPDElaalrreRFGFIFQRYNLLSSL 100
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG--------EARPAPGI-------KVGYLPQEPQLDPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 101 TARDNVA------------LPAVYMGMGgkERSARADKL------LQDLgLASKEG----NK-----------PGE---- 143
Cdd:PRK11819 86 TVRENVEegvaevkaaldrFNEIYAAYA--EPDADFDALaaeqgeLQEI-IDAADAwdldSQleiamdalrcpPWDakvt 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 144 -LSGGQQQRVSIARALMNGGEIIFADEPTGALDTASgknVMEIIRRLHKAGHTVIMVTHD 202
Cdd:PRK11819 163 kLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLHDYPGTVVAVTHD 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-202 |
5.47e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.11 E-value: 5.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 26 ISLSIEKGDFVAIIGQSGSGKSTLmniLGCLD--TAGSGSYRIDGIETAKMQPDELAALRrerfGFIFQRYNLLSSLTAR 103
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTL---LARMAglLPGSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 104 DNVALpavYMGMGGKERSARA--DKLLQDLGLASKEGNKPGELSGGQQQRVSIA-------RALMNGGEIIFADEPTGAL 174
Cdd:PRK03695 88 QYLTL---HQPDKTRTEAVASalNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSL 164
|
170 180
....*....|....*....|....*...
gi 2559317375 175 DTASGKNVMEIIRRLHKAGHTVIMVTHD 202
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGIAVVMSSHD 192
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-220 |
5.55e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 6 CKNINRYFGSGenrvhiLKDISLSIEKGDFVAIIGQSGSGKSTLMNIL-GCLDTAgSGSYRIDGIETAKMQP-DELAAlr 83
Cdd:PRK10762 257 RLKVDNLSGPG------VNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPRT-SGYVTLDGHEVVTRSPqDGLAN-- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 rerfGFIF-----QRYNLLSSLTARDNVALPAV-YMGMGG------KERSARAD-KLLQDLGLASKEgNKPGELSGGQQQ 150
Cdd:PRK10762 328 ----GIVYisedrKRDGLVLGMSVKENMSLTALrYFSRAGgslkhaDEQQAVSDfIRLFNIKTPSME-QAIGLLSGGNQQ 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 151 RVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRDGEI 220
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEmPEVLGMSDRILVMHEGRI 473
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-218 |
5.55e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 69.17 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTL-MNILGcldtagsgsyridgietaKMQPDELAALRRERFGFIFQrYNLLSSL 100
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLlMMIMG------------------ELEPSEGKIKHSGRISFSPQ-TSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 101 TARDNVALPAVYMGMggKERSA-RADKLLQDLGLASKEGNKP-GE----LSGGQQQRVSIARALMNGGEIIFADEPTGAL 174
Cdd:TIGR01271 502 TIKDNIIFGLSYDEY--RYTSViKACQLEEDIALFPEKDKTVlGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2559317375 175 DTASGKNVMEiiRRLHK--AGHTVIMVTHDPGIAANANRIIEIRDG 218
Cdd:TIGR01271 580 DVVTEKEIFE--SCLCKlmSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-202 |
1.87e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.14 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 30 IEKGDFVAIIGQSGSGKSTLMNILgcldtagSGSYRID-GIETAKMQPDELaaLRRERfGFIFQRYnlLSSLTARD-NVA 107
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL-------SGELIPNlGDYEEEPSWDEV--LKRFR-GTELQNY--FKKLYNGEiKVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 108 --------LPAVYMGMGGK------ERSArADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGA 173
Cdd:PRK13409 164 hkpqyvdlIPKVFKGKVREllkkvdERGK-LDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180
....*....|....*....|....*....
gi 2559317375 174 LDTASGKNVMEIIRRLHKaGHTVIMVTHD 202
Cdd:PRK13409 243 LDIRQRLNVARLIRELAE-GKYVLVVEHD 270
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
19-229 |
2.18e-11 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 67.35 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 19 RVHILKDISLSIEKGDFVAIIGQSGSGKSTLMN--ILGCLDT------AGSGSYR-IDGIE---------------TAKM 74
Cdd:TIGR00630 620 RENNLKNITVSIPLGLFTCITGVSGSGKSTLINdtLYPALANrlngakTVPGRYTsIEGLEhldkvihidqspigrTPRS 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 75 QP-------DELAALRRE------------RFGFifqryNL----------LSSLTARDNVaLPAVY------------- 112
Cdd:TIGR00630 700 NPatytgvfDEIRELFAEtpeakvrgytpgRFSF-----NVkggrceacqgDGVIKIEMHF-LPDVYvpcevckgkrynr 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 113 ---------------MGMGGKERS---------ARADKLLQDLGLAS-KEGNKPGELSGGQQQRVSIARALM---NGGEI 164
Cdd:TIGR00630 774 etlevkykgkniadvLDMTVEEAYeffeavpsiSRKLQTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELSkrsTGRTL 853
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 165 IFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEI------RDGEIISdtSKNPE 229
Cdd:TIGR00630 854 YILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVA--SGTPE 922
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-237 |
2.94e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.53 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGsgenRVHILKDISLSIEKGDFVAIIGQSGSG--KSTLMNILGCLDtAGSGSYRIDGIETAKMqpdelaA 81
Cdd:NF000106 14 VEVRGLVKHFG----EVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPD-AGRRPWRF*TWCANRR------A 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 82 LRRERFGFIFQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNG 161
Cdd:NF000106 83 LRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2559317375 162 GEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAAN-ANRIIEIRDGEIISDtSKNPEIPTSNVGR 237
Cdd:NF000106 163 PAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIAD-GKVDELKTKVGGR 238
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-201 |
3.10e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 66.86 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCLDTagSGSYRIDGI--ETAKMQPdelaalRRERFGFIFQRYNLLS 98
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSaLLRLLST--EGEIQIDGVswNSVTLQT------WRKAFGVIPQKVFIFS 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 99 SlTARDNVALPAVYmgmggkeRSARADKLLQDLGLASKEGNKPGE-----------LSGGQQQRVSIARALMNGGEIIFA 167
Cdd:TIGR01271 1306 G-TFRKNLDPYEQW-------SDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190
....*....|....*....|....*....|....*..
gi 2559317375 168 DEPTGALDTASgknvMEIIRRLHK---AGHTVIMVTH 201
Cdd:TIGR01271 1378 DEPSAHLDPVT----LQIIRKTLKqsfSNCTVILSEH 1410
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-222 |
4.37e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 1 MSLIECKNINRYFGSgenrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILG---CLDTaGSGSYRIDgIETAKMQPD 77
Cdd:PRK11147 1 MSLISIHGAWLSFSD----APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLDD-GRIIYEQD-LIVARLQQD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 78 ELAALRRERFGFI----------FQRYNLLSSLTARD----NVA----LPAVYMGMGGKERSARADKLLQDLGLaskEGN 139
Cdd:PRK11147 75 PPRNVEGTVYDFVaegieeqaeyLKRYHDISHLVETDpsekNLNelakLQEQLDHHNLWQLENRINEVLAQLGL---DPD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 140 KP-GELSGGQQQRVSIARALMNGGEIIFADEPTGALDtasgknvMEIIRRLHK-----AGhTVIMVTHDPG-IAANANRI 212
Cdd:PRK11147 152 AAlSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-------IETIEWLEGflktfQG-SIIFISHDRSfIRNMATRI 223
|
250
....*....|
gi 2559317375 213 IEIRDGEIIS 222
Cdd:PRK11147 224 VDLDRGKLVS 233
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-176 |
4.77e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.53 E-value: 4.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGsgeNRVHIlKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIdGiETAKMqpdelaalr 83
Cdd:PRK11819 325 IEAENLSKSFG---DRLLI-DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G-ETVKL--------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 rerfGFIFQ-RYNLLSSLTARDNVALPAVYMGMGGKERSARAdkLLQDLGLASKEGNKP-GELSGGQQQRVSIARALMNG 161
Cdd:PRK11819 390 ----AYVDQsRDALDPNKTVWEEISGGLDIIKVGNREIPSRA--YVGRFNFKGGDQQKKvGVLSGGERNRLHLAKTLKQG 463
|
170
....*....|....*
gi 2559317375 162 GEIIFADEPTGALDT 176
Cdd:PRK11819 464 GNVLLLDEPTNDLDV 478
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-220 |
1.17e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.16 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 26 ISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDElaALR---------RERFGFIFQRynl 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD--AIRagimlcpedRKAEGIIPVH--- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 97 lsslTARDNVALPA----VYMGM---GGKERsARADKLLQDLGLASKEGNKP-GELSGGQQQRVSIARALMNGGEIIFAD 168
Cdd:PRK11288 347 ----SVADNINISArrhhLRAGClinNRWEA-ENADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2559317375 169 EPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRDGEI 220
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlPEVLGVADRIVVMREGRI 474
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-214 |
3.09e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.20 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPdelAALRRerfGF-IFQRYNLLSSL 100
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLRQ---GVaMVQQDPVVLAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 101 TARDNVALpavymgmgGKERSarADKLLQDL--------------GLASKEGNKPGELSGGQQQRVSIARALMNGGEIIF 166
Cdd:PRK10790 430 TFLANVTL--------GRDIS--EEQVWQALetvqlaelarslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2559317375 167 ADEPTGALDTASGKNVMEIIRRLHKagHTVIMVthdpgIAANANRIIE 214
Cdd:PRK10790 500 LDEATANIDSGTEQAIQQALAAVRE--HTTLVV-----IAHRLSTIVE 540
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-205 |
4.29e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 15 SGENRVhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGsgsYRIDGIETAKMQPDELAALRRerFGFIFQRY 94
Cdd:TIGR00956 772 KKEKRV-ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTG---VITGGDRLVNGRPLDSSFQRS--IGYVQQQD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 95 NLLSSLTARDNVALPAvYM----GMGGKERSARADKLLQDLGLAS-KEG--NKPGE-LSGGQQQRVSIARALM-NGGEII 165
Cdd:TIGR00956 846 LHLPTSTVRESLRFSA-YLrqpkSVSKSEKMEYVEEVIKLLEMESyADAvvGVPGEgLNVEQRKRLTIGVELVaKPKLLL 924
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2559317375 166 FADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGI 205
Cdd:TIGR00956 925 FLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSA 964
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-213 |
4.31e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.12 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGENrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCL-----------------DTAGSGSYRI 66
Cdd:PTZ00265 1166 IEIMDVNFRYISRPN-VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtnDMTNEQDYQG 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 67 DGIETAKMQ-PDELAALRRERFG---FIFQR-------------YNL-----LSSLTARDnvalPAVY-MGMGGKERSAR 123
Cdd:PTZ00265 1245 DEEQNVGMKnVNEFSLTKEGGSGedsTVFKNsgkilldgvdicdYNLkdlrnLFSIVSQE----PMLFnMSIYENIKFGK 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 124 ADKLLQDLGLASK------------------EGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEI 185
Cdd:PTZ00265 1321 EDATREDVKRACKfaaidefieslpnkydtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
250 260
....*....|....*....|....*....
gi 2559317375 186 IRRLH-KAGHTVIMVTHDPGIAANANRII 213
Cdd:PTZ00265 1401 IVDIKdKADKTIITIAHRIASIKRSDKIV 1429
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-201 |
4.40e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKmqpdELAALRRErFGFIFQRYNLLSSLT 101
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTYQKQ-LCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNValpavYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKN 181
Cdd:PRK13540 91 LRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|
gi 2559317375 182 VMEIIRRLHKAGHTVIMVTH 201
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSH 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-220 |
6.02e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.99 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 15 SGENrvhiLKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDElaalrRERFGFIF--- 91
Cdd:PRK15439 275 TGEG----FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpe 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 92 --QRYNL-LSSLTARDNVALPAVYMGM---GGKERsARADKLLQDLGLASKEGNKP-GELSGGQQQRVSIARALMNGGEI 164
Cdd:PRK15439 346 drQSSGLyLDAPLAWNVCALTHNRRGFwikPAREN-AVLERYRRALNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQL 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2559317375 165 IFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRDGEI 220
Cdd:PRK15439 425 LIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDlEEIEQMADRVLVMHQGEI 481
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-202 |
8.77e-10 |
|
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: 59.69 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 33 GDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRidgietakmQPDELAALRRERFGFIFQRY------NLLSSLTARDNV 106
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD---------DPPDWDEILDEFRGSELQNYftklleGDVKVIVKPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 107 AL-PAVYMGMGG-----KERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGK 180
Cdd:cd03236 97 DLiPKAVKGKVGellkkKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|..
gi 2559317375 181 NVMEIIRRLHKAGHTVIMVTHD 202
Cdd:cd03236 177 NAARLIRELAEDDNYVLVVEHD 198
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
15-216 |
2.73e-09 |
|
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: 56.60 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 15 SGENRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGcldtagsgsyridgietakmqpdeLAALRRerfgfiFQRY 94
Cdd:cd03227 3 VLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG------------------------LALGGA------QSAT 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 95 NLLSSLTARDNVALP-AVYMGMggkersaradkLLQdlglaskegnkpgeLSGGQQQRVSIARAL----MNGGEIIFADE 169
Cdd:cd03227 53 RRRSGVKAGCIVAAVsAELIFT-----------RLQ--------------LSGGEKELSALALILalasLKPRPLYILDE 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2559317375 170 PTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEIR 216
Cdd:cd03227 108 IDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-217 |
3.57e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 27 SLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALRRErfgfIFQRYN--LLSSltARD 104
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSD----EWQRNNtdMLSP--GED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 105 NVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVME 184
Cdd:PRK10938 97 DTGRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
170 180 190
....*....|....*....|....*....|...
gi 2559317375 185 IIRRLHKAGHTVIMVThdpgiaanaNRIIEIRD 217
Cdd:PRK10938 177 LLASLHQSGITLVLVL---------NRFDEIPD 200
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-189 |
5.62e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.35 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 18 NRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGClDTAGS-----GSYRIDGIEtakmqPDELAALRRERFGFIFQ 92
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS-NTDGFhigveGVITYDGIT-----PEEIKKHYRGDVVYNAE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 93 RYNLLSSLTARDNVALPAV-------YMGMGGKERSAR-ADKLLQDLGLASKEGNKPGE-----LSGGQQQRVSIARALM 159
Cdd:TIGR00956 146 TDVHFPHLTVGETLDFAARcktpqnrPDGVSREEYAKHiADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASL 225
|
170 180 190
....*....|....*....|....*....|
gi 2559317375 160 NGGEIIFADEPTGALDTASGknvMEIIRRL 189
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATA---LEFIRAL 252
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-221 |
5.83e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGEnrvhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSyrIDGIETAKMqpdelaalr 83
Cdd:PRK15064 320 LEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT--VKWSENANI--------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 rerfGFIFQ--RYNLLSSLTARDNVALpavYMGMGGKERSARAdkLLQDLGLASKEGNKPGE-LSGGQQQRVSIARALMN 160
Cdd:PRK15064 385 ----GYYAQdhAYDFENDLTLFDWMSQ---WRQEGDDEQAVRG--TLGRLLFSQDDIKKSVKvLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2559317375 161 GGEIIFADEPTGALDtasgknvMEIIRRLHKA-----GhTVIMVTHDPG-IAANANRIIEIRDGEII 221
Cdd:PRK15064 456 KPNVLVMDEPTNHMD-------MESIESLNMAlekyeG-TLIFVSHDREfVSSLATRIIEITPDGVV 514
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-241 |
6.09e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 4 IECKNINRYFGSGENrVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKmqpDELAALR 83
Cdd:PTZ00265 383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLK---DINLKWW 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGFIFQ-------------RYNL-----LSSLTARDNVALPAVYMGMGGKE--------------RSARADKLLQ-- 129
Cdd:PTZ00265 459 RSKIGVVSQdpllfsnsiknniKYSLyslkdLEALSNYYNEDGNDSQENKNKRNscrakcagdlndmsNTTDSNELIEmr 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 130 ---------DLGLASKE------------------GNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNV 182
Cdd:PTZ00265 539 knyqtikdsEVVDVSKKvlihdfvsalpdkyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 183 MEIIRRLH-KAGHTVIMVTHDPGIAANANRIIEI--RDGEIISDTSKNPEIPTSNVGRIREK 241
Cdd:PTZ00265 619 QKTINNLKgNENRITIIIAHRLSTIRYANTIFVLsnRERGSTVDVDIIGEDPTKDNKENNNK 680
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
69-218 |
6.32e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 59.46 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 69 IETAKMQPDELaalrrerfgFIFqrynlLSSLTARDnVALPAVYMGMggKERSAradkLLQDLGLASKEGNKP-GELSGG 147
Cdd:PRK00635 422 AEFQQMSLQEL---------FIF-----LSQLPSKS-LSIEEVLQGL--KSRLS----ILIDLGLPYLTPERAlATLSGG 480
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 148 QQQRVSIARALmnGGEII----FADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDG 218
Cdd:PRK00635 481 EQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPG 553
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-225 |
7.45e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQpdeLAALRRERFgfIFQRYNLLSSLT 101
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRRVLS--IIPQSPVLFSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNVALPAVYMGMGGKERSARADklLQD------LGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALD 175
Cdd:PLN03232 1326 VRFNIDPFSEHNDADLWEALERAH--IKDvidrnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2559317375 176 TASGKNVMEIIRRLHKAGhTVIMVTHDPGIAANANRIIEIRDGEIISDTS 225
Cdd:PLN03232 1404 VRTDSLIQRTIREEFKSC-TMLVIAHRLNTIIDCDKILVLSSGQVLEYDS 1452
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-214 |
9.71e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQpdeLAALRReRFGFIFQRYNLLSSlT 101
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRK-VLGIIPQAPVLFSG-T 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNV-------------ALpavymgmggkERSARADKLLQD-LGLASkEGNKPGE-LSGGQQQRVSIARALMNGGEIIF 166
Cdd:PLN03130 1329 VRFNLdpfnehndadlweSL----------ERAHLKDVIRRNsLGLDA-EVSEAGEnFSVGQRQLLSLARALLRRSKILV 1397
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2559317375 167 ADEPTGALDTASGKNVMEIIRRLHKAGHTVImvthdpgIAANANRIIE 214
Cdd:PLN03130 1398 LDEATAAVDVRTDALIQKTIREEFKSCTMLI-------IAHRLNTIID 1438
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-200 |
1.22e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILgcldtAGSgsyRidgietaKMQPDELAAL------RRERFGfIFQR--Y 94
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-----AGA---R-------KIQQGRVEVLggdmadARHRRA-VCPRiaY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 95 -------NLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFA 167
Cdd:NF033858 81 mpqglgkNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 2559317375 168 DEPTGALDTASGKNVMEIIRRL--HKAGHTVIMVT 200
Cdd:NF033858 161 DEPTTGVDPLSRRQFWELIDRIraERPGMSVLVAT 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-223 |
1.27e-08 |
|
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: 57.91 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 25 DISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCLDTAGSGSYRIDGIETAKMQPDE-----LAALRRERfgfifQRYNLLS 98
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQairagIAMVPEDR-----KRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 99 SLTARDNVALPAV--YMGMGGKERSARADKLLQDLGLASKEGNKP----GELSGGQQQRVSIARALMNGGEIIFADEPTG 172
Cdd:TIGR02633 353 ILGVGKNITLSVLksFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 173 ALDTASGKNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRDGEIISD 223
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-223 |
1.50e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 19 RVHILKDISLSIEKGDFVAIIGQSGSGKSTLMN-ILGCLDTAGSGSYRIDGIETAKMQPDE-----LAALRRERfgfifQ 92
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKIRNPQQaiaqgIAMVPEDR-----K 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 93 RYNLLSSLTARDNVALPAV--YMGMGGKERSARADKLLQDLGLASKEGNKP----GELSGGQQQRVSIARALMNGGEIIF 166
Cdd:PRK13549 349 RDGIVPVMGVGKNITLAALdrFTGGSRIDDAAELKTILESIQRLKVKTASPelaiARLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 167 ADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRDGEIISD 223
Cdd:PRK13549 429 LDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSElPEVLGLSDRVLVMHEGKLKGD 486
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-202 |
1.77e-08 |
|
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: 55.88 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDF-----VAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGiETAKMQPDELAALRRERFgfifqrYNLL 97
Cdd:cd03237 10 LGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL-DTVSYKPQYIKADYEGTV------RDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 98 SSLTArdnvalpavymGMGgkERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTA 177
Cdd:cd03237 83 SSITK-----------DFY--THPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180
....*....|....*....|....*.
gi 2559317375 178 SGKNVMEIIRRL-HKAGHTVIMVTHD 202
Cdd:cd03237 150 QRLMASKVIRRFaENNEKTAFVVEHD 175
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
22-227 |
1.90e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 55.69 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELaalrRERFGFIFQRYNLLSSlT 101
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL----RSRLSIILQDPILFSG-S 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 102 ARDNValpavymgmgGKERSARADKLLQDLGLASKEG---NKPGEL-----------SGGQQQRVSIARALMNGGEIIFA 167
Cdd:cd03288 111 IRFNL----------DPECKCTDDRLWEALEIAQLKNmvkSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559317375 168 DEPTGALDTASgKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEIRDGEIIS-DTSKN 227
Cdd:cd03288 181 DEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVEcDTPEN 240
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-213 |
2.34e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.48 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKST-LMNILGCLDTAGsGSYRIDGIETAKMQPDELaalrRERFGFIFQRYNLLSSl 100
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTlLLTFMRMVEVCG-GEIRVNGREIGAYGLREL----RRQFSMIPQDPVLFDG- 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 101 TARDNV-----ALPA-VYMGM---GGKERSARADKllqdlGLASK--EGNKpgELSGGQQQRVSIARALMNGGE-IIFAD 168
Cdd:PTZ00243 1399 TVRQNVdpfleASSAeVWAALelvGLRERVASESE-----GIDSRvlEGGS--NYSVGQRQLMCMARALLKKGSgFILMD 1471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2559317375 169 EPTGALDTASGKNVMEIIRRLHKAgHTVIMVTHDPGIAANANRII 213
Cdd:PTZ00243 1472 EATANIDPALDRQIQATVMSAFSA-YTVITIAHRLHTVAQYDKII 1515
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-201 |
3.80e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.95 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 26 ISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDElaalrRERFGFIFQRYNLLSSLTARDN 105
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV-----HQNMGYCPQFDAIDDLLTGREH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 106 VALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEI 185
Cdd:TIGR01257 2033 LYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170
....*....|....*.
gi 2559317375 186 IRRLHKAGHTVIMVTH 201
Cdd:TIGR01257 2113 IVSIIREGRAVVLTSH 2128
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-222 |
5.59e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 20 VHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDElaALRrERFGFIFQRYNLLSS 99
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALE-NGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 100 LTARDNVAL---PAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDT 176
Cdd:PRK10982 88 RSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2559317375 177 ASGKNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRDGEIIS 222
Cdd:PRK10982 168 KEVNHLFTIIRKLKERGCGIVYISHKmEEIFQLCDEITILRDGQWIA 214
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
143-219 |
1.29e-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: 51.80 E-value: 1.29e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 143 ELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRL-HKAGHTVIMVTHDPGIAANANRIIEIRDGE 219
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLsEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| FtsX |
COG2177 |
Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning]; |
466-629 |
1.66e-07 |
|
Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441780 [Multi-domain] Cd Length: 292 Bit Score: 53.29 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 466 NSITVKIKDNANIQVAEkgLTELLKARHGTEDffMNNSDSIRQMVESTTGTMKLLISSIALISLVVGGIGVMNIMLVSVT 545
Cdd:COG2177 119 ASIEVKLKPEDPEDLEA--LAAALEALPGVAE--VDYDREWVERLFALLNLLRLVGLVLAALLLLAAVLLIGNTIRLAIY 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 546 ERTKEIGI-RMaIGARRGNILQQFLIEAVLICVIGGLVGVGLSAAVSLVFNH-------FVTDFPMDISAMSVIGAVAcs 617
Cdd:COG2177 195 SRREEIEImKL-VGATDGFIRRPFLLEGALLGLLGGLLALLLLALLYLLLVSaladglaFLSLLSLGGLLLLLLLLLL-- 271
|
170
....*....|..
gi 2559317375 618 tGIGIAFGFMPA 629
Cdd:COG2177 272 -LLGALLGALGS 282
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-201 |
4.32e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.00 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 18 NRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGietakmQPDELAalRRERF-GFIFQRYNL 96
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG------KTATRG--DRSRFmAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 97 LSSLTARDNVALPAVYMGMGGKERSARAdklLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDT 176
Cdd:PRK13543 94 KADLSTLENLHFLCGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
170 180
....*....|....*....|....*
gi 2559317375 177 ASGKNVMEIIRRLHKAGHTVIMVTH 201
Cdd:PRK13543 171 EGITLVNRMISAHLRGGGAALVTTH 195
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
126-215 |
2.46e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.78 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 126 KLLQDLGLASKEGNKP-GELSGGQQQRVSIARALMNG--GEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD 202
Cdd:TIGR00630 470 GFLIDVGLDYLSLSRAaGTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD 549
|
90
....*....|...
gi 2559317375 203 PGIAANANRIIEI 215
Cdd:TIGR00630 550 EDTIRAADYVIDI 562
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
18-82 |
4.24e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.48 E-value: 4.24e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559317375 18 NRVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNILgcldtAGSGSYRI-------DGIETAKMQPDELAAL 82
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI-----AGHPAYKIlegdilfKGESILDLEPEERAHL 84
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-219 |
4.47e-06 |
|
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: 46.98 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 32 KGDFVAIIGQSGSGKSTLMN-ILGCLDTAGSGSYRIDGIETAKMQPDELAALRRERfgfifqrynllssltardnvalpa 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGG------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 111 vymgmggkersaradkllqdlglaskegnKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIR--- 187
Cdd:smart00382 57 -----------------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2559317375 188 ---RLHKAGHTVIMVTHDPG------IAANANRIIEIRDGE 219
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKdlgpalLRRRFDRRIVLLLIL 148
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
141-222 |
4.54e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.99 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 141 PGELSGGQQQ------RVSIARALMNGGEIIFADEPTGALDTASGKNVM-EIIR-RLHKAGHTVIMVTHDPGIAANANRI 212
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLaEIIEeRKSQKNFQLIVITHDEELVDAADHI 192
|
90
....*....|.
gi 2559317375 213 IEI-RDGEIIS 222
Cdd:cd03240 193 YRVeKDGRQKS 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
142-226 |
7.82e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 142 GELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHD-PGIAANANRIIEIRDGEI 220
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEmPELLGITDRILVMSNGLV 469
|
....*...
gi 2559317375 221 --ISDTSK 226
Cdd:PRK10982 470 agIVDTKT 477
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-202 |
1.24e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 19 RVhILKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIETAKMQPDELAALRRERFGFIFQRYNLLS 98
Cdd:PRK10636 14 RV-LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIDGDREYR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 99 SLTAR--------DNVALPAVYmgmgGKERS-------ARADKLLQDLGLASKEGNKP-GELSGGQQQRVSIARALMNGG 162
Cdd:PRK10636 93 QLEAQlhdanernDGHAIATIH----GKLDAidawtirSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2559317375 163 EIIFADEPTGALDTASgknVMEIIRRLHKAGHTVIMVTHD 202
Cdd:PRK10636 169 DLLLLDEPTNHLDLDA---VIWLEKWLKSYQGTLILISHD 205
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-218 |
1.46e-05 |
|
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: 48.24 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDF-----VAIIGQSGSGKSTLMNILgcldtAGsgsyridgietaKMQPDELAALRRERFGFIFQRYNLL 97
Cdd:COG1245 351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKIL-----AG------------VLKPDEGEVDEDLKISYKPQYISPD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 98 SSLTARDNValpavymgmggkeRSARADKL---------LQDLGLaSKEGNKP-GELSGGQQQRVSIARALMNGGEIIFA 167
Cdd:COG1245 414 YDGTVEEFL-------------RSANTDDFgssyykteiIKPLGL-EKLLDKNvKDLSGGELQRVAIAACLSRDADLYLL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 168 DEPTGALDTASGKNVMEIIRRL-HKAGHTVIMVTHD-----------------PGIAANANRIIEIRDG 218
Cdd:COG1245 480 DEPSAHLDVEQRLAVAKAIRRFaENRGKTAMVVDHDiylidyisdrlmvfegePGVHGHASGPMDMREG 548
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
12-201 |
2.65e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 12 YFGSGENRVHI-LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGIetakmqpdelAALrrerfgfI 90
Cdd:PRK13545 28 FFRSKDGEYHYaLNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS----------AAL-------I 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 91 FQRYNLLSSLTARDNVALPAVYMGMGGKERSARADKLLQ--DLGlasKEGNKPGE-LSGGQQQRVSIARALMNGGEIIFA 167
Cdd:PRK13545 91 AISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEfaDIG---KFIYQPVKtYSSGMKSRLGFAISVHINPDILVI 167
|
170 180 190
....*....|....*....|....*....|....
gi 2559317375 168 DEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTH 201
Cdd:PRK13545 168 DEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISH 201
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-198 |
3.07e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 19 RVHILKDISLSIEKGDFVAIIGQSGSGKSTLMNIL-GCLDTA--GSGSYRIDGIETAKMQPDELAAL------------R 83
Cdd:PLN03140 177 KLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALaGKLDPSlkVSGEITYNGYRLNEFVPRKTSAYisqndvhvgvmtV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 84 RERFGF------IFQRYNLLSSLTARDNVA--LPA----VYM---GMGGKERSARADKLLQDLGLASKEGNKPGE----- 143
Cdd:PLN03140 257 KETLDFsarcqgVGTRYDLLSELARREKDAgiFPEaevdLFMkatAMEGVKSSLITDYTLKILGLDICKDTIVGDemirg 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2559317375 144 LSGGQQQRVSIARALMNGGEIIFADEPTGALDTASgknVMEIIRRLHKAGH----TVIM 198
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSST---TYQIVKCLQQIVHlteaTVLM 392
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
142-218 |
3.35e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 142 GELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRL---HKAghTVIMVTHD---------------- 202
Cdd:PRK13409 452 KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIaeeREA--TALVVDHDiymidyisdrlmvfeg 529
|
90
....*....|....*..
gi 2559317375 203 -PGIAANANRIIEIRDG 218
Cdd:PRK13409 530 ePGKHGHASGPMDMREG 546
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
23-51 |
4.50e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.60 E-value: 4.50e-05
10 20
....*....|....*....|....*....
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMN 51
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
19-49 |
5.51e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.56 E-value: 5.51e-05
10 20 30
....*....|....*....|....*....|.
gi 2559317375 19 RVHILKDISLSIEKGDFVAIIGQSGSGKSTL 49
Cdd:COG0178 12 REHNLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
19-53 |
6.10e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.17 E-value: 6.10e-05
10 20 30
....*....|....*....|....*....|....*.
gi 2559317375 19 RVHILKDISLSIEKGDFVAIIGQSGSGKSTLMN-IL 53
Cdd:COG0178 617 RENNLKNVDVEIPLGVLTCVTGVSGSGKSTLVNdIL 652
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
19-49 |
1.18e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 1.18e-04
10 20 30
....*....|....*....|....*....|.
gi 2559317375 19 RVHILKDISLSIEKGDFVAIIGQSGSGKSTL 49
Cdd:TIGR00630 8 REHNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-215 |
1.23e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.59 E-value: 1.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 144 LSGGQQQRVSIARALMNGGE---IIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEI 215
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-220 |
1.60e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILgcldtagSG----SYRIDGIetakmqpdeLAALRR---ERFGFIFQRY 94
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-------TGdhpqGYSNDLT---------LFGRRRgsgETIWDIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 95 NLLSS---------LTARdNVALPA------VYMGMGGKERSaRADKLLQDLGLASKEGNKP-GELSGGQQQRVSIARAL 158
Cdd:PRK10938 339 GYVSSslhldyrvsTSVR-NVILSGffdsigIYQAVSDRQQK-LAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRAL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559317375 159 MNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHT-VIMVTHDPGIAAN--ANRIIEIRDGEI 220
Cdd:PRK10938 417 VKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHHAEDAPAciTHRLEFVPDGDI 481
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
142-199 |
1.70e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 1.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2559317375 142 GELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMV 199
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI 460
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
124-221 |
1.82e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.63 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 124 ADKL--LQDLGL--------ASkegnkpgELSGGQQQRVSIARALM---NGGEIIFADEPTGALDTASGKNVMEIIRRLH 190
Cdd:COG0178 804 ARKLqtLQDVGLgyiklgqpAT-------TLSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFHDIRKLLEVLHRLV 876
|
90 100 110
....*....|....*....|....*....|....*..
gi 2559317375 191 KAGHTVIMVTHDPGIAANANRIIEI------RDGEII 221
Cdd:COG0178 877 DKGNTVVVIEHNLDVIKTADWIIDLgpeggdGGGEIV 913
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
19-49 |
2.82e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.29 E-value: 2.82e-04
10 20 30
....*....|....*....|....*....|.
gi 2559317375 19 RVHILKDISLSIEKGDFVAIIGQSGSGKSTL 49
Cdd:PRK00349 12 REHNLKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-202 |
4.25e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILgcldtagsgsyridgieTAKMQPDELAALRRERFGF-IFQRYNLlssl 100
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLI-----------------SGELQPSSGTVFRSAKVRMaVFSQHHV---- 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 101 TARDNVALPAVYMGM---GGKERSARADklLQDLGLASKEGNKPG-ELSGGQQQRVSIARALMNGGEIIFADEPTGALDT 176
Cdd:PLN03073 583 DGLDLSSNPLLYMMRcfpGVPEQKLRAH--LGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL 660
|
170 180
....*....|....*....|....*.
gi 2559317375 177 ASgknVMEIIRRLHKAGHTVIMVTHD 202
Cdd:PLN03073 661 DA---VEALIQGLVLFQGGVLMVSHD 683
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
22-201 |
4.49e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGDFVAIIGQSGSGKSTLMNILgcldtAGSGSYRIDGIETAKMQPDELAALRRERFG-FIFQRYNLLSSL 100
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATL-----AGREDYEVTGGTVEFKGKDLLELSPEDRAGeGIFMAFQYPVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 101 TARDN-----VALPAV--YMGMGGKERSARADKLLQDLGLAskegNKPGEL---------SGGQQQRVSIARALMNGGEI 164
Cdd:PRK09580 91 PGVSNqfflqTALNAVrsYRGQEPLDRFDFQDLMEEKIALL----KMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPEL 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 2559317375 165 IFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTH 201
Cdd:PRK09580 167 CILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
36-202 |
5.94e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.53 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 36 VAIIGQSGSGKSTLMN-ILGCLD---------------------------TAGSGSYRI-----DGIETAKMQPDELAAL 82
Cdd:COG0419 26 NLIVGPNGAGKSTILEaIRYALYgkarsrsklrsdlinvgseeasvelefEHGGKRYRIerrqgEFAEFLEAKPSERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 83 RRERFG--FIFQRYNLLSSLTARDNVALpavymgmggkERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMn 160
Cdd:COG0419 106 LKRLLGleIYEELKERLKELEEALESAL----------EELAELQKLKQEILAQLSGLDPIETLSGGERLRLALADLLS- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2559317375 161 ggeiIFADepTGALDTASGKNVMEIIRRLHkaghtviMVTHD 202
Cdd:COG0419 175 ----LILD--FGSLDEERLERLLDALEELA-------IITHV 203
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-204 |
1.02e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.34 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 23 LKDISLSIEKGDFVAIIGQSGSGKSTLMNILGCLDTAGSGSYRIDGietakmqpdelaalrreRFGFIFQRYNLLSSLTA 102
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------------EVSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 103 RDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNKPGELSGGQQQRVSIARALMNGGEIIFADEPTGALDTASGKNV 182
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180
....*....|....*....|..
gi 2559317375 183 MEIIRRLHKAGHTVIMVTHDPG 204
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNLG 204
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
144-216 |
2.17e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.94 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 144 LSGGQQQRVSIARAL-------MNGG---EIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGIAANANRII 213
Cdd:cd03279 124 LSGGETFLASLSLALalsevlqNRGGarlEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRL 203
|
...
gi 2559317375 214 EIR 216
Cdd:cd03279 204 EVI 206
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
144-221 |
2.38e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 144 LSGGQQQRVSIARA----LMNggeIIFA-DEPTGAL---DTAsgkNVMEIIRRLHKAGHTVIMVTHDPGIAANANRIIEI 215
Cdd:COG0178 486 LSGGEAQRIRLATQigsgLVG---VLYVlDEPSIGLhqrDND---RLIETLKRLRDLGNTVIVVEHDEDTIRAADYIIDI 559
|
90
....*....|..
gi 2559317375 216 ------RDGEII 221
Cdd:COG0178 560 gpgageHGGEVV 571
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
75-205 |
5.21e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.30 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 75 QPDELAALRRERFGFIFQRY-------NLLSSLTARDNVALPAVYMGMGGKERSARADKLLQDLGLASKEGNK-----PG 142
Cdd:pfam13304 156 LLDEGLLLEDWAVLDLAADLalfpdlkELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGggelpAF 235
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2559317375 143 ELSGGQQQ---RVSIARALMNGGEIIFADEPTGALDTASGKNVMEIIRRLHKAGHTVIMVTHDPGI 205
Cdd:pfam13304 236 ELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLL 301
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
22-211 |
9.86e-03 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to 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 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 38.34 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 22 ILKDISLSIEKGdFVAIIGQSGSGKSTLMN-ILGCLdtAGSGSYRI--DGIETAKMQ------PDELAALRRERFGFIFQ 92
Cdd:cd03241 11 LIEELELDFEEG-LTVLTGETGAGKSILLDaLSLLL--GGRASADLirSGAEKAVVEgvfdisDEEEAKALLLELGIEDD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 93 RYNLLSSLTARDnvalpavymgmgGKERsARAD------KLLQDLG--------------LASKE--------------- 137
Cdd:cd03241 88 DDLIIRREISRK------------GRSR-YFINgqsvtlKLLRELGsllvdihgqhdhqnLLNPErqldlldgglddvef 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559317375 138 ------GNKPGEL----SGGQQQRV-----SIARALMNGGEIIFaDEptgaLDTA-SGKNVMEIIRRLHK--AGHTVIMV 199
Cdd:cd03241 155 lfstnpGEPLKPLakiaSGGELSRLmlalkAILARKDAVPTLIF-DE----IDTGiSGEVAQAVGKKLKElsRSHQVLCI 229
|
250
....*....|..
gi 2559317375 200 THDPGIAANANR 211
Cdd:cd03241 230 THLPQVAAMADN 241
|
|
| |
