|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-489 |
0e+00 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 1058.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 1 MSSLQILQGTFRLSDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVS 80
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 81 DEWQRNNTDMLGPGEDDTGRTTAEIIQDEVKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
Cdd:PRK10938 81 DEWQRNNTDMLSPGEDDTGRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 161 EPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQALVAQLAHSEQLEGV 240
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQLAHSEQLEGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 241 QLPEPDEPSARHALPANEPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYSNDLTL 320
Cdd:PRK10938 241 QLPEPDEPSARHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 321 FGRRRGSGETIWDIKKHIGYVSSSLHLDYRVSTTVRNVILSGYFDSIGIYQAVSDRQQKLVQQWLDILGIDKRTADAPFH 400
Cdd:PRK10938 321 FGRRRGSGETIWDIKKHIGYVSSSLHLDYRVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPFH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDAPACITHRLEFVPDGG 480
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPACITHRLEFVPDGD 480
|
....*....
gi 16128728 481 LYRYVLTKI 489
Cdd:PRK10938 481 IYRYVQTKL 489
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
258-477 |
1.16e-119 |
|
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: 350.54 E-value: 1.16e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 258 EPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYSNDLTLFGRRRGsGETIWDIKKH 337
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRG-GEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 338 IGYVSSSLHLDYRVSTTVRNVILSGYFDSIGIYQAVSDRQQKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALV 417
Cdd:COG1119 80 IGLVSPALQLRFPRDETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHL-ADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 418 KHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDAPACITHRLEFVP 477
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKD 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-460 |
4.13e-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: 173.17 E-value: 4.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 3 SLQILQGTFRLSDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELP---LLKGERQSQFSHITRLSFEQLQKLV 79
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 80 SDEWQ--RNNTDMLGPGED-----DTGRTTAEIIQDEVKDaprcmqLAQQFGITALLDRRFKYLSTGETRKTLLCQALMS 152
Cdd:COG1123 86 GMVFQdpMTQLNPVTVGDQiaealENLGLSRAEARARVLE------LLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 153 EPDLLILDEPFDGLDVASRQQLAERLASLHQ-SGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELlqqalvaqL 231
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI--------L 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 232 AHSEQLEGVQLPEPDEPSARHALPANEPRIVLNNGVVSYNDR-----PILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLV 306
Cdd:COG1123 232 AAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 307 TG-DHPQgySNDLTLFGR--RRGSGETIWDIKKHIGYV----SSSlhLDYRVstTVRNVILsgyfDSIGIYQAVSDRQ-Q 378
Cdd:COG1123 312 LGlLRPT--SGSILFDGKdlTKLSRRSLRELRRRVQMVfqdpYSS--LNPRM--TVGDIIA----EPLRLHGLLSRAErR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 379 KLVQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNR-QLIRRFVDVLISEGETqLL 456
Cdd:COG1123 382 ERVAELLERVGLPPDLADRYPHELSGGQrQRVA-IARALALEPKLLILDEPTSALDVSVQaQILNLLRDLQRELGLT-YL 459
|
....
gi 16128728 457 FVSH 460
Cdd:COG1123 460 FISH 463
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
256-471 |
2.10e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 153.71 E-value: 2.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 256 ANEPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRRGSGetiwdiK 335
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP-TSGTVRLFGKPPRRA------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 336 KHIGYVSSSLHLDYRVSTTVRNVILSGYFDSIGIYQAVSDRQQKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRA 415
Cdd:COG1121 75 RRIGYVPQRAEVDWDFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDL-ADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128728 416 LVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSHHAEDAPACITH 471
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKT-ILVVTHDLGAVREYFDR 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
263-460 |
4.86e-41 |
|
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: 146.14 E-value: 4.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 263 LNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRrgsgetIWDIKKHIGYVS 342
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP-TSGSIRVFGKP------LEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 343 SSLHLDYRVSTTVRNVILSGYFDSIGIYQAVSDRQQKLVQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPTL 422
Cdd:cd03235 75 QRRSIDRDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSE-LADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128728 423 LILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSH 460
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMT-ILVVTH 190
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-460 |
9.53e-38 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 144.82 E-value: 9.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGE------------RQSQFSHITRLSFEQ----LQKLVSDEWQRNN 87
Cdd:COG0488 19 LSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEvsipkglrigylPQEPPLDDDLTVLDTvldgDAELRALEAELEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 88 TDMLGPGEDDTGRTTAEIIQD-EVKDA----PRCMQLAQQFGIT-ALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
Cdd:COG0488 99 LEAKLAEPDEDLERLAELQEEfEALGGweaeARAEEILSGLGFPeEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 162 PFDGLDVASRQQLAERLASLHqsgITLVLV------LNRF-DEIPEfvqfagvLADCTLAE-TG-------AKEELL--- 223
Cdd:COG0488 179 PTNHLDLESIEWLEEFLKNYP---GTVLVVshdryfLDRVaTRILE-------LDRGKLTLyPGnysayleQRAERLeqe 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 224 ------QQALVAQL----------------AHS-----EQLEGVQLPEPDEPsARHALPANEPR----IVLNNGVVSYND 272
Cdd:COG0488 249 aaayakQQKKIAKEeefirrfrakarkakqAQSrikalEKLEREEPPRRDKT-VEIRFPPPERLgkkvLELEGLSKSYGD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 273 RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQGysndltlfGRRRgSGETIwdikkHIGYVS---SSLHLD 348
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELePDS--------GTVK-LGETV-----KIGYFDqhqEELDPD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 349 YRVSTTVRnvilsgyfdsigiyQAVSDRQQKLVQQWLDILGIDKRTADAPFHSLSWGQQ-RLALIvRALVKHPTLLILDE 427
Cdd:COG0488 394 KTVLDELR--------------DGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKaRLALA-KLLLSPPNVLLLDE 458
|
490 500 510
....*....|....*....|....*....|....
gi 16128728 428 PLQGLDPLNRQLIrrfVDVLIS-EGeTqLLFVSH 460
Cdd:COG0488 459 PTNHLDIETLEAL---EEALDDfPG-T-VLLVSH 487
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
276-428 |
1.48e-34 |
|
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: 126.61 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdHPQGYSNDLTLFGRRRgSGETIWDIKKHIGYVSSSLHLDYRvSTTV 355
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG-LLSPTEGTILLDGQDL-TDDERKSLRKEIGYVFQDPQLFPR-LTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128728 356 RNVILSGYFDsiGIYQAVSDRQQKLVQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEP 428
Cdd:pfam00005 78 ENLRLGLLLK--GLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
261-465 |
5.24e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 127.87 E-value: 5.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPqgYSNDLTLFGRRRGSGETiwDIKKHIG 339
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGlLRP--TSGEVRVLGEDVARDPA--EVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 340 YVSSSLHLDYRVstTVR-NVILSGyfdsiGIYQAVSDRQQKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVK 418
Cdd:COG1131 77 YVPQEPALYPDL--TVReNLRFFA-----RLYGLPRKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128728 419 HPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSHHAEDA 465
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKT-VLLSTHYLEEA 194
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
24-231 |
2.14e-30 |
|
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: 118.65 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHitRLSFEQLQKL------VSDEWQRNNT------DML 91
Cdd:COG1119 24 WTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGE--RRGGEDVWELrkriglVSPALQLRFPrdetvlDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 92 GPGEDDT----GRTTAEIIQdevkdapRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
Cdd:COG1119 102 LSGFFDSiglyREPTDEQRE-------RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 168 VASRQQLAERLASLHQSG-ITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQALVAQL 231
Cdd:COG1119 175 LGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEA 239
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
260-461 |
3.65e-30 |
|
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: 117.84 E-value: 3.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 260 RIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRrgsgetIWDIK---- 335
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKP-SSGEVLLDGRD------LASLSrrel 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 336 -KHIGYVSSSLHLDYRVstTVRNVILSGYFDSIGIYQAVSDRQQKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVR 414
Cdd:COG1120 74 aRRIAYVPQEPPAPFGL--TVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHL-ADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128728 415 ALVKHPTLLILDEPLQGLDPLNR----QLIRRFVDvliSEGETqLLFVSHH 461
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQlevlELLRRLAR---ERGRT-VVMVLHD 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
261-465 |
9.96e-30 |
|
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: 116.50 E-value: 9.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQgysndltlfgrrrgSGETIWD------ 333
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLlKPD--------------SGSILIDgedvrk 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 334 ----IKKHIGYVSSSLHLDYRvsTTVRNVILsgYFdsIGIYQAVSDRQQKLVQQWLDILGIDKrTADAPFHSLSWGQQRL 409
Cdd:COG4555 68 epreARRQIGVLPDERGLYDR--LTVRENIR--YF--AELYGLFDEELKKRIEELIELLGLEE-FLDRRVGELSTGMKKK 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128728 410 ALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSHHAEDA 465
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKT-VLFSSHIMQEV 195
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
261-465 |
6.28e-29 |
|
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: 113.97 E-value: 6.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYND-RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRRRgSGETIWDIKKHI 338
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGlLKPT--SGEVLVDGKDI-TKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 339 GYV----SSSLhldyrVSTTV--------RNvilsgyfdsigiyQAVSDRQ-QKLVQQWLDILGIDKRtADAPFHSLSWG 405
Cdd:COG1122 78 GLVfqnpDDQL-----FAPTVeedvafgpEN-------------LGLPREEiRERVEEALELVGLEHL-ADRPPHELSGG 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 406 QQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSHHAEDA 465
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKT-VIIVTHDLDLV 197
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
259-474 |
1.22e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 112.19 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 259 PRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPqgYSNDLTLFGRRRGSGETiwDIKKH 337
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGlLPP--SAGEVLWNGEPIRDARE--DYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 338 IGYVSsslHLD--YRVSTTVRNVILSGyfdsiGIYQAVSDRQQklVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRA 415
Cdd:COG4133 77 LAYLG---HADglKPELTVRENLRFWA-----ALYGLRADREA--IDEALEAVGLAGL-ADLPVRQLSAGQKRRVALARL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 416 LVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSHHAEDAPACITHRLE 474
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQPLELAAARVLDLG 203
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
262-475 |
3.23e-28 |
|
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: 111.40 E-value: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 262 VLNNGVVSYND--RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRRGSgETIWDIKKHIG 339
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP-TSGEVLVDGKDLTK-LSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 340 YV----SSSLhldyrVSTTVRNVILSGyFDSIGIYQavsDRQQKLVQQWLDILGIDKRtADAPFHSLSWGQ-QRLALIVr 414
Cdd:cd03225 79 LVfqnpDDQF-----FGPTVEEEVAFG-LENLGLPE---EEIEERVEEALELVGLEGL-RDRSPFTLSGGQkQRVAIAG- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128728 415 ALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSHHAEDAPACITHRLEF 475
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKT-IIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
261-465 |
8.33e-28 |
|
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: 109.02 E-value: 8.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGrrRGSGETIWDIKKHIGY 340
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKP-DSGEIKVLG--KDIKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 341 VSSSLHLDYRVstTVR-NVILSGyfdsigiyqavsdrqqklvqqwldilgidkrtadapfhslswGQQRLALIVRALVKH 419
Cdd:cd03230 78 LPEEPSLYENL--TVReNLKLSG------------------------------------------GMKQRLALAQALLHD 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128728 420 PTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSHHAEDA 465
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKEGKT-ILLSSHILEEA 158
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
268-463 |
3.89e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 108.36 E-value: 3.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 268 VSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRRRgSGETIWDIKKHIGYVSSSLH 346
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADlDPPT--SGEIYLDGKPL-SAMPPPEWRRQVAYVPQEPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 347 LdyrVSTTVRNVILSGYfdsiGIYQAVSDRQQklVQQWLDILGIDKRTADAPFHSLSWGQ-QRLALIvRALVKHPTLLIL 425
Cdd:COG4619 85 L---WGGTVRDNLPFPF----QLRERKFDRER--ALELLERLGLPPDILDKPVERLSGGErQRLALI-RALLLQPDVLLL 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128728 426 DEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAE 463
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPE 192
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
263-473 |
5.33e-27 |
|
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: 106.18 E-value: 5.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 263 LNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRRGSGEtIWDIKKHIGYVS 342
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP-TSGEILIDGKDIAKLP-LEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 343 SslhldyrvsttvrnviLSGyfdsigiyqavsdrqqklvqqwldilgidkrtadapfhslswGQQRLALIVRALVKHPTL 422
Cdd:cd00267 80 Q----------------LSG------------------------------------------GQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128728 423 LILDEPLQGLDPLNRQLIRRFVDVLISEGeTQLLFVSHHAEDAPACITHRL 473
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAADRVI 151
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-210 |
1.64e-26 |
|
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: 105.02 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 5 QILQGTFRLSDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVSDEWQ 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 85 rnntdmlgpgeddtgrttaeiiqdevkdaprcmqlaqqfgitalldrrfkyLSTGETRKTLLCQALMSEPDLLILDEPFD 164
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128728 165 GLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLAD 210
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
269-465 |
1.29e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 103.47 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 269 SYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgysndltLFGRRRGSGetiwdiKKHIGYVSSSLHLD 348
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRP-------TSGTVRRAG------GARVAYVPQRSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 349 YRVSTTVRNVILSGYFDSIGIYQAVSDRQQKLVQQWLDILGIDkRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEP 428
Cdd:NF040873 68 DSLPLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 16128728 429 LQGLDPLNRQLIRRFVDVLISEGETqLLFVSHHAEDA 465
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGAT-VVVVTHDLELV 182
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
263-484 |
4.06e-25 |
|
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: 101.74 E-value: 4.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 263 LNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqGYSNDLTLFGRrrgsgeTIWDIK-----KH 337
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK-PSSGEILLDGK------DLASLSpkelaRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 338 IGYVSsslhldyrvsttvrnvilsgyfdsigiyqavsdrqqklvqQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALV 417
Cdd:cd03214 75 IAYVP----------------------------------------QALELLGLAH-LADRPFNELSGGERQRVLLARALA 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128728 418 KHPTLLILDEPLQGLDPLNR----QLIRRFVDvliSEGETqLLFVSHHAEDApACITHRLEFVPDGGLYRY 484
Cdd:cd03214 114 QEPPILLLDEPTSHLDIAHQiellELLRRLAR---ERGKT-VVMVLHDLNLA-ARYADRVILLKDGRIVAQ 179
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
24-231 |
4.95e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 103.25 E-value: 4.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshITRLSfeqlqKLVSDEW-------QRNNTD------- 89
Cdd:COG1121 27 LTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGT-------VRLFG-----KPPRRARrrigyvpQRAEVDwdfpitv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 90 ----MLG--PGEDDTGRTTAeiiqdevKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
Cdd:COG1121 95 rdvvLMGryGRRGLFRRPSR-------ADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 164 DGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAEtGAKEELLQQALVAQL 231
Cdd:COG1121 168 AGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPENLSRA 234
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-202 |
9.03e-25 |
|
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: 101.77 E-value: 9.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 14 SDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVSDEWQRNNTDMLGP 93
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPDDQFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 94 geddtgRTTAEII---------QDEVKDapRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
Cdd:cd03225 92 ------TVEEEVAfglenlglpEEEIEE--RVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128728 165 GLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFV 202
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELA 201
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-198 |
1.27e-24 |
|
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: 101.46 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 10 TFRLSDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshITRL--SFEQLQKLVSDEWQRNN 87
Cdd:cd03235 6 TVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGS-------IRVFgkPLEKERKRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 88 TD-----------MLGPgeddTGRTTAEIIQDEvKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDL 156
Cdd:cd03235 79 IDrdfpisvrdvvLMGL----YGHKGLFRRLSK-ADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16128728 157 LILDEPFDGLDVASRQQLAERLASLHQSGITLV-------LVLNRFDEI 198
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILvvthdlgLVLEYFDRV 202
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
24-225 |
3.45e-24 |
|
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: 101.09 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKL--VSDE---WQRN----NTDMLGPG 94
Cdd:COG4555 22 FTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIgvLPDErglYDRLtvreNIRYFAEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 95 EDDTGRTTAEIIQDevkdaprcmqLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
Cdd:COG4555 102 YGLFDEELKKRIEE----------LIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 175 AERLASLHQSGITLVL-------VLNRFDEIpefvqfaGVLADCTLAETGAKEELLQQ 225
Cdd:COG4555 172 REILRALKKEGKTVLFsshimqeVEALCDRV-------VILHKGKVVAQGSLDELREE 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
261-474 |
6.64e-24 |
|
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: 98.22 E-value: 6.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDR--PILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHpQGYSNDLTLFGrRRGSGETIWDIKKHI 338
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLY-DPTSGEILIDG-VDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 339 GYVSSSLHLdyrVSTTVRNVILSGyfdsigiyqavsdrqqklvqqwldilgidkrtadapfhslswGQ-QRLAlIVRALV 417
Cdd:cd03228 79 AYVPQDPFL---FSGTIRENILSG------------------------------------------GQrQRIA-IARALL 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128728 418 KHPTLLILDEPLQGLDPLNRQLIRRFVDVLiSEGETQLLfvshhaedapacITHRLE 474
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRAL-AKGKTVIV------------IAHRLS 156
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
261-465 |
1.37e-23 |
|
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: 98.60 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGR--RRGSGEtiwdIKKH 337
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTlLKPT--SGRATVAGHdvVREPRE----VRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 338 IGYVSSSLHLDyRVSTTVRNVILSGyfdsiGIYQAVSDRQQKLVQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALV 417
Cdd:cd03265 75 IGIVFQDLSVD-DELTGWENLYIHA-----RLYGVPGAERRERIDELLDFVGLLE-AADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16128728 418 KHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEA 195
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
243-468 |
1.65e-23 |
|
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: 103.69 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 243 PEPDEPSARHALPAnEPRIVLNNGVVSY--NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHP--QGysnDL 318
Cdd:COG4987 317 PAVTEPAEPAPAPG-GPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDpqSG---SI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 319 TLFGR--RRGSGETIWdikKHIGYVSSSLHLdyrVSTTVRNVILSGYfdsigiyQAVSDRQqklVQQWLDILGIDKRTAD 396
Cdd:COG4987 393 TLGGVdlRDLDEDDLR---RRIAVVPQRPHL---FDTTLRENLRLAR-------PDATDEE---LWAALERVGLGDWLAA 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 397 APF----------HSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLN-RQLIRRFVDVLisEGETqLLFVSHHAED 464
Cdd:COG4987 457 LPDgldtwlgeggRRLSGGErRRLAL-ARALLRDAPILLLDEPTEGLDAATeQALLADLLEAL--AGRT-VLLITHRLAG 532
|
....
gi 16128728 465 APAC 468
Cdd:COG4987 533 LERM 536
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
258-483 |
3.36e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 97.81 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 258 EPRIVLNNGVVSY----NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQG-------------YSNDLT 319
Cdd:COG1136 2 SPLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGlDRPTSgevlidgqdisslSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 320 LFgRRRgsgetiwdikkHIGYVSSSLHLdyrVST-TVR-NVILSGYFDSIGIYQAvsdrqQKLVQQWLDILGIDKRtADA 397
Cdd:COG1136 82 RL-RRR-----------HIGFVFQFFNL---LPElTALeNVALPLLLAGVSRKER-----RERARELLERVGLGDR-LDH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 398 PFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNR----QLIRRFVDvliSEGETqLLFVSHHAEDAPACitHR 472
Cdd:COG1136 141 RPSQLSGGQqQRVA-IARALVNRPKLILADEPTGNLDSKTGeevlELLRELNR---ELGTT-IVMVTHDPELAARA--DR 213
|
250
....*....|.
gi 16128728 473 LEFVPDGGLYR 483
Cdd:COG1136 214 VIRLRDGRIVS 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
24-227 |
3.59e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 97.83 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELP------LLKGERqsqfshITRLSFEQLQKL--VSDEwqrnntdmLGPGE 95
Cdd:COG1131 21 LTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRptsgevRVLGED------VARDPAEVRRRIgyVPQE--------PALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 96 DDTGRTTAEIIQ-----DEVKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
Cdd:COG1131 87 DLTVRENLRFFArlyglPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128728 171 RQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQAL 227
Cdd:COG1131 167 RRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
24-190 |
4.05e-23 |
|
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: 96.78 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshITRlsFEQLQKLVSDEWQRnntDMLGPGEDD---TGR 100
Cdd:COG4133 23 FTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGE-------VLW--NGEPIRDAREDYRR---RLAYLGHADglkPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 101 TTAEIIQ------DEVKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
Cdd:COG4133 91 TVRENLRfwaalyGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
|
170
....*....|....*.
gi 16128728 175 AERLASLHQSGITLVL 190
Cdd:COG4133 171 AELIAAHLARGGAVLL 186
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
24-226 |
1.09e-22 |
|
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: 96.25 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELP------LLKGErqsqfsHITRLSFEQLQKLV------SDewqrnntDML 91
Cdd:COG1122 22 LSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKptsgevLVDGK------DITKKNLRELRRKVglvfqnPD-------DQL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 92 -GPG-EDD-------TGRTTAEIIQdevkdapRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
Cdd:COG1122 89 fAPTvEEDvafgpenLGLPREEIRE-------RVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128728 163 FDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQA 226
Cdd:COG1122 162 TAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
241-465 |
1.14e-22 |
|
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: 100.99 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 241 QLPEPDEPSARHALPANEP-RIVLNNGVVSY-NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDL 318
Cdd:COG4988 316 DAPEPAAPAGTAPLPAAGPpSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP-YSGSI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 319 TLFGRRRgSGETIWDIKKHIGYVSSSLHLdyrVSTTVRnvilsgyfDSIGIYQAVSDRQQklVQQWLDILGIDKRTADAP 398
Cdd:COG4988 395 LINGVDL-SDLDPASWRRQIAWVPQNPYL---FAGTIR--------ENLRLGRPDASDEE--LEAALEAAGLDEFVAALP 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 399 F----------HSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLiSEGETqLLFVSHHAEDA 465
Cdd:COG4988 461 DgldtplgeggRGLSGGQaQRLAL-ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRT-VILITHRLALL 535
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
261-479 |
1.42e-22 |
|
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: 95.63 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYND----RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRR-RGSGETIWD- 333
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGlDRPT--SGEVRVDGTDiSKLSEKELAa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 334 -IKKHIGYVSSSLHL-DYRvstTVR-NVILsgyfdsIGIYQAVSDRQQKL-VQQWLDILGIDKRtADAPFHSLSWG-QQR 408
Cdd:cd03255 79 fRRRHIGFVFQSFNLlPDL---TALeNVEL------PLLLAGVPKKERRErAEELLERVGLGDR-LNHYPSELSGGqQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128728 409 LAlIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDAPACitHRLEFVPDG 479
Cdd:cd03255 149 VA-IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYA--DRIIELRDG 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-459 |
2.19e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 100.13 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQK----LVSDEwqrnntDMLGPGEddtg 99
Cdd:PRK15439 32 FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlgiyLVPQE------PLLFPNL---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 100 rTTAEII----QDEVKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
Cdd:PRK15439 102 -SVKENIlfglPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 176 ERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQALVAQL---AHSEQLEGVQLPEPDEPSARH 252
Cdd:PRK15439 181 SRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAItpaAREKSLSASQKLWLELPGNRR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 253 ALPANEPRIVLNN----GVVsyndrpilnNLSWQVNPGEHWQIVGPNGAGKSTLLSlvtgdhpqgysndlTLFGRRRGSG 328
Cdd:PRK15439 261 QQAAGAPVLTVEDltgeGFR---------NISLEVRAGEILGLAGVVGAGRTELAE--------------TLYGLRPARG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 329 ETIW----DIKK-------HIGYV-------SSSLHLDYRVSTTVRNVIlsgyFDSIGIYQAVSdRQQKLVQQWLDILGI 390
Cdd:PRK15439 318 GRIMlngkEINAlstaqrlARGLVylpedrqSSGLYLDAPLAWNVCALT----HNRRGFWIKPA-RENAVLERYRRALNI 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128728 391 DKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR----QLIRRfvdvlISEGETQLLFVS 459
Cdd:PRK15439 393 KFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARndiyQLIRS-----IAAQNVAVLFIS 460
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
261-490 |
3.31e-22 |
|
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: 95.44 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSY-NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLL----SLVTGDhpqgySNDLTLFGR--RRGSGETIWD 333
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLrcinRLVEPS-----SGSILLEGTdiTKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 334 IKKHIGYVSSSLHLDYRvSTTVRNViLSGYFDSI----GIYQAVSDRQQKLVQQWLDILGIDKRtADAPFHSLSWGQQRL 409
Cdd:TIGR02315 77 LRRRIGMIFQHYNLIER-LTVLENV-LHGRLGYKptwrSLLGRFSEEDKERALSALERVGLADK-AYQRADQLSGGQQQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 410 ALIVRALVKHPTLLILDEPLQGLDPLN-RQLIRRFVDVLISEGETQLLFVsHHAEDAPACITHRL-----EFVPDGG--- 480
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTsKQVMDYLKRINKEDGITVIINL-HQVDLAKKYADRIVglkagEIVFDGApse 232
|
250
....*....|
gi 16128728 481 LYRYVLTKIY 490
Cdd:TIGR02315 233 LDDEVLRHIY 242
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
261-434 |
5.85e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 93.96 E-value: 5.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSY-NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQgySNDLTLFGR--RRGSGETIWDIKK 336
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEeRPT--SGQVLVNGQdlSRLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 337 HIGYVssslHLDYRVSTTvRNVilsgyFDSIGI---YQAVSDRQ-QKLVQQWLDILGIDKRtADAPFHSLSWG-QQRLAl 411
Cdd:COG2884 80 RIGVV----FQDFRLLPD-RTV-----YENVALplrVTGKSRKEiRRRVREVLDLVGLSDK-AKALPHELSGGeQQRVA- 147
|
170 180
....*....|....*....|...
gi 16128728 412 IVRALVKHPTLLILDEPLQGLDP 434
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDP 170
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
258-465 |
5.94e-22 |
|
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: 98.82 E-value: 5.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 258 EPRIVLNNGVVSY--NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGysndLTLFGRRRGSGETIWDIK 335
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHG----GRISGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 336 -----KHIGYV----SSSLhldyrVSTTVRNVILsgyfDSIGIYQAVSDRQQKLVQQWLDILGIDKRtADAPFHSLSWGQ 406
Cdd:COG1123 78 ealrgRRIGMVfqdpMTQL-----NPVTVGDQIA----EALENLGLSRAEARARVLELLEAVGLERR-LDRYPHQLSGGQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 407 QRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVV 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
261-460 |
9.44e-22 |
|
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: 94.10 E-value: 9.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSY----NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRRGSGETIWdIKK 336
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP-WSGEVTFDGRPVTRRRRKA-FRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 337 HIGYVS----SSLHLDYRVSTTVRNVILSgyfdsigiyQAVSDRQQKlVQQWLDILGIDKRTADAPFHSLSWGQ-QRLAl 411
Cdd:COG1124 80 RVQMVFqdpyASLHPRHTVDRILAEPLRI---------HGLPDREER-IAELLEQVGLPPSFLDRYPHQLSGGQrQRVA- 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16128728 412 IVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSH 460
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSH 197
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
254-479 |
1.66e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.87 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 254 LPANEPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETIW 332
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGlTHPDA--------GSISLCGEPVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 333 DIKKH----IGYVSS--SLHLDYRVSTTVRnvILSGYFdsiGIYQAVSdrqQKLVQQWLDILGIDKRtADAPFHSLSWGQ 406
Cdd:PRK13537 73 SRARHarqrVGVVPQfdNLDPDFTVRENLL--VFGRYF---GLSAAAA---RALVPPLLEFAKLENK-ADAKVGELSGGM 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128728 407 QRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLfVSHHAEDAPAcITHRLEFVPDG 479
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILL-TTHFMEEAER-LCDRLCVIEEG 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
222-465 |
1.68e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 95.28 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 222 LLQQALVAQLAHSEQLEGVQLPEPDEPSARHALPANEPRIVLNNGVV--SYNDRPILNNLSWQVNPGEHWQIVGPNGAGK 299
Cdd:PRK13536 1 LLTRAVAEEAPRRLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVskSYGDKAVVNGLSFTVASGECFGLLGPNGAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 300 STLLSLVTGDHPQGYSNdLTLFG-----RRRGSgetiwdiKKHIGYVSSSLHLDYRVstTVRNVILSgyfdsIGIYQAVS 374
Cdd:PRK13536 81 STIARMILGMTSPDAGK-ITVLGvpvpaRARLA-------RARIGVVPQFDNLDLEF--TVRENLLV-----FGRYFGMS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 375 DRQ-QKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGET 453
Cdd:PRK13536 146 TREiEAVIPSLLEFARLESK-ADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKT 224
|
250
....*....|..
gi 16128728 454 QLLfVSHHAEDA 465
Cdd:PRK13536 225 ILL-TTHFMEEA 235
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
269-460 |
3.46e-21 |
|
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: 91.51 E-value: 3.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 269 SYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRRRGSGETIWdikKHIGyvssSLhL 347
Cdd:cd03268 9 TYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGlIKPD--SGEITFDGKSYQKNIEAL---RRIG----AL-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 348 DYRvsttvrnvILSGY---FDSIGIYQAVSDRQQKLVQQWLDILGIdKRTADAPFHSLSWG-QQRLAlIVRALVKHPTLL 423
Cdd:cd03268 79 EAP--------GFYPNltaRENLRLLARLLGIRKKRIDEVLDVVGL-KDSAKKKVKGFSLGmKQRLG-IALALLGNPDLL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 16128728 424 ILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSH 460
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQGIT-VLISSH 184
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
269-463 |
3.88e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 93.63 E-value: 3.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 269 SYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG--DHPQGYsndLTLFGRRRGSgetiwDIKKHIGYV--SSS 344
Cdd:COG4152 10 RFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGilAPDSGE---VLWDGEPLDP-----EDRRRIGYLpeERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 345 LhldYRvSTTVRNVILsgYFDSI-GIYQAVSDRQqklVQQWLDILGIDKRtADAPFHSLSWG-QQRLALIVrALVKHPTL 422
Cdd:COG4152 82 L---YP-KMKVGEQLV--YLARLkGLSKAEAKRR---ADEWLERLGLGDR-ANKKVEELSKGnQQKVQLIA-ALLHDPEL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16128728 423 LILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSH---HAE 463
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAKGTT-VIFSSHqmeLVE 193
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
255-460 |
4.80e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 92.46 E-value: 4.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 255 PANEPRIVLNNGVVSY----NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGE 329
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGlEKPTS--------GEVLVDGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 330 TIWDIKKHIGYV--SSSLhLDYRvstTVR-NVILSgyFDSIGIYQAvsdRQQKLVQQWLDILGIDKRtADA-PfHSLSWG 405
Cdd:COG1116 74 PVTGPGPDRGVVfqEPAL-LPWL---TVLdNVALG--LELRGVPKA---ERRERARELLELVGLAGF-EDAyP-HQLSGG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128728 406 -QQRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSH 460
Cdd:COG1116 143 mRQRVA-IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTH 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
263-428 |
5.52e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 5.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 263 LNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgysndltlfgrrrgSGETIWDIKKHIGYV 341
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGeLEPD--------------SGEVSIPKGLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 342 SSSLHLDyrVSTTVRNVILSGY---------------------------------FDSIGIYQAVSDrqqklVQQWLDIL 388
Cdd:COG0488 67 PQEPPLD--DDLTVLDTVLDGDaelraleaeleeleaklaepdedlerlaelqeeFEALGGWEAEAR-----AEEILSGL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16128728 389 GIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEP 428
Cdd:COG0488 140 GFPEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
261-461 |
7.02e-21 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 91.66 E-value: 7.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSY-NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqGYSNDLTLFGRR--RGSGETIWDIKKH 337
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVE-PTSGEILVDGQDvtALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 338 IGYVSSSLHLDYRvSTTVRNViLSGYFDSIGIYQAV----SDRQQKLVQQWLDILGIDKRtADAPFHSLSWGQ-QRLAlI 412
Cdd:COG3638 82 IGMIFQQFNLVPR-LSVLTNV-LAGRLGRTSTWRSLlglfPPEDRERALEALERVGLADK-AYQRADQLSGGQqQRVA-I 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16128728 413 VRALVKHPTLLILDEPLQGLDPLN-RQLIRRFVDVLISEGETqLLFVSHH 461
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTaRQVMDLLRRIAREDGIT-VVVNLHQ 206
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
261-465 |
1.06e-20 |
|
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: 90.27 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGYSndlTLFGRRRGSGETIWdiKKHIG 339
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlERPDSGE---ILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 340 YV--SSSL--HLdyrvstTVR-NVilsgyfdSIGIYQAVSDRQQ--KLVQQWLDILGIDkRTADAPFHSLSWGQQRLALI 412
Cdd:cd03259 76 MVfqDYALfpHL------TVAeNI-------AFGLKLRGVPKAEirARVRELLELVGLE-GLLNRYPHELSGGQQQRVAL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128728 413 VRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEA 194
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
24-192 |
2.55e-20 |
|
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: 88.26 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVSdewqrnntdmLGPgeddtgrtta 103
Cdd:cd03214 20 LSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIA----------YVP---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 104 eiiqdevkdaprcmQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASL-H 182
Cdd:cd03214 80 --------------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLaR 145
|
170
....*....|
gi 16128728 183 QSGITLVLVL 192
Cdd:cd03214 146 ERGKTVVMVL 155
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
261-456 |
2.56e-20 |
|
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: 89.93 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSY-NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLS----LVTGDHPQGYSNDLtlfGRRRGSGETIWDIK 335
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRclngLVEPTSGSVLIDGT---DINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 336 KHIGYVSSSLHLDYRVStTVRNViLSGYFDSIGIYQA----VSDRQQKLVQQWLDILGIDKRtADAPFHSLSWGQQRLAL 411
Cdd:cd03256 78 RQIGMIFQQFNLIERLS-VLENV-LSGRLGRRSTWRSlfglFPKEEKQRALAALERVGLLDK-AYQRADQLSGGQQQRVA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128728 412 IVRALVKHPTLLILDEPLQGLDPLN-RQLIRRFVDVLISEGETQLL 456
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASsRQVMDLLKRINREEGITVIV 200
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
274-460 |
3.37e-20 |
|
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: 89.07 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 274 PILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETIWDIKKHIGYV--SSSLhLDYR 350
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGlERPTS--------GEVLVDGEPVTGPGPDRGYVfqQDAL-LPWL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 351 vstTVR-NVILsgyfdsiGI-YQAVSDRQQK-LVQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPTLLILDE 427
Cdd:cd03293 89 ---TVLdNVAL-------GLeLQGVPKAEAReRAEELLELVGLSG-FENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190
....*....|....*....|....*....|...
gi 16128728 428 PLQGLDPLNRQLIRRFVDVLISEGETQLLFVSH 460
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTH 190
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
225-468 |
3.93e-20 |
|
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: 93.12 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 225 QALVAQLAHSEQLEGVQLPEPDEPSarhalpanePRIVLNNGVVSYNDR-PILNNLSWQVNPGEHWQIVGPNGAGKSTLL 303
Cdd:TIGR02857 295 EALFAVLDAAPRPLAGKAPVTAAPA---------SSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 304 SLVTGDHPQGYsndltlfGRRRGSGETIWDIK-----KHIGYVSSSLHLdyrVSTTVRnvilsgyfDSIGIYQAVSDRQQ 378
Cdd:TIGR02857 366 NLLLGFVDPTE-------GSIAVNGVPLADADadswrDQIAWVPQHPFL---FAGTIA--------ENIRLARPDASDAE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 379 klVQQWLDILGIDKRTADAPF----------HSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVL 447
Cdd:TIGR02857 428 --IREALERAGLDEFVAALPQgldtpigeggAGLSGGQaQRLAL-ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL 504
|
250 260
....*....|....*....|.
gi 16128728 448 iSEGETqLLFVSHHAEDAPAC 468
Cdd:TIGR02857 505 -AQGRT-VLLVTHRLALAALA 523
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
223-476 |
4.77e-20 |
|
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: 93.36 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 223 LQQALVA--QLAHSEQLEgvqlPEPDEPSARHALPANEPRIVLNNgvVSY----NDRPILNNLSWQVNPGEHWQIVGPNG 296
Cdd:COG2274 438 FQDAKIAleRLDDILDLP----PEREEGRSKLSLPRLKGDIELEN--VSFrypgDSPPVLDNISLTIKPGERVAIVGRSG 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 297 AGKSTLLSLVTG-DHPQ-------GYsnDLTLFGRRrgsgetiwDIKKHIGYVSSSLHLdyrVSTTVRNVILSGYFDsig 368
Cdd:COG2274 512 SGKSTLLKLLLGlYEPTsgrilidGI--DLRQIDPA--------SLRRQIGVVLQDVFL---FSGTIRENITLGDPD--- 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 369 iyqaVSDRQqklVQQWLDILGIDKRTADAP--FH--------SLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNR 437
Cdd:COG2274 576 ----ATDEE---IIEAARLAGLHDFIEALPmgYDtvvgeggsNLSGGQrQRLA-IARALLRNPRILILDEATSALDAETE 647
|
250 260 270
....*....|....*....|....*....|....*....
gi 16128728 438 QLIRRFVDvLISEGETQLLfvshhaedapacITHRLEFV 476
Cdd:COG2274 648 AIILENLR-RLLKGRTVII------------IAHRLSTI 673
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
24-231 |
8.01e-20 |
|
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: 88.56 E-value: 8.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGE-----RQsqfshITRLSFEQLQKLVSdeW--QRNNTD------- 89
Cdd:COG1120 22 LSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvlldgRD-----LASLSRRELARRIA--YvpQEPPAPfgltvre 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 90 --MLG--PGEDDTGRTTAEiiqdevkDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
Cdd:COG1120 95 lvALGryPHLGLFGRPSAE-------DREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128728 166 LDVASRQQLAERLASL-HQSGITLVLV---LN---RF-DEIpefvqfaGVLADCTLAETGAKEELLQQALVAQL 231
Cdd:COG1120 168 LDLAHQLEVLELLRRLaRERGRTVVMVlhdLNlaaRYaDRL-------VLLKDGRIVAQGPPEEVLTPELLEEV 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
257-465 |
1.21e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 90.16 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 257 NEPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRrrgsgetiwDI- 334
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfETPD--SGRILLDGR---------DVt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 335 -----KKHIGYVSSSL----HLdyrvstTVR-NVilsGYfdsiGI-YQAVS-DRQQKLVQQWLDILGIDKRtADAPFHSL 402
Cdd:COG3842 71 glppeKRNVGMVFQDYalfpHL------TVAeNV---AF----GLrMRGVPkAEIRARVAELLELVGLEGL-ADRYPHQL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128728 403 SWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:COG3842 137 SGGQqQRVAL-ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEA 199
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
269-465 |
1.68e-19 |
|
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: 86.95 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 269 SYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgysndLTLfgrrRGSGETIWD-------IKKHIGYV 341
Cdd:cd03269 9 RFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG---------IIL----PDSGEVLFDgkpldiaARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 342 SSSLHLdYRvSTTVRNVILsgYFDSIgiyQAVSDRQ-QKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHP 420
Cdd:cd03269 76 PEERGL-YP-KMKVIDQLV--YLAQL---KGLKKEEaRRRIDEWLERLELSEY-ANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16128728 421 TLLILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSHHAEDA 465
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARAGKT-VILSTHQMELV 191
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
261-465 |
2.62e-19 |
|
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: 86.79 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFG--RRRGSGETIWDIKKH 337
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGlLRPD--SGEVLIDGedISGLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 338 IGYV--SSSLhldyrvsttvrnvilsgyFDSIGIYQAVS-----------DRQQKLVQQWLDILGI----DKRTADapfh 400
Cdd:cd03261 79 MGMLfqSGAL------------------FDSLTVFENVAfplrehtrlseEEIREIVLEKLEAVGLrgaeDLYPAE---- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 401 sLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR----QLIRRFVDVLiseGETQLLfVSHHAEDA 465
Cdd:cd03261 137 -LSGGMKKRVALARALALDPELLLYDEPTAGLDPIASgvidDLIRSLKKEL---GLTSIM-VTHDLDTA 200
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
273-460 |
2.63e-19 |
|
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: 86.79 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 273 RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQG-----YSNDLTLFGRRRGSgetiwDIKKHIGYV----S 342
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGlLKPTSgsiifDGKDLLKLSRRLRK-----IRRKEIQMVfqdpM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 343 SSLHLDYRVSTTVRNVILsgyfdsigIYQAVSDRQQKLVQQWLDI--LGIDKRTADAPFHSLSWGQQRLALIVRALVKHP 420
Cdd:cd03257 93 SSLNPRMTIGEQIAEPLR--------IHGKLSKKEARKEAVLLLLvgVGLPEEVLNRYPHELSGGQRQRVAIARALALNP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16128728 421 TLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSH 460
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITH 204
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
276-461 |
3.92e-19 |
|
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: 86.34 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQGysndltlfGRRRGSGETIWDIKKH------IGY---VSSSL 345
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLrPTS--------GSVLFDGEDITGLPPHeiarlgIGRtfqIPRLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 346 HldyrvSTTVR-NVILSGYFDSIGIYQAVSDRQQKL-----VQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKH 419
Cdd:cd03219 88 P-----ELTVLeNVMVAAQARTGSGLLLARARREERearerAEELLERVGLADL-ADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16128728 420 PTLLILDEPLQGldpLNRQLIRRFVDVL--ISEGETQLLFVSHH 461
Cdd:cd03219 162 PKLLLLDEPAAG---LNPEETEELAELIreLRERGITVLLVEHD 202
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
261-461 |
4.75e-19 |
|
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: 85.32 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGeHWQIVGPNGAGKSTLLSLVTGDHPQGYSNdLTLFGRRRGSGETiwDIKKHIGY 340
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGT-IRIDGQDVLKQPQ--KLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 341 VSSslHLDYRVSTTVRNvilsgYFDSIGIYQAVSDRQQK-LVQQWLDILGIDKRtADAPFHSLSWGQ-QRLAlIVRALVK 418
Cdd:cd03264 77 LPQ--EFGVYPNFTVRE-----FLDYIAWLKGIPSKEVKaRVDEVLELVNLGDR-AKKKIGSLSGGMrRRVG-IAQALVG 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16128728 419 HPTLLILDEPLQGLDPLNRQlirRFVDVLISEGETQLLFVSHH 461
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERI---RFRNLLSELGEDRIVILSTH 187
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
261-461 |
1.42e-18 |
|
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: 83.13 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSY--NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQgySNDLTLFGRRRGSGETiwDIKKH 337
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDlKPQ--QGEITLDGVPVSDLEK--ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 338 IGYVSSSLHLdyrVSTTVRNvilsgyfdSIGIyqavsdrqqklvqqwldilgidkrtadapfhSLSWG-QQRLALiVRAL 416
Cdd:cd03247 77 ISVLNQRPYL---FDTTLRN--------NLGR-------------------------------RFSGGeRQRLAL-ARIL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128728 417 VKHPTLLILDEPLQGLDPLN-RQLIRRFVDVLisEGETqLLFVSHH 461
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITeRQLLSLIFEVL--KDKT-LIWITHH 156
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
258-465 |
1.60e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.45 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 258 EPRIVLNNGVVSY--NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRRRgSGETIWDI 334
Cdd:PRK13635 3 EEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGlLLPE--AGTITVGGMVL-SEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 335 KKHIGYVSSSLHLDYrVSTTVRNVILSGyFDSIGIYQavsDRQQKLVQQWLDILGIDKRTADAPfHSLSWGQ-QRLAlIV 413
Cdd:PRK13635 80 RRQVGMVFQNPDNQF-VGATVQDDVAFG-LENIGVPR---EEMVERVDQALRQVGMEDFLNREP-HRLSGGQkQRVA-IA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16128728 414 RALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA 204
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
276-461 |
2.37e-18 |
|
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: 84.71 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHP--QGysnDLTLFGR-----------RRGSGETiwdikkhigYVS 342
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRptSG---RILFDGRditglpphriaRLGIART---------FQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 343 SSL--HLdyrvstTVR-NVIL-------SGYFDSIGIYQAVSDRQQKL---VQQWLDILGIDKRtADAPFHSLSWGQQRL 409
Cdd:COG0411 88 PRLfpEL------TVLeNVLVaaharlgRGLLAALLRLPRARREEREArerAEELLERVGLADR-ADEPAGNLSYGQQRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128728 410 ALIVRALVKHPTLLILDEPLQGldpLNRQLIRRFVDVLIS----EGETqLLFVSHH 461
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAG---LNPEETEELAELIRRlrdeRGIT-ILLIEHD 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
268-443 |
2.77e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.44 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 268 VSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqGYSNDLTLFGRRRGSGETiWDIKKHIGyV---SSS 344
Cdd:PRK13548 10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS-PDSGEVRLNGRPLADWSP-AELARRRA-VlpqHSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 345 LHLDYrvstTVRNVILSGyfdsIGIYQAVSDRQQKLVQQWLDILGIDKrTADAPFHSLSWG-QQRLALiVRALV------ 417
Cdd:PRK13548 87 LSFPF----TVEEVVAMG----RAPHGLSRAEDDALVAAALAQVDLAH-LAGRDYPQLSGGeQQRVQL-ARVLAqlwepd 156
|
170 180 190
....*....|....*....|....*....|
gi 16128728 418 KHPTLLILDEPLQGLDPLNRQ----LIRRF 443
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHhvlrLARQL 186
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
268-445 |
2.87e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 84.40 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 268 VSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqGYSNDLTLFGRRRGSgETIWDIKKHIGyV---SSS 344
Cdd:COG4559 9 VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELT-PSSGEVRLNGRPLAA-WSPWELARRRA-VlpqHSS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 345 LHLDYrvstTVRNVILsgyfdsIGIY--QAVSDRQQKLVQQWLDILGIDkRTADAPFHSLSWG-QQR------LALIVRA 415
Cdd:COG4559 86 LAFPF----TVEEVVA------LGRAphGSSAAQDRQIVREALALVGLA-HLAGRSYQTLSGGeQQRvqlarvLAQLWEP 154
|
170 180 190
....*....|....*....|....*....|....
gi 16128728 416 LVKHPTLLILDEPLQGLDPLNRQ----LIRRFVD 445
Cdd:COG4559 155 VDGGPRWLFLDEPTSALDLAHQHavlrLARQLAR 188
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
261-460 |
3.26e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.01 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgysndltlfgrrrgSGETIWDIKKHIG 339
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGlVAPD--------------EGVIKRNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 340 YVSSSLHLDYRVSTTV-RNVILSGyfdsiGIYQAvsdrqqklvqqwlDILGIDKRTA-----DAPFHSLSWGQQRLALIV 413
Cdd:PRK09544 71 YVPQKLYLDTTLPLTVnRFLRLRP-----GTKKE-------------DILPALKRVQaghliDAPMQKLSGGETQRVLLA 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16128728 414 RALVKHPTLLILDEPLQGLDpLNRQL-IRRFVDVLISEGETQLLFVSH 460
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVD-VNGQVaLYDLIDQLRRELDCAVLMVSH 179
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
270-465 |
3.83e-18 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 84.75 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 270 YNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGetiWDI-------KKHIGYV 341
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTlLRPTS--------GTARVAG---YDVvreprkvRRSIGIV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 342 SSSLHLDyRVSTTVRNVILSGyfdsiGIYQAVSDRQQKLVQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRALVKHPT 421
Cdd:TIGR01188 72 PQYASVD-EDLTGRENLEMMG-----RLYGLPKDEAEERAEELLELFEL-GEAADRPVGTYSGGMRRRLDIAASLIHQPD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16128728 422 LLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLfVSHHAEDA 465
Cdd:TIGR01188 145 VLFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILL-TTHYMEEA 187
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
24-190 |
4.27e-18 |
|
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: 81.68 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshITRLsfeqlqklvsdewqrnntdmlgpGEDdtgrtta 103
Cdd:cd03230 21 LTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGE-------IKVL-----------------------GKD------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 104 eiIQDEVKDAPR----CMQLAQQFG-ITAlldRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERL 178
Cdd:cd03230 64 --IKKEPEEVKRrigyLPEEPSLYEnLTV---RENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELL 138
|
170
....*....|..
gi 16128728 179 ASLHQSGITLVL 190
Cdd:cd03230 139 RELKKEGKTILL 150
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
263-467 |
8.55e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 81.76 E-value: 8.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 263 LNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQG--YSNDLTLFGRRRGSGETiwdIKKHIGY 340
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsASGEVLLNGRRLTALPA---EQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 341 vsssL--------HLdyrvsTTVRNVILsgyfdsiGIYQAVSDRQQK-LVQQWLDILGIDKRtADAPFHSLSWGQQ-RLA 410
Cdd:COG4136 81 ----LfqddllfpHL-----SVGENLAF-------ALPPTIGRAQRRaRVEQALEEAGLAGF-ADRDPATLSGGQRaRVA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 411 LiVRALVKHPTLLILDEPLQGLDPLNRQLIRRFV-DVLISEGETQLLfVSHHAEDAPA 467
Cdd:COG4136 144 L-LRALLAEPRALLLDEPFSKLDAALRAQFREFVfEQIRQRGIPALL-VTHDEEDAPA 199
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
260-475 |
8.90e-18 |
|
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: 81.87 E-value: 8.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 260 RIVLNNGVVSYNDRPI--LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgysndltLFGRRRGS----GETIW- 332
Cdd:cd03245 2 RIEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAG-----------LYKPTSGSvlldGTDIRq 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 333 ----DIKKHIGYVSSSLHLdyrVSTTVRNVILSGyfdsigiYQAVSDRQqklVQQWLDILGIDKRTADAPF--------- 399
Cdd:cd03245 71 ldpaDLRRNIGYVPQDVTL---FYGTLRDNITLG-------APLADDER---ILRAAELAGVTDFVNKHPNgldlqiger 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128728 400 -HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDplnRQLIRRFVDVLISEGETQLLFVshhaedapacITHRLEF 475
Cdd:cd03245 138 gRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD---MNSEERLKERLRQLLGDKTLII----------ITHRPSL 201
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
222-473 |
9.04e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 85.99 E-value: 9.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 222 LLQQALVAqlahSEQLEGV--QLPEPDEPSARHALPANEPRIVLNNgvVSY---NDRPILNNLSWQVNPGEHWQIVGPNG 296
Cdd:COG1132 303 QLQRALAS----AERIFELldEPPEIPDPPGAVPLPPVRGEIEFEN--VSFsypGDRPVLKDISLTIPPGETVALVGPSG 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 297 AGKSTLLSLVTG--DHPQGysnDLTLFGRrrgsgetiwDIK--------KHIGYVSSSLHLdyrVSTTVRNVILSGYFDs 366
Cdd:COG1132 377 SGKSTLVNLLLRfyDPTSG---RILIDGV---------DIRdltleslrRQIGVVPQDTFL---FSGTIRENIRYGRPD- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 367 igiyqaVSDRQqklVQQWLDILGIDKRTADAPF----------HSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPL 435
Cdd:COG1132 441 ------ATDEE---VEEAAKAAQAHEFIEALPDgydtvvgergVNLSGGQrQRIA-IARALLKDPPILILDEATSALDTE 510
|
250 260 270
....*....|....*....|....*....|....*...
gi 16128728 436 NRQLIRRFVDVLiSEGETqlLFVshhaedapacITHRL 473
Cdd:COG1132 511 TEALIQEALERL-MKGRT--TIV----------IAHRL 535
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
136-433 |
9.45e-18 |
|
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: 85.76 E-value: 9.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLaERLasLHQSGITLVLV----------------LNRFDEIP 199
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWL-ERH--LQEYPGTVVAVthdryfldnvagwileLDRGRGIP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 200 EFVQFAGVL--ADCTLAETGAKEELLQQALV------------------AQLAHSEQLEGVQLPEPDEPSARHALPAneP 259
Cdd:TIGR03719 239 WEGNYSSWLeqKQKRLEQEEKEESARQKTLKrelewvrqspkgrqakskARLARYEELLSQEFQKRNETAEIYIPPG--P 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 260 RivLNNGVV-------SYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHpQGYSNDLTLfgrrrgsGETIw 332
Cdd:TIGR03719 317 R--LGDKVIeaenltkAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQE-QPDSGTIEI-------GETV- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 333 dikkHIGYVSSSL-HLDyrVSTTVRNVIlSGYFDSI--GIYQaVSDR------------QQKLVQQwldilgidkrtada 397
Cdd:TIGR03719 386 ----KLAYVDQSRdALD--PNKTVWEEI-SGGLDIIklGKRE-IPSRayvgrfnfkgsdQQKKVGQ-------------- 443
|
330 340 350
....*....|....*....|....*....|....*.
gi 16128728 398 pfhsLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:TIGR03719 444 ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
276-479 |
1.14e-17 |
|
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: 81.65 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgysndltLFGRRRGSGETI--------WDIKKHIGYVSSSLHL 347
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAG-----------LLEPDAGFATVDgfdvvkepAEARRRLGFVSDSTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 348 DYRVstTVRNVIlsGYFDsiGIY----QAVSDRQQKLVQQwLDILG-IDKRTADapfhsLSWGQQRLALIVRALVKHPTL 422
Cdd:cd03266 90 YDRL--TARENL--EYFA--GLYglkgDELTARLEELADR-LGMEElLDRRVGG-----FSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128728 423 LILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSHHAEDAPA-C----ITHRLEFVPDG 479
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKC-ILFSTHIMQEVERlCdrvvVLHRGRVVYEG 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-468 |
1.19e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.61 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELP------LLKGERQSQFSHitRLSFEQ-----LQKL-VSDEW--QRNntd 89
Cdd:PRK09700 26 LTVYPGEIHALLGENGAGKSTLMKVLSGIHEptkgtiTINNINYNKLDH--KLAAQLgigiiYQELsVIDELtvLEN--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 90 mLGPGEDDTGRTTAEIIQDEVKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
Cdd:PRK09700 101 -LYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 170 SRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQALVAQLAHSEQlegvqlpEPDEPS 249
Cdd:PRK09700 180 EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGREL-------QNRFNA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 250 ARHALPANEPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRGSGE 329
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRA-GGEIRLNGKDISPRS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 330 TIWDIKKHIGYVSSSL-------HLDYRVSTTV-RNVILSGYFDSIGIYQavSDRQQKLVQQWLDILGIDKRTADAPFHS 401
Cdd:PRK09700 332 PLDAVKKGMAYITESRrdngffpNFSIAQNMAIsRSLKDGGYKGAMGLFH--EVDEQRTAENQRELLALKCHSVNQNITE 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128728 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDAPAC 468
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVC 476
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-191 |
1.33e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 80.74 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQS----------QFSHITR---LSFEQLQKLvsDEWQRnntdm 90
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaggarvayvpQRSEVPDslpLTVRDLVAM--GRWAR----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 91 LGPGEDDTGRTTAEIIqdevkdapRCMqlaQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
Cdd:NF040873 86 RGLWRRLTRDDRAAVD--------DAL---ERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180
....*....|....*....|.
gi 16128728 171 RQQLAERLASLHQSGITLVLV 191
Cdd:NF040873 155 RERIIALLAEEHARGATVVVV 175
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
270-468 |
1.72e-17 |
|
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: 81.61 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 270 YNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQGysndltlfGRRRGSGETIWDIKK----HIGYV--- 341
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLlQPTS--------GEVRVAGLVPWKRRKkflrRIGVVfgq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 342 SSSLHLDYRVsttvrnviLSGYFDSIGIYQAVSDRQQKLVQQWLDILGIDkRTADAPFHSLSWGQQRLALIVRALVKHPT 421
Cdd:cd03267 103 KTQLWWDLPV--------IDSFYLLAAIYDLPPARFKKRLDELSELLDLE-ELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128728 422 LLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDAPAC 468
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAL 220
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
274-475 |
2.26e-17 |
|
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: 80.94 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 274 PILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVtgdhpqgYSNDLTLFGR---RRGSGE---------TIWDIKKH-IGY 340
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCI-------YGNYLPDSGSilvRHDGGWvdlaqasprEILALRRRtIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 341 VSSSLHLDYRVSTtvRNVILSGYFDSiGIYQAVSDRQqklVQQWLDILGIDKRTADAPFHSLSWG-QQRLAlIVRALVKH 419
Cdd:COG4778 98 VSQFLRVIPRVSA--LDVVAEPLLER-GVDREEARAR---ARELLARLNLPERLWDLPPATFSGGeQQRVN-IARGFIAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128728 420 PTLLILDEPLQGLDPLNRQLIRRFVDVLISEGeTQLLFVSHHAEDAPACITHRLEF 475
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEEAKARG-TAIIGIFHDEEVREAVADRVVDV 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
261-479 |
2.28e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 80.95 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPIlnNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgysndltlfgrrrgSGETIWDIKKHIG 339
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGfLPPD--------------SGRILWNGQDLTA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 340 YVS-----SSL--------HLdyrvstTVRNVIlsgyfdSIGIYQA--VSDRQQKLVQQWLDILGID---KRTADApfhs 401
Cdd:COG3840 66 LPPaerpvSMLfqennlfpHL------TVAQNI------GLGLRPGlkLTAEQRAQVEQALERVGLAgllDRLPGQ---- 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 402 LSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDApACITHRLEFVPDG 479
Cdd:COG3840 130 LSGGQrQRVAL-ARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDA-ARIADRVLLVADG 206
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
291-465 |
2.63e-17 |
|
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: 80.42 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 291 IVGPNGAGKSTLLSLVTG----DHPQGYSNDLTLFGRRRGSgetiwDI---KKHIGYVSSSL----HLdyrvstTVRNVI 359
Cdd:cd03297 28 IFGASGAGKSTLLRCIAGlekpDGGTIVLNGTVLFDSRKKI-----NLppqQRKIGLVFQQYalfpHL------NVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 360 LSGYfdsigiyQAVSDRQQK-LVQQWLDILGIDKrTADAPFHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNR 437
Cdd:cd03297 97 AFGL-------KRKRNREDRiSVDELLDLLGLDH-LLNRYPAQLSGGEkQRVAL-ARALAAQPELLLLDEPFSALDRALR 167
|
170 180
....*....|....*....|....*...
gi 16128728 438 QLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEA 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
115-449 |
3.31e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.91 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 115 RCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLNR 194
Cdd:COG1129 120 RARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHR 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 195 FDEIPEFVQFAGVLADCTLAETGAKEELLQQALVAQLAhseqleGVQLpepDEPSARHALPANEPRIVLNNgvvsYNDRP 274
Cdd:COG1129 200 LDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMV------GREL---EDLFPKRAAAPGEVVLEVEG----LSVGG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 275 ILNNLSWQVNPGEhwqIV---GPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRRGSGeTIWD-IKKHIGYVS-----SSL 345
Cdd:COG1129 267 VVRDVSFSVRAGE---ILgiaGLVGAGRTELARALFGADPA-DSGEIRLDGKPVRIR-SPRDaIRAGIAYVPedrkgEGL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 346 HLDyrvsTTVR-NVILSGyFDSIGIYQAVSDR-QQKLVQQWLDILGIDKRTADAPFHSLSWG-QQRlALIVRALVKHPTL 422
Cdd:COG1129 342 VLD----LSIReNITLAS-LDRLSRGGLLDRRrERALAEEYIKRLRIKTPSPEQPVGNLSGGnQQK-VVLAKWLATDPKV 415
|
330 340 350
....*....|....*....|....*....|....*.
gi 16128728 423 LILDEPLQGLDPLNR----QLIRRFVD-----VLIS 449
Cdd:COG1129 416 LILDEPTRGIDVGAKaeiyRLIRELAAegkavIVIS 451
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
276-482 |
3.60e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.78 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSW-----------QVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFG---------RRRGSgetiwdik 335
Cdd:PRK10771 4 LTDITWlyhhlpmrfdlTVERGERVAILGPSGAGKSTLLNLIAGFLTPA-SGSLTLNGqdhtttppsRRPVS-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 336 khIGYVSSSL--HLdyrvstTVRNVIlsgyfdSIGIYQAV--SDRQQKLVQQWLDILGIDKRTADAPfHSLSWGQ-QRLA 410
Cdd:PRK10771 75 --MLFQENNLfsHL------TVAQNI------GLGLNPGLklNAAQREKLHAIARQMGIEDLLARLP-GQLSGGQrQRVA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128728 411 LiVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDApACITHRLEFVPDGGLY 482
Cdd:PRK10771 140 L-ARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDA-ARIAPRSLVVADGRIA 209
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
270-465 |
3.93e-17 |
|
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: 79.39 E-value: 3.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 270 YNDRP-ILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQgySNDLTLFGR-----RRGsgetIWDIKKHIGYVS 342
Cdd:TIGR01166 1 YPGGPeVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLlRPQ--SGAVLIDGEpldysRKG----LLERRQRVGLVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 343 S-------SLHLDYRVSTTVRNVILSGyfdsigiyqavsDRQQKLVQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRA 415
Cdd:TIGR01166 75 QdpddqlfAADVDQDVAFGPLNLGLSE------------AEVERRVREALTAVGASG-LRERPTHCLSGGEKKRVAIAGA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16128728 416 LVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSHHAEDA 465
Cdd:TIGR01166 142 VAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMT-VVISTHDVDLA 190
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
267-475 |
4.53e-17 |
|
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: 79.61 E-value: 4.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 267 VVSYNDRP-ILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgysndltLFGRRRGS----GETI--WDIKKHIG 339
Cdd:cd03226 6 SFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG-----------LIKESSGSillnGKPIkaKERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 340 YVSSslHLDYRV-STTVRNVILSGYfdsigiyQAVSDRQQKlVQQWLDILGIDKRTADAPfHSLSWGQ-QRLALIVrALV 417
Cdd:cd03226 75 YVMQ--DVDYQLfTDSVREELLLGL-------KELDAGNEQ-AETVLKDLDLYALKERHP-LSLSGGQkQRLAIAA-ALL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 418 KHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLfvshhaedapacITHRLEF 475
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIV------------ITHDYEF 188
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
115-461 |
1.21e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.86 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 115 RCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ---LAERLASlHQSGITlVLV 191
Cdd:NF033858 116 RIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQfweLIDRIRA-ERPGMS-VLV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 192 LNRFDEipEFVQF-------AG-VLADCT----LAETGAKEelLQQALVAQLAHSEQlegvQLPEPDEPSARHALPANEP 259
Cdd:NF033858 194 ATAYME--EAERFdwlvamdAGrVLATGTpaelLARTGADT--LEAAFIALLPEEKR----RGHQPVVIPPRPADDDDEP 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 260 RIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRGSGETiwDIKKHIG 339
Cdd:NF033858 266 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAS-EGEAWLFGQPVDAGDI--ATRRRVG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 340 YVSSSLHLdYRvSTTVR-NVILSGYfdsigIYQAVSDRQQKLVQQWLDILGIdKRTADAPFHSLSWGQ-QRLALIVrALV 417
Cdd:NF033858 343 YMSQAFSL-YG-ELTVRqNLELHAR-----LFHLPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIrQRLSLAV-AVI 413
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 16128728 418 KHPTLLILDEPLQGLDPLNRQlirRFVDVLIS----EGETqlLFVSHH 461
Cdd:NF033858 414 HKPELLILDEPTSGVDPVARD---MFWRLLIElsreDGVT--IFISTH 456
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
261-460 |
1.86e-16 |
|
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: 75.95 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDhpqgysndltlfgRRRGSGETIWDIKKHIGY 340
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGE-------------LEPDEGIVTWGSTVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 341 vssslhldyrvsttvrnvilsgyfdsigiyqavsdrqqklvqqwldilgidkrtadapFHSLSWGQQRLALIVRALVKHP 420
Cdd:cd03221 68 ----------------------------------------------------------FEQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16128728 421 TLLILDEPLQGLDPLNRQLIRRFvdvlISEGETQLLFVSH 460
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEA----LKEYPGTVILVSH 125
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-163 |
1.86e-16 |
|
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: 76.15 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVSDEWQRNNTD-MLGPGEDDTGRTT 102
Cdd:pfam00005 6 LTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENLRLGLL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 103 AEIIQDEVKDApRCMQLAQQFGITALLDRRFKY----LSTGETRKTLLCQALMSEPDLLILDEPF 163
Cdd:pfam00005 86 LKGLSKREKDA-RAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
269-465 |
1.91e-16 |
|
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: 78.32 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 269 SYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHP--QGysnDLTLFGRRRGSgeTIWDIKKHIGYVSSSLH 346
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRptSG---TAYINGYSIRT--DRKAARQSLGYCPQFDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 347 LDYRVstTVRNVIlsgYFdsIGIYQAVSDRQQKLVQQW-LDILGIDKRtADAPFHSLSWGQQR-LALIVrALVKHPTLLI 424
Cdd:cd03263 86 LFDEL--TVREHL---RF--YARLKGLPKSEIKEEVELlLRVLGLTDK-ANKRARTLSGGMKRkLSLAI-ALIGGPSVLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16128728 425 LDEPLQGLDPlnrqLIRRFVDVLISEGETQ--LLFVSHHAEDA 465
Cdd:cd03263 157 LDEPTSGLDP----ASRRAIWDLILEVRKGrsIILTTHSMDEA 195
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
268-434 |
2.00e-16 |
|
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: 77.78 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 268 VSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgysndltlfgrrrgSGETIWDiKKHIGYVSSSLH 346
Cdd:TIGR01189 8 CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGlLRPD--------------SGEVRWN-GTPLAEQRDEPH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 347 ldyrvsttvRNVILSGYFDSIG----------IYQAVSDRQQKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRAL 416
Cdd:TIGR01189 73 ---------ENILYLGHLPGLKpelsalenlhFWAAIHGGAQRTIEDALAAVGLTGF-EDLPAAQLSAGQQRRLALARLW 142
|
170
....*....|....*...
gi 16128728 417 VKHPTLLILDEPLQGLDP 434
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDK 160
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
225-461 |
2.71e-16 |
|
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: 81.25 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 225 QALVAQLAHSEQLEGVQLPEPDEPSARH----ALPANEPRIVLNNGVVSYNDRPI-LNNLSWQVNPGEHWQIVGPNGAGK 299
Cdd:TIGR02868 295 QQLTRVRAAAERIVEVLDAAGPVAEGSApaagAVGLGKPTLELRDLSAGYPGAPPvLDGVSLDLPPGERVAILGPSGSGK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 300 STLLSLVTG--DHPQGysnDLTLfgrrrgSGETIW-----DIKKHIGYVSSSLHLdyrVSTTVRNVILSGYFDSIGiyQA 372
Cdd:TIGR02868 375 STLLATLAGllDPLQG---EVTL------DGVPVSsldqdEVRRRVSVCAQDAHL---FDTTVRENLRLARPDATD--EE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 373 VSD--RQQKLvQQWLDIL--GIDKR-TADAPfhSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLN-RQLIRRFVD 445
Cdd:TIGR02868 441 LWAalERVGL-ADWLRALpdGLDTVlGEGGA--RLSGGErQRLAL-ARALLADAPILLLDEPTEHLDAETaDELLEDLLA 516
|
250
....*....|....*.
gi 16128728 446 VLisEGETQLLfVSHH 461
Cdd:TIGR02868 517 AL--SGRTVVL-ITHH 529
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
276-465 |
5.60e-16 |
|
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: 77.38 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQGysndltlfGRRRGSGETIWD---IKKHIGYVSSslhlDYRV 351
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIkPDS--------GKILLNGKDITNlppEKRDISYVPQ----NYAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 352 --STTVRNVIlsgyfdSIGIYQAVSDRQQ--KLVQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDE 427
Cdd:cd03299 83 fpHMTVYKNI------AYGLKKRKVDKKEieRKVLEIAEMLGIDHLLNRKP-ETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128728 428 PLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEA 193
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
256-460 |
5.74e-16 |
|
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: 77.33 E-value: 5.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 256 ANEPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRR--RGSGETIW 332
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGlLRPD--SGEILVDGQDitGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 333 DIKKHIGYV--SSSLhldyrvsttvrnvilsgyFDSIGIYQAV----------SDRQ-QKLVQQWLDILG----IDKRTA 395
Cdd:COG1127 79 ELRRRIGMLfqGGAL------------------FDSLTVFENVafplrehtdlSEAEiRELVLEKLELVGlpgaADKMPS 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 396 DapfhsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR----QLIRRFVDVLiseGETQLLfVSH 460
Cdd:COG1127 141 E-----LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSavidELIRELRDEL---GLTSVV-VTH 200
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-190 |
6.01e-16 |
|
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: 76.38 E-value: 6.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGerqsqfshitRLSFEQLQ-KLVSDEWQRNntdMLGPGEDDTGRTT 102
Cdd:cd03231 21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG----------RVLLNGGPlDFQRDSIARG---LLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 103 AEIIQD-----EVKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAER 177
Cdd:cd03231 88 LSVLENlrfwhADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|...
gi 16128728 178 LASLHQSGITLVL 190
Cdd:cd03231 168 MAGHCARGGMVVL 180
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
24-191 |
6.25e-16 |
|
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: 77.09 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELP------LLKGERqsqfshITRLSFEQLQKL-VSDEWQ----------RN 86
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRptsgsvLFDGED------ITGLPPHEIARLgIGRTFQiprlfpeltvLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 87 NTdMLGPGEDDTGRTTAEIIQDEVKDAP-RCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
Cdd:cd03219 95 NV-MVAAQARTGSGLLLARARREEREAReRAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180
....*....|....*....|....*.
gi 16128728 166 LDVASRQQLAERLASLHQSGITLVLV 191
Cdd:cd03219 174 LNPEETEELAELIRELRERGITVLLV 199
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
261-460 |
7.35e-16 |
|
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: 76.41 E-value: 7.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRR-RGSGETIWDIKKHI 338
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLlEEPD--SGTIIIDGLKlTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 339 GYVSSSLHLdYRVSTTVRNVILsgyfdSIGIYQAVSDRQ-QKLVQQWLDILGIDKRtADAPFHSLSWGQ-QRLAlIVRAL 416
Cdd:cd03262 79 GMVFQQFNL-FPHLTVLENITL-----APIKVKGMSKAEaEERALELLEKVGLADK-ADAYPAQLSGGQqQRVA-IARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128728 417 VKHPTLLILDEPLQGLDPlnrQLIRRFVDVLIS---EGETQLLfVSH 460
Cdd:cd03262 151 AMNPKVMLFDEPTSALDP---ELVGEVLDVMKDlaeEGMTMVV-VTH 193
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
261-465 |
1.05e-15 |
|
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: 74.92 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRRRGSGE-TIWDIKKHI 338
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEPD--SGSILIDGEDLTDLEdELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 339 GYVssslhldyrvsttvrnvilsgyFdsigiyqavsdrQQKLVQQWLDILgiDKRTadapfHSLSWGQ-QRLAlIVRALV 417
Cdd:cd03229 79 GMV----------------------F------------QDFALFPHLTVL--ENIA-----LGLSGGQqQRVA-LARALA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16128728 418 KHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEA 164
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
258-449 |
1.33e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.22 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 258 EPRIVLNNGVVSYNDRPILNNLSWQVNPGEhwqIV---GPNGAGKSTLLSLVTG----DHPQGYSND-----LTLFGR-R 324
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGE---IVgllGPNGAGKTTTFYMIVGlvkpDSGRIFLDGedithLPMHKRaR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 325 RGsgetiwdikkhIGYVS--SSL--HLdyrvstTVRNVILsgyfdsigiyqAV--------SDRQQKLvQQWLDILGIDK 392
Cdd:COG1137 78 LG-----------IGYLPqeASIfrKL------TVEDNIL-----------AVlelrklskKEREERL-EELLEEFGITH 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 393 RtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLN----RQLIRRFVD----VLIS 449
Cdd:COG1137 129 L-RKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAvadiQKIIRHLKErgigVLIT 192
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
184-475 |
2.60e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 78.35 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 184 SGITL-----VLVLnrfdeIPEFVQfagvladcTLAETG----AKeellQQALVAQLAHSEQLEgvqLPEPDEPSARHAL 254
Cdd:PRK11174 283 TGVTLfagffVLIL-----APEFYQ--------PLRDLGtfyhAK----AQAVGAAESLVTFLE---TPLAHPQQGEKEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 255 PANEP-RIVLNNGVV-SYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqgYSNDLTLFGRR-RGSGETI 331
Cdd:PRK11174 343 ASNDPvTIEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP--YQGSLKINGIElRELDPES 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 332 WdiKKHIGYVSSSLHLdyrVSTTVRNVILSGYFDS--IGIYQAVsdrQQKLVQQWLDIL--GIDKRTADAPFhSLSWGQ- 406
Cdd:PRK11174 421 W--RKHLSWVGQNPQL---PHGTLRDNVLLGNPDAsdEQLQQAL---ENAWVSEFLPLLpqGLDTPIGDQAA-GLSVGQa 491
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 407 QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVlISEGETQLLfvshhaedapacITHRLEF 475
Cdd:PRK11174 492 QRLAL-ARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLM------------VTHQLED 546
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-463 |
2.81e-15 |
|
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: 77.94 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 15 DTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELP-------LLKGERQSQFSHITRLS------FEQLQKLVSD 81
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtwdgeIYWSGSPLKASNIRDTEragiviIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 82 EWQRNNTDMLGPGEDDTGRTT-AEIIQdevkdapRCMQLAQQFGITALLD-RRFKYLSTGETRKTLLCQALMSEPDLLIL 159
Cdd:TIGR02633 93 LSVAENIFLGNEITLPGGRMAyNAMYL-------RAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 160 DEPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQALVAQLAHSEqLEG 239
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGRE-ITS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 240 VQLPEPDEPS-----ARHaLPANEPrivlnngvvSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGY 314
Cdd:TIGR02633 245 LYPHEPHEIGdvileARN-LTCWDV---------INPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 315 SNDLTLFGRRRGSGETIWDIKKHIGYVSSSLHLDYRVSTTV--RNVILSGYFDSIGIYQAVSDRQQKLVQQWLDILGIDK 392
Cdd:TIGR02633 315 EGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGvgKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKT 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128728 393 RTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAE 463
Cdd:TIGR02633 395 ASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAE 465
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-201 |
2.86e-15 |
|
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: 74.62 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 4 LQILQGTFRLSDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGE-----RQSQFSHITRLSF--EQlQ 76
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEvlfdgKPLDIAARNRIGYlpEE-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 77 KLVSDEWQRNNTDMLGpgeDDTGRTTAEIiqdevkdAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDL 156
Cdd:cd03269 80 GLYPKMKVIDQLVYLA---QLKGLKKEEA-------RRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16128728 157 LILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEF 201
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEEL 194
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
269-447 |
3.14e-15 |
|
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: 74.89 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 269 SYNDRPILNNLSWQVNPGEhwqIV---GPNGAGKSTLLSLVTG----DHPQGY--SNDLT---LFGR-RRGsgetiwdik 335
Cdd:cd03218 9 RYGKRKVVNGVSLSVKQGE---IVgllGPNGAGKTTTFYMIVGlvkpDSGKILldGQDITklpMHKRaRLG--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 336 khIGYV--SSSLHLDYRVSTTVRNVILSGYFDSigiyqavsDRQQKLVQQWLDILGIDKrTADAPFHSLSWGQQRLALIV 413
Cdd:cd03218 77 --IGYLpqEASIFRKLTVEENILAVLEIRGLSK--------KEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIA 145
|
170 180 190
....*....|....*....|....*....|....
gi 16128728 414 RALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVL 447
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL 179
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-460 |
3.14e-15 |
|
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: 77.92 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 10 TFRLSDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAG--ELPLLKG---------------ERQSQFSHITRLSF 72
Cdd:TIGR03269 7 TKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGriiyhvalcekcgyvERPSKVGEPCPVCG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 73 EQLQKLVSDEW----------QRNNTDMLG------------------------PGEDDTGRTtAEIIqDEVKDAPRCMQ 118
Cdd:TIGR03269 87 GTLEPEEVDFWnlsdklrrriRKRIAIMLQrtfalygddtvldnvlealeeigyEGKEAVGRA-VDLI-EMVQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 119 LAQQfgitalldrrfkyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERL-ASLHQSGITLVLVLNRFDE 197
Cdd:TIGR03269 165 IARD-------------LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeEAVKASGISMVLTSHWPEV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 198 IPEFVQFAGVLADCTLAETGAKEELLQQALvAQLAHSEQLEGVQLPEP----DEPSARHalpaneprIVLNNGVVSYNDr 273
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEGTPDEVVAVFM-EGVSEVEKECEVEVGEPiikvRNVSKRY--------ISVDRGVVKAVD- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 274 pilnNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHP--QGYSN--------DLT---LFGRRRgsgetiwdIKKHIGY 340
Cdd:TIGR03269 302 ----NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEptSGEVNvrvgdewvDMTkpgPDGRGR--------AKRYIGI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 341 vsssLHLDYRVSTtvRNVILSGYFDSIGIYQAVSDRQQKLVQQwLDILGIDKRTA----DAPFHSLSWGQQ-RLALiVRA 415
Cdd:TIGR03269 370 ----LHQEYDLYP--HRTVLDNLTEAIGLELPDELARMKAVIT-LKMVGFDEEKAeeilDKYPDELSEGERhRVAL-AQV 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 16128728 416 LVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSH 460
Cdd:TIGR03269 442 LIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSH 486
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
260-461 |
3.47e-15 |
|
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: 74.57 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 260 RIVLNNGVVSYN-DRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG--DHPQGYsndlTLFGRRRGSGETIWDIKK 336
Cdd:cd03254 2 EIEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfyDPQKGQ----ILIDGIDIRDISRKSLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 337 HIGYVSSSLHLdyrVSTTVR-NVILSGyfdsigiyqavSDRQQKLVQQWLDILGIDKRTADAP----------FHSLSWG 405
Cdd:cd03254 78 MIGVVLQDTFL---FSGTIMeNIRLGR-----------PNATDEEVIEAAKEAGAHDFIMKLPngydtvlgenGGNLSQG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128728 406 QQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLiSEGETqLLFVSHH 461
Cdd:cd03254 144 ERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRT-SIIIAHR 197
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-460 |
4.94e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.44 E-value: 4.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELP------------------------LLKGERQSQFSHITRLSFEQLQKLV 79
Cdd:PRK15134 30 LQIEAGETLALVGESGSGKSVTALSILRLLPsppvvypsgdirfhgesllhaseqTLRGVRGNKIAMIFQEPMVSLNPLH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 80 SDEWQRNNTDMLGPG-EDDTGRttAEIIQdevkdaprCMQlaqQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPD 155
Cdd:PRK15134 110 TLEKQLYEVLSLHRGmRREAAR--GEILN--------CLD---RVGIRQAAKRLTDYphqLSGGERQRVMIAMALLTRPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 156 LLILDEPFDGLDVASRQQLAERLASLHQS-GITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELL---QQALVAQL 231
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFsapTHPYTQKL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 232 AHSE-QLEGVQLPEPDEPSAR-HALPANEP-RIVLNNGVVSYNDrpILNNLSWQVNPGEHWQIVGPNGAGKST----LLS 304
Cdd:PRK15134 257 LNSEpSGDPVPLPEPASPLLDvEQLQVAFPiRKGILKRTVDHNV--VVKNISFTLRPGETLGLVGESGSGKSTtglaLLR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 305 LVTGDHPQGYSND-LTLFGRRRgsgetIWDIKKHIGYV----SSSlhLDYRVSttVRNVILSGyfdsIGIYQ---AVSDR 376
Cdd:PRK15134 335 LINSQGEIWFDGQpLHNLNRRQ-----LLPVRHRIQVVfqdpNSS--LNPRLN--VLQIIEEG----LRVHQptlSAAQR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 377 QQKLVQQwLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQL 455
Cdd:PRK15134 402 EQQVIAV-MEEVGLDPETRHRYPAEFSGGQrQRIA-IARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAY 479
|
....*
gi 16128728 456 LFVSH 460
Cdd:PRK15134 480 LFISH 484
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
29-479 |
7.10e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 76.85 E-value: 7.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 29 GDSWAFVGSNGSGKSALARALAGEL-P------LLKGER-----QSQFShitrlsFEQLQKL------------VSDEWQ 84
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLePsagnvsLDPNERlgklrQDQFA------FEEFTVLdtvimghtelweVKQERD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 85 R--NNTDMlgpGEDDtGRTTAEIiqdEVKDA--------PRCMQLAQQFGITalLDRRFKYLST---GETRKTLLCQALM 151
Cdd:PRK15064 101 RiyALPEM---SEED-GMKVADL---EVKFAemdgytaeARAGELLLGVGIP--EEQHYGLMSEvapGWKLRVLLAQALF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 152 SEPDLLILDEPFDGLDVASRQQLAErlaSLHQSGITLVLV------LNR---------FDEIPefvQFAGVLADCTLAET 216
Cdd:PRK15064 172 SNPDILLLDEPTNNLDINTIRWLED---VLNERNSTMIIIshdrhfLNSvcthmadldYGELR---VYPGNYDEYMTAAT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 217 GAKEELL-----QQALVAQL----------------AHS--EQLEGVQL----------P----EPDEPSARHALpanep 259
Cdd:PRK15064 246 QARERLLadnakKKAQIAELqsfvsrfsanaskakqATSraKQIDKIKLeevkpssrqnPfirfEQDKKLHRNAL----- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 260 riVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgysndltlfgrrrGSGETIWDIKKHIG 339
Cdd:PRK15064 321 --EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEP-------------DSGTVKWSENANIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 340 YVSSSLHLDYRVSTTVrnvilsgyFDSIGIYQAVSDRQQkLVQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKH 419
Cdd:PRK15064 386 YYAQDHAYDFENDLTL--------FDWMSQWRQEGDDEQ-AVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQK 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 420 PTLLILDEPLQGLD-----PLNRQLirrfvdvliSEGETQLLFVSHHAEDAPACITHRLEFVPDG 479
Cdd:PRK15064 457 PNVLVMDEPTNHMDmesieSLNMAL---------EKYEGTLIFVSHDREFVSSLATRIIEITPDG 512
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
263-456 |
7.92e-15 |
|
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: 73.62 E-value: 7.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 263 LNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGR--RRGSGETIwdIKKHIGY 340
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPP-RSGSIRFDGRdiTGLPPHER--ARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 341 VS------SSLhldyrvstTVR-NVILSGYFDSIGIYQAVSDRqqklVQQWLDILGiDKRTADApfHSLSWGQQRLALIV 413
Cdd:cd03224 80 VPegrrifPEL--------TVEeNLLLGAYARRRAKRKARLER----VYELFPRLK-ERRKQLA--GTLSGGEQQMLAIA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16128728 414 RALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLL 456
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILL 187
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
257-465 |
1.13e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.02 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 257 NEPRIVLNNGVVSYN-DRPI-LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdhPQGYSNDLTLFGRRRGSGETIWDI 334
Cdd:PRK13648 4 KNSIIVFKNVSFQYQsDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG--IEKVKSGEIFYNNQAITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 335 KKHIGYVSSSLHLDYrVSTTVRnvilsgyFD-SIGIY-QAVS-DRQQKLVQQWLDILGIDKRTADAPfHSLSWGQ-QRLA 410
Cdd:PRK13648 82 RKHIGIVFQNPDNQF-VGSIVK-------YDvAFGLEnHAVPyDEMHRRVSEALKQVDMLERADYEP-NALSGGQkQRVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 411 lIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:PRK13648 153 -IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA 206
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
269-481 |
1.16e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 73.59 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 269 SYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLL----SLVTGDhpqgySNDLTLFGRR-RGSGETIWDIKKHIGYVSS 343
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrcinKLEEIT-----SGDLIVDGLKvNDPKVDERLIRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 344 SLHLdYRVSTTVRNVIlsgyFDSIGIYQAVSDRQQKLVQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLL 423
Cdd:PRK09493 85 QFYL-FPHLTALENVM----FGPLRVRGASKEEAEKQARELLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 424 ILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSHHAEDAPACIThRLEFVPDGGL 481
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMT-MVIVTHEIGFAEKVAS-RLIFIDKGRI 214
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
277-460 |
1.19e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.87 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 277 NNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQGysndltlfGRRRGSGETIWDIKKH----IGYVSSSLHLD-YR 350
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkPTG--------GTILLRGQHIEGLPGHqiarMGVVRTFQHVRlFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 351 VSTTVRNV-----------ILSGYFDSIGIYQAVSDRQQKlVQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRALVKH 419
Cdd:PRK11300 94 EMTVIENLlvaqhqqlktgLFSGLLKTPAFRRAESEALDR-AATWLERVGL-LEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16128728 420 PTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSH 460
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEH 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
259-445 |
1.44e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.26 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 259 PRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRGSGETIwDIKKHI 338
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT-AGTVLVAGDDVEALSAR-AASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 339 GYV--SSSLHLDYRVSTTVRnvilSGYFDSIGIYQAVSDRQQKLVQQWLDILGIDkRTADAPFHSLSWGQQRLALIVRAL 416
Cdd:PRK09536 80 ASVpqDTSLSFEFDVRQVVE----MGRTPHRSRFDTWTETDRAAVERAMERTGVA-QFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190
....*....|....*....|....*....|....
gi 16128728 417 VKHPTLLILDEPLQGLDpLNRQ-----LIRRFVD 445
Cdd:PRK09536 155 AQATPVLLLDEPTASLD-INHQvrtleLVRRLVD 187
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
269-460 |
1.45e-14 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 72.82 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 269 SYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDhpqgysndltlfgRRRGSGETIWDIK-------KHIG-- 339
Cdd:TIGR03740 9 RFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGI-------------LRPTSGEIIFDGHpwtrkdlHKIGsl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 340 ------YVSSSLHLDYRVSTTVRnvilsgyfdsigiyqAVSDRQQKLVQQWLDILGIDKRTADapfhSLSWG-QQRLAlI 412
Cdd:TIGR03740 76 iespplYENLTARENLKVHTTLL---------------GLPDSRIDEVLNIVDLTNTGKKKAK----QFSLGmKQRLG-I 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16128728 413 VRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLfVSH 460
Cdd:TIGR03740 136 AIALLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVIL-SSH 182
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
261-465 |
1.97e-14 |
|
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: 72.76 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGYSndlTLFGRRRGSGETIWDikKHIG 339
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERPDSGT---ILFGGEDATDVPVQE--RNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 340 YVSSSLHLdYRVSTTVRNVILsGYFDSIGIYQAVSDRQQKLVQQWLDILGIDKRTADAPfHSLSWGQ-QRLALiVRALVK 418
Cdd:cd03296 78 FVFQHYAL-FRHMTVFDNVAF-GLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYP-AQLSGGQrQRVAL-ARALAV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128728 419 HPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEA 200
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
261-465 |
2.25e-14 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 73.25 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNgvVSY-------NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGR--RRGSGET 330
Cdd:TIGR04521 1 IKLKN--VSYiyqpgtpFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGlLKPT--SGTVTIDGRdiTAKKKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 331 IWDIKKHIGYV----SSSLhldyrVSTTV--------RNVILSGyfdsigiyqavsDRQQKLVQQWLDILGIDKRTAD-A 397
Cdd:TIGR04521 77 LKDLRKKVGLVfqfpEHQL-----FEETVykdiafgpKNLGLSE------------EEAEERVKEALELVGLDEEYLErS 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 398 PFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR-QLIRRFVDVLISEGETqLLFVSHHAEDA 465
Cdd:TIGR04521 140 PFE-LSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRkEILDLFKRLHKEKGLT-VILVTHSMEDV 206
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-188 |
2.29e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 71.62 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRlsfeqlqklVSDEWQRNntdMLGPGEDDTGRTT- 102
Cdd:TIGR01189 21 FTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE---------QRDEPHEN---ILYLGHLPGLKPEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 103 ---------AEIIQDEVKDaprCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
Cdd:TIGR01189 89 salenlhfwAAIHGGAQRT---IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170
....*....|....*.
gi 16128728 174 LAERLAS-LHQSGITL 188
Cdd:TIGR01189 166 LAGLLRAhLARGGIVL 181
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
271-449 |
2.57e-14 |
|
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: 72.30 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 271 NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGY--SNDLTLFGRRRGSGETiwdiKKHIGYVSSSlhlD 348
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttSGQILFNGQPRKPDQF----QKCVAYVRQD---D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 349 YRVST-TVRNVIlsgYFDSIGIYQAVSD--RQQKLVQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLIL 425
Cdd:cd03234 91 ILLPGlTVRETL---TYTAILRLPRKSSdaIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190
....*....|....*....|....*....|..
gi 16128728 426 DEPLQGLDPLN--------RQLIRRFVDVLIS 449
Cdd:cd03234 168 DEPTSGLDSFTalnlvstlSQLARRNRIVILT 199
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
261-474 |
3.29e-14 |
|
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: 70.71 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSY--NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQGysndltlfGRRRGSGETI--WD-- 333
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLlRPTS--------GRVRLDGADIsqWDpn 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 334 -IKKHIGYVSSSLHLdyrVSTTVRNVILSGyfdsigiyqavsdrqqklvqqwldilgidkrtadapfhslswGQ-QRLAL 411
Cdd:cd03246 73 eLGDHVGYLPQDDEL---FSGSIAENILSG------------------------------------------GQrQRLGL 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128728 412 iVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLfvshhaedapacITHRLE 474
Cdd:cd03246 108 -ARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIV------------IAHRPE 157
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
269-465 |
3.56e-14 |
|
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: 71.88 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 269 SYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRRrgsgetIWDI---KKHIGYVSSS 344
Cdd:cd03300 9 FYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfETPT--SGEILLDGKD------ITNLpphKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 345 L----HLdyrvsTTVRNVilsgyfdSIGIYQAVSDRQ--QKLVQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVK 418
Cdd:cd03300 81 YalfpHL-----TVFENI-------AFGLRLKKLPKAeiKERVAEALDLVQLEGYANRKP-SQLSGGQQQRVAIARALVN 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128728 419 HPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEA 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
261-479 |
3.59e-14 |
|
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: 71.37 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPIlnNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRRRGSGETIwDIKKHIG 339
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQ--SGRVLINGVDVTAAPPA-DRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 340 YVSSSL--HLdyrvsTTVRNVILSgyfDSIGIYQAVSDRQQ-KLVQQWLDILGIDKRTADApfhsLSWGQQRLALIVRAL 416
Cdd:cd03298 76 FQENNLfaHL-----TVEQNVGLG---LSPGLKLTAEDRQAiEVALARVGLAGLEKRLPGE----LSGGERQRVALARVL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128728 417 VKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDAPAcITHRLEFVPDG 479
Cdd:cd03298 144 VRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKR-LAQRVVFLDNG 205
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-245 |
3.99e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 72.47 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLS----FEQLQKLVSDEWQRNNTDMLgpgeddtg 99
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQIRKKVGLVFQFPESQLF-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 100 rttAEIIQDEVKDAPrcmqlaQQFGIT-------------------ALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
Cdd:PRK13649 100 ---EETVLKDVAFGP------QNFGVSqeeaealareklalvgiseSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 161 EPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQAlvaqlahsEQLEGV 240
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDV--------DFLEEK 242
|
....*
gi 16128728 241 QLPEP 245
Cdd:PRK13649 243 QLGVP 247
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
268-433 |
4.16e-14 |
|
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: 70.98 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 268 VSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRGSGETIWdiKKHIGYVSSSLHL 347
Cdd:cd03231 8 CERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPL-AGRVLLNGGPLDFQRDSI--ARGLLYLGHAPGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 348 DYRVSTTvrnvilsgyfDSIGIYQAVSDRQQklVQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPTLLILDE 427
Cdd:cd03231 85 KTTLSVL----------ENLRFWHADHSDEQ--VEEALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
....*.
gi 16128728 428 PLQGLD 433
Cdd:cd03231 152 PTTALD 157
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
261-472 |
4.72e-14 |
|
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: 71.28 E-value: 4.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSY-NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVtgdhpqgYSNDLTLFGRRRGSGETIWDIKK--- 336
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLI-------YKEELPTSGTIRVNGQDVSDLRGrai 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 337 -----HIGYVSSslhlDYRVSTTvRNVilsgyFDSIGIYQAVSDRQQKLVQQ----WLDILGIDKRTADAPfHSLSWG-Q 406
Cdd:cd03292 74 pylrrKIGVVFQ----DFRLLPD-RNV-----YENVAFALEVTGVPPREIRKrvpaALELVGLSHKHRALP-AELSGGeQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128728 407 QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETqlLFVSHHAEDAPACITHR 472
Cdd:cd03292 143 QRVA-IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTT--VVVATHAKELVDTTRHR 205
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-217 |
5.26e-14 |
|
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: 71.24 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 1 MSSLQILQGTFRLSDTKTLQLPQLTLNAGDS--WAFVGSNGSGKSALARALAGELPLLKGErqsqfshITRLSFEQLQKl 78
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGevTGLLGPNGAGKTTTLRMLAGLLEPDAGF-------ATVDGFDVVKE- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 79 vSDEWQRNntdmLGPGEDDTG---RTTA-EIIQ----------DEVKDapRCMQLAQQFGITALLDRRFKYLSTGETRKT 144
Cdd:cd03266 73 -PAEARRR----LGFVSDSTGlydRLTArENLEyfaglyglkgDELTA--RLEELADRLGMEELLDRRVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128728 145 LLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETG 217
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
261-433 |
6.14e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.22 E-value: 6.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHP--QG---YSNDLTLfgRR------RGSGE 329
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLldDGriiYEQDLIV--ARlqqdppRNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 330 TIWDikkhigYVSSSL-----------HLDYRVSTTVRNVILSgyfdSIGIYQAVSDRQ-----QKLVQQWLDILGIDkr 393
Cdd:PRK11147 82 TVYD------FVAEGIeeqaeylkryhDISHLVETDPSEKNLN----ELAKLQEQLDHHnlwqlENRINEVLAQLGLD-- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16128728 394 tADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:PRK11147 150 -PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
10-191 |
7.91e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 68.63 E-value: 7.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 10 TFRLSDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQfSHITRLSFEQLqklvsdewqrnntd 89
Cdd:cd03221 7 SKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-STVKIGYFEQL-------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 90 mlgpgeddtgrttaeiiqdevkdaprcmqlaqqfgitalldrrfkylSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
Cdd:cd03221 72 -----------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180
....*....|....*....|..
gi 16128728 170 SRQQLAERLASLHQsgiTLVLV 191
Cdd:cd03221 105 SIEALEEALKEYPG---TVILV 123
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
260-465 |
8.47e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 72.41 E-value: 8.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 260 RIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHP-QGysnDLTLFGRR--------RGsge 329
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDPtSG---EILIGGRDvtdlppkdRN--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 330 tiwdikkhIGYVSSSL----HLdyrvstTVRnvilsgyfDSIGIY---QAVS-DRQQKLVQQWLDILGID---KRTADAp 398
Cdd:COG3839 77 --------IAMVFQSYalypHM------TVY--------ENIAFPlklRKVPkAEIDRRVREAAELLGLEdllDRKPKQ- 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 399 fhsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:COG3839 134 ---LSGGQrQRVA-LGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEA 197
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
275-468 |
9.64e-14 |
|
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: 70.54 E-value: 9.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 275 ILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFG------------RRRGsgetiwdikKHIGYV 341
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGlDRPT--SGTVRLAGqdlfaldedaraRLRA---------RHVGFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 342 SSSLHLdyrVS--TTVRNVI----LSGYFDSigiyqavsdrqQKLVQQWLDILGIDKRTADAPfHSLSWG-QQRLAlIVR 414
Cdd:COG4181 96 FQSFQL---LPtlTALENVMlpleLAGRRDA-----------RARARALLERVGLGHRLDHYP-AQLSGGeQQRVA-LAR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128728 415 ALVKHPTLLILDEPLQGLDPLNRQLIrrfVDVLIS---EGETQLLFVSHHAEDAPAC 468
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQI---IDLLFElnrERGTTLVLVTHDPALAARC 213
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
259-465 |
1.44e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.29 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 259 PRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDhPQGYSNDLTLFGRRRGSGETIWDIKKHI 338
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 339 GYVSSSLHLDYRVsTTVRNVILSGYFDSIGIYQAVSDRQQKLVQQWLDilgidKRTADApfHSLSWGQQRLALIVRALVK 418
Cdd:PRK11614 83 AIVPEGRRVFSRM-TVEENLAMGGFFAERDQFQERIKWVYELFPRLHE-----RRIQRA--GTMSGGEQQMLAIGRALMS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128728 419 HPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLfVSHHAEDA 465
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFL-VEQNANQA 200
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-191 |
1.45e-13 |
|
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: 69.59 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 16 TKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGelpLLKGERQSQFSHITRLSFEQLQK---LVSDEWQRNNT---- 88
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG---LIKESSGSILLNGKPIKAKERRKsigYVMQDVDYQLFtdsv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 89 -DMLGPGEDDTGRTtAEIIQDEVKDaprcmqlaqqFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
Cdd:cd03226 90 rEELLLGLKELDAG-NEQAETVLKD----------LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180
....*....|....*....|....
gi 16128728 168 VASRQQLAERLASLHQSGITLVLV 191
Cdd:cd03226 159 YKNMERVGELIRELAAQGKAVIVI 182
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
263-461 |
1.49e-13 |
|
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: 69.86 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 263 LNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRGSGETIWDIKKHIGYVS 342
Cdd:TIGR03410 3 VSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVK-SGSIRLDGEDITKLPPHERARAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 343 ------SSLhldyrvstTVRNVILSGYfdsigiyQAVSDRQQKLVQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRA 415
Cdd:TIGR03410 82 qgreifPRL--------TVEENLLTGL-------AALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQqQQLA-IARA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128728 416 LVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHH 461
Cdd:TIGR03410 146 LVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQY 191
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
33-226 |
1.80e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.60 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 33 AFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVSDEWQRNNTDMLGPG-EDDTGRTTAEIIQDEVK 111
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIFSPTvEQDIAFGPINLGLDEET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 112 DAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQS-GITLVL 190
Cdd:PRK13652 114 VAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16128728 191 VLNRFDEIPEFVQFAGVL------ADCTLAETGAKEELLQQA 226
Cdd:PRK13652 194 STHQLDLVPEMADYIYVMdkgrivAYGTVEEIFLQPDLLARV 235
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
268-472 |
1.83e-13 |
|
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: 69.63 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 268 VSYNDRPILNNLSWQVNPGEhwqIV---GPNGAGKSTLLSLVTGDHPqgysndltlfgRRRGS----GETIWDIKKH--- 337
Cdd:COG0410 11 AGYGGIHVLHGVSLEVEEGE---IVallGRNGAGKTTLLKAISGLLP-----------PRSGSirfdGEDITGLPPHria 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 338 ---IGYVS------SSLhldyrvstTVR-NVILSGYFdsigiyQAVSDRQQKLVQQWLD---ILGiDKRTADApfHSLSW 404
Cdd:COG0410 77 rlgIGYVPegrrifPSL--------TVEeNLLLGAYA------RRDRAEVRADLERVYElfpRLK-ERRRQRA--GTLSG 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 405 GQQR-LAlIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLfVSHHAEDAPAcITHR 472
Cdd:COG0410 140 GEQQmLA-IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILL-VEQNARFALE-IADR 205
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
261-473 |
1.84e-13 |
|
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: 69.95 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYND--RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVtgdhPQGYsnDLTLfGRRRGSGETIWDIK--- 335
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI----PRFY--DVDS-GRILIDGHDVRDYTlas 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 336 --KHIGYVSSSLHLdyrVSTTVRNVILSGYFDsIGIYQAVSDRQQKLVQQWLDIL--GIDKRTADAPFhSLSWGQ-QRLA 410
Cdd:cd03251 74 lrRQIGLVSQDVFL---FNDTVAENIAYGRPG-ATREEVEEAARAANAHEFIMELpeGYDTVIGERGV-KLSGGQrQRIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128728 411 lIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLiSEGETQLLfvshhaedapacITHRL 473
Cdd:cd03251 149 -IARALLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFV------------IAHRL 197
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
261-465 |
2.09e-13 |
|
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: 67.84 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqgysndltlfgrrRGSGETIWDIKKhigy 340
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK-------------PDSGEILVDGKE---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 341 VSsslhldyrvsttvrnvilsgyFDSigiyqaVSDRQQklvqqwldiLGIdkrtadAPFHSLSWGQQRLALIVRALVKHP 420
Cdd:cd03216 64 VS---------------------FAS------PRDARR---------AGI------AMVYQLSVGERQMVEIARALARNA 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16128728 421 TLLILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSHHAEDA 465
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGVA-VIFISHRLDEV 145
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
260-463 |
2.15e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 260 RIVLNNGVVSYND--RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHpqgysndltlfgrRRGSGETIWDIKKH 337
Cdd:COG2401 28 AIVLEAFGVELRVveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL-------------KGTPVAGCVDVPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 338 IGYVSSSL--HLDYRVSTTvrnvilsgyfDSIGIYQAV--SDrqqklVQQWLdilgidkrtadAPFHSLSWGQQRLALIV 413
Cdd:COG2401 95 QFGREASLidAIGRKGDFK----------DAVELLNAVglSD-----AVLWL-----------RRFKELSTGQKFRFRLA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16128728 414 RALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAE 463
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
118-198 |
2.16e-13 |
|
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: 69.25 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 118 QLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQS-GITLVLVLNRFD 196
Cdd:cd03297 114 ELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLS 193
|
..
gi 16128728 197 EI 198
Cdd:cd03297 194 EA 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-460 |
2.24e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.58 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARAL-------AGEL---PLLKGERQSQFSHITRLSFEQLQKLVSDE----WQRNNTD 89
Cdd:PRK10261 37 FSLQRGETLAIVGESGSGKSVTALALmrlleqaGGLVqcdKMLLRRRSRQVIELSEQSAAQMRHVRGADmamiFQEPMTS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 90 mLGPgEDDTGRTTAEII--------QDEVKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
Cdd:PRK10261 117 -LNP-VFTVGEQIAESIrlhqgasrEEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 162 PFDGLDVASRQQLAERLASLHQS-GITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQ-------QALVAQLAH 233
Cdd:PRK10261 195 PTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHapqhpytRALLAAVPQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 234 SEQLEGVQLP-----------EPDEPSA-RHALPANEPRIVLNNGVVSYNDRP-ILN----------NLSWQVNPGEHWQ 290
Cdd:PRK10261 275 LGAMKGLDYPrrfplislehpAKQEPPIeQDTVVDGEPILQVRNLVTRFPLRSgLLNrvtrevhaveKVSFDLWPGETLS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 291 IVGPNGAGKST----LLSLVtgdhpQGYSNDLTLFGRRRG--SGETIWDIKKHIGYVSSslhlDYRVSTTVRNVILSGYF 364
Cdd:PRK10261 355 LVGESGSGKSTtgraLLRLV-----ESQGGEIIFNGQRIDtlSPGKLQALRRDIQFIFQ----DPYASLDPRQTVGDSIM 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 365 DSIGIYQAVS-DRQQKLVQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR-QLIRR 442
Cdd:PRK10261 426 EPLRVHGLLPgKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRgQIINL 505
|
490
....*....|....*...
gi 16128728 443 FVDvLISEGETQLLFVSH 460
Cdd:PRK10261 506 LLD-LQRDFGIAYLFISH 522
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-223 |
2.53e-13 |
|
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: 69.29 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 3 SLQILQGTFRLSDTKtlqlpqLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVSde 82
Cdd:cd03299 5 NLSKDWKEFKLKNVS------LEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYV-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 83 wqrNNTDMLGPG---EDDTGRTTAEIIQDEVKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLIL 159
Cdd:cd03299 77 ---PQNYALFPHmtvYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 160 DEPFDGLDVASRQQLAERLASLHQS-GITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELL 223
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
24-224 |
3.83e-13 |
|
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: 68.61 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKL----VSDEwqRN---------NTDM 90
Cdd:cd03224 21 LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgigyVPEG--RRifpeltveeNLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 91 lgpGEDDTGRTTAEIIQDEVKDA-PRCMQLAQQFGITalldrrfkyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
Cdd:cd03224 99 ---GAYARRRAKRKARLERVYELfPRLKERRKQLAGT---------LSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 170 SRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQ 224
Cdd:cd03224 167 IVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
272-481 |
4.75e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 272 DRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgysndLTlfgrRRGSGETIW---DIKKHIGYVSSSL--- 345
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG---------LA----RPDAGEVLWqgePIRRQRDEYHQDLlyl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 346 -HLD--YRVSTTVRNVIlsgyfdsigIYQAVSDRQ-QKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPT 421
Cdd:PRK13538 80 gHQPgiKTELTALENLR---------FYQRLHGPGdDEALWEALAQVGLAGF-EDVPVRQLSAGQQRRVALARLWLTRAP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128728 422 LLILDEPLQGLDplnrqliRRFVDVLisegeTQLLfvSHHAEDAPACI--THRLEFVPDGGL 481
Cdd:PRK13538 150 LWILDEPFTAID-------KQGVARL-----EALL--AQHAEQGGMVIltTHQDLPVASDKV 197
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
247-433 |
5.17e-13 |
|
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: 71.32 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 247 EPSARHALPANEPRIVLNNGVVSY--NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgysndltlfgrR 324
Cdd:COG4618 317 AEPERMPLPRPKGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP-----------T 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 325 RGS----GETI--WD---IKKHIGYVSSSLHLdyrVSTTVR-NVILSGYFDSIGIYQA-----VSDRQQKLVQqwldilG 389
Cdd:COG4618 386 AGSvrldGADLsqWDreeLGRHIGYLPQDVEL---FDGTIAeNIARFGDADPEKVVAAaklagVHEMILRLPD------G 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16128728 390 IDKRTADAPfHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLD 433
Cdd:COG4618 457 YDTRIGEGG-ARLSGGQrQRIGL-ARALYGDPRLVVLDEPNSNLD 499
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
269-465 |
5.34e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 70.36 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 269 SYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETIWDI---KKHIGYVSSS 344
Cdd:PRK09452 23 SFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfETPDS--------GRIMLDGQDITHVpaeNRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 345 L----HLdyrvstTVR-NVilsgyfdsigiyqAVSDRQQKLVQQwldilGIDKRTADA-------------PfHSLSWGQ 406
Cdd:PRK09452 95 YalfpHM------TVFeNV-------------AFGLRMQKTPAA-----EITPRVMEAlrmvqleefaqrkP-HQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128728 407 QRLALIVRALVKHPTLLILDEPLQGLD------------PLNRQLIRRFVdvlisegetqllFVSHHAEDA 465
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDyklrkqmqnelkALQRKLGITFV------------FVTHDQEEA 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
261-460 |
5.70e-13 |
|
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: 68.36 E-value: 5.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgySNDLTLFGRRRGS----GETIWDIKK 336
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNR------LNDLIPGAPDEGEvlldGKDIYDLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 337 HIgyvsssLHLDYRV----------STTVR-NVilsgyfdSIGI-YQAVSDRQQ--KLVQQWLDILGIDKRTAD-APFHS 401
Cdd:cd03260 75 DV------LELRRRVgmvfqkpnpfPGSIYdNV-------AYGLrLHGIKLKEEldERVEEALRKAALWDEVKDrLHALG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128728 402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLIRRfvdvLISE--GETQLLFVSH 460
Cdd:cd03260 142 LSGGQqQRLC-LARALANEPEVLLLDEPTSALDPISTAKIEE----LIAElkKEYTIVIVTH 198
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-485 |
7.24e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.75 E-value: 7.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 1 MSSLQILQGTFRLSDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQ-SQFSHITRL--------- 70
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIyEQDLIVARLqqdpprnve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 71 -------------------SFEQLQKLVSDEWQRNNTDMLgpgeddtgrttaEIIQDEVKDA------PRCMQLAQQFGI 125
Cdd:PRK11147 81 gtvydfvaegieeqaeylkRYHDISHLVETDPSEKNLNEL------------AKLQEQLDHHnlwqleNRINEVLAQLGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 126 TAllDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQSGI-------------TLVLVL 192
Cdd:PRK11147 149 DP--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIfishdrsfirnmaTRIVDL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 193 NRfdeipefvqfaGVLA----DCTLAETGAKEEL----LQQALV-AQLAHSEQL--EGV---------------QLPEpd 246
Cdd:PRK11147 227 DR-----------GKLVsypgNYDQYLLEKEEALrveeLQNAEFdRKLAQEEVWirQGIkarrtrnegrvralkALRR-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 247 EPSARHALPANEP----------RIVLNNGVVSYN--DRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQg 313
Cdd:PRK11147 294 ERSERREVMGTAKmqveeasrsgKIVFEMENVNYQidGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQlQAD- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 314 ysndltlfgrrrgSGETiwdikkHIGyvsssLHLDYrvsttvrnvilsGYFDSigiYQAVSDRQQKLV------QQWLDI 387
Cdd:PRK11147 373 -------------SGRI------HCG-----TKLEV------------AYFDQ---HRAELDPEKTVMdnlaegKQEVMV 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 388 LGID--------------KRtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRfvdvLISEGET 453
Cdd:PRK11147 414 NGRPrhvlgylqdflfhpKR-AMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEE----LLDSYQG 488
|
570 580 590
....*....|....*....|....*....|..
gi 16128728 454 QLLFVSHHAEDAPACITHRLEFVPDGGLYRYV 485
Cdd:PRK11147 489 TVLLVSHDRQFVDNTVTECWIFEGNGKIGRYV 520
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
24-217 |
9.94e-13 |
|
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: 67.24 E-value: 9.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshITrlsfeQLQKLVSDE---WQRNNTDMLGPG--EDDT 98
Cdd:cd03268 21 LHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGE-------IT-----FDGKSYQKNieaLRRIGALIEAPGfyPNLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 99 GR----TTAEIIQdeVKDApRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
Cdd:cd03268 89 ARenlrLLARLLG--IRKK-RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKEL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16128728 175 AERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETG 217
Cdd:cd03268 166 RELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
261-473 |
1.36e-12 |
|
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: 67.26 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYND-RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLvtgdhpqgysndltLF-------GRRRGSGETIW 332
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRL--------------LFrfydvssGSILIDGQDIR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 333 DIK-----KHIGYVSSSLHLdyrVSTTVRNVILSGYFDS--IGIYQA-----VSDRQQKLVQQWLDILGidKRTAdapfh 400
Cdd:cd03253 67 EVTldslrRAIGVVPQDTVL---FNDTIGYNIRYGRPDAtdEEVIEAakaaqIHDKIMRFPDGYDTIVG--ERGL----- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 401 SLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLI-RRFVDVliSEGETQLLfvshhaedapacITHRL 473
Cdd:cd03253 137 KLSGGEkQRVA-IARAILKNPPILLLDEATSALDTHTEREIqAALRDV--SKGRTTIV------------IAHRL 196
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
261-465 |
1.58e-12 |
|
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: 67.33 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYND-RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVtgdhpqgysNDLT--LFGRRRGSGETI--WD-- 333
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI---------NRLIepTSGEIFIDGEDIreQDpv 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 334 -IKKHIGYVSSSL----HLdyrvsTTVRNVI----LSGYfdsigiyqaVSDRQQKLVQQWLDILGIDKRT-ADAPFHSLS 403
Cdd:cd03295 72 eLRRKIGYVIQQIglfpHM-----TVEENIAlvpkLLKW---------PKEKIRERADELLALVGLDPAEfADRYPHELS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128728 404 WGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR-QLIRRFVDVLISEGETqLLFVSHHAEDA 465
Cdd:cd03295 138 GGQQQRVGVARALAADPPLLLMDEPFGALDPITRdQLQEEFKRLQQELGKT-IVFVTHDIDEA 199
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
273-434 |
1.68e-12 |
|
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: 66.04 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 273 RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQGYSNDLTLFGRRRGSGEtiwdIKKHIGYVssslhldyrv 351
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrTGLGVSGEVLINGRPLDKRS----FRKIIGYV---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 352 sttVRNVILSGYFDsigiyqavsdrqqklVQQWLDIlgidkrtaDAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQG 431
Cdd:cd03213 88 ---PQDDILHPTLT---------------VRETLMF--------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
...
gi 16128728 432 LDP 434
Cdd:cd03213 142 LDS 144
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
261-465 |
1.73e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.57 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYsndltlfGRRRGSGETIWDI---KKH 337
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTS-------GHIRFHGTDVSRLharDRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 338 IGYVSSSLHLdYRVSTTvrnvilsgyFDSIGIYQAVSDRQQ--------KLVQQWLDILGIDkRTADAPFHSLSWGQ-QR 408
Cdd:PRK10851 76 VGFVFQHYAL-FRHMTV---------FDNIAFGLTVLPRRErpnaaaikAKVTQLLEMVQLA-HLADRYPAQLSGGQkQR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128728 409 LALiVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:PRK10851 145 VAL-ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEA 200
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
238-480 |
1.80e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.45 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 238 EGVQLPEPDEPSARHALPANEPRIVLNN-GVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-------- 308
Cdd:COG4178 340 EALEAADALPEAASRIETSEDGALALEDlTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwpygsgr 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 309 -DHPQGYSndlTLFGRRRGsgetiwdikkhigyvssslhldYRVSTTVRNVILsgYFDSIGiyqAVSDRQqklVQQWLDI 387
Cdd:COG4178 420 iARPAGAR---VLFLPQRP----------------------YLPLGTLREALL--YPATAE---AFSDAE---LREALEA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 388 LG----IDKRTADAPF-HSLSWG-QQRLAlIVRALVKHPTLLILDEPLQGLDPLN-RQLIRRFVDVLiseGETQLLFVSH 460
Cdd:COG4178 467 VGlghlAERLDEEADWdQVLSLGeQQRLA-FARLLLHKPDWLFLDEATSALDEENeAALYQLLREEL---PGTTVISVGH 542
|
250 260
....*....|....*....|
gi 16128728 461 HAEDAPACiTHRLEFVPDGG 480
Cdd:COG4178 543 RSTLAAFH-DRVLELTGDGS 561
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
261-473 |
1.88e-12 |
|
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: 66.79 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRP---ILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVtgdhpQGY---SNDLTLFGRRRGSGETIWDI 334
Cdd:cd03249 1 IEFKNVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL-----ERFydpTSGEILLDGVDIRDLNLRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 335 KKHIGYVSSSLHLdyrVSTTVRNVILSGYFdsigiyqavsDRQQKLVQQWLDILGIDKRTADAP--FH--------SLSW 404
Cdd:cd03249 76 RSQIGLVSQEPVL---FDGTIAENIRYGKP----------DATDEEVEEAAKKANIHDFIMSLPdgYDtlvgergsQLSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 405 GQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDvLISEGETQLLfvshhaedapacITHRL 473
Cdd:cd03249 143 GQkQRIA-IARALLRNPKILLLDEATSALDAESEKLVQEALD-RAMKGRTTIV------------IAHRL 198
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-237 |
2.05e-12 |
|
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: 69.48 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 10 TFRLSDTKTLQL--PQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGE--------RQsqfshitrLSFEQLQKLV 79
Cdd:COG2274 480 SFRYPGDSPPVLdnISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRilidgidlRQ--------IDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 80 SDEWQ---------RNNTDMLGPGEDDtgrttaeiiqDEVKDAprcmqlAQQFGITALLDR-----------RFKYLSTG 139
Cdd:COG2274 552 GVVLQdvflfsgtiRENITLGDPDATD----------EEIIEA------ARLAGLHDFIEAlpmgydtvvgeGGSNLSGG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 140 ETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQsGITLVLVLNRfdeiPEFVQFAG---VLADCTLAET 216
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHR----LSTIRLADriiVLDKGRIVED 690
|
250 260
....*....|....*....|.
gi 16128728 217 GAKEELLQQALVAQLAHSEQL 237
Cdd:COG2274 691 GTHEELLARKGLYAELVQQQL 711
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
291-460 |
2.13e-12 |
|
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: 68.21 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 291 IVGPNGAGKSTLLSLVTG----DHPQGYSNDLTLFGRRRGSGETIWdiKKHIGYV--SSSL--HLdyrvstTVRNVILSG 362
Cdd:TIGR02142 28 IFGRSGSGKTTLIRLIAGltrpDEGEIVLNGRTLFDSRKGIFLPPE--KRRIGYVfqEARLfpHL------SVRGNLRYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 363 YFDSIGIYQAVSDrqqklvQQWLDILGIDKRTADAPfHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLIR 441
Cdd:TIGR02142 100 MKRARPSERRISF------ERVIELLGIGHLLGRLP-GRLSGGEkQRVA-IGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170
....*....|....*....
gi 16128728 442 RFVDVLISEGETQLLFVSH 460
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSH 190
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
24-191 |
2.37e-12 |
|
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: 66.34 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQ---LQKLVSDEWqRNNTD--MLGPgeDDT 98
Cdd:cd03293 25 LSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRgyvFQQDALLPW-LTVLDnvALGL--ELQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 99 GRTTAEIiqdevkdAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERL 178
Cdd:cd03293 102 GVPKAEA-------RERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEEL 174
|
170
....*....|....
gi 16128728 179 ASL-HQSGITLVLV 191
Cdd:cd03293 175 LDIwRETGKTVLLV 188
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
261-465 |
2.49e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 67.86 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETiWDI----- 334
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETPDS--------GRIVLNGRD-LFTnlppr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 335 KKHIGYVSSS--L--HLdyrvstTVR-NVilsgyfdSIGIYQAVSDRQQ--KLVQQWLDILGID---KRTadaPfHSLSW 404
Cdd:COG1118 74 ERRVGFVFQHyaLfpHM------TVAeNI-------AFGLRVRPPSKAEirARVEELLELVQLEglaDRY---P-SQLSG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128728 405 GQ-QRLALIvRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:COG1118 137 GQrQRVALA-RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEA 197
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
272-488 |
2.75e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.14 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 272 DRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYSNDLTlfgrrRG---SGETIWDIKKHIGYVSSSLHlD 348
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLI-----RGepiTKENIREVRKFVGLVFQNPD-D 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 349 YRVSTTVRNVILSGYFDSIGIYQAVSDRqqklVQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEP 428
Cdd:PRK13652 90 QIFSPTVEQDIAFGPINLGLDEETVAHR----VSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 429 LQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHaedapacithrLEFVPDGGLYRYVLTK 488
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQ-----------LDLVPEMADYIYVMDK 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
261-460 |
2.82e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 66.56 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETIWD------ 333
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLlEEPDS--------GTITVDGEDLTDskkdin 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 334 -IKKHIGYV--SSSL--HLdyrvsTTVRNVILSgyfdsigiyqavsdrqQKLVQQW------------LDILGI-DKrtA 395
Cdd:COG1126 74 kLRRKVGMVfqQFNLfpHL-----TVLENVTLA----------------PIKVKKMskaeaeeramelLERVGLaDK--A 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 396 DA-PfHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPlnrQLIRRFVDVLIS---EGETQLLfVSH 460
Cdd:COG1126 131 DAyP-AQLSGGQqQRVA-IARALAMEPKVMLFDEPTSALDP---ELVGEVLDVMRDlakEGMTMVV-VTH 194
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-225 |
2.83e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.07 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQ----LQKLVSDEWQRNNTDML-------- 91
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQFPESQLFeetvlkdv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 92 --GPGEDDTGRTTAEIIQDEVKDAprcMQLAQQFGITALLDrrfkyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
Cdd:PRK13643 107 afGPQNFGIPKEKAEKIAAEKLEM---VGLADEFWEKSPFE-----LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128728 170 SRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQ 225
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
254-465 |
2.86e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.94 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 254 LPANEPRIVLNNGVVSYND--RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQgySNDLTLFGRRRgSGET 330
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLlKPQ--SGEIKIDGITI-SKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 331 IWDIKKHIG---------YVSSSLHLDYRVSTTVRNVilsgyfDSIGIYQAVSDRQQKlvqqwldiLGIDKRTADAPfHS 401
Cdd:PRK13632 78 LKEIRKKIGiifqnpdnqFIGATVEDDIAFGLENKKV------PPKKMKDIIDDLAKK--------VGMEDYLDKEP-QN 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:PRK13632 143 LSGGQkQRVA-IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA 206
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
24-222 |
2.96e-12 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 67.42 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSfEQLQKLVSDEWQRNNTDmlgpgEDDTGRTTA 103
Cdd:TIGR01188 14 FKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREP-RKVRRSIGIVPQYASVD-----EDLTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 104 EII-------QDEVKDapRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
Cdd:TIGR01188 88 EMMgrlyglpKDEAEE--RAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128728 177 RLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEEL 222
Cdd:TIGR01188 166 YIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
261-477 |
2.97e-12 |
|
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: 65.57 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDR-----PILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgysndltLFGRRRGSGetiwdik 335
Cdd:cd03250 1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEK-------LSGSVSVPG------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 336 kHIGYVSSSLHLdyrVSTTVRNVILSGY-FDsigiyqavSDRQQKLV-----QQWLDIL-----------GIdkrtadap 398
Cdd:cd03250 67 -SIAYVSQEPWI---QNGTIRENILFGKpFD--------EERYEKVIkacalEPDLEILpdgdlteigekGI-------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 399 fhSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDP-LNRQLIRRFVDVLISEGETQLLfvshhaedapacITHRLEFV 476
Cdd:cd03250 127 --NLSGGQkQRISL-ARAVYSDADIYLLDDPLSAVDAhVGRHIFENCILGLLLNNKTRIL------------VTHQLQLL 191
|
.
gi 16128728 477 P 477
Cdd:cd03250 192 P 192
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
274-476 |
3.16e-12 |
|
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: 66.07 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 274 PILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRR--RGSGETIWDIKKHIGYVSSSLHLdyR 350
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERPT--SGSVLVDGTDltLLSGKELRKARRRIGMIFQHFNL--L 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 351 VSTTVR-NVILsgyfdSIGIYQAVSDRQQKLVQQWLDILGI-DKrtADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDE 427
Cdd:cd03258 95 SSRTVFeNVAL-----PLEIAGVPKAEIEERVLELLELVGLeDK--ADAYPAQLSGGQkQRVG-IARALANNPKVLLCDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16128728 428 PLQGLDPLN-RQLIRRFVDVLISEGETQLLfvshhaedapacITHRLEFV 476
Cdd:cd03258 167 ATSALDPETtQSILALLRDINRELGLTIVL------------ITHEMEVV 204
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-210 |
3.74e-12 |
|
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: 64.37 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPllkgerqsqfshitrlsfeqlqklvsdewqrnntdmlgpgeddtgRTTA 103
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMKILSGLYK---------------------------------------------PDSG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 104 EIIQDEVKDAPRCMQLAQQFGItalldrRFKY-LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLH 182
Cdd:cd03216 56 EILVDGKEVSFASPRDARRAGI------AMVYqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLR 129
|
170 180
....*....|....*....|....*...
gi 16128728 183 QSGITLVLVLNRFDEIPEFVQFAGVLAD 210
Cdd:cd03216 130 AQGVAVIFISHRLDEVFEIADRVTVLRD 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
24-191 |
3.80e-12 |
|
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: 65.99 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLqklvsdEWQRNNTDMLG--PGED-DTGR 100
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR------KIRRKEIQMVFqdPMSSlNPRM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 101 TTAEII-------QDEVKDAPR---CMQLAQQFGitalLDRRF--KY---LSTGETRKTLLCQALMSEPDLLILDEPFDG 165
Cdd:cd03257 100 TIGEQIaeplrihGKLSKKEARkeaVLLLLVGVG----LPEEVlnRYpheLSGGQRQRVAIARALALNPKLLIADEPTSA 175
|
170 180
....*....|....*....|....*..
gi 16128728 166 LDVASRQQLAERLASLHQS-GITLVLV 191
Cdd:cd03257 176 LDVSVQAQILDLLKKLQEElGLTLLFI 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
263-488 |
4.18e-12 |
|
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: 68.31 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 263 LNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQG-YSNDLtLFGRRRGSGETIWDI-KKHIGY 340
Cdd:TIGR02633 4 MKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtWDGEI-YWSGSPLKASNIRDTeRAGIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 341 VSSSLHLDYRVStTVRNVILSGYFDSIGI---YQAVSDRQQKLVQQwldiLGIDKRTADAPFHSLSWGQQRLALIVRALV 417
Cdd:TIGR02633 83 IHQELTLVPELS-VAENIFLGNEITLPGGrmaYNAMYLRAKNLLRE----LQLDADNVTRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128728 418 KHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGeTQLLFVSHHAEDAPAcITHRLEFVPDGglyRYVLTK 488
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHG-VACVYISHKLNEVKA-VCDTICVIRDG---QHVATK 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-224 |
4.28e-12 |
|
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: 65.24 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGeLP---------LLKGErqsqfsHITRLSFEQLQKL---VSdeWQRnntdml 91
Cdd:cd03217 21 LTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyevtegeiLFKGE------DITDLPPEERARLgifLA--FQY------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 92 gPgEDDTGRTTAEIIQDevkdaprcmqlaqqfgitalLDRRFkylSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
Cdd:cd03217 86 -P-PEIPGVKNADFLRY--------------------VNEGF---SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 172 QQLAERLASLHQSGITLVLVLNRfDEIPEFVQ--FAGVLADCTLAETGAKEELLQ 224
Cdd:cd03217 141 RLVAEVINKLREEGKSVLIITHY-QRLLDYIKpdRVHVLYDGRIVKSGDKELALE 194
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
261-441 |
4.32e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 66.68 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYN---DRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdHPQGYSNDLTLFGRRRgSGETIWDIKKH 337
Cdd:PRK13650 5 IEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDG-LLEAESGQIIIDGDLL-TEENVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 338 IGYVSSSLHLDYrVSTTVRNVILSGyFDSIGI-YQAVSDRqqklVQQWLDILGIDKRTADAPfHSLSWGQ-QRLAlIVRA 415
Cdd:PRK13650 83 IGMVFQNPDNQF-VGATVEDDVAFG-LENKGIpHEEMKER----VNEALELVGMQDFKEREP-ARLSGGQkQRVA-IAGA 154
|
170 180
....*....|....*....|....*..
gi 16128728 416 LVKHPTLLILDEPLQGLDPLNRQ-LIR 441
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLeLIK 181
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-225 |
4.46e-12 |
|
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: 68.29 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 23 QLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshitrlsfeqLQKLVSDEWqrnnTDMLGPGEDDTGRTT 102
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE---------------VNVRVGDEW----VDMTKPGPDGRGRAK 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 103 AEI--------------IQDEVKDAPRcMQLAQQFGI-----------------TALLDRRFKYLSTGETRKTLLCQALM 151
Cdd:TIGR03269 365 RYIgilhqeydlyphrtVLDNLTEAIG-LELPDELARmkavitlkmvgfdeekaEEILDKYPDELSEGERHRVALAQVLI 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 152 SEPDLLILDEPFDGLDVASRQQLAER-LASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQ 225
Cdd:TIGR03269 444 KEPRIVILDEPTGTMDPITKVDVTHSiLKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
252-473 |
4.74e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.31 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 252 HALPANEPRIVLNNGVVSYNDR--PILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG--DHPQGysnDLTLFGRR-RG 326
Cdd:PRK11160 330 STAAADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRawDPQQG---EILLNGQPiAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 327 SGETiwDIKKHIGYVSSSLHLdyrVSTTVRNVILsgyfdsIGIYQAvSDRQ----------QKLVQQ------WLDILGi 390
Cdd:PRK11160 407 YSEA--ALRQAISVVSQRVHL---FSATLRDNLL------LAAPNA-SDEAlievlqqvglEKLLEDdkglnaWLGEGG- 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 391 dkRTadapfhsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIrrfvdvlisegeTQLLFvsHHAEDAPAC-I 469
Cdd:PRK11160 474 --RQ-------LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQI------------LELLA--EHAQNKTVLmI 530
|
....
gi 16128728 470 THRL 473
Cdd:PRK11160 531 THRL 534
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
24-224 |
5.05e-12 |
|
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: 65.60 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLvsdewqRNNTDML---GPGEDD--- 97
Cdd:cd03261 21 LDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRL------RRRMGMLfqsGALFDSltv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 98 ----------TGRTTAEIIQDEVKdaprcMQLAQqFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
Cdd:cd03261 95 fenvafplreHTRLSEEEIREIVL-----EKLEA-VGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 168 VASRQQLAERLASLHQS-GITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQ 224
Cdd:cd03261 169 PIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-451 |
6.03e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.65 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELP--------LLKGERQsQFSHItRLSFE-------QLQKLVSDEWQRNNT 88
Cdd:PRK13549 26 LKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtyegeiIFEGEEL-QASNI-RDTERagiaiihQELALVKELSVLENI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 89 dMLGpgeddtgrttAEIIQDEVKDAP----RCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
Cdd:PRK13549 104 -FLG----------NEITPGGIMDYDamylRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 165 GLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQALVAQLAhseqleGVQLPE 244
Cdd:PRK13549 173 SLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMV------GRELTA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 245 --PDEP--------SARH--ALPANEPRivlnngvvsyndRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQ 312
Cdd:PRK13549 247 lyPREPhtigevilEVRNltAWDPVNPH------------IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 313 GYSNDLTLFGRR---RGSGETIwdiKKHIGYVSSslhlDYRVSTTV------RNVILSGYFDSIGIYQAVSDRQQKLVQQ 383
Cdd:PRK13549 315 RWEGEIFIDGKPvkiRNPQQAI---AQGIAMVPE----DRKRDGIVpvmgvgKNITLAALDRFTGGSRIDDAAELKTILE 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 384 WLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEG 451
Cdd:PRK13549 388 SIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQG 455
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
261-438 |
6.45e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 65.81 E-value: 6.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLL-SLVTGDHPQG-----YSNDLTLFGRRRgsgetiwdI 334
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLkCFARLLTPQSgtvflGDKPISMLSSRQ--------L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 335 KKHIGYVSSslHLDYRVSTTVRNVILSGYFDSIGIYQAVSDRQQKLVQQWLDILGIDKrTADAPFHSLSWGQQRLALIVR 414
Cdd:PRK11231 75 ARRLALLPQ--HHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINH-LADRRLTDLSGGQRQRAFLAM 151
|
170 180
....*....|....*....|....
gi 16128728 415 ALVKHPTLLILDEPLQGLDpLNRQ 438
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLD-INHQ 174
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
24-225 |
6.84e-12 |
|
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: 67.48 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVSdeW--Q---------RNNTDMLG 92
Cdd:COG4987 356 LTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIA--VvpQrphlfdttlRENLRLAR 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 93 PGEDDtgrttaeiiqDEVKDAprcmqlAQQFGITALLDRRFKYLST-----------GETRKTLLCQALMSEPDLLILDE 161
Cdd:COG4987 434 PDATD----------EELWAA------LERVGLGDWLAALPDGLDTwlgeggrrlsgGERRRLALARALLRDAPILLLDE 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 162 PFDGLDVASRQQLAERLASlHQSGITLVLV------LNRFDEIPefvqfagVLADCTLAETGAKEELLQQ 225
Cdd:COG4987 498 PTEGLDAATEQALLADLLE-ALAGRTVLLIthrlagLERMDRIL-------VLEDGRIVEQGTHEELLAQ 559
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
260-465 |
8.16e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.49 E-value: 8.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 260 RIVLNNGVVsyNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHP--QGY----SNDLTlfgrrrgsGETIWD 333
Cdd:COG1101 8 SKTFNPGTV--NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPpdSGSilidGKDVT--------KLPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 334 IKKHIGYV--------SSSLhldyrvstTVR-NVILS---GYFDSIGIyqAVSDRQQKLVQQWLDIL--GIDKRTaDAPF 399
Cdd:COG1101 78 RAKYIGRVfqdpmmgtAPSM--------TIEeNLALAyrrGKRRGLRR--GLTKKRRELFRELLATLglGLENRL-DTKV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128728 400 HSLSWGQ-QRLALIVrALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:COG1101 147 GLLSGGQrQALSLLM-ATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQA 212
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
252-479 |
9.28e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.08 E-value: 9.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 252 HALPANEPrIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGYsndlTLFGRRRGSGET 330
Cdd:PRK11247 5 ARLNQGTP-LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGlETPSAG----ELLAGTAPLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 331 IWDIKKhigyvsssLHLDYRVsTTVRNVIlsgyfDSIGIYQAVSDRQQKLvqQWLDILGIDKRTADAPfHSLSWGQ-QRL 409
Cdd:PRK11247 80 REDTRL--------MFQDARL-LPWKKVI-----DNVGLGLKGQWRDAAL--QALAAVGLADRANEWP-AALSGGQkQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128728 410 ALiVRALVKHPTLLILDEPLQGLDPLNR----QLIRRfvdvLISEGETQLLFVSHHAEDAPAcITHRLEFVPDG 479
Cdd:PRK11247 143 AL-ARALIHRPGLLLLDEPLGALDALTRiemqDLIES----LWQQHGFTVLLVTHDVSEAVA-MADRVLLIEEG 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
24-433 |
1.09e-11 |
|
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: 67.02 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELP----------LLKGERqsqfshITRLSFEQLQKLvsdewqRnntdmlgp 93
Cdd:COG4172 31 FDIAAGETLALVGESGSGKSVTALSILRLLPdpaahpsgsiLFDGQD------LLGLSERELRRI------R-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 94 geddtGRTTAEIIQD----------------EV---------KDA-PRCMQLAQQFGITALLDRRFKY---LSTGETRKT 144
Cdd:COG4172 91 -----GNRIAMIFQEpmtslnplhtigkqiaEVlrlhrglsgAAArARALELLERVGIPDPERRLDAYphqLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 145 LLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASL-HQSGITLVLV---LN---RF-DEIpefvqfaGVLADCTLAET 216
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLIthdLGvvrRFaDRV-------AVMRQGEIVEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 217 GAKEELLQ-------QALVAqlahseqlegvqlpepDEPSARHALPANEPRIVL--NNGVVSYndrPI------------ 275
Cdd:COG4172 239 GPTAELFAapqhpytRKLLA----------------AEPRGDPRPVPPDAPPLLeaRDLKVWF---PIkrglfrrtvghv 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 --LNNLSWQVNPGEHWQIVGPNGAGKSTL----LSLVtgdhpqGYSNDLTLFGRR--RGSGETIWDIKKHIGYV-----S 342
Cdd:COG4172 300 kaVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI------PSEGEIRFDGQDldGLSRRALRPLRRRMQVVfqdpfG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 343 SslhLDYRVstTVRNVILSGyFDSIGIYQAVSDRQQKlVQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPT 421
Cdd:COG4172 374 S---LSPRM--TVGQIIAEG-LRVHGPGLSAAERRAR-VAEALEEVGLDPAARHRYPHEFSGGQrQRIA-IARALILEPK 445
|
490
....*....|..
gi 16128728 422 LLILDEPLQGLD 433
Cdd:COG4172 446 LLVLDEPTSALD 457
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
257-464 |
1.13e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.35 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 257 NEPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTgdhpqgysndlTLFGRRRGS----GETIW 332
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVA-----------SLISPTSGTllfeGEDIS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 333 DIKKHIgyvssslhldYR--VSTTVRNVILSG---YFDSIGIYQAVSDR-QQKLVQQWLDILGIDKRTADAPFHSLSWGQ 406
Cdd:PRK10247 73 TLKPEI----------YRqqVSYCAQTPTLFGdtvYDNLIFPWQIRNQQpDPAIFLDDLERFALPDTILTKNIAELSGGE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 407 -QRLALIvRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSH------HAED 464
Cdd:PRK10247 143 kQRISLI-RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHdkdeinHADK 206
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
276-456 |
1.18e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.14 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQGYSndLTLFGRRRgSGETIWDIKKHIGYVSSSLHlDYRVSTT 354
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYlPQRGR--VKVMGREV-NAENEKWVRSKVGLVFQDPD-DQVFSST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 355 VRNVILSGYFDsIGIYQAVSDRQqklVQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
Cdd:PRK13647 97 VWDDVAFGPVN-MGLDKDEVERR---VEEALKAVRMWDFRDKPPYH-LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180
....*....|....*....|..
gi 16128728 435 LNRQLIRRFVDVLISEGETQLL 456
Cdd:PRK13647 172 RGQETLMEILDRLHNQGKTVIV 193
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
276-476 |
1.21e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQG-YsndltlfgrrrgSGETIWD--------IK----KHIGYVS 342
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtY------------EGEIIFEgeelqasnIRdterAGIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 343 SSLHLdyrVS--TTVRNVIL------SGYFDsigiYQAVSDRQQKLVQQwldiLGIDKrTADAPFHSLSWGQQRLALIVR 414
Cdd:PRK13549 89 QELAL---VKelSVLENIFLgneitpGGIMD----YDAMYLRAQKLLAQ----LKLDI-NPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128728 415 ALVKHPTLLILDEPLQGLdplnrqlirrfvdvliSEGETQLLF--VSHHAEDAPAC--ITHRLEFV 476
Cdd:PRK13549 157 ALNKQARLLILDEPTASL----------------TESETAVLLdiIRDLKAHGIACiyISHKLNEV 206
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
291-460 |
1.24e-11 |
|
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: 65.89 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 291 IVGPNGAGKSTLLSLVTG-DHP-QGY--SNDLTLFGRRRGsgetIWdIKKH---IGYV--SSSL--HLdyrvstTVRNVI 359
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAGlERPdSGRirLGGEVLQDSARG----IF-LPPHrrrIGYVfqEARLfpHL------SVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 360 LSGYFDSigiyqAVSDRQQKLvQQWLDILGI----DKRTadapfHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDP 434
Cdd:COG4148 99 LYGRKRA-----PRAERRISF-DEVVELLGIghllDRRP-----ATLSGGErQRVA-IGRALLSSPRLLLMDEPLAALDL 166
|
170 180
....*....|....*....|....*.
gi 16128728 435 LNRQLIRRFVDVLISEGETQLLFVSH 460
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSH 192
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
269-440 |
1.30e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.03 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 269 SYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLL----SLVTGDHPQGysNDLTLFGRR-RGSGETIWDIKK---HIGY 340
Cdd:PRK09984 13 TFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAG--SHIELLGRTvQREGRLARDIRKsraNTGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 341 VSSSLHLDYRVsTTVRNVILsGYFDSIGIYQAV----SDRQQKLVQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRAL 416
Cdd:PRK09984 91 IFQQFNLVNRL-SVLENVLI-GALGSTPFWRTCfswfTREQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRVAIARAL 167
|
170 180
....*....|....*....|....
gi 16128728 417 VKHPTLLILDEPLQGLDPLNRQLI 440
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIV 191
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
270-471 |
1.66e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.61 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 270 YNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHP-QG--YSNDLTLFGRRRGSGETIWDIKKHIGYVSSSL 345
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFlEKPsEGsiVVNGQTINLVRDKDGQLKVADKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 346 -----HLDYRVSTTVRNVILSGYFDSIGIYQAVSdRQQKLvqQWLDILGIDKRTADA-PFHsLSWGQQRLALIVRALVKH 419
Cdd:PRK10619 95 tmvfqHFNLWSHMTVLENVMEAPIQVLGLSKQEA-RERAV--KYLAKVGIDERAQGKyPVH-LSGGQQQRVSIARALAME 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16128728 420 PTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSHHAEDAPACITH 471
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFARHVSSH 221
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
271-481 |
1.66e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 64.30 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 271 NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSlVTGDHPQGYSNDLTLFGRRRGSGETIWDI-----KKHIGYVSSSL 345
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLK-VLNRLIEIYDSKIKVDGKVLYFGKDIFQIdaiklRKEVGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 346 HLDYRVSTtvrnvilsgyFDSIGI---YQAVSDRQQ--KLVQQWLDILGIDKRTAD---APFHSLSWGQQRLALIVRALV 417
Cdd:PRK14246 100 NPFPHLSI----------YDNIAYplkSHGIKEKREikKIVEECLRKVGLWKEVYDrlnSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128728 418 KHPTLLILDEPLQGLDPLNRQLIRRFVDVLisEGETQLLFVSHHAEDApACITHRLEFVPDGGL 481
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQV-ARVADYVAFLYNGEL 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
275-460 |
1.67e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.07 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 275 ILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGR--RRGSGETIWDIKKH-IGYVSSSLHL--D 348
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGlDTPT--SGDVIFNGQpmSKLSSAAKAELRNQkLGFIYQFHHLlpD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 349 YrvsTTVRNVILsgyfdSIGIYQAVSDRQQKLVQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEP 428
Cdd:PRK11629 102 F---TALENVAM-----PLLIGKKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|..
gi 16128728 429 LQGLDPLNRQLIRRFVDVLISEGETQLLFVSH 460
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTH 204
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
24-225 |
2.10e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.93 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGeLP---------LLKGERqsqfshITRLSFEQLQKL--------------VS 80
Cdd:COG0396 21 LTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPkyevtsgsiLLDGED------ILELSPDERARAgiflafqypveipgVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 81 dewqrnNTDMLgpgeddtgRTTAEIIQDEVKDAP----RCMQLAQQFGITA-LLDRrfkYL----STGETRKTLLCQALM 151
Cdd:COG0396 94 ------VSNFL--------RTALNARRGEELSAReflkLLKEKMKELGLDEdFLDR---YVnegfSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 152 SEPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLVLV--LNRF-DEI-PEFVQfagVLADCTLAETGAKeELLQQ 225
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIIthYQRIlDYIkPDFVH---VLVDGRIVKSGGK-ELALE 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
258-488 |
2.33e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.03 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 258 EPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTgdhpqgYSNDL----TLFGRRRGSGETIW- 332
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN------RMNDLnpevTITGSIVYNGHNIYs 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 333 ------DIKKHIGYVSSslHLDYRVSTTVRNVI----LSGYFDSIGIYQAVsDRQQKLVQQWLDIlgiDKRTADAPFhSL 402
Cdd:PRK14239 77 prtdtvDLRKEIGMVFQ--QPNPFPMSIYENVVyglrLKGIKDKQVLDEAV-EKSLKGASIWDEV---KDRLHDSAL-GL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRrfvDVLIS-EGETQLLFVSHHAEDAPAcITHRLEFVPDGGL 481
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIE---ETLLGlKDDYTMLLVTRSMQQASR-ISDRTGFFLDGDL 225
|
....*..
gi 16128728 482 YRYVLTK 488
Cdd:PRK14239 226 IEYNDTK 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
259-478 |
2.54e-11 |
|
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: 63.28 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 259 PRIVLNNGVVSYND--RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLslvtgdhpqgysndLTLFGRRRGSGETIW---- 332
Cdd:cd03244 1 GDIEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLL--------------LALFRLVELSSGSILidgv 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 333 DIKKhIGyvsssLHlDYR------------VSTTVR-NVILSGYFDSIGIYQAVSDRQQK-LVQQWLDilGIDKRTADAP 398
Cdd:cd03244 67 DISK-IG-----LH-DLRsrisiipqdpvlFSGTIRsNLDPFGEYSDEELWQALERVGLKeFVESLPG--GLDTVVEEGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 399 FHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRfvdvLISE---GETQLlfvshhaedapaCITHRLEF 475
Cdd:cd03244 138 EN-LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQK----TIREafkDCTVL------------TIAHRLDT 200
|
...
gi 16128728 476 VPD 478
Cdd:cd03244 201 IID 203
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
24-222 |
2.66e-11 |
|
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: 63.16 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEqLQKLVSDEWQRNNTDmlgpgEDDTGRTTA 103
Cdd:cd03265 21 FRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLSVD-----DELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 104 EII-------QDEVKDapRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
Cdd:cd03265 95 YIHarlygvpGAERRE--RIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128728 177 RLASLHQS-GITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEEL 222
Cdd:cd03265 173 YIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
261-434 |
2.84e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.62 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLL-SLVTGDHPQGYS---NDLTLFGRRRGSGET--IWDI 334
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLrCINLLEQPEAGTirvGDITIDTARSLSQQKglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 335 KKHIGYVSSSLHLdYRVSTTVRNVILSgyfdSIGIYQAVSDRQQKLVQQWLDILGIDKRTADAPfHSLSWGQQRLALIVR 414
Cdd:PRK11264 84 RQHVGFVFQNFNL-FPHRTVLENIIEG----PVIVKGEPKEEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIAR 157
|
170 180
....*....|....*....|
gi 16128728 415 ALVKHPTLLILDEPLQGLDP 434
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDP 177
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-191 |
3.44e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 64.71 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 1 MSSLQILQGTFRLSDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGelpLLKgerqsqfshIT--RLSFEQlqKL 78
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG---LED---------PTsgEILIGG--RD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 79 VSDewqrnntdmLGPGEDDTG-------------------------RTTAEIIQDEVKDAprcmqlAQQFGITALLDRRF 133
Cdd:COG3839 67 VTD---------LPPKDRNIAmvfqsyalyphmtvyeniafplklrKVPKAEIDRRVREA------AELLGLEDLLDRKP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 134 KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQS-GITLVLV 191
Cdd:COG3839 132 KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYV 190
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
267-479 |
3.55e-11 |
|
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: 66.19 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 267 VVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRGSgeTIWDIKKHIGYVSSSLH 346
Cdd:TIGR01257 1946 VYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVT-SGDATVAGKSILT--NISDVHQNMGYCPQFDA 2022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 347 LDYrvsttvrnvILSGYfDSIGIY---QAVSDRQQKLVQQW-LDILGIdKRTADAPFHSLSWGQQRLALIVRALVKHPTL 422
Cdd:TIGR01257 2023 IDD---------LLTGR-EHLYLYarlRGVPAEEIEKVANWsIQSLGL-SLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128728 423 LILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLfVSHHAEDAPACIThRLEFVPDG 479
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL-TSHSMEECEALCT-RLAIMVKG 2146
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
269-451 |
3.62e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.37 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 269 SYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYSN------DLTLFG----RRRGsgetiwdikkhI 338
Cdd:PRK10895 12 AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddeDISLLPlharARRG-----------I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 339 GYVSSSLHLDYRvsttvrnviLSGYFDSIGIYQAVSD----RQQKLVQQWLDILGIDkRTADAPFHSLSWGQQRLALIVR 414
Cdd:PRK10895 81 GYLPQEASIFRR---------LSVYDNLMAVLQIRDDlsaeQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIAR 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 16128728 415 ALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEG 451
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSG 187
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
261-465 |
3.67e-11 |
|
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: 62.66 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETIWDI---KK 336
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGlEEPTS--------GRIYIGGRDVTDLppkDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 337 HIGYV--SSSLHLDYRVsttvrnvilsgyFDSI--GIYQAVSDRQQ--KLVQQWLDILGIDKRTADAPfHSLSWGQ-QRL 409
Cdd:cd03301 73 DIAMVfqNYALYPHMTV------------YDNIafGLKLRKVPKDEidERVREVAELLQIEHLLDRKP-KQLSGGQrQRV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128728 410 ALiVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:cd03301 140 AL-GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEA 194
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
276-466 |
4.02e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 63.71 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG------------DHPQGYSndltlfgrRRGsgetIWDIKKHIGYV-- 341
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGilkpssgrilfdGKPIDYS--------RKG----LMKLRESVGMVfq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 342 -------SSSLHLDyrVSTTVRNVILSgyfdsigiyqavSDRQQKLVQQWLDILGIDkRTADAPFHSLSWGQQRLALIVR 414
Cdd:PRK13636 90 dpdnqlfSASVYQD--VSFGAVNLKLP------------EDEVRKRVDNALKRTGIE-HLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16128728 415 ALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDAP 466
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVP 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
24-222 |
4.20e-11 |
|
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: 62.52 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfSHITRLSFEQLQKLVSDewqrnntdMLG--PGED--DTG 99
Cdd:cd03263 23 LNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGT-----AYINGYSIRTDRKAARQ--------SLGycPQFDalFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 100 RTTAEIIQ-------DEVKDAPRCM-QLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
Cdd:cd03263 90 LTVREHLRfyarlkgLPKSEIKEEVeLLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128728 172 QQLAERLASLhQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEEL 222
Cdd:cd03263 170 RAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
256-481 |
5.14e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.19 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 256 ANEPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVT--GDHPQGY--SNDLTLFGRRRGSGETI 331
Cdd:PRK14271 17 AAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmNDKVSGYrySGDVLLGGRSIFNYRDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 332 WDIKKHIGYVssslhldYRVSTTVRNVILSGYFDSIGIYQAVSDRQ-QKLVQQWLDILG----IDKRTADAPFHsLSWGQ 406
Cdd:PRK14271 97 LEFRRRVGML-------FQRPNPFPMSIMDNVLAGVRAHKLVPRKEfRGVAQARLTEVGlwdaVKDRLSDSPFR-LSGGQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 407 QRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISegETQLLFVSHHAEDApACITHRLEFVPDGGL 481
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQA-ARISDRAALFFDGRL 240
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-190 |
5.32e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.94 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELP-----LLKGERQSQFS--HITR----LSFEQLQKLVSDEWQRnnTDMLG 92
Cdd:COG4138 17 AQVNAGELIHLIGPNGAGKSTLLARMAGLLPgqgeiLLNGRPLSDWSaaELARhrayLSQQQSPPFAMPVFQY--LALHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 93 PGEDDTGRTTAEIiqdevkdaprcMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALM-------SEPDLLILDEPFDG 165
Cdd:COG4138 95 PAGASSEAVEQLL-----------AQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNS 163
|
170 180
....*....|....*....|....*..
gi 16128728 166 LDVAsrQQLA--ERLASLHQSGITLVL 190
Cdd:COG4138 164 LDVA--QQAAldRLLRELCQQGITVVM 188
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
15-245 |
5.69e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.72 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 15 DTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALA-------GELpLLKGERQSQFS---HITRLSF--EQL------- 75
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFArlltpqsGTV-FLGDKPISMLSsrqLARRLALlpQHHltpegit 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 76 -QKLVsdEWQRNntdmlgPGEDDTGRTTAEiiqdevkDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEP 154
Cdd:PRK11231 93 vRELV--AYGRS------PWLSLWGRLSAE-------DNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 155 DLLILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQALVAQLAhs 234
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVF-- 235
|
250
....*....|.
gi 16128728 235 eQLEGVQLPEP 245
Cdd:PRK11231 236 -DVEAEIHPEP 245
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
276-488 |
7.29e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.83 E-value: 7.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG--DHPQGYSNDLTLFGRRRGSGETIWDIKKHIGYVSSSLHLDYRVST 353
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 354 TVRNVILSGyfDSIGIYQavsDRQQKLVQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:PRK13643 102 VLKDVAFGP--QNFGIPK---EKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 434 PLNRQLIRRFVDVLISEGETQLLfvshhaedapacITHRLEFVPDGGLYRYVLTK 488
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVL------------VTHLMDDVADYADYVYLLEK 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
10-230 |
7.85e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.83 E-value: 7.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 10 TFRLSD-TKTLQLPQLTLNAGDSWAFVGSNGSGKSALaralageLPLLKGERQSQFSHITRLSFEQLQKlvSDEWQRNNT 88
Cdd:PRK13647 11 HFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTL-------LLHLNGIYLPQRGRVKVMGREVNAE--NEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 89 DMLGPGEDDtgRTTAEIIQDEVKDAPRCMQLAQQ------------FGITALLDRRFKYLSTGETRKTLLCQALMSEPDL 156
Cdd:PRK13647 82 GLVFQDPDD--QVFSSTVWDDVAFGPVNMGLDKDeverrveealkaVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 157 LILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADC-TLAEtGAKEELLQQALVAQ 230
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGrVLAE-GDKSLLTDEDIVEQ 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
276-461 |
9.94e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.88 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGE-HwQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRgSGETIWDIKKH-IGYVSSSLHLdyrVST 353
Cdd:COG1129 20 LDGVSLELRPGEvH-ALLGENGAGKSTLMKILSGVYQPD-SGEILLDGEPV-RFRSPRDAQAAgIAIIHQELNL---VPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 354 -TVR-NVILSGYFDSIGIyqaVSDRQQ-KLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQ 430
Cdd:COG1129 94 lSVAeNIFLGREPRRGGL---IDWRAMrRRARELLARLGLDID-PDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTA 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 16128728 431 GLDP-----LNRqLIRRfvdvLISEGETqLLFVSHH 461
Cdd:COG1129 170 SLTEreverLFR-IIRR----LKAQGVA-IIYISHR 199
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
136-433 |
1.08e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDvasrqqlAERLASLHQ-----SGiTLVLV----------------LNR 194
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD-------AESVAWLEQflhdyPG-TVVAVthdryfldnvagwileLDR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 195 FDEIPEFVQFAGVLA--DCTLAETGAKEELLQQALvaqlahSEQLEGVQLpepdEPSARHA------------------- 253
Cdd:PRK11819 236 GRGIPWEGNYSSWLEqkAKRLAQEEKQEAARQKAL------KRELEWVRQ----SPKARQAkskarlaryeellseeyqk 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 254 -LPANE------PRivLNNGVV-------SYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHpQGYSNDLT 319
Cdd:PRK11819 306 rNETNEifippgPR--LGDKVIeaenlskSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQE-QPDSGTIK 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 320 LfgrrrgsGETIwdikkHIGYVSSSL-HLDyrVSTTVRNVIlSGYFDSI--GIYQaVSDR------------QQKLVQQw 384
Cdd:PRK11819 383 I-------GETV-----KLAYVDQSRdALD--PNKTVWEEI-SGGLDIIkvGNRE-IPSRayvgrfnfkggdQQKKVGV- 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 16128728 385 ldilgidkrtadapfhsLSWGQQ-RLALiVRALVKHPTLLILDEPLQGLD 433
Cdd:PRK11819 446 -----------------LSGGERnRLHL-AKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-443 |
1.09e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 17 KTLQLPQLTLNAGDSWAFVGSNGSGKSALARAL-------AGELPLL------KGERQSQFSHITRLSfeqlQKLvsdew 83
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLtgiytrdAGSILYLgkevtfNGPKSSQEAGIGIIH----QEL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 84 qrNNTDMLGPGEDD-TGR--TTAEIIQDEVKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
Cdd:PRK10762 89 --NLIPQLTIAENIfLGRefVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 161 EPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQALVaqlahsEQLEGV 240
Cdd:PRK10762 167 EPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLI------EMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 241 QLpepDEPSARHALPANEPRIVLNN----GVvsyndrpilNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySN 316
Cdd:PRK10762 241 KL---EDQYPRLDKAPGEVRLKVDNlsgpGV---------NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRT-SG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 317 DLTLFGRRRGSGETIWDIKKHIGYVSSSLHLDYRV-STTVR-NVILS--GYFDSIGIyQAVSDRQQKLVQQWLDILGIDK 392
Cdd:PRK10762 308 YVTLDGHEVVTRSPQDGLANGIVYISEDRKRDGLVlGMSVKeNMSLTalRYFSRAGG-SLKHADEQQAVSDFIRLFNIKT 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 393 RTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR----QLIRRF 443
Cdd:PRK10762 387 PSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKkeiyQLINQF 441
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
24-191 |
1.16e-10 |
|
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: 60.28 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshitrLSFEqlqklvsdewqrnntdmlgpgeddtGRTTA 103
Cdd:cd03229 21 LNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGS----------ILID-------------------------GEDLT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 104 EIIQDEVKDAPRCMQLAQQFGI----TALLDRRFKyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLA 179
Cdd:cd03229 66 DLEDELPPLRRRIGMVFQDFALfphlTVLENIALG-LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLK 144
|
170
....*....|...
gi 16128728 180 SLH-QSGITLVLV 191
Cdd:cd03229 145 SLQaQLGITVVLV 157
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
269-465 |
1.18e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.12 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 269 SYND--RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-----DHPQgysNDLTLFGRRRGSgETIWDIKKHIGYV 341
Cdd:PRK13640 14 TYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpdDNPN---SKITVDGITLTA-KTVWDIREKVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 342 SSSLHLDYrVSTTVRNVILSGYFDsigiyQAVSDRQ-QKLVQQWLDILGIdKRTADAPFHSLSWGQ-QRLAlIVRALVKH 419
Cdd:PRK13640 90 FQNPDNQF-VGATVGDDVAFGLEN-----RAVPRPEmIKIVRDVLADVGM-LDYIDSEPANLSGGQkQRVA-IAGILAVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128728 420 PTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
242-479 |
1.26e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.93 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 242 LPEPdEPSARHALpanEPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgysndltl 320
Cdd:PRK11607 5 IPRP-QAKTRKAL---TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPT-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 321 fgrrrgSGETIWDikkhigYVSSSLHLDYRVSTtvrNVILSGY--FDSIGIYQ--AVSDRQQKL--------VQQWLDIL 388
Cdd:PRK11607 73 ------AGQIMLD------GVDLSHVPPYQRPI---NMMFQSYalFPHMTVEQniAFGLKQDKLpkaeiasrVNEMLGLV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 389 GIDKRTADAPfHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLD-PLNRQLIRRFVDVLISEGETQLLfVSHHAEDAP 466
Cdd:PRK11607 138 HMQEFAKRKP-HQLSGGQrQRVAL-ARSLAKRPKLLLLDEPMGALDkKLRDRMQLEVVDILERVGVTCVM-VTHDQEEAM 214
|
250
....*....|....*...
gi 16128728 467 A-----CITHRLEFVPDG 479
Cdd:PRK11607 215 TmagriAIMNRGKFVQIG 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
24-225 |
1.49e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.10 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQS---QFSHITRLSF-EQLQKLVSDEWQRNNTDMLgpgEDDTG 99
Cdd:PRK13646 28 TEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVddiTITHKTKDKYiRPVRKRIGMVFQFPESQLF---EDTVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 100 RttaEII---------QDEVKDapRCMQLAQQFGITA-LLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
Cdd:PRK13646 105 R---EIIfgpknfkmnLDEVKN--YAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128728 170 SRQQLAERLASLH-QSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQ 225
Cdd:PRK13646 180 SKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-198 |
1.62e-10 |
|
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: 60.14 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshITRLsfeqlqklvsdewqrnntdmlgpGEDDTGRTTA 103
Cdd:cd03215 21 FEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGE-------ITLD-----------------------GKPVTRRSPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 104 EIIQDEVKDAP---RCMQLAQQFGI---TALLDrrfkYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAER 177
Cdd:cd03215 71 DAIRAGIAYVPedrKREGLVLDLSVaenIALSS----LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRL 146
|
170 180
....*....|....*....|.
gi 16128728 178 LASLHQSGITLVLVLNRFDEI 198
Cdd:cd03215 147 IRELADAGKAVLLISSELDEL 167
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
24-178 |
1.82e-10 |
|
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: 61.19 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGEL-P---------LLKGERQSQFSHITRLSFEQLQKLVSDewqrnntdmLGP 93
Cdd:cd03267 42 FTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPtsgevrvagLVPWKRRKKFLRRIGVVFGQKTQLWWD---------LPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 94 GedDTGRTTAEIIQ-DEVKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ 172
Cdd:cd03267 113 I--DSFYLLAAIYDlPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
....*.
gi 16128728 173 QLAERL 178
Cdd:cd03267 191 NIRNFL 196
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
197-476 |
1.89e-10 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 63.18 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 197 EIPEFVQFAGVLAdctlAETGAKEEL---LQQALVAQLAHSEQLEGVqlPEPDEPSARHALPANEP-RIVLNNGVVSY-- 270
Cdd:TIGR02204 276 TLGQFVFYAVMVA----GSIGTLSEVwgeLQRAAGAAERLIELLQAE--PDIKAPAHPKTLPVPLRgEIEFEQVNFAYpa 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 271 -NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQGysndltlfGRRRGSGETIW-----DIKKHIGYVSS 343
Cdd:TIGR02204 350 rPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYdPQS--------GRILLDGVDLRqldpaELRARMALVPQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 344 SLHLdyrVSTTVRNVILSGYFDSIG---IYQAVSDRQQKLVQQWLDilGIDKRTADAPFhSLSWGQ-QRLAlIVRALVKH 419
Cdd:TIGR02204 422 DPVL---FAASVMENIRYGRPDATDeevEAAARAAHAHEFISALPE--GYDTYLGERGV-TLSGGQrQRIA-IARAILKD 494
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128728 420 PTLLILDEPLQGLDPLNRQLIRRFVDVLISeGETQLLfvshhaedapacITHRLEFV 476
Cdd:TIGR02204 495 APILLLDEATSALDAESEQLVQQALETLMK-GRTTLI------------IAHRLATV 538
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
276-464 |
1.92e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.60 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgysndltLFGRRRGS----GETIWD-------IKKHIGYVSSs 344
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNG-----------LLKPTSGKiiidGVDITDkkvklsdIRKKVGLVFQ- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 345 lHLDYRV-STTV--------RNVILSGyfdsigiyQAVSDRqqklVQQWLDILGIDKRT-AD-APFhSLSWGQQRLALIV 413
Cdd:PRK13637 91 -YPEYQLfEETIekdiafgpINLGLSE--------EEIENR----VKRAMNIVGLDYEDyKDkSPF-ELSGGQKRRVAIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128728 414 RALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAED 464
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMED 207
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
29-190 |
2.05e-10 |
|
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: 60.13 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 29 GDSWAFVGSNGSGKSALARALAGELPLLKG--ERQSQFSHITRLSFEQLQKLVSDEWQRNNTDMLGP--GED------DT 98
Cdd:TIGR01166 18 GEVLALLGANGAGKSTLLLHLNGLLRPQSGavLIDGEPLDYSRKGLLERRQRVGLVFQDPDDQLFAAdvDQDvafgplNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 99 GRTTAEIiQDEVKDAprcmqlAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERL 178
Cdd:TIGR01166 98 GLSEAEV-ERRVREA------LTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAIL 170
|
170
....*....|..
gi 16128728 179 ASLHQSGITLVL 190
Cdd:TIGR01166 171 RRLRAEGMTVVI 182
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
24-198 |
2.24e-10 |
|
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: 59.32 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshItRLSFEQLQKLVSDEWQRNntdmlgpgeddtgrtTA 103
Cdd:cd03228 23 LTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE-------I-LIDGVDLRDLDLESLRKN---------------IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 104 EIIQDevkdaprcmqlaqqfgiTALLDR--RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASL 181
Cdd:cd03228 80 YVPQD-----------------PFLFSGtiRENILSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAL 142
|
170 180
....*....|....*....|...
gi 16128728 182 HQsGITLVLV------LNRFDEI 198
Cdd:cd03228 143 AK-GKTVIVIahrlstIRDADRI 164
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-198 |
2.35e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.16 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 16 TKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELP------LLKGERQSQFSHItrlsfEQLQKLVSDEWQRNNTD 89
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRpqkgkvLVSGIDTGDFSKL-----QGIRKLVGIVFQNPETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 90 MLGPG-EDDTGRTTAEIIQDEVKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
Cdd:PRK13644 90 FVGRTvEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190
....*....|....*....|....*....|
gi 16128728 169 ASRQQLAERLASLHQSGITLVLVLNRFDEI 198
Cdd:PRK13644 170 DSGIAVLERIKKLHEKGKTIVYITHNLEEL 199
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-194 |
2.36e-10 |
|
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: 59.54 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 10 TFRLSDTKTLQLPQL--TLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVSDEWQRnn 87
Cdd:cd03246 7 SFRYPGAEPPVLRNVsfSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 88 tDMLGPGeddtgrTTAEIIqdevkdaprcmqlaqqfgitalldrrfkyLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
Cdd:cd03246 85 -DELFSG------SIAENI-----------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180
....*....|....*....|....*..
gi 16128728 168 VASRQQLAERLASLHQSGITLVLVLNR 194
Cdd:cd03246 129 VEGERALNQAIAALKAAGATRIVIAHR 155
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
275-481 |
2.44e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.56 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 275 ILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdHPQGYSNDLTLFGR--RRGSGETIWDIK-KHIGYVSSSLHLdyrV 351
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAG-LDDGSSGEVSLVGQplHQMDEEARAKLRaKHVGFVFQSFML---I 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 352 ST--TVRNVILSgyfdsiGIYQAVSDRQQKL-VQQWLDILGIDKRTADAPfHSLSWG-QQRLALiVRALVKHPTLLILDE 427
Cdd:PRK10584 101 PTlnALENVELP------ALLRGESSRQSRNgAKALLEQLGLGKRLDHLP-AQLSGGeQQRVAL-ARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128728 428 PLQGLDplnRQLIRRFVDVLIS---EGETQLLFVSHHAEDAPACiTHRLEFVpDGGL 481
Cdd:PRK10584 173 PTGNLD---RQTGDKIADLLFSlnrEHGTTLILVTHDLQLAARC-DRRLRLV-NGQL 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-189 |
2.57e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.89 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 25 TLNAGDSWAFVGSNGSGKSALARALAGELPLLKGerqsqfshitRLSFEqlqklvsdewqrnntdmlgpGEDDTGRTTAE 104
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAG----------TIKLD--------------------GGDIDDPDVAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 105 II-----QDEVKDA------------------PRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
Cdd:PRK13539 74 AChylghRNAMKPAltvaenlefwaaflggeeLDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180
....*....|....*....|....*....
gi 16128728 162 PFDGLDVASRQQLAERLAS-LHQSGITLV 189
Cdd:PRK13539 154 PTAALDAAAVALFAELIRAhLAQGGIVIA 182
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
271-433 |
2.60e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.89 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 271 NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqgysndlTLFGRRRGSGETIwDIKKHIG---YVSsslHL 347
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP-------PAAGTIKLDGGDI-DDPDVAEachYLG---HR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 348 DY-RVSTTVRnvilsgyfDSIGIYQAVSDRQQKLVQQWLDILGIDkRTADAPFHSLSWGQQRLALIVRALVKHPTLLILD 426
Cdd:PRK13539 82 NAmKPALTVA--------ENLEFWAAFLGGEELDIAAALEAVGLA-PLAHLPFGYLSAGQKRRVALARLLVSNRPIWILD 152
|
....*..
gi 16128728 427 EPLQGLD 433
Cdd:PRK13539 153 EPTAALD 159
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
261-433 |
2.70e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.97 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG--DHPQGysnDLtLFGRRRGSgetiwDI---K 335
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleDITSG---DL-FIGEKRMN-----DVppaE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 336 KHIGYVSSSLHLdYRVSTTVRNVilsgyfdSIGIYQAVSDRQ--QKLVQQWLDILGIDKRTADAPfHSLSWGQ-QRLAlI 412
Cdd:PRK11000 75 RGVGMVFQSYAL-YPHLSVAENM-------SFGLKLAGAKKEeiNQRVNQVAEVLQLAHLLDRKP-KALSGGQrQRVA-I 144
|
170 180
....*....|....*....|.
gi 16128728 413 VRALVKHPTLLILDEPLQGLD 433
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLD 165
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
256-461 |
2.87e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.05 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 256 ANEPRIVLNNGVVSY-NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdHPQGYSNDLTLFGRrrgsgETIWDI 334
Cdd:PRK15056 2 MQQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMG-FVRLASGKISILGQ-----PTRQAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 335 KKH-IGYVSSSLHLDYRVSTTVRNVILSGYFDSIGIYQAVSDRQQKLVQQWL---DILGIDKRTadapFHSLSWGQQRLA 410
Cdd:PRK15056 76 QKNlVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALarvDMVEFRHRQ----IGELSGGQKKRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128728 411 LIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLlfVSHH 461
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTML--VSTH 200
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-245 |
3.61e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 60.63 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 4 LQILQGTFRLSD-TKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGE--RQSQFSHITRLSFEQLQKLVS 80
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRilFDGKPIDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 81 DEWQRNNTDMLGPG--EDDT-GRTTAEIIQDEVKDapRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLL 157
Cdd:PRK13636 86 MVFQDPDNQLFSASvyQDVSfGAVNLKLPEDEVRK--RVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 158 ILDEPFDGLDVASRQQLAERLASLHQS-GITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELlqqalvaqLAHSEQ 236
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV--------FAEKEM 235
|
....*....
gi 16128728 237 LEGVQLPEP 245
Cdd:PRK13636 236 LRKVNLRLP 244
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
127-246 |
4.03e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.80 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 127 ALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQ-SGITLVLVLNRFDEIPEFVQFA 205
Cdd:PRK13634 137 ELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQI 216
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 16128728 206 GVLADCTLAETGAKEELLQqalvaqlaHSEQLEGVQLPEPD 246
Cdd:PRK13634 217 VVMHKGTVFLQGTPREIFA--------DPDELEAIGLDLPE 249
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
261-465 |
4.37e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 60.03 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLV-------TGD-HPQGYSNDLTlfgrRRGSGETIW 332
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQlNIAGHQFDFS----QKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 333 DIKKHIGYVSSSLHLDYRVstTVRNVILSGYFDSIGIY-QAVSDRQQKLVQQwldiLGIDKRTADAPFHsLSWGQQRLAL 411
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHL--TVMENLIEAPCKVLGLSkEQAREKAMKLLAR----LRLTDKADRFPLH-LSGGQQQRVA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16128728 412 IVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLfVSHHAEDA 465
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVI-VTHEVEFA 204
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
276-433 |
5.15e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.85 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqgYSNDLTLFGRRRGSgetiWDIK---KHIGYVS--SSLHLDYR 350
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP--GQGEILLNGRPLSD----WSAAelaRHRAYLSqqQSPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 351 VsttvrnvilsgyFDSIGIYQ---AVSDRQQKLVQQWLDILGIDKRTAdAPFHSLSWG-QQRLALIVRALVKHPT----- 421
Cdd:COG4138 86 V------------FQYLALHQpagASSEAVEQLLAQLAEALGLEDKLS-RPLTQLSGGeWQRVRLAAVLLQVWPTinpeg 152
|
170
....*....|...
gi 16128728 422 -LLILDEPLQGLD 433
Cdd:COG4138 153 qLLLLDEPMNSLD 165
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-223 |
5.15e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.09 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 8 QGTFRLSDTKT-LQLPQLTLNAGDSWAFVGSNGSGKSALARALAG-ELPLlKGERQSQFSHITRLSFEQLQKLvsdewqR 85
Cdd:PRK10419 16 GGLSGKHQHQTvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlESPS-QGNVSWRGEPLAKLNRAQRKAF------R 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 86 NNTDML---GPGEDDTGRTTAEIIQ---------DEVKDAPRCMQLAQQFGITA-LLDRRFKYLSTGETRKTLLCQALMS 152
Cdd:PRK10419 89 RDIQMVfqdSISAVNPRKTVREIIReplrhllslDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128728 153 EPDLLILDEPFDGLDVASRQQLAERLASL-HQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELL 223
Cdd:PRK10419 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKL 240
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
270-490 |
5.30e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.02 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 270 YNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG------------DHPQGYSNDlTLFGRRRGSGETIWDIKKH 337
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGllrpqkgavlwqGKPLDYSKR-GLLALRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 338 IGYVSsslhLDYRVSTTVRNvilsgyfdsIGIYQAVSDRQQKLVQQWLDILGIDKRtadaPFHSLSWGQQRLALIVRALV 417
Cdd:PRK13638 90 IFYTD----IDSDIAFSLRN---------LGVPEAEITRRVDEALTLVDAQHFRHQ----PIQCLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 418 KHPTLLILDEPLQGLDPLNRQ----LIRRFVD----VLISEGETQLL-------FVSHHAE----DAPACITHRLEFVPD 478
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTqmiaIIRRIVAqgnhVIISSHDIDLIyeisdavYVLRQGQilthGAPGEVFACTEAMEQ 232
|
250
....*....|..
gi 16128728 479 GGLYRYVLTKIY 490
Cdd:PRK13638 233 AGLTQPWLVKLH 244
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
257-465 |
5.47e-10 |
|
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: 60.82 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 257 NEPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRrrgsgetiwDI-- 334
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQT-AGTIYQGGR---------DItr 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 335 ----KKHIGYVSSSLHLdYRVSTTVRNVilsGYfdsiGIYQAVSDRQQKL--VQQWLDILGIDKRTADAPfHSLSWGQQ- 407
Cdd:TIGR03265 71 lppqKRDYGIVFQSYAL-FPNLTVADNI---AY----GLKNRGMGRAEVAerVAELLDLVGLPGSERKYP-GQLSGGQQq 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 408 RLALiVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:TIGR03265 142 RVAL-ARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEA 198
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
259-461 |
5.55e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 259 PRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVtgDHPQGYSNDLTLFGRRRGSGETIWD----- 333
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL--NRMNELESEVRVEGRVEFFNQNIYErrvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 334 --IKKHIGYVSSSLHLdYRVST---TVRNVILSGYFDSIGIyQAVSDRQQKLVQQWLDILG-IDKRTADapfhsLSWGQQ 407
Cdd:PRK14258 84 nrLRRQVSMVHPKPNL-FPMSVydnVAYGVKIVGWRPKLEI-DDIVESALKDADLWDEIKHkIHKSALD-----LSGGQQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16128728 408 RLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHH 461
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
268-465 |
5.88e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.71 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 268 VSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRR-RGSGETIWDIKKHIGYvssslh 346
Cdd:PRK11248 9 ADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGKPvEGPGAERGVVFQNEGL------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 347 LDYRvsTTVRNVILSGYFDSIGIYQAVSDRQQKLVQqwLDILGIDKRtadaPFHSLSWGQQRLALIVRALVKHPTLLILD 426
Cdd:PRK11248 82 LPWR--NVQDNVAFGLQLAGVEKMQRLEIAHQMLKK--VGLEGAEKR----YIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 16128728 427 EPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA 465
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-192 |
6.65e-10 |
|
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: 59.50 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 14 SDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVSDE---WQRNN--- 87
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIgmiFQQFNlie 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 88 -----TDMLGP--GEDDTGRTTAEIIQDEvkDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
Cdd:cd03256 92 rlsvlENVLSGrlGRRSTWRSLFGLFPKE--EKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILAD 169
|
170 180 190
....*....|....*....|....*....|...
gi 16128728 161 EPFDGLDVASRQQLAERLASLHQS-GITLVLVL 192
Cdd:cd03256 170 EPVASLDPASSRQVMDLLKRINREeGITVIVSL 202
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
259-474 |
7.00e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 59.49 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 259 PRIVLNNGVVSY----NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRR-RGSG---- 328
Cdd:COG4525 2 SMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGfLAPS--SGEITLDGVPvTGPGadrg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 329 -----ETI--WdikkhigyvssslhldyrvsttvRNVIlsgyfDSIGI---YQAVSDRQ-QKLVQQWLDILGIDKrTADA 397
Cdd:COG4525 80 vvfqkDALlpW-----------------------LNVL-----DNVAFglrLRGVPKAErRARAEELLALVGLAD-FARR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 398 PFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDA------------ 465
Cdd:COG4525 131 RIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEAlflatrlvvmsp 210
|
250
....*....|
gi 16128728 466 -PACITHRLE 474
Cdd:COG4525 211 gPGRIVERLE 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
276-460 |
8.09e-10 |
|
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: 60.07 E-value: 8.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGysndltlfGRRRGS----GETIWDIK---------KHIGYV- 341
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPP--------GITSGEilfdGEDLLKLSekelrkirgREIQMIf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 342 ---SSSLHLDYRVSTTVRNVILsgyfdsigIYQAVSDRQ-QKLVQQWLDILGID--KRTADA-PfHSLSWGQ-QRlALIV 413
Cdd:COG0444 93 qdpMTSLNPVMTVGDQIAEPLR--------IHGGLSKAEaRERAIELLERVGLPdpERRLDRyP-HELSGGMrQR-VMIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128728 414 RALVKHPTLLILDEPLQGLDPLNR----QLIRRfvdvLISEGETQLLFVSH 460
Cdd:COG0444 163 RALALEPKLLIADEPTTALDVTIQaqilNLLKD----LQRELGLAILFITH 209
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
276-467 |
8.60e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 59.72 E-value: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRRgSGETIWDIKKHIGYVSSSLHLDYrVSTTV 355
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE-FEGKVKIDGELL-TAENVWNLRRKIGMVFQNPDNQF-VGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 356 RNVILSGyFDSIGIYQavSDRQQKLVQQWLDILGIDKRTADAPfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPL 435
Cdd:PRK13642 100 EDDVAFG-MENQGIPR--EEMIKRVDEALLAVNMLDFKTREPA--RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190
....*....|....*....|....*....|..
gi 16128728 436 NRQLIRRFVDVLISEGETQLLFVSHHAEDAPA 467
Cdd:PRK13642 175 GRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS 206
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-197 |
8.76e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.64 E-value: 8.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 10 TFRLSDTKTLQLPQ--LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGErqSQFSHITrLSFE---QLQKLVSDEWQ 84
Cdd:PRK13635 12 SFRYPDAATYALKDvsFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGT--ITVGGMV-LSEEtvwDVRRQVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 85 RNNTDMLGPG-EDDT--GRTTAEIIQDEVkdAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
Cdd:PRK13635 89 NPDNQFVGATvQDDVafGLENIGVPREEM--VERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDE 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 16128728 162 PFDGLDVASRQQLAERLASL-HQSGITLVLVLNRFDE 197
Cdd:PRK13635 167 ATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDE 203
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
263-461 |
1.06e-09 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 58.81 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 263 LNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYSNDLTLFGrrrgsGETIWDIK------- 335
Cdd:TIGR01978 3 IKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILFK-----GQDLLELEpderara 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 336 ---------KHIGYVSSSLHLdyRVSTTVRNvilsgyfdSIGIYQAVSDRQ-QKLVQQWLDILGID----KRTADAPFhs 401
Cdd:TIGR01978 78 glflafqypEEIPGVSNLEFL--RSALNARR--------SARGEEPLDLLDfEKLLKEKLALLDMDeeflNRSVNEGF-- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 402 lSWGQQRLALIVRALVKHPTLLILDEPLQGLDplnrqlirrfVDVL--ISEG-------ETQLLFVSHH 461
Cdd:TIGR01978 146 -SGGEKKRNEILQMALLEPKLAILDEIDSGLD----------IDALkiVAEGinrlrepDRSFLIITHY 203
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
24-191 |
1.07e-09 |
|
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: 58.42 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGerqsqfshitRLSFEQlqKLVSDewqrnntdmLGPGEddtgRTTA 103
Cdd:cd03301 21 LDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSG----------RIYIGG--RDVTD---------LPPKD----RDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 104 EIIQD-----------------EVKDAP------RCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
Cdd:cd03301 76 MVFQNyalyphmtvydniafglKLRKVPkdeideRVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190
....*....|....*....|....*....|..
gi 16128728 161 EPFDGLDVASRQQLAERLASLHQS-GITLVLV 191
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRlGTTTIYV 187
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
24-196 |
1.23e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.43 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSqfshitrlsfeqlqKLVSDEWQRNntdmlGPGEDDTGRtta 103
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV--------------DVPDNQFGRE-----ASLIDAIGR--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 104 eiiQDEVKDAprcMQLAQQFGIT--ALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASL 181
Cdd:COG2401 109 ---KGDFKDA---VELLNAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKL 182
|
170
....*....|....*.
gi 16128728 182 -HQSGITLVLVLNRFD 196
Cdd:COG2401 183 aRRAGITLVVATHHYD 198
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-460 |
1.23e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.57 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 2 SSLQILQGTFRLSDTKTLqlpqlTLNAGDSWAFVGSNGSGKSALaralageLPLLKGERQSQFSHITRLS---------- 71
Cdd:PRK10636 5 SSLQIRRGVRVLLDNATA-----TINPGQKVGLVGKNGCGKSTL-------LALLKNEISADGGSYTFPGnwqlawvnqe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 72 ------------------FEQLQKLVSDEWQRNNTDMLGPGEDDTGRTTAEIIQdevkdaPRCMQLAQQFGIT-ALLDRR 132
Cdd:PRK10636 73 tpalpqpaleyvidgdreYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWTIR------SRAASLLHGLGFSnEQLERP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 133 FKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLhqSGiTLVLVLNRFDEIPEFVQFAGVLADCT 212
Cdd:PRK10636 147 VSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY--QG-TLILISHDRDFLDPIVDKIIHIEQQS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 213 LAE-TG-------------AKEELL---QQALVAQLAHS------------------EQLEGVQLPEP---DEP---SAR 251
Cdd:PRK10636 224 LFEyTGnyssfevqratrlAQQQAMyesQQERVAHLQSYidrfrakatkakqaqsriKMLERMELIAPahvDNPfhfSFR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 252 HalPANEPRIVLNNGVVS--YNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQgysndltlfgrrrgSG 328
Cdd:PRK10636 304 A--PESLPNPLLKMEKVSagYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGElAPV--------------SG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 329 ETIWDIKKHIGYVSSSlHLDYRVSttvrnvilsgyfDSIGIYQAVSDRQQKLVQQWLDILGI-----DKRTadAPFHSLS 403
Cdd:PRK10636 368 EIGLAKGIKLGYFAQH-QLEFLRA------------DESPLQHLARLAPQELEQKLRDYLGGfgfqgDKVT--EETRRFS 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 404 WGQQR---LALIVRalvKHPTLLILDEPLQGLDPLNRQLIrrfVDVLIsEGETQLLFVSH 460
Cdd:PRK10636 433 GGEKArlvLALIVW---QRPNLLLLDEPTNHLDLDMRQAL---TEALI-DFEGALVVVSH 485
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
241-482 |
1.29e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.18 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 241 QLPEPDEPSARH------ALPANEPRIVLNNGVVSYN--DRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQ 312
Cdd:TIGR01257 903 EMEDPEHPEGINdsfferELPGLVPGVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 313 gySNDLTLFGRRrgsgetiwDIKKHIGYVSSSLHLDYRVSTTVRNVILSgyfDSIGIYQAVSDRQQKLVQQWLDILGID- 391
Cdd:TIGR01257 983 --TSGTVLVGGK--------DIETNLDAVRQSLGMCPQHNILFHHLTVA---EHILFYAQLKGRSWEEAQLEMEAMLEDt 1049
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 392 ----KRTADApfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRqliRRFVDVLISEGETQLLFVSHHAEDAPA 467
Cdd:TIGR01257 1050 glhhKRNEEA--QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR---RSIWDLLLKYRSGRTIIMSTHHMDEAD 1124
|
250
....*....|....*
gi 16128728 468 CITHRLEFVPDGGLY 482
Cdd:TIGR01257 1125 LLGDRIAIISQGRLY 1139
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
275-433 |
1.31e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.45 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 275 ILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQG--YSNDLTLFGRRRGSgetiWDIKKHIGYVSSSlhlDYRVS 352
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkGSGSVLLNGMPIDA----KEMRAISAYVQQD---DLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 353 T-TVRNVIlsgyfdsigIYQA-------VSDRQQKL-VQQWLDILGI----DKRTADAPFH-SLSWGQ-QRLALIVRALv 417
Cdd:TIGR00955 113 TlTVREHL---------MFQAhlrmprrVTKKEKRErVDEVLQALGLrkcaNTRIGVPGRVkGLSGGErKRLAFASELL- 182
|
170
....*....|....*.
gi 16128728 418 KHPTLLILDEPLQGLD 433
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLD 198
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-223 |
1.50e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 59.86 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 13 LSDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELP------LLKGERQSQFS------------HITRLSFEQ 74
Cdd:PRK09536 13 FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTptagtvLVAGDDVEALSaraasrrvasvpQDTSLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 75 LQKLVSDEWQRNNTDMLGPgEDDTGRTTAEiiqdevkdapRCMQlaqQFGITALLDRRFKYLSTGETRKTLLCQALMSEP 154
Cdd:PRK09536 93 DVRQVVEMGRTPHRSRFDT-WTETDRAAVE----------RAME---RTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 155 DLLILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELL 223
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3-250 |
1.57e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.84 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 3 SLQILQGTFRLSDTKTLQLPQltlnaGDSWAFVGSNGSGKSALARALAGELPLLKGerqsqfsHITrLSFEQLQKLVSDE 82
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPD-----GHFTAIIGPNGCGKSTLLRTLSRLMTPAHG-------HVW-LDGEHIQHYASKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 83 WQRNnTDMLGPGEDDTGRTTaeiIQDEV----------------KDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLL 146
Cdd:PRK10253 79 VARR-IGLLAQNATTPGDIT---VQELVargryphqplftrwrkEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 147 CQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQS-GITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQ 225
Cdd:PRK10253 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
250 260
....*....|....*....|....*
gi 16128728 226 ALVaqlahsEQLEGVQLPEPDEPSA 250
Cdd:PRK10253 235 ELI------ERIYGLRCMIIDDPVA 253
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
253-474 |
1.69e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.94 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 253 ALPANEPRIVLNNGVV-SYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGYSNDLTLFGRRRGsget 330
Cdd:PRK13543 3 EPLHTAPPLLAAHALAfSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGlLHVESGQIQIDGKTATRG---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 331 iwDIKKHIGYVSSSLHLDYRVSTTVRNVILSGYFDSigiyqavsdRQQKLVQQWLDILGIDKRtADAPFHSLSWGQQRLA 410
Cdd:PRK13543 79 --DRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGR---------RAKQMPGSALAIVGLAGY-EDTLVRQLSAGQKKRL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128728 411 LIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLfVSHHAEDAPACITHRLE 474
Cdd:PRK13543 147 ALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALV-TTHGAYAAPPVRTRMLT 209
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
291-465 |
1.72e-09 |
|
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: 59.04 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 291 IVGPNGAGKSTLLSLVTG-DHPQgysndltlFGRRRGSGETIWDIKKHIGYVssslhldyrvsttvrNVILSGY--FDSI 367
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGfEQPD--------SGSIMLDGEDVTNVPPHLRHI---------------NMVFQSYalFPHM 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 368 GIYQAVSD--RQQKL--------VQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD-PLN 436
Cdd:TIGR01187 58 TVEENVAFglKMRKVpraeikprVLEALRLVQLEEFADRKP-HQLSGGQQQRVALARALVFKPKILLLDEPLSALDkKLR 136
|
170 180
....*....|....*....|....*....
gi 16128728 437 RQLIRRFVDVLISEGETqLLFVSHHAEDA 465
Cdd:TIGR01187 137 DQMQLELKTIQEQLGIT-FVFVTHDQEEA 164
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
260-460 |
1.94e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.17 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 260 RIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgysndltlfgrrrgSGEtiwdIKKHi 338
Cdd:COG1134 26 ELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEPT--------------SGR----VEVN- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 339 GYVSS------SLHLDYrvstTVR-NVILSGYfdsigiyqavsdrqqklvqqwldILG-----IDKRTA----------- 395
Cdd:COG1134 87 GRVSAllelgaGFHPEL----TGReNIYLNGR-----------------------LLGlsrkeIDEKFDeivefaelgdf 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128728 396 -DAPFHSLSWGQQ-RLALIVrALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSH 460
Cdd:COG1134 140 iDQPVKTYSSGMRaRLAFAV-ATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRT-VIFVSH 204
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
263-461 |
1.98e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.15 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 263 LNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdHPqGY---SNDLTLFGRrrgsgetiwDI----- 334
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HP-KYevtSGSILLDGE---------DIlelsp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 335 ----KKHIGY----------VSsslhldyrvsttVRNVILSgyfdsigIYQAVSDRQ------QKLVQQWLDILGIDKRT 394
Cdd:COG0396 72 deraRAGIFLafqypveipgVS------------VSNFLRT-------ALNARRGEElsarefLKLLKEKMKELGLDEDF 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128728 395 ADAPFH-SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDplnrqlirrfVDVL--ISEG-------ETQLLFVSHH 461
Cdd:COG0396 133 LDRYVNeGFSGGEKKRNEILQMLLLEPKLAILDETDSGLD----------IDALriVAEGvnklrspDRGILIITHY 199
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-197 |
2.12e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 59.07 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 25 TLNAGDSWAFVGSNGSGKSALARAL-------AGELPLLkGERQSQFSHITRLSF---EQLQKLVSDEWQRNNTDMLGPG 94
Cdd:PRK13536 63 TVASGECFGLLGPNGAGKSTIARMIlgmtspdAGKITVL-GVPVPARARLARARIgvvPQFDNLDLEFTVRENLLVFGRY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 95 EDDTGRTTAEIIqdevkdaPRCMQLAQqfgITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
Cdd:PRK13536 142 FGMSTREIEAVI-------PSLLEFAR---LESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
170 180
....*....|....*....|...
gi 16128728 175 AERLASLHQSGITLVLVLNRFDE 197
Cdd:PRK13536 212 WERLRSLLARGKTILLTTHFMEE 234
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-196 |
2.15e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.10 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 12 RLSDT----KTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGelpLLKGERQSQfSHITRLS---------------- 71
Cdd:PRK09984 9 KLAKTfnqhQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSG---LITGDKSAG-SHIELLGrtvqregrlardirks 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 72 -------FEQLQkLVSDEWQRNNTDMLGPGEDDTGRTTAEIIQDEVKDapRCMQLAQQFGITALLDRRFKYLSTGETRKT 144
Cdd:PRK09984 85 rantgyiFQQFN-LVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQ--RALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128728 145 LLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQS-GITLVLVLNRFD 196
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVD 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
24-191 |
2.37e-09 |
|
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: 57.44 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAG-ELP-----LLKGERqsqfshITRLSFEQLQKLvsdewqRNntDMLG----- 92
Cdd:COG4181 33 LEVEAGESVAIVGASGSGKSTLLGLLAGlDRPtsgtvRLAGQD------LFALDEDARARL------RA--RHVGfvfqs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 93 ----PGeddtgrTTA--------EIIQDevKDA-PRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLIL 159
Cdd:COG4181 99 fqllPT------LTAlenvmlplELAGR--RDArARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFA 170
|
170 180 190
....*....|....*....|....*....|...
gi 16128728 160 DEPFDGLDVASRQQLAERLASLHQ-SGITLVLV 191
Cdd:COG4181 171 DEPTGNLDAATGEQIIDLLFELNReRGTTLVLV 203
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
261-445 |
2.55e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 57.79 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgysndltLFGRRRGS----GETIWDIK- 335
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISR-----------LLPPDSGEvlvdGLDVATTPs 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 336 ----KHIGYVSSSLHLDYRVstTVRNVILSGYFD-SIGiyqAVSDRQQKLVQQWLDILGIDKrTADAPFHSLSWGQQRLA 410
Cdd:COG4604 71 relaKRLAILRQENHINSRL--TVRELVAFGRFPySKG---RLTAEDREIIDEAIAYLDLED-LADRYLDELSGGQRQRA 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 16128728 411 LIVRALVKHPTLLILDEPLQGLDPLN-RQ---LIRRFVD 445
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHsVQmmkLLRRLAD 183
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
264-479 |
2.67e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.17 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 264 NNGVVSYND-RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHpqgysndltlfgrRRGSGETIWDIKKhIGYVS 342
Cdd:PRK13639 5 RDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGIL-------------KPTSGEVLIKGEP-IKYDK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 343 SSLhldYRVSTTVrNVILSGYFDSI---GIYQAVS----------DRQQKLVQQWLDILGIDKRTADAPfHSLSWGQQRL 409
Cdd:PRK13639 71 KSL---LEVRKTV-GIVFQNPDDQLfapTVEEDVAfgplnlglskEEVEKRVKEALKAVGMEGFENKPP-HHLSGGQKKR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 410 ALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETqlLFVSHHAEDAPACITHRLEFVPDG 479
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGIT--IIISTHDVDLVPVYADKVYVMSDG 213
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
291-460 |
2.95e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 58.73 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 291 IVGPNGAGKSTLLSLVTG-DHPQ-GYS--NDLTLFGRRRGsgetIW--DIKKHIGYV--SSSLHLDYRVSTTVR---NVI 359
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGlTRPQkGRIvlNGRVLFDAEKG----IClpPEKRRIGYVfqDARLFPHYKVRGNLRygmAKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 360 LSGYFDSIgiyqavsdrqqklvqqwLDILGIDKRTADAPfHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD-PLNR 437
Cdd:PRK11144 105 MVAQFDKI-----------------VALLGIEPLLDRYP-GSLSGGEkQRVA-IGRALLTAPELLLMDEPLASLDlPRKR 165
|
170 180
....*....|....*....|...
gi 16128728 438 QLIrRFVDVLISEGETQLLFVSH 460
Cdd:PRK11144 166 ELL-PYLERLAREINIPILYVSH 187
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
260-465 |
3.29e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 57.62 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 260 RIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLvtgdhpqgYSNDLTLFGRRRGSGETIWD----IK 335
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRV--------FNRLIELYPEARVSGEVYLDgqdiFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 336 KHIGYVSSSLHLDYRVSTTVRNVILsgyFDSIG-------IYQAVSDRQQKL------VQQWLDIlgidKRTADAPFHSL 402
Cdd:PRK14247 75 MDVIELRRRVQMVFQIPNPIPNLSI---FENVAlglklnrLVKSKKELQERVrwalekAQLWDEV----KDRLDAPAGKL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128728 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFvdVLISEGETQLLFVSHHAEDA 465
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESL--FLELKKDMTIVLVTHFPQQA 208
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-217 |
3.87e-09 |
|
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: 56.77 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshITRLSfeqlqKLVSdewqrnntdMLGPG----EDDTG 99
Cdd:cd03220 43 FEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT-------VTVRG-----RVSS---------LLGLGggfnPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 100 R------------TTAEIiqDEVKDapRCMQLAqqfGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
Cdd:cd03220 102 ReniylngrllglSRKEI--DEKID--EIIEFS---ELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16128728 168 VASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETG 217
Cdd:cd03220 175 AAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-191 |
3.98e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.18 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshITRLSfEQLQKLVSDEWQ--RNNTDM--------LGP 93
Cdd:PRK15079 42 LRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGE-------VAWLG-KDLLGMKDDEWRavRSDIQMifqdplasLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 94 geddtgR-TTAEII------------QDEVKDAPRCMQLaqQFGITALLDRRFKY-LSTGETRKTLLCQALMSEPDLLIL 159
Cdd:PRK15079 114 ------RmTIGEIIaeplrtyhpklsRQEVKDRVKAMML--KVGLLPNLINRYPHeFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190
....*....|....*....|....*....|...
gi 16128728 160 DEPFDGLDVASRQQLAERLASLHQS-GITLVLV 191
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQLQREmGLSLIFI 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
276-464 |
4.19e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.48 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYS----NDLTLFGRRRGsgETIWDIKKHIGYV----SSSLHL 347
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGtvtvDDITITHKTKD--KYIRPVRKRIGMVfqfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 348 DyrvstTVRNVILSGYFDSIGIYQAVSDRQQKLVQQwldiLGIDKRT-ADAPFHsLSWGQQRLALIVRALVKHPTLLILD 426
Cdd:PRK13646 101 D-----TVEREIIFGPKNFKMNLDEVKNYAHRLLMD----LGFSRDVmSQSPFQ-MSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128728 427 EPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAED 464
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNE 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
276-464 |
4.51e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.53 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSlvtgdHPQGY----SNDLTLFGRR---RGSGETIWDIKKHIGYVssslhLD 348
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQ-----HFNALlkpsSGTITIAGYHitpETGNKNLKKLRKKVSLV-----FQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 349 YRVSTTVRNVILSGYFDSIGIYQAVSDRQQKLVQQWLDILGIDKRTAD-APFhSLSWGQQRLALIVRALVKHPTLLILDE 427
Cdd:PRK13641 93 FPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISkSPF-ELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128728 428 PLQGLDPLNR-QLIRRFVDVLiSEGETQLLfVSHHAED 464
Cdd:PRK13641 172 PAAGLDPEGRkEMMQLFKDYQ-KAGHTVIL-VTHNMDD 207
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
24-191 |
4.65e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.12 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAG-------ELpLLKGER---------------QSQ--FSHIT---RLSFeqlq 76
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGleditsgDL-FIGEKRmndvppaergvgmvfQSYalYPHLSvaeNMSF---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 77 klvsdewqrnntdmlgpGEDDTGRTTAEIiQDEVKDAPRCMQLAqqfgitALLDRRFKYLSTGETRKTLLCQALMSEPDL 156
Cdd:PRK11000 99 -----------------GLKLAGAKKEEI-NQRVNQVAEVLQLA------HLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 16128728 157 LILDEPFDGLDVASRQQLAERLASLHQS-GITLVLV 191
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYV 190
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
243-305 |
4.89e-09 |
|
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: 58.68 E-value: 4.89e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 243 PEP-DEPSARhALPANEPRIVLNNGVVSYN-DRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSL 305
Cdd:COG5265 340 PEVaDAPDAP-PLVVGGGEVRFENVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARL 403
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
23-191 |
5.30e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.99 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 23 QLTLNAGDSWAFVGSNGSGKSALARALAG-ELP----LLKGERQ-SQFSHITRLSFEQLQKLvsdEWQRnNTDMLGPGED 96
Cdd:PRK11247 32 DLHIPAGQFVAVVGRSGCGKSTLLRLLAGlETPsageLLAGTAPlAEAREDTRLMFQDARLL---PWKK-VIDNVGLGLK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 97 DTGRTTAEIIQDEVKDAPRcmqlAQQFGITalldrrfkyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR---QQ 173
Cdd:PRK11247 108 GQWRDAALQALAAVGLADR----ANEWPAA---------LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRiemQD 174
|
170
....*....|....*...
gi 16128728 174 LAERLasLHQSGITLVLV 191
Cdd:PRK11247 175 LIESL--WQQHGFTVLLV 190
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
276-483 |
5.56e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.40 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKST-------LLSLVTG---------------DHPQGYSNDLTLFGRRRGSGETIWD 333
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTfiehlnaLLLPDTGtiewifkdeknkkktKEKEKVLEKLVIQKTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 334 IKKHIGYVSSslHLDYRV-STTVRNVILSGYFdSIGIYQAvsdRQQKLVQQWLDILGIDKRTAD-APFhSLSWGQQRLAL 411
Cdd:PRK13651 103 IRRRVGVVFQ--FAEYQLfEQTIEKDIIFGPV-SMGVSKE---EAKKRAAKYIELVGLDESYLQrSPF-ELSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128728 412 IVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLfVSHHAEDAPAcITHRLEFVPDGGLYR 483
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIIL-VTHDLDNVLE-WTKRTIFFKDGKIIK 245
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
276-464 |
6.83e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.40 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEhwqIV---GPNGAGKSTLLSLVTGD-HPQGYS---NDLTLFGRRRgsgetiwDIKKHIGYVS---SSL 345
Cdd:COG4586 38 VDDISFTIEPGE---IVgfiGPNGAGKSTTIKMLTGIlVPTSGEvrvLGYVPFKRRK-------EFARRIGVVFgqrSQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 346 HLDYRVSttvrnvilsgyfDSIGIYQAVSDRQQKLVQQWLD----ILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPT 421
Cdd:COG4586 108 WWDLPAI------------DSFRLLKAIYRIPDAEYKKRLDelveLLDLGE-LLDTPVRQLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16128728 422 LLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAED 464
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDD 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
268-463 |
7.81e-09 |
|
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: 55.61 E-value: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 268 VSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdHPqgysndltlfgrrrgsgetiwdikkhigyvssslhl 347
Cdd:cd03217 8 VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HP------------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 348 DYRVsttVRNVILsgyFDSIGIYQA-VSDRQQKLV----QQWLDILGIdkRTADapF-----HSLSWGQQRLALIVRALV 417
Cdd:cd03217 51 KYEV---TEGEIL---FKGEDITDLpPEERARLGIflafQYPPEIPGV--KNAD--FlryvnEGFSGGEKKRNEILQLLL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128728 418 KHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGeTQLLFVSHHAE 463
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKLREEG-KSVLIITHYQR 165
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
123-190 |
8.55e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 56.66 E-value: 8.55e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 123 FGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLVL 190
Cdd:COG4152 117 LGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIF 184
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
118-433 |
1.03e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.34 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 118 QLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDE 197
Cdd:COG3845 124 ELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLRE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 198 IPEFVQFAGVL------ADCTLAETGAKEelLQQALVAQlahseqlegvqlpEPDEPSARHALPANEPRIVLNN-GVVSY 270
Cdd:COG3845 204 VMAIADRVTVLrrgkvvGTVDTAETSEEE--LAELMVGR-------------EVLLRVEKAPAEPGEVVLEVENlSVRDD 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 271 NDRPILNNLSWQVNPGEhwqIV---GPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRRRGsGETIWDIKKH-IGYVSSSL 345
Cdd:COG3845 269 RGVPALKDVSLEVRAGE---ILgiaGVAGNGQSELAEALAGlRPPA--SGSIRLDGEDIT-GLSPRERRRLgVAYIPEDR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 346 H-----LDYRVsttVRNVILSGY----FDSIGI--YQAVSDRQQKLVQQWlDIlgidkRTA--DAPFHSLSWG-QQRLaL 411
Cdd:COG3845 343 LgrglvPDMSV---AENLILGRYrrppFSRGGFldRKAIRAFAEELIEEF-DV-----RTPgpDTPARSLSGGnQQKV-I 412
|
330 340
....*....|....*....|..
gi 16128728 412 IVRALVKHPTLLILDEPLQGLD 433
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLD 434
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
33-201 |
1.05e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 56.38 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 33 AFVGSNGSGKSALARALAGELPLLKGERQSQFSHIT----RLSFEQLQKLVSDEWQRNNTD----------MLGPgeDDT 98
Cdd:PRK13641 37 ALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRKKVSLVFQFPEAQlfentvlkdvEFGP--KNF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 99 GRTtaeiiQDEVKDAprCMQLAQQFGI-TALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAER 177
Cdd:PRK13641 115 GFS-----EDEAKEK--ALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQL 187
|
170 180
....*....|....*....|....
gi 16128728 178 LASLHQSGITLVLVLNRFDEIPEF 201
Cdd:PRK13641 188 FKDYQKAGHTVILVTHNMDDVAEY 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
271-488 |
1.12e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.78 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 271 NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG--DHPQG-------YSNDLTLFGRRRGSGET--IWDIKKHIG 339
Cdd:PRK13631 37 NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGliKSKYGtiqvgdiYIGDKKNNHELITNPYSkkIKNFKELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 340 YVSSSLHL-DYRV-STTVRNVILsgyFDSIGIYQAVSDRQQKlVQQWLDILGIDKRTAD-APFhSLSWGQQRLALIVRAL 416
Cdd:PRK13631 117 RVSMVFQFpEYQLfKDTIEKDIM---FGPVALGVKKSEAKKL-AKFYLNKMGLDDSYLErSPF-GLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128728 417 VKHPTLLILDEPLQGLDPLNRQLIRRFvdVLISEGETQLLFVshhaedapacITHRLEFVPDGGLYRYVLTK 488
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQL--ILDAKANNKTVFV----------ITHTMEHVLEVADEVIVMDK 251
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
273-456 |
1.24e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.27 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 273 RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPqgySNDLTLFG----RRRGSGETIWdIKKHIGYVSSSLHL 347
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGiERP---SAGKIWFSghdiTRLKNREVPF-LRRQIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 348 --DYRVSTTVR-NVILSGyfdsigiyqAVSDRQQKLVQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLI 424
Cdd:PRK10908 91 lmDRTVYDNVAiPLIIAG---------ASGDDIRRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16128728 425 LDEPLQGLD-PLNRQLIRRF-------VDVLISEGETQLL 456
Cdd:PRK10908 161 ADEPTGNLDdALSEGILRLFeefnrvgVTVLMATHDIGLI 200
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
268-445 |
1.25e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 268 VSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGY--SNDLTLFGRRRGSgetiwDIKKHIGYVSSS- 344
Cdd:TIGR00956 771 IKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVitGGDRLVNGRPLDS-----SFQRSIGYVQQQd 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 345 LHLDyrvSTTVR-NVILSGYF---DSIGIYQavsdrQQKLVQQWLDILGIDKrTADA----PFHSLSWGQQRLALIVRAL 416
Cdd:TIGR00956 846 LHLP---TSTVReSLRFSAYLrqpKSVSKSE-----KMEYVEEVIKLLEMES-YADAvvgvPGEGLNVEQRKRLTIGVEL 916
|
170 180 190
....*....|....*....|....*....|....
gi 16128728 417 VKHPTLLI-LDEPLQGLDPLNR----QLIRRFVD 445
Cdd:TIGR00956 917 VAKPKLLLfLDEPTSGLDSQTAwsicKLMRKLAD 950
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
118-231 |
1.27e-08 |
|
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: 55.63 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 118 QLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDE 197
Cdd:cd03218 116 ELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRE 195
|
90 100 110
....*....|....*....|....*....|....
gi 16128728 198 IPEFVQFAGVLADCTLAETGAKEELLQQALVAQL 231
Cdd:cd03218 196 TLSITDRAYIIYEGKVLAEGTPEEIAANELVRKV 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-197 |
1.36e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 56.35 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARAL-------AGELPLLkGERQSQFSHITRLSF---EQLQKLVSDEWQRNNTDMLGP 93
Cdd:PRK13537 28 FHVQRGECFGLLGPNGAGKTTTLRMLlglthpdAGSISLC-GEPVPSRARHARQRVgvvPQFDNLDPDFTVRENLLVFGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 94 GEDDTGRTTAEIIqdevkdaPRCMQLAQqfgITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
Cdd:PRK13537 107 YFGLSAAAARALV-------PPLLEFAK---LENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHL 176
|
170 180
....*....|....*....|....
gi 16128728 174 LAERLASLHQSGITLVLVLNRFDE 197
Cdd:PRK13537 177 MWERLRSLLARGKTILLTTHFMEE 200
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
272-440 |
1.48e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.04 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 272 DRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHpQGYSNDLTLFGRRRGSGETIWdIKKHIGYVSSSLHLdyrV 351
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLY-QPTGGQVLLDGVPLVQYDHHY-LHRQVALVGQEPVL---F 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 352 STTVRNVILSGyFDSIGIYQAVSDRQQKLVQQWLDILGIDKRTADAPFHS-LSWGQ-QRLAlIVRALVKHPTLLILDEPL 429
Cdd:TIGR00958 568 SGSVRENIAYG-LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSqLSGGQkQRIA-IARALVRKPRVLILDEAT 645
|
170
....*....|.
gi 16128728 430 QGLDPLNRQLI 440
Cdd:TIGR00958 646 SALDAECEQLL 656
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
10-210 |
1.56e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.77 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 10 TFRLSDTKTLQLPQLTL--NAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVSDEWQRNN 87
Cdd:PRK13632 14 SFSYPNSENNALKNVSFeiNEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 88 TDMLGPG-EDDTG------RTTAEIIQDEVKDaprcmqLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
Cdd:PRK13632 94 NQFIGATvEDDIAfglenkKVPPKKMKDIIDD------LAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128728 161 EPFDGLDVASRQQLAERLASLHQSGI-TLVLVLNRFDEIpefvqfagVLAD 210
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA--------ILAD 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-226 |
1.61e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.97 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSfeQLQKLVSDEWQRNN-------TDMLGPGED 96
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP--PSRRPVSMLFQENNlfshltvAQNIGLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 97 DTGRTTAEIiQDEVKdaprcmQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
Cdd:PRK10771 98 PGLKLNAAQ-REKLH------AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128728 177 RLASL-HQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQA 226
Cdd:PRK10771 171 LVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
24-224 |
1.85e-08 |
|
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: 54.99 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELP------LLKGERqsqfshITRLSFEQLQKL------------------V 79
Cdd:COG1127 26 LDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpdsgeiLVDGQD------ITGLSEKELYELrrrigmlfqggalfdsltV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 80 sdeWQ------RNNTDMlgpgeddtgrtTAEIIQDEVKdaprcMQLAQqFGitaLLDRRFKY---LSTGETRKTLLCQAL 150
Cdd:COG1127 100 ---FEnvafplREHTDL-----------SEAEIRELVL-----EKLEL-VG---LPGAADKMpseLSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 151 MSEPDLLILDEPFDGLDVASRQQLAERLASLHQS-GITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQ 224
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-233 |
1.99e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.27 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 18 TLQLPqltlnAGDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshITRLSFEQLQKLvsdewqRNNTDMLGPGEDD 97
Cdd:PRK15056 27 SFTVP-----GGSIAALVGVNGSGKSTLFKALMGFVRLASGK-------ISILGQPTRQAL------QKNLVAYVPQSEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 98 TGRTTAEIIQDEV----------------KDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
Cdd:PRK15056 89 VDWSFPVLVEDVVmmgryghmgwlrrakkRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128728 162 PFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLA----ETGAKEELLQQALVAQLAH 233
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLAsgptETTFTAENLELAFSGVLRH 244
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
24-191 |
2.20e-08 |
|
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: 54.60 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELP------LLKGERqsqfshITRLSFEQLQKL----VSDEwqRN------- 86
Cdd:COG0410 24 LEVEEGEIVALLGRNGAGKTTLLKAISGLLPprsgsiRFDGED------ITGLPPHRIARLgigyVPEG--RRifpsltv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 87 --NTDMLGPGEDDTGRTTAEIiqDEVKDA-PRcmqLAQqfgitaLLDRRFKYLSTGEtRKTL-LCQALMSEPDLLILDEP 162
Cdd:COG0410 96 eeNLLLGAYARRDRAEVRADL--ERVYELfPR---LKE------RRRQRAGTLSGGE-QQMLaIGRALMSRPKLLLLDEP 163
|
170 180
....*....|....*....|....*....
gi 16128728 163 FDGLDVASRQQLAERLASLHQSGITLVLV 191
Cdd:COG0410 164 SLGLAPLIVEEIFEIIRRLNREGVTILLV 192
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
201-460 |
2.60e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 56.26 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 201 FVQFAGVLADcTLAETGAKEELLQQALVAQLAHSEQLEGvqlpePDEPSARHALPANEPRIVLNNGVVSY-NDRPILNNL 279
Cdd:PRK10790 287 FISYLGRLNE-PLIELTTQQSMLQQAVVAGERVFELMDG-----PRQQYGNDDRPLQSGRIDIDNVSFAYrDDNLVLQNI 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 280 SWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHP--QGysnDLTLFGRRRGS-GETIwdIKKHIGYVSSslhlDYRV--STT 354
Cdd:PRK10790 361 NLSVPSRGFVALVGHTGSGKSTLASLLMGYYPltEG---EIRLDGRPLSSlSHSV--LRQGVAMVQQ----DPVVlaDTF 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 355 VRNVILSGYFDSIGIYQAVSDRQ-QKLVQQWLDilGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:PRK10790 432 LANVTLGRDISEEQVWQALETVQlAELARSLPD--GLYTPLGEQG-NNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
250 260
....*....|....*....|....*..
gi 16128728 434 PLNRQLIRRFVdVLISEgETQLLFVSH 460
Cdd:PRK10790 509 SGTEQAIQQAL-AAVRE-HTTLVVIAH 533
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
261-434 |
2.70e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 55.47 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSY--NDRPI--LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGYS-----NDLTLFGRRRgsget 330
Cdd:COG1135 2 IELENLSKTFptKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLlERPTSGSvlvdgVDLTALSERE----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 331 IWDIKKHIGYV--SSSLhLDYRvstTVR-NV----ILSGYfdsigiyqAVSDRQQKlVQQWLDILGIDKRtADAPFHSLS 403
Cdd:COG1135 77 LRAARRKIGMIfqHFNL-LSSR---TVAeNValplEIAGV--------PKAEIRKR-VAELLELVGLSDK-ADAYPSQLS 142
|
170 180 190
....*....|....*....|....*....|..
gi 16128728 404 WGQ-QRLAlIVRALVKHPTLLILDEPLQGLDP 434
Cdd:COG1135 143 GGQkQRVG-IARALANNPKVLLCDEATSALDP 173
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
9-171 |
2.72e-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: 54.72 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 9 GTFRLSDTKTlqlpqlTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHItrlSFEQlQKLVSDeWQRNNT 88
Cdd:cd03237 11 GEFTLEVEGG------SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV---SYKP-QYIKAD-YEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 89 DMLgpgeddtgrttAEIIQDEVKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
Cdd:cd03237 80 DLL-----------SSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
...
gi 16128728 169 ASR 171
Cdd:cd03237 149 EQR 151
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
100-191 |
3.85e-08 |
|
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: 54.17 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 100 RTTAEIIQDEVKDAPRCMQLaqqfgiTALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLA 179
Cdd:cd03300 101 KLPKAEIKERVAEALDLVQL------EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELK 174
|
90
....*....|...
gi 16128728 180 SLHQS-GITLVLV 191
Cdd:cd03300 175 RLQKElGITFVFV 187
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
23-191 |
4.01e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 54.25 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 23 QLTLNAGDSWAFVGSNGSGKSALARAL-------AGELPLlkgeRQSQFSHITRLSFEQLQKLvsdewqRNNTDM----- 90
Cdd:COG4161 22 NLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNI----AGHQFDFSQKPSEKAIRLL------RQKVGMvfqqy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 91 -LGPGeddtgRTtaeiIQDEVKDAP-------------RCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDL 156
Cdd:COG4161 92 nLWPH-----LT----VMENLIEAPckvlglskeqareKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190
....*....|....*....|....*....|....*
gi 16128728 157 LILDEPFDGLDVASRQQLAERLASLHQSGITLVLV 191
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIV 197
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
256-460 |
4.71e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.42 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 256 ANEPRIVLNN------GVVSyNDrpilnNLSWQVNPGE-HwQIVGPNGAGKSTLLSLVTGdhpqGYSNDltlfgrrrgSG 328
Cdd:COG3845 1 MMPPALELRGitkrfgGVVA-ND-----DVSLTVRPGEiH-ALLGENGAGKSTLMKILYG----LYQPD---------SG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 329 ETIWD------------IKKHIGYVSSSLHLdyrVST-TVR-NVILsGYFDSIGIyqaVSDRQQ--KLVQQWLDILG--I 390
Cdd:COG3845 61 EILIDgkpvrirsprdaIALGIGMVHQHFML---VPNlTVAeNIVL-GLEPTKGG---RLDRKAarARIRELSERYGldV 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128728 391 DkrtADAPFHSLSWG-QQRLAlIVRALVKHPTLLILDEPLQGLDPlnrQLIRRFVDV---LISEGETqLLFVSH 460
Cdd:COG3845 134 D---PDAKVEDLSVGeQQRVE-ILKALYRGARILILDEPTAVLTP---QEADELFEIlrrLAAEGKS-IIFITH 199
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
24-191 |
4.73e-08 |
|
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: 53.65 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVSDE----WQRNNtdmLGPgeddtg 99
Cdd:cd03255 25 LSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRRHigfvFQSFN---LLP------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 100 RTTA--------EIIQDEVKDAP-RCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
Cdd:cd03255 96 DLTAlenvelplLLAGVPKKERReRAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSET 175
|
170 180
....*....|....*....|..
gi 16128728 171 RQQLAERLASL-HQSGITLVLV 191
Cdd:cd03255 176 GKEVMELLRELnKEAGTTIVVV 197
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
223-460 |
4.91e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.90 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 223 LQQALVAQlahseqlEGVQLPEPdepsarhALPANEPRIVLNNGVVSY---NDRPILNNLSWQVNPGEHWQIVGPNGAGK 299
Cdd:PLN03130 591 LEELLLAE-------ERVLLPNP-------PLEPGLPAISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGK 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 300 STLLSLVTGDHPQGYSNDLTLfgrrRGSgetiwdikkhIGYVSsslHLDYRVSTTVRNVILSGY-FDSIGIYQAVsdrQQ 378
Cdd:PLN03130 657 TSLISAMLGELPPRSDASVVI----RGT----------VAYVP---QVSWIFNATVRDNILFGSpFDPERYERAI---DV 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 379 KLVQQWLDIL-GIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP-LNRQL--------IRRFVDVLI 448
Cdd:PLN03130 717 TALQHDLDLLpGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVfdkcikdeLRGKTRVLV 796
|
250
....*....|..
gi 16128728 449 SegeTQLLFVSH 460
Cdd:PLN03130 797 T---NQLHFLSQ 805
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
272-488 |
5.25e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.37 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 272 DRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQgySNDLTLFGRRRGSGETIWDIK---KHIGYVSSSLHL 347
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvPT--QGSVRVDDTLITSTSKNKDIKqirKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 348 DYRVSTTVRNVILSGyfDSIGIYQavsDRQQKLVQQWLDILGIDKRTAD-APFhSLSWGQQRLALIVRALVKHPTLLILD 426
Cdd:PRK13649 97 QLFEETVLKDVAFGP--QNFGVSQ---EEAEALAREKLALVGISESLFEkNPF-ELSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128728 427 EPLQGLDPLNRQLIRRFVDVLISEGETQLLfvshhaedapacITHRLEFVPDGGLYRYVLTK 488
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKLHQSGMTIVL------------VTHLMDDVANYADFVYVLEK 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
33-225 |
5.36e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.49 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 33 AFVGSNGSGKSALARALAGELPLLKGERQ------SQFSH-ITRLSFEQLQK---LVSDEWQRNNTdmlgpgeddTGRtt 102
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYPLTEGEIRldgrplSSLSHsVLRQGVAMVQQdpvVLADTFLANVT---------LGR-- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 103 aEIIQDEVKDAPRCMQLAQQF-----GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAER 177
Cdd:PRK10790 440 -DISEEQVWQALETVQLAELArslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQA 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16128728 178 LASLHQSgITLVLVLNRFDEIPEFVQFAgVLADCTLAETGAKEELLQQ 225
Cdd:PRK10790 519 LAAVREH-TTLVVIAHRLSTIVEADTIL-VLHRGQAVEQGTHQQLLAA 564
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
24-227 |
5.53e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 54.53 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPllkgERQsqfsHIT--RLSFeqlqklvsdewqrNNTDMLG--PGEDD-- 97
Cdd:COG4170 28 LTLNEGEIRGLVGESGSGKSLIAKAICGITK----DNW----HVTadRFRW-------------NGIDLLKlsPRERRki 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 98 TGRTTAEIIQDevkdAPRCMQLAQQFG---ITALLDRRFK--------------------------------Y---LSTG 139
Cdd:COG4170 87 IGREIAMIFQE----PSSCLDPSAKIGdqlIEAIPSWTFKgkwwqrfkwrkkraiellhrvgikdhkdimnsYpheLTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 140 ETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQ-SGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGA 218
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGP 242
|
....*....
gi 16128728 219 KEELLQQAL 227
Cdd:COG4170 243 TEQILKSPH 251
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
257-315 |
5.78e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 5.78e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 257 NEPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdHPqGYS 315
Cdd:CHL00131 4 NKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HP-AYK 60
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
272-453 |
6.21e-08 |
|
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: 52.63 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 272 DRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGY-SNDLTLFGRRRGSgetiwDIKKHIGYVSS-SLHLDy 349
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGViTGEILINGRPLDK-----NFQRSTGYVEQqDVHSP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 350 rvSTTVRNVILsgyfdsigiYQAvsdrqqklvqqWLDILGIDKRtadapfhslswgqQRLALIVRaLVKHPTLLILDEPL 429
Cdd:cd03232 93 --NLTVREALR---------FSA-----------LLRGLSVEQR-------------KRLTIGVE-LAAKPSILFLDEPT 136
|
170 180
....*....|....*....|....
gi 16128728 430 QGLDPLNRQLIRRFVDVLISEGET 453
Cdd:cd03232 137 SGLDSQAAYNIVRFLKKLADSGQA 160
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
269-433 |
6.74e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.27 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 269 SYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQGYSNDLTLFGRRRGSgetiwDIKKHIGYVSSS--- 344
Cdd:PLN03211 77 QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiQGNNFTGTILANNRKPTK-----QILKRTGFVTQDdil 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 345 -LHLdyrvstTVRNVILsgyFDSIGIYQAVSDRQQKL--VQQWLDILGIDK----RTADAPFHSLSWGQQRLALIVRALV 417
Cdd:PLN03211 152 yPHL------TVRETLV---FCSLLRLPKSLTKQEKIlvAESVISELGLTKcentIIGNSFIRGISGGERKRVSIAHEML 222
|
170
....*....|....*.
gi 16128728 418 KHPTLLILDEPLQGLD 433
Cdd:PLN03211 223 INPSLLILDEPTSGLD 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
24-225 |
7.46e-08 |
|
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: 53.00 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVS----DEWQRNNTDMlgpgedDTG 99
Cdd:cd03254 24 FSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGvvlqDTFLFSGTIM------ENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 100 RTTAEIIQDEVkdaprCMQLAQQFGITALLDR-----------RFKYLSTGEtrKTLLC--QALMSEPDLLILDEPFDGL 166
Cdd:cd03254 98 RLGRPNATDEE-----VIEAAKEAGAHDFIMKlpngydtvlgeNGGNLSQGE--RQLLAiaRAMLRDPKILILDEATSNI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 167 DVASRQQLAERLASLhQSGITLVLVLNRFDEIpEFVQFAGVLADCTLAETGAKEELLQQ 225
Cdd:cd03254 171 DTETEKLIQEALEKL-MKGRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
279-433 |
7.47e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.40 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 279 LSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqgYSNDLTLFGRRRgSGETIWDIKKHIGYVSSSlhldyrvSTTVRNV 358
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP--GSGSIQFAGQPL-EAWSAAELARHRAYLSQQ-------QTPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 359 ILSGYFDSIGIYQAVSDRQQKLVQQWLDILGIDKRTAdAPFHSLSWGQ-QRLAL------IVRALVKHPTLLILDEPLQG 431
Cdd:PRK03695 85 PVFQYLTLHQPDKTRTEAVASALNEVAEALGLDDKLG-RSVNQLSGGEwQRVRLaavvlqVWPDINPAGQLLLLDEPMNS 163
|
..
gi 16128728 432 LD 433
Cdd:PRK03695 164 LD 165
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-185 |
7.52e-08 |
|
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: 53.04 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGEL---------------PLLKGERQSQFSHItrlsfEQLQKLVS----DEWQ 84
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVegggttsgqilfngqPRKPDQFQKCVAYV-----RQDDILLPgltvRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 85 RNNTDMLGPgeddtgRTTAEIIQDEVKDAPRCMQLAqqfgITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
Cdd:cd03234 103 TYTAILRLP------RKSSDAIRKKRVEDVLLRDLA----LTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190
....*....|....*....|....*....|..
gi 16128728 165 GLD-------VASRQQLAER----LASLHQSG 185
Cdd:cd03234 173 GLDsftalnlVSTLSQLARRnrivILTIHQPR 204
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
261-480 |
7.83e-08 |
|
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: 51.77 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNN-GVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgysndltlfgrrrGSGetiwDIKKHIG 339
Cdd:cd03223 1 IELENlSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPW-------------GSG----RIGMPEG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 340 yvSSSLHLDYRvsttvrnvilsGYFdSIGiyqavSDRQQkLVQQWLDILGIDKrtadapfhslswgQQRLALIvRALVKH 419
Cdd:cd03223 64 --EDLLFLPQR-----------PYL-PLG-----TLREQ-LIYPWDDVLSGGE-------------QQRLAFA-RLLLHK 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128728 420 PTLLILDEPLQGLDPlnrQLIRRFVDVLISEGETqLLFVSHHaEDAPACITHRLEFVPDGG 480
Cdd:cd03223 110 PKFVFLDEATSALDE---ESEDRLYQLLKELGIT-VISVGHR-PSLWKFHDRVLDLDGEGG 165
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-191 |
9.17e-08 |
|
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: 53.90 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELP---------LLKGERqsqfshITRLSFEQLQKLvsdewqRnntdmlgpg 94
Cdd:COG0444 26 FDVRRGETLGLVGESGSGKSTLARAILGLLPppgitsgeiLFDGED------LLKLSEKELRKI------R--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 95 eddtGRTTAEIIQD----------------------------EVKDapRCMQLAQQFGITALLDRRFKY---LSTGETRK 143
Cdd:COG0444 85 ----GREIQMIFQDpmtslnpvmtvgdqiaeplrihgglskaEARE--RAIELLERVGLPDPERRLDRYpheLSGGMRQR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16128728 144 TLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQS-GITLVLV 191
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFI 207
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
24-223 |
9.18e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.04 E-value: 9.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAG---ELPLLKGERQsQFSHIT--RLSFEQLQKLVsdewqRNNTDM-------- 90
Cdd:PRK15093 28 MTLTEGEIRGLVGESGSGKSLIAKAICGvtkDNWRVTADRM-RFDDIDllRLSPRERRKLV-----GHNVSMifqepqsc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 91 LGPGEDdTGRTTAEIIQDEVKDAP----------RCMQLAQQFGITALLD--RRFKY-LSTGETRKTLLCQALMSEPDLL 157
Cdd:PRK15093 102 LDPSER-VGRQLMQNIPGWTYKGRwwqrfgwrkrRAIELLHRVGIKDHKDamRSFPYeLTEGECQKVMIAIALANQPRLL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128728 158 ILDEPFDGLDVASRQQLAERLASLHQ-SGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELL 223
Cdd:PRK15093 181 IADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELV 247
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
261-465 |
1.12e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 52.71 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLL-SLVTGDHPQgySNDLTLFGRR-----RGSGETIWDI 334
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLrVLNLLEMPR--SGTLNIAGNHfdfskTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 335 KKHIGYVSSSLHLdYRVSTTVRNVI-----LSGYFDSIGIYQAvsdrqqklvQQWLDILGIDKRTADAPFHsLSWGQQRL 409
Cdd:PRK11124 81 RRNVGMVFQQYNL-WPHLTVQQNLIeapcrVLGLSKDQALARA---------EKLLERLRLKPYADRFPLH-LSGGQQQR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 410 ALIVRALVKHPTLLILDEPLQGLDPlnrQLIRRFVDVlISE----GETQLLfVSHHAEDA 465
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDP---EITAQIVSI-IRElaetGITQVI-VTHEVEVA 204
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
246-442 |
1.24e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.53 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 246 DEPSARHALPaNEPRIVLNNGVVSYND--RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLS-----LVTGDHPQ--GYS- 315
Cdd:TIGR01271 1204 ENPHAQKCWP-SGGQMDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSallrlLSTEGEIQidGVSw 1282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 316 NDLTLfgrrrgsgeTIWdiKKHIGYVSSSLhldyrvsttvrnVILSGYF-DSIGIYQAVSDRQ----------QKLVQQW 384
Cdd:TIGR01271 1283 NSVTL---------QTW--RKAFGVIPQKV------------FIFSGTFrKNLDPYEQWSDEEiwkvaeevglKSVIEQF 1339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 385 LDILgiDKRTADAPFhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRR 442
Cdd:TIGR01271 1340 PDKL--DFVLVDGGY-VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRK 1394
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-198 |
1.29e-07 |
|
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: 51.55 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 7 LQGTFRLSDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSfEQLQKLVSdewqrn 86
Cdd:cd03247 6 VSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 87 ntdmlgpgeddtgrttaeIIQdevkdaprcmQLAQQFGITAL--LDRRFkylSTGETRKTLLCQALMSEPDLLILDEPFD 164
Cdd:cd03247 79 ------------------VLN----------QRPYLFDTTLRnnLGRRF---SGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16128728 165 GLDVASRQQLAERLASlHQSGITLVLV------LNRFDEI 198
Cdd:cd03247 128 GLDPITERQLLSLIFE-VLKDKTLIWIthhltgIEHMDKI 166
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
272-461 |
1.34e-07 |
|
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: 52.47 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 272 DRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQGysndltlfgrrrgsGETIWDIKKHIGYVSSSLHLDYR 350
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYqPQG--------------GQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 351 V--------STTVRNVILSGyfdsigiYQAVSDRQQKLVQQWLDI--------LGIDKRTADAPfHSLSWGQ-QRLAlIV 413
Cdd:cd03248 92 LvgqepvlfARSLQDNIAYG-------LQSCSFECVKEAAQKAHAhsfiselaSGYDTEVGEKG-SQLSGGQkQRVA-IA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16128728 414 RALVKHPTLLILDEPLQGLDPLNRQLIRRfvdvLISEG--ETQLLFVSHH 461
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQ----ALYDWpeRRTVLVIAHR 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
271-460 |
1.44e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.94 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 271 NDRPILNNLSWQVNPGEHWQIVGPNGAGKS-TLLSLV------TGDHPQG----------YSNDLTLFGRRRGSGETIW- 332
Cdd:PRK15134 20 TVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpspPVVYPSGdirfhgesllHASEQTLRGVRGNKIAMIFq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 333 ----------DIKKHIgYVSSSLHLDYRvSTTVRNVILSGyFDSIGIYQAVsdrqqklvqqwldilgidKRTADAPfHSL 402
Cdd:PRK15134 100 epmvslnplhTLEKQL-YEVLSLHRGMR-REAARGEILNC-LDRVGIRQAA------------------KRLTDYP-HQL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSH 460
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITH 215
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
260-311 |
1.45e-07 |
|
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: 52.15 E-value: 1.45e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 16128728 260 RIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHP 311
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiYPP 74
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-433 |
1.49e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.10 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGE----LP----LLKGERQSQFSHITRLS------FEQLQkLVSDEWQRNNTD 89
Cdd:PLN03073 198 VTLAFGRHYGLVGRNGTGKTTFLRYMAMHaidgIPkncqILHVEQEVVGDDTTALQcvlntdIERTQ-LLEEEAQLVAQQ 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 90 MLGPGEDDTGRTTAEIIQDEVKDaPRCMQLAQQFGITALLD-----------------------RRFKYLSTGETRKTLL 146
Cdd:PLN03073 277 RELEFETETGKGKGANKDGVDKD-AVSQRLEEIYKRLELIDaytaearaasilaglsftpemqvKATKTFSGGWRMRIAL 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 147 CQALMSEPDLLILDEPFDGLDVASRQQLAERLAS----------------------LHQSGITLVLVLNRFDEIpEFVQF 204
Cdd:PLN03073 356 ARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKwpktfivvshareflntvvtdiLHLHGQKLVTYKGDYDTF-ERTRE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 205 AGVLADCTLAETGAKEELLQQALV---------AQLAHS-----EQLEGV-----------QLPEPDE-PSArhalpane 258
Cdd:PLN03073 435 EQLKNQQKAFESNERSRSHMQAFIdkfrynakrASLVQSrikalDRLGHVdavvndpdykfEFPTPDDrPGP-------- 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 259 PRIVLNNGVVSYNDRPIL-NNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQgysndltlfgrrrgSGETIWDIKK 336
Cdd:PLN03073 507 PIISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGElQPS--------------SGTVFRSAKV 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 337 HIGyVSSSLHLDYRVSTTVRNVILSGYFDSIgiyqavsdRQQKLvQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRAL 416
Cdd:PLN03073 573 RMA-VFSQHHVDGLDLSSNPLLYMMRCFPGV--------PEQKL-RAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKIT 642
|
490
....*....|....*..
gi 16128728 417 VKHPTLLILDEPLQGLD 433
Cdd:PLN03073 643 FKKPHILLLDEPSNHLD 659
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-171 |
1.61e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 35 VGSNGSGKSALARALAGELPLLKGERQSQFshitRLSFEQlQKLVSD------EWQRNNTDMLGpgeddtgrttAEIIQD 108
Cdd:PRK13409 371 VGPNGIGKTTFAKLLAGVLKPDEGEVDPEL----KISYKP-QYIKPDydgtveDLLRSITDDLG----------SSYYKS 435
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128728 109 EvkdaprcmqLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
Cdd:PRK13409 436 E---------IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
16-183 |
1.83e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 53.16 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 16 TKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGelpllkgeRQSQFSHITRLSFEQLQKLVSDEWQ----------- 84
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG--------LEHQTSGHIRFHGTDVSRLHARDRKvgfvfqhyalf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 85 RNNT---------DMLGPGEddtgRTTAEIIQDEVkdaprcMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPD 155
Cdd:PRK10851 87 RHMTvfdniafglTVLPRRE----RPNAAAIKAKV------TQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180
....*....|....*....|....*...
gi 16128728 156 LLILDEPFDGLDVASRQQLAERLASLHQ 183
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHE 184
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
276-463 |
1.88e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHpQGYSNDLTLFGRRRGSGETIWDIKKHIGYVSSSLHLdyrV-STT 354
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNY-QPDAGSILIDGQEMRFASTTAALAAGVAIIYQELHL---VpEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 355 VRNVILSGYFDSIGiyqAVSDRQQ--KLVQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGL 432
Cdd:PRK11288 96 VAENLYLGQLPHKG---GIVNRRLlnYEAREQLEHLGVDI-DPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180 190
....*....|....*....|....*....|.
gi 16128728 433 DPLNRQLIRRFVDVLISEGeTQLLFVSHHAE 463
Cdd:PRK11288 172 SAREIEQLFRVIRELRAEG-RVILYVSHRME 201
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
272-433 |
2.08e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.40 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 272 DRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgysndltlfgrrrgSGETIWDIKKHIGYVSSSLHLDyr 350
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvDKDF--------------NGEARPQPGIKVGYLPQEPQLD-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 351 VSTTVRNVILSGY---------FDSIGI--------YQAVSDRQQKLvQQWLDILG---IDKR-----------TADAPF 399
Cdd:TIGR03719 81 PTKTVRENVEEGVaeikdaldrFNEISAkyaepdadFDKLAAEQAEL-QEIIDAADawdLDSQleiamdalrcpPWDADV 159
|
170 180 190
....*....|....*....|....*....|....
gi 16128728 400 HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
115-186 |
2.08e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 51.95 E-value: 2.08e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 115 RCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD---VASRQQLaerLASLHQSGI 186
Cdd:COG1137 116 RLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiaVADIQKI---IRHLKERGI 187
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-230 |
2.11e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.32 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 11 FRLSDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQ-----FSHITRLSF-EQLQKLVSD-EW 83
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgkpldYSKRGLLALrQQVATVFQDpEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 84 QRNNTDM----------LGPGEDDTGRttaeiiqdEVKDAPRCMQlAQQFgitalLDRRFKYLSTGETRKTLLCQALMSE 153
Cdd:PRK13638 89 QIFYTDIdsdiafslrnLGVPEAEITR--------RVDEALTLVD-AQHF-----RHQPIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 154 PDLLILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPE-----FVQFAG-VLADCTLAETGAKEELLQQAL 227
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEisdavYVLRQGqILTHGAPGEVFACTEAMEQAG 234
|
...
gi 16128728 228 VAQ 230
Cdd:PRK13638 235 LTQ 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
268-473 |
2.19e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 53.43 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 268 VSY---NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQgysndltlFGRRRGSGETIWDI-----KKHI 338
Cdd:PRK13657 340 VSFsydNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFdPQ--------SGRILIDGTDIRTVtraslRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 339 GYVSSSLHLDYRvstTVRNVILSGYFDSIG--IYQAVSdrqqklVQQWLDIlgIDKRTADAPFH------SLSWGQ-QRL 409
Cdd:PRK13657 412 AVVFQDAGLFNR---SIEDNIRVGRPDATDeeMRAAAE------RAQAHDF--IERKPDGYDTVvgergrQLSGGErQRL 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128728 410 AlIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLiSEGETQllFVshhaedapacITHRL 473
Cdd:PRK13657 481 A-IARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTT--FI----------IAHRL 530
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
272-433 |
2.24e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 272 DRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPqgysndltlfgrrrGSGETIWDIKKHIGYVSSSLHLDyr 350
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvDKE--------------FEGEARPAPGIKVGYLPQEPQLD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 351 VSTTVRNVILSGY---------FDSIGI--------YQAVSDRQQKLvQQWLDILG---IDKR-----------TADAPF 399
Cdd:PRK11819 83 PEKTVRENVEEGVaevkaaldrFNEIYAayaepdadFDALAAEQGEL-QEIIDAADawdLDSQleiamdalrcpPWDAKV 161
|
170 180 190
....*....|....*....|....*....|....
gi 16128728 400 HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-445 |
2.26e-07 |
|
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: 53.25 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 35 VGSNGSGKSALARALAGEL-PLLkGERQSQFSH---ITRLS----FEQLQKLVSDEW------QrnNTDMLGPGEDDTGR 100
Cdd:COG1245 105 LGPNGIGKSTALKILSGELkPNL-GDYDEEPSWdevLKRFRgtelQDYFKKLANGEIkvahkpQ--YVDLIPKVFKGTVR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 101 TTAEIIqDEVKDAprcMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLAS 180
Cdd:COG1245 182 ELLEKV-DERGKL---DELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 181 LHQSGITLVLV---LNRFDEIPEFVQFA-------GVLAdctlaetgakeellqQALVAQLAHSEQLEGVqLPEP----- 245
Cdd:COG1245 258 LAEEGKYVLVVehdLAILDYLADYVHILygepgvyGVVS---------------KPKSVRVGINQYLDGY-LPEEnvrir 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 246 DEPSA--RHALPANEPRIVLnngvVSYND-RPILNNLSWQVNPGEHWQ-----IVGPNGAGKSTLLSLVTG-DHPQgysn 316
Cdd:COG1245 322 DEPIEfeVHAPRREKEEETL----VEYPDlTKSYGGFSLEVEGGEIREgevlgIVGPNGIGKTTFAKILAGvLKPD---- 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 317 dltlfgrrrgSGETIWDIKkhIGY----VSSSlhLDYRVSTTVRNVILSGYFDSIgIYQAVSDRqqklvqqwldiLGIDk 392
Cdd:COG1245 394 ----------EGEVDEDLK--ISYkpqyISPD--YDGTVEEFLRSANTDDFGSSY-YKTEIIKP-----------LGLE- 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 393 RTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNR----QLIRRFVD 445
Cdd:COG1245 447 KLLDKNVKDLSGGElQRVA-IAACLSRDADLYLLDEPSAHLDVEQRlavaKAIRRFAE 503
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-194 |
2.37e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 53.19 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 2 SSLQILQG-TFrlsdtktlqlpqlTLNAGDSWAFVGSNGSGKSALARAL-------AGELpLLKGERQSQFSHItrlSFE 73
Cdd:TIGR00958 492 PDVPVLKGlTF-------------TLHPGEVVALVGPSGSGKSTVAALLqnlyqptGGQV-LLDGVPLVQYDHH---YLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 74 QLQKLVSDE---WQRNNTDMLGPGEDDTgrtTAEIIQDEVKDApRCMQLAQQF--GITALLDRRFKYLSTGETRKTLLCQ 148
Cdd:TIGR00958 555 RQVALVGQEpvlFSGSVRENIAYGLTDT---PDEEIMAAAKAA-NAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIAR 630
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128728 149 ALMSEPDLLILDEPFDGLDVASRQQLAErlaSLHQSGITLVLVLNR 194
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQE---SRSRASRTVLLIAHR 673
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
15-225 |
2.56e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.00 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 15 DTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELP------LLKGERQSqFSHITRLSFEQLQKLVsdeWQRNNT 88
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKptsgevLIKGEPIK-YDKKSLLEVRKTVGIV---FQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 89 DMLGPG-EDDT--GRTTAEIIQDEVKDapRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
Cdd:PRK13639 90 QLFAPTvEEDVafGPLNLGLSKEEVEK--RVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 166 LDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQ 225
Cdd:PRK13639 168 LDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-194 |
2.73e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.86 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 25 TLNAGDSWAFVGSNGSGKSALARALAGELP-----LLKGERQSQFSHIT----RLSFEQLQKLVS--DEWQrnntdMLGP 93
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLPgsgsiQFAGQPLEAWSAAElarhRAYLSQQQTPPFamPVFQ-----YLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 94 GEDDTGRTTAeiIQDEVKDaprcmqLAQQFGITALLDRRFKYLSTGETRKTLLCQALM-----SEPD--LLILDEPFDGL 166
Cdd:PRK03695 93 HQPDKTRTEA--VASALNE------VAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSL 164
|
170 180 190
....*....|....*....|....*....|.
gi 16128728 167 DVASRQQLAERLASLHQSGITLVLV---LNR 194
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGIAVVMSshdLNH 195
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-245 |
2.88e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 51.97 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 15 DTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHIT--RLSFEQLQKLVS-----DEWQ--- 84
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGlvfqyPEYQlfe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 85 -----------RNntdmLGPGEDDtgrttaeiIQDEVKDAPRCMQLAQQfgitALLDRRFKYLSTGETRKTLLCQALMSE 153
Cdd:PRK13637 99 etiekdiafgpIN----LGLSEEE--------IENRVKRAMNIVGLDYE----DYKDKSPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 154 PDLLILDEPFDGLDVASRQQLAERLASLHQS-GITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQAlvaqla 232
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEV------ 236
|
250
....*....|...
gi 16128728 233 hsEQLEGVQLPEP 245
Cdd:PRK13637 237 --ETLESIGLAVP 247
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
275-476 |
2.89e-07 |
|
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: 51.33 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 275 ILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRGSGETIWdIKKHIGYVSSSlhldyrvstt 354
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE-NGRVLVDGHDLALADPAW-LRRQVGVVLQE---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 355 vrNVILSGYF-DSIGIYQAVSDRQQ---------------KLVQQWLDILGidKRTAdapfhSLSWGQ-QRLAlIVRALV 417
Cdd:cd03252 85 --NVLFNRSIrDNIALADPGMSMERvieaaklagahdfisELPEGYDTIVG--EQGA-----GLSGGQrQRIA-IARALI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 418 KHPTLLILDEPLQGLDPLNRQLIRRFVDVlISEGETQLLfvshhaedapacITHRLEFV 476
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHD-ICAGRTVII------------IAHRLSTV 200
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-190 |
3.00e-07 |
|
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: 51.32 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 14 SDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVSdewqrnntdMLGP 93
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS---------LVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 94 GEDDTGRTTAEIIQDEVKDAP--RCMQLAQ-----------QFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
Cdd:cd03248 96 EPVLFARSLQDNIAYGLQSCSfeCVKEAAQkahahsfiselASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190
....*....|....*....|....*....|
gi 16128728 161 EPFDGLDVASRQQLAERLASLHQSGITLVL 190
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPERRTVLVI 205
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
222-477 |
3.27e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 222 LLQQALVAQLAhSEQLEGVQLPEPDEPSARHALPANEPRIVLNNGVVSYN---DRPILNNLSWQVNPGEHWQIVGPNGAG 298
Cdd:PLN03232 577 LLSQVVNANVS-LQRIEELLLSEERILAQNPPLQPGAPAISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEG 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 299 KSTLLSLVTGDHPQGYSNDLtlfgrrrgsgetiwDIKKHIGYVSsslHLDYRVSTTVRNVILSGY-FDSIGIYQAVSdrq 377
Cdd:PLN03232 656 KTSLISAMLGELSHAETSSV--------------VIRGSVAYVP---QVSWIFNATVRENILFGSdFESERYWRAID--- 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 378 QKLVQQWLDIL-GIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLIRRFVDVLISE---GET 453
Cdd:PLN03232 716 VTALQHDLDLLpGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA---HVAHQVFDSCMKDelkGKT 792
|
250 260
....*....|....*....|....
gi 16128728 454 QLLfvshhaedapacITHRLEFVP 477
Cdd:PLN03232 793 RVL------------VTNQLHFLP 804
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
118-445 |
3.31e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 118 QLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLVL-----VL 192
Cdd:PRK13409 195 EVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVehdlaVL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 193 nrfDEIPEFVQFA-------GVLAdctlaetgakeellqQALVAQLAHSEQLEGVqLPEP-----DEPSA--RHALPANE 258
Cdd:PRK13409 275 ---DYLADNVHIAygepgayGVVS---------------KPKGVRVGINEYLKGY-LPEEnmrirPEPIEfeERPPRDES 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 259 PRIVLnngvVSYND-RPILNNLSWQVNPGEHWQ-----IVGPNGAGKSTLLSLVTGD-HPQgysndltlfgrrrgSGETI 331
Cdd:PRK13409 336 ERETL----VEYPDlTKKLGDFSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVlKPD--------------EGEVD 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 332 WDIKkhIGYVSSSLHLDY--RVSTTVRNVilSGYFDSIGIYQAVSDRqqklvqqwldiLGIDkRTADAPFHSLSWGQ-QR 408
Cdd:PRK13409 398 PELK--ISYKPQYIKPDYdgTVEDLLRSI--TDDLGSSYYKSEIIKP-----------LQLE-RLLDKNVKDLSGGElQR 461
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 16128728 409 LAlIVRALVKHPTLLILDEPLQGLDPLNR----QLIRRFVD 445
Cdd:PRK13409 462 VA-IAACLSRDADLYLLDEPSAHLDVEQRlavaKAIRRIAE 501
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
24-237 |
3.34e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.43 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshITrLSFEQLQKLVSDEWQRNNTDMLgPGEDDTGRTTA 103
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGN-------II-IDDEDISLLPLHARARRGIGYL-PQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 104 ---------EIIQDEVKD--APRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ 172
Cdd:PRK10895 95 vydnlmavlQIRDDLSAEqrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 173 QLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQALVAQLAHSEQL 237
Cdd:PRK10895 175 DIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGEDF 239
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
24-248 |
3.89e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 51.31 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVSDEWQRNNTD----------Mlgp 93
Cdd:PRK13548 23 LTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSfpftveevvaM--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 94 geddtGRTTAEIIQDEVKDAP-RCMQLAqqfGITALLDRRFKYLSTGETRKTLLCQALM------SEPDLLILDEPFDGL 166
Cdd:PRK13548 100 -----GRAPHGLSRAEDDALVaAALAQV---DLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 167 DVASRQ---QLAERLAslHQSGITLVLVLN------RF-DEIPefvqfagVLADCTLAETGAKEELLQQALVAQLAHSEq 236
Cdd:PRK13548 172 DLAHQHhvlRLARQLA--HERGLAVIVVLHdlnlaaRYaDRIV-------LLHQGRLVADGTPAEVLTPETLRRVYGAD- 241
|
250
....*....|..
gi 16128728 237 LEGVQLPEPDEP 248
Cdd:PRK13548 242 VLVQPHPETGAP 253
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
276-479 |
6.00e-07 |
|
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: 50.72 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG----DHPQGYSN--DLTLFGRRRgsgetIWDIKKH-IGYVSSSLHL- 347
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRliepTSGKVLIDgqDIAAMSRKE-----LRELRRKkISMVFQSFALl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 348 DYRvsTTVRNVILSgyFDSIGIYQAVsdRQQKLVQQwLDILGIDKRTADAPfHSLSWG-QQRLALiVRALVKHPTLLILD 426
Cdd:cd03294 115 PHR--TVLENVAFG--LEVQGVPRAE--REERAAEA-LELVGLEGWEHKYP-DELSGGmQQRVGL-ARALAVDPDILLMD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 427 EPLQGLDPlnrqLIRR-----FVDVLISEGETqLLFVSHHAEDAPAcITHRLEFVPDG 479
Cdd:cd03294 186 EAFSALDP----LIRRemqdeLLRLQAELQKT-IVFITHDLDEALR-LGDRIAIMKDG 237
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
379-465 |
7.05e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 50.79 E-value: 7.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 379 KLVQQWLDILGIDKRTAD-APFhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLF 457
Cdd:PRK13634 123 QKAREMIELVGLPEELLArSPF-ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVL 201
|
....*...
gi 16128728 458 VSHHAEDA 465
Cdd:PRK13634 202 VTHSMEDA 209
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-189 |
7.72e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.80 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVsdeWqrnntdmLG--PGEDDtgRT 101
Cdd:PRK13538 22 FTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLL---Y-------LGhqPGIKT--EL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 102 TAE-------IIQDEVkDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
Cdd:PRK13538 90 TALenlrfyqRLHGPG-DDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL 168
|
170
....*....|....*.
gi 16128728 175 AERLAS-LHQSGITLV 189
Cdd:PRK13538 169 EALLAQhAEQGGMVIL 184
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
24-189 |
8.63e-07 |
|
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: 49.50 E-value: 8.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGdSWAFVGSNGSGKSALARALAGELPLLKGerqsqfsHITRL------SFEQLQKLVSDEWQRNNTDMLGPGED- 96
Cdd:cd03264 21 LTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSG-------TIRIDgqdvlkQPQKLRRRIGYLPQEFGVYPNFTVREf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 97 -DTGRTTAEIIQDEVKDapRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
Cdd:cd03264 93 lDYIAWLKGIPSKEVKA--RVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFR 170
|
170
....*....|....
gi 16128728 176 ERLASLHQSGITLV 189
Cdd:cd03264 171 NLLSELGEDRIVIL 184
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
24-191 |
9.15e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 51.10 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAG-ELP-----LLKGERQSQ-----------------FSHITrlSFE------Q 74
Cdd:PRK09452 35 LTINNGEFLTLLGPSGCGKTTVLRLIAGfETPdsgriMLDGQDITHvpaenrhvntvfqsyalFPHMT--VFEnvafglR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 75 LQKLVSDEwqrnntdmlgpgeddtgrttaeiIQDEVKDAPRCMQLAQqfgitaLLDRRFKYLSTGETRKTLLCQALMSEP 154
Cdd:PRK09452 113 MQKTPAAE-----------------------ITPRVMEALRMVQLEE------FAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128728 155 DLLILDEPFDGLDVASRQQLAERLASLH-QSGITLVLV 191
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFV 201
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
255-443 |
9.90e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.92 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 255 PANEPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHP-----------QGYSNDLTLFG- 322
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLApdagevhyrmrDGQLRDLYALSe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 323 -RRRGSGETIWdikkhiGYVssslHLDYRvsTTVRNVILSGyfDSIG-IYQAVSDRQ----QKLVQQWLDILGID-KRTA 395
Cdd:PRK11701 81 aERRRLLRTEW------GFV----HQHPR--DGLRMQVSAG--GNIGeRLMAVGARHygdiRATAGDWLERVEIDaARID 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128728 396 DAPfHSLSWG-QQRLAlIVRALVKHPTLLILDEPLQGLD--------PLNRQLIRRF 443
Cdd:PRK11701 147 DLP-TTFSGGmQQRLQ-IARNLVTHPRLVFMDEPTGGLDvsvqarllDLLRGLVREL 201
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
270-461 |
9.96e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.18 E-value: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 270 YNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRrrgsgetiwDIKKHIgyvssslhld 348
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGlLNPE--KGEILFERQ---------SIKKDL---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 349 yrvSTTVRNVILSGYFDSIGIYQAVSDRQQKLVQQWLDILGIDK--------RTADAPFHSLSWGQQRLALIVRALVKHP 420
Cdd:PRK13540 70 ---CTYQKQLCFVGHRSGINPYLTLRENCLYDIHFSPGAVGITElcrlfsleHLIDYPCGLLSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16128728 421 TLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLfVSHH 461
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLL-TSHQ 186
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
255-447 |
1.21e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.79 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 255 PANEPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVtGDHPQGYSNDLTLFGRRRGSgetiWDI 334
Cdd:PRK10575 6 NHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAQPLES----WSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 335 K---KHIGYVSSslHLDYRVSTTVRNVILSGYF---DSIGIYqAVSDRQQklVQQWLDILGIdKRTADAPFHSLSWGQQR 408
Cdd:PRK10575 81 KafaRKVAYLPQ--QLPAAEGMTVRELVAIGRYpwhGALGRF-GAADREK--VEEAISLVGL-KPLAHRLVDSLSGGERQ 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 16128728 409 LALIVRALVKHPTLLILDEPLQGLDplnrqlIRRFVDVL 447
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALD------IAHQVDVL 187
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
272-466 |
1.31e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 49.76 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 272 DRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgysndltlfgrrrGSGEtIWDIKKHIGYVSSSlHLdYRV 351
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAP-------------DHGE-ILFDGENIPAMSRS-RL-YTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 352 STTVRNVILSG-YFDSIGIYQAVS---DRQQKL--------VQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRALVKH 419
Cdd:PRK11831 83 RKRMSMLFQSGaLFTDMNVFDNVAyplREHTQLpapllhstVMMKLEAVGL-RGAAKLMPSELSGGMARRAALARAIALE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128728 420 PTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHhaeDAP 466
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSH---DVP 205
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
261-467 |
1.32e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 50.49 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETIWDI---KK 336
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKPTE--------GQIFIDGEDVTHRsiqQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 337 HIGYVSSSLHLDYRVSTTvRNVilsGYfdsiGI-YQAVS--DRQQKlVQQWL---DILGIDKRTADapfhSLSWGQQ-RL 409
Cdd:PRK11432 79 DICMVFQSYALFPHMSLG-ENV---GY----GLkMLGVPkeERKQR-VKEALelvDLAGFEDRYVD----QISGGQQqRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128728 410 ALiVRALVKHPTLLILDEPLQGLDPlNrqlIRRFVDVLISEGETQL----LFVSHHAEDAPA 467
Cdd:PRK11432 146 AL-ARALILKPKVLLFDEPLSNLDA-N---LRRSMREKIRELQQQFnitsLYVTHDQSEAFA 202
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
261-477 |
1.37e-06 |
|
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: 49.25 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSY-NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHpQGYSNDLTLFGRRRGSGETIWDIKKHIG 339
Cdd:cd03290 1 VQVTNGYFSWgSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEM-QTLEGKVHWSNKNESEPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 340 YVSSSLHLDYRVSTTVR-NVILSGYFDSiGIYQAVSDRQQklVQQWLDILGIDKRTADAPFH-SLSWGQQRLALIVRALV 417
Cdd:cd03290 80 SVAYAAQKPWLLNATVEeNITFGSPFNK-QRYKAVTDACS--LQPDIDLLPFGDQTEIGERGiNLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 418 KHPTLLILDEPLQGLDPlnrqlirRFVDVLISEGETQLLfvsHHAEDAPACITHRLEFVP 477
Cdd:cd03290 157 QNTNIVFLDDPFSALDI-------HLSDHLMQEGILKFL---QDDKRTLVLVTHKLQYLP 206
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
23-191 |
1.58e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 49.24 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 23 QLTLNAGDSWAFVGSNGSGKSALARAL-------AGELPLlkgeRQSQFSHITRLSFEQLQKLvsdewqRNNTDM----- 90
Cdd:PRK11124 22 TLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNI----AGNHFDFSKTPSDKAIREL------RRNVGMvfqqy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 91 -LGPgeddtgRTTaeiIQDEVKDAP-------------RCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDL 156
Cdd:PRK11124 92 nLWP------HLT---VQQNLIEAPcrvlglskdqalaRAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190
....*....|....*....|....*....|....*
gi 16128728 157 LILDEPFDGLDVASRQQLAERLASLHQSGITLVLV 191
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIV 197
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
260-478 |
1.64e-06 |
|
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: 48.95 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 260 RIVLNNGVVSY--NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLslvtgdhpqgysndLTLF-------GRRRGSGET 330
Cdd:cd03369 6 EIEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLI--------------LALFrfleaeeGKIEIDGID 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 331 IwdikKHIGYVssslhlDYRVSTTV---RNVILSGYFDS-IGIYQAVSDRQqklvqqwldILGIDKRTADApfHSLSWGQ 406
Cdd:cd03369 72 I----STIPLE------DLRSSLTIipqDPTLFSGTIRSnLDPFDEYSDEE---------IYGALRVSEGG--LNLSQGQ 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128728 407 QRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISeGETQLLfvshhaedapacITHRLEFVPD 478
Cdd:cd03369 131 RQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILT------------IAHRLRTIID 189
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
263-461 |
1.73e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.40 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 263 LNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSL--------VTGDHPQGYSNDLTLFGRRRGSGETIWDI 334
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATlagredyeVTGGTVEFKGKDLLELSPEDRAGEGIFMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 335 KKH---IGYVSSSLHLDYRVStTVRNVILSGYFDSIGiYQAVSDRQQKLVQQWLDILgidKRTADAPFhslSWGQQRLAL 411
Cdd:PRK09580 84 FQYpveIPGVSNQFFLQTALN-AVRSYRGQEPLDRFD-FQDLMEEKIALLKMPEDLL---TRSVNVGF---SGGEKKRND 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16128728 412 IVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLiSEGETQLLFVSHH 461
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHY 204
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
136-201 |
1.74e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 49.70 E-value: 1.74e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128728 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEF 201
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEW 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
24-191 |
1.89e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 49.83 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAG-ELP-----LLKGERQSQ-----------------FSHIT---RLSFEQLQ- 76
Cdd:PRK11607 40 LTIYKGEIFALLGASGCGKSTLLRMLAGfEQPtagqiMLDGVDLSHvppyqrpinmmfqsyalFPHMTveqNIAFGLKQd 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 77 KLVSDEWQRNNTDMLGpgeddtgrttaeiiqdevkdaprcMQLAQQFGitallDRRFKYLSTGETRKTLLCQALMSEPDL 156
Cdd:PRK11607 120 KLPKAEIASRVNEMLG------------------------LVHMQEFA-----KRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 16128728 157 LILDEPFDGLD--VASRQQLaERLASLHQSGITLVLV 191
Cdd:PRK11607 171 LLLDEPMGALDkkLRDRMQL-EVVDILERVGVTCVMV 206
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
33-198 |
1.99e-06 |
|
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: 48.32 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 33 AFVGSNGSGKSALARALAGELP--------LLKGERQSQFSHITRLSFeqlqklVSDEwqrnntDMLGPgeddtgrttae 104
Cdd:cd03213 39 AIMGPSGAGKSTLLNALAGRRTglgvsgevLINGRPLDKRSFRKIIGY------VPQD------DILHP----------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 105 iiQDEVKDAprcmqlaqqFGITALLdrrfKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQS 184
Cdd:cd03213 96 --TLTVRET---------LMFAAKL----RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT 160
|
170 180
....*....|....*....|..
gi 16128728 185 GITLVLVL--------NRFDEI 198
Cdd:cd03213 161 GRTIICSIhqpsseifELFDKL 182
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-222 |
2.54e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.99 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQL---QKLVSDEWQRNN--TDM------LG 92
Cdd:PRK11831 28 LTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGAlfTDMnvfdnvAY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 93 PGEDDTgRTTAEIIQDEVkdaprCMQLaQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ 172
Cdd:PRK11831 108 PLREHT-QLPAPLLHSTV-----MMKL-EAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128728 173 QLAERLASL-HQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEEL 222
Cdd:PRK11831 181 VLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
136-236 |
2.61e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.66 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAe 215
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEIS- 482
|
90 100
....*....|....*....|....*
gi 16128728 216 tgakEELLQQAL----VAQLAHSEQ 236
Cdd:PRK15439 483 ----GALTGAAInvdtIMRLAFGEH 503
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-192 |
2.96e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 49.66 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 26 LNAGDSWAFVGSNGSGKSALARALAGELP---------LLKGER--QSQFSHITrlSFEQ-----LQKLVSDEwQRNNTD 89
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPkgvkgsgsvLLNGMPidAKEMRAIS--AYVQqddlfIPTLTVRE-HLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 90 MLGPGEDDTGRTTAEIIQdevkdaprcmQLAQQFGITALLD------RRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
Cdd:TIGR00955 125 HLRMPRRVTKKEKRERVD----------EVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180
....*....|....*....|....*....
gi 16128728 164 DGLDVASRQQLAERLASLHQSGITLVLVL 192
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTI 223
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
24-191 |
3.33e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 48.34 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGElpllkgERQSQFSHITRlsfeqlQKLVSDeWQ-----RNNTDMLGPGEDDT 98
Cdd:PRK11614 26 LHINQGEIVTLIGANGAGKTTLLGTLCGD------PRATSGRIVFD------GKDITD-WQtakimREAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 99 GRTTAE-------IIQDEVKDAPRCMQLAQQFgiTALLDRRFK---YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
Cdd:PRK11614 93 SRMTVEenlamggFFAERDQFQERIKWVYELF--PRLHERRIQragTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180
....*....|....*....|...
gi 16128728 169 ASRQQLAERLASLHQSGITLVLV 191
Cdd:PRK11614 171 IIIQQIFDTIEQLREQGMTIFLV 193
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-225 |
3.46e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 49.44 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSAL----ARAL---AGELpLLKGERqsqfshITRLSFEQLQKLVSDEWQRnnTDMLgpgeD 96
Cdd:PRK11160 361 LQIKAGEKVALLGRTGCGKSTLlqllTRAWdpqQGEI-LLNGQP------IADYSEAALRQAISVVSQR--VHLF----S 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 97 DTGRTTAEIIQDEVKDApRCMQLAQQFGITALLD-------------RRfkyLSTGETRKTLLCQALMSEPDLLILDEPF 163
Cdd:PRK11160 428 ATLRDNLLLAAPNASDE-ALIEVLQQVGLEKLLEddkglnawlgeggRQ---LSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128728 164 DGLDVASRQQLAERLASlHQSGITLVLVLNRFDEIPEFVQFAgVLADCTLAETGAKEELLQQ 225
Cdd:PRK11160 504 EGLDAETERQILELLAE-HAQNKTVLMITHRLTGLEQFDRIC-VMDNGQIIEQGTHQELLAQ 563
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-433 |
3.68e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 17 KTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHI----TRLSFEQLQKLVSDEW----QRNNT 88
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksSKEALENGISMVHQELnlvlQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 89 DMLGPG----------EDDTGRTTAEIIQD-EVKDAPRcmqlaqqfgitalldRRFKYLSTGETRKTLLCQALMSEPDLL 157
Cdd:PRK10982 92 DNMWLGryptkgmfvdQDKMYRDTKAIFDElDIDIDPR---------------AKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 158 ILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQALVAQLAHSEQL 237
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 238 EgvQLPEPDepsarhalpaNEPR--IVLNNGVVSYNdRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGyS 315
Cdd:PRK10982 237 Q--RFPDKE----------NKPGevILEVRNLTSLR-QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKS-A 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 316 NDLTLFGRRRGSGETIWDIKKHIGYVSSS-------LHLDYRVSTTVRNVilSGYFDSIGIyqaVSDRQQKLVQQWLdil 388
Cdd:PRK10982 303 GTITLHGKKINNHNANEAINHGFALVTEErrstgiyAYLDIGFNSLISNI--RNYKNKVGL---LDNSRMKSDTQWV--- 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 16128728 389 gIDKRTADAPFH-----SLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:PRK10982 375 -IDSMRVKTPGHrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
275-433 |
3.75e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 49.34 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 275 ILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETIWDI---------KKHIGYVSSS 344
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGClDKPTS--------GTYRVAGQDVATLdadalaqlrREHFGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 345 LHLDYRVsTTVRNVILSgyfdsiGIYQAVSDRQQKL-VQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLL 423
Cdd:PRK10535 95 YHLLSHL-TAAQNVEVP------AVYAGLERKQRLLrAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVI 166
|
170
....*....|
gi 16128728 424 ILDEPLQGLD 433
Cdd:PRK10535 167 LADEPTGALD 176
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
261-463 |
3.95e-06 |
|
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: 49.42 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG--DHPQ---------------GYSNDLTLFGR 323
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPtsgriiyhvalcekcGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 324 R-RGSGETI-------WD--------IKKHIGYVSSSLHLDYRVSTTVRNVILS----GYFDSIGIYQAVsdrqqklvqQ 383
Cdd:TIGR03269 81 PcPVCGGTLepeevdfWNlsdklrrrIRKRIAIMLQRTFALYGDDTVLDNVLEAleeiGYEGKEAVGRAV---------D 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 384 WLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAE 463
Cdd:TIGR03269 152 LIEMVQLSHRITHIA-RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-191 |
5.22e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.47 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 8 QGTFRLSdtkTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKL----VSDEW 83
Cdd:PRK10584 18 QGEHELS---ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhVGFVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 84 QrnnTDMLGPGeddtgRTTAEIIQ--------DEVKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPD 155
Cdd:PRK10584 95 Q---SFMLIPT-----LNALENVElpallrgeSSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 16128728 156 LLILDEPFDGLDVASRQQLAERLASL-HQSGITLVLV 191
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILV 203
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
276-463 |
5.54e-06 |
|
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: 46.66 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRRGSGETIWDIKKHIGYVS-----SSLHLDYR 350
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPP-ASGEITLDGKPVTRRSPRDAIRAGIAYVPedrkrEGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 351 VSttvRNVILSgyfdsigiyqavsdrqqklvqqwldilgidkrtadapfHSLSWG-QQRlALIVRALVKHPTLLILDEPL 429
Cdd:cd03215 95 VA---ENIALS--------------------------------------SLLSGGnQQK-VVLARWLARDPRVLILDEPT 132
|
170 180 190
....*....|....*....|....*....|....
gi 16128728 430 QGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAE 463
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELADAGKAVLLISSELDE 166
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
10-226 |
5.98e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.87 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 10 TFRLSDTKTLQLPQLTLN-AGDSW-AFVGSNGSGKSALARALAGelpLLKGERQSQfSHITRLSFEQLQKLVSDEWQRNN 87
Cdd:PRK13640 12 SFTYPDSKKPALNDISFSiPRGSWtALIGHNGSGKSTISKLING---LLLPDDNPN-SKITVDGITLTAKTVWDIREKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 88 TDMLGPGEDDTGRTtaeiIQDEV------KDAPR------CMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPD 155
Cdd:PRK13640 88 IVFQNPDNQFVGAT----VGDDVafglenRAVPRpemikiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 156 LLILDEPFDGLDVASRQQLAERLASLH-QSGITLVLVLNRFDEIPEFVQFAgVLADCTLAETGA------KEELLQQA 226
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEANMADQVL-VLDDGKLLAQGSpveifsKVEMLKEI 240
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
276-428 |
6.55e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQG-YSNDLTLFGRRRGSGetiwDIK--KHIGYV--SSSLHLDYR 350
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsYEGEILFDGEVCRFK----DIRdsEALGIViiHQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 351 VSTTvRNVILSGYFDSIGI--YQAVSDRQQKLvqqwLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEP 428
Cdd:NF040905 93 LSIA-ENIFLGNERAKRGVidWNETNRRAREL----LAKVGLDES-PDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
261-463 |
7.10e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.70 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSYNDR-PI----LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG----DHPQGYSNDLTLFGRRRGSGEtI 331
Cdd:PRK13645 7 IILDNVSYTYAKKtPFefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGliisETGQTIVGDYAIPANLKKIKE-V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 332 WDIKKHIGYVSSSLHLDYRVSTTVRNVilsgyfdSIGIYQAVSDRQQ--KLVQQWLDILGIDKRTAD-APFHsLSWGQQR 408
Cdd:PRK13645 86 KRLRKEIGLVFQFPEYQLFQETIEKDI-------AFGPVNLGENKQEayKKVPELLKLVQLPEDYVKrSPFE-LSGGQKR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAE 463
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMD 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
274-460 |
7.75e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 274 PILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLV------TGDH----PQGYSNDLTLFGRRRGSGETIWDIKKHIGYVSS 343
Cdd:PTZ00265 1182 PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlKNDHhivfKNEHTNDMTNEQDYQGDEEQNVGMKNVNEFSLT 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 344 SLHLDYRVSTTVRN---VILSG----------------------YFDSIGIYQAV----SDRQQKLVQQWLDILGIDK-- 392
Cdd:PTZ00265 1262 KEGGSGEDSTVFKNsgkILLDGvdicdynlkdlrnlfsivsqepMLFNMSIYENIkfgkEDATREDVKRACKFAAIDEfi 1341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128728 393 -------RTADAPF-HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSH 460
Cdd:PTZ00265 1342 eslpnkyDTNVGPYgKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
24-168 |
8.06e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.42 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKG--ERQSQFshitRLSFEQlQKLVSDEWQRNNTD---MLGPGeddt 98
Cdd:PRK09544 25 LELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGviKRNGKL----RIGYVP-QKLYLDTTLPLTVNrflRLRPG---- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 99 grttaeIIQDEVKDAPRCMQLAQqfgitaLLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
Cdd:PRK09544 96 ------TKKEDILPALKRVQAGH------LIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
24-191 |
8.19e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 47.00 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshIT---RLSFeqlqklvsdewqrnntdMLGPG----ED 96
Cdd:COG1134 47 FEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR-------VEvngRVSA-----------------LLELGagfhPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 97 DTGR------------TTAEIIQ--DEVKDaprcmqlaqqF-GITALLDRRFKYLSTGE-TRktlLCQALMS--EPDLLI 158
Cdd:COG1134 103 LTGReniylngrllglSRKEIDEkfDEIVE----------FaELGDFIDQPVKTYSSGMrAR---LAFAVATavDPDILL 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 16128728 159 LDEpfdGL---DVASRQQLAERLASLHQSGITLVLV 191
Cdd:COG1134 170 VDE---VLavgDAAFQKKCLARIRELRESGRTVIFV 202
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
229-427 |
9.93e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 47.87 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 229 AQLAHsEQLEGVQLPEPDEPSARHALPANEP-----RIVLNNGVVSYNDR---------PIlnNLSwqVNPGEHWQIVGP 294
Cdd:COG4615 292 ANVAL-RKIEELELALAAAEPAAADAAAPPApadfqTLELRGVTYRYPGEdgdegftlgPI--DLT--IRRGELVFIVGG 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 295 NGAGKSTLLSLVTG-DHPQgysndltlfgrrrgSGETIWDIKKhigyVSSSLHLDYR--VSttvrnVILSGY--FDS-IG 368
Cdd:COG4615 367 NGSGKSTLAKLLTGlYRPE--------------SGEILLDGQP----VTADNREAYRqlFS-----AVFSDFhlFDRlLG 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128728 369 IYQAVSDRQqklVQQWLDILGIDKRTA--DAPFHS--LSWGQQ-RLALIVrALVKHPTLLILDE 427
Cdd:COG4615 424 LDGEADPAR---ARELLERLELDHKVSveDGRFSTtdLSQGQRkRLALLV-ALLEDRPILVFDE 483
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
275-460 |
9.98e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 46.99 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 275 ILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETIwdikkhiGYVSSSLHLDYRvst 353
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlESPSQ--------GNVSWRGEPL-------AKLNRAQRKAFR--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 354 tvRNVILSgYFDSIGiyqAVSDR---------------------QQKLVQQWLDILGIDKRTADAPFHSLSWGQQRLALI 412
Cdd:PRK10419 89 --RDIQMV-FQDSIS---AVNPRktvreiireplrhllsldkaeRLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16128728 413 VRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSH 460
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITH 210
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
5-183 |
1.01e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.65 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 5 QILQGTFRLSDT-KTLQLPQLTLNAGDSWAFVGSNGSGKSALARAL-------AGELpLLKGERQSQFSHITRlsfEQLQ 76
Cdd:PRK11308 16 PVKRGLFKPERLvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLtmietptGGEL-YYQGQDLLKADPEAQ---KLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 77 KLVSDEWQrNNTDMLGPgEDDTGRTTAE--IIQDEVKDAPRCMQLAQQFGITAL----LDRRFKYLSTGETRKTLLCQAL 150
Cdd:PRK11308 92 QKIQIVFQ-NPYGSLNP-RKKVGQILEEplLINTSLSAAERREKALAMMAKVGLrpehYDRYPHMFSGGQRQRIAIARAL 169
|
170 180 190
....*....|....*....|....*....|...
gi 16128728 151 MSEPDLLILDEPFDGLDVASRQQLAERLASLHQ 183
Cdd:PRK11308 170 MLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQ 202
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
126-200 |
1.02e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 1.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 126 TALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLNrfdEIPE 200
Cdd:PRK13549 396 TASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISS---ELPE 467
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
111-238 |
1.04e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.42 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 111 KDA-PRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLV 189
Cdd:NF000106 119 KDArARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVL 198
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 16128728 190 LVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQ----ALVAQLAHSEQLE 238
Cdd:NF000106 199 LTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKvggrTLQIRPAHAAELD 251
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
9-191 |
1.06e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.09 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 9 GTFRLSDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGE-----RQSQF------SHITRLSFE---- 73
Cdd:PRK15112 19 GWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGElliddHPLHFgdysyrSQRIRMIFQdpst 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 74 -----QLQKLVSDEWQRNNTDMLGPGEDDtgrttaeiiqdevkdapRCMQLAQQFGItaLLDRRFKY---LSTGETRKTL 145
Cdd:PRK15112 99 slnprQRISQILDFPLRLNTDLEPEQREK-----------------QIIETLRQVGL--LPDHASYYphmLAPGQKQRLG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128728 146 LCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQS-GITLVLV 191
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYV 206
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
227-438 |
1.31e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 227 LVAQLAHsEQLEGVQLPEPDEPSARHALPANEPRIVLNNGVVSYNDRpilnnlSWQVNP-------GEHWQIVGPNGAGK 299
Cdd:PRK10522 290 LSAQVAF-NKLNKLALAPYKAEFPRPQAFPDWQTLELRNVTFAYQDN------GFSVGPinltikrGELLFLIGGNGSGK 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 300 STLLSLVTG-DHPQgySNDLTLFGRRRgSGETIWDIKKHIGYVSSSLHLdyrvsttvrnvilsgyFDSIgIYQAVSDRQQ 378
Cdd:PRK10522 363 STLAMLLTGlYQPQ--SGEILLDGKPV-TAEQPEDYRKLFSAVFTDFHL----------------FDQL-LGPEGKPANP 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 379 KLVQQWLDILGI-------DKRTADApfhSLSWGQ-QRLALIVrALVKHPTLLILDEPLQGLDPLNRQ 438
Cdd:PRK10522 423 ALVEKWLERLKMahkleleDGRISNL---KLSKGQkKRLALLL-ALAEERDILLLDEWAADQDPHFRR 486
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
271-433 |
1.37e-05 |
|
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: 46.10 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 271 NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYSndltlfgrrrgsgetiwdikkhigyVSSSLHLDyr 350
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS-------------------------VEGDIHYN-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 351 vstTVRNVILSGYFDSIGIYQAVSDRQQKL--VQQWLDILGidKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEP 428
Cdd:cd03233 71 ---GIPYKEFAEKYPGEIIYVSEEDVHFPTltVRETLDFAL--RCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNS 145
|
....*
gi 16128728 429 LQGLD 433
Cdd:cd03233 146 TRGLD 150
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-365 |
1.39e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.02 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 3 SLQILQGTFRL--SDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFShitrLSFEQLQKLVS 80
Cdd:TIGR00957 636 SITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----VAYVPQQAWIQ 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 81 DEWQRNNTDMLGPGEDDTGRTTAE---IIQD-EVKDAPRCMQLAQQfGITalldrrfkyLSTGETRKTLLCQALMSEPDL 156
Cdd:TIGR00957 712 NDSLRENILFGKALNEKYYQQVLEacaLLPDlEILPSGDRTEIGEK-GVN---------LSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 157 LILDEPFDGLDVASRQQLAERLASLHQ--SGITLVLVLNRFDEIPEfVQFAGVLADCTLAETGAKEELLQQ-----ALVA 229
Cdd:TIGR00957 782 YLFDDPLSAVDAHVGKHIFEHVIGPEGvlKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLQRdgafaEFLR 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 230 QLAHSEQlegvQLPEPDEPSARHALPANEPRIVLNNGVVSYN-----DRPILN------NLSWQVNPGEHWQIVGpngaG 298
Cdd:TIGR00957 861 TYAPDEQ----QGHLEDSWTALVSGEGKEAKLIENGMLVTDVvgkqlQRQLSAsssdsgDQSRHHGSSAELQKAE----A 932
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128728 299 KSTLLSLVTGDHPQGYSNDLTLFgrrrgsgetiWDIKKHIG----YVSSSLHLDYRVSTTVRNVILSGYFD 365
Cdd:TIGR00957 933 KEETWKLMEADKAQTGQVELSVY----------WDYMKAIGlfitFLSIFLFVCNHVSALASNYWLSLWTD 993
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
291-463 |
1.62e-05 |
|
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: 45.04 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 291 IVGPNGAGKSTLL---SLVTGDHpqgysndlTLFGRRRGSGetiwdikkHIGYVSSSLHLDYRVSttvrnvilsgyfdsi 367
Cdd:cd03227 26 ITGPNGSGKSTILdaiGLALGGA--------QSATRRRSGV--------KAGCIVAAVSAELIFT--------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 368 giyqavsdrqqklvqqwldilgidkrtadapFHSLSWGQQ---RLALIVR-ALVKHPTLLILDEPLQGLDPLNRQ----L 439
Cdd:cd03227 75 -------------------------------RLQLSGGEKelsALALILAlASLKPRPLYILDEIDRGLDPRDGQalaeA 123
|
170 180
....*....|....*....|....
gi 16128728 440 IRRFVDvliseGETQLLFVSHHAE 463
Cdd:cd03227 124 ILEHLV-----KGAQVIVITHLPE 142
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-204 |
1.84e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.18 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 33 AFVGSNGSGKSALARALaGELPLLKGERQ--------SQFSHITRLSFEQLQKLVSDEWQRNNT------DMLGPGEDDT 98
Cdd:PRK14258 37 AIIGPSGCGKSTFLKCL-NRMNELESEVRvegrveffNQNIYERRVNLNRLRRQVSMVHPKPNLfpmsvyDNVAYGVKIV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 99 G-RTTAE---IIQDEVKDAPRCMQLAQQFGITALldrrfkYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
Cdd:PRK14258 116 GwRPKLEiddIVESALKDADLWDEIKHKIHKSAL------DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKV 189
|
170 180 190
....*....|....*....|....*....|.
gi 16128728 175 AERLASLH-QSGITLVLVLNRFDEIPEFVQF 204
Cdd:PRK14258 190 ESLIQSLRlRSELTMVIVSHNLHQVSRLSDF 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-197 |
1.92e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 46.23 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFE-----QLQKLVSdeWqRNNTDMLGPGEDDT 98
Cdd:PRK11248 22 LTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAErgvvfQNEGLLP--W-RNVQDNVAFGLQLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 99 GRTTAEIIQdevkdapRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERL 178
Cdd:PRK11248 99 GVEKMQRLE-------IAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLL 171
|
170 180
....*....|....*....|
gi 16128728 179 ASL-HQSGITLVLVLNRFDE 197
Cdd:PRK11248 172 LKLwQETGKQVLLITHDIEE 191
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
111-198 |
1.94e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.79 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 111 KDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA---ERLAslHQSGIT 187
Cdd:PRK11144 104 SMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLpylERLA--REINIP 181
|
90
....*....|.
gi 16128728 188 LVLVLNRFDEI 198
Cdd:PRK11144 182 ILYVSHSLDEI 192
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-61 |
2.62e-05 |
|
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: 45.15 E-value: 2.62e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128728 4 LQILQGTFR-----LSDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQ 61
Cdd:cd03250 1 ISVEDASFTwdsgeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS 63
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
271-306 |
2.91e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 46.63 E-value: 2.91e-05
10 20 30
....*....|....*....|....*....|....*.
gi 16128728 271 NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLV 306
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI 361
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
387-460 |
3.00e-05 |
|
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: 45.84 E-value: 3.00e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 387 ILGIDKRTADAPFHSLSWGQQRLALIVRAL---VKHPTLLILDEPLQGLDPlnrQLIRRFVDVL--ISEGETQLLFVSH 460
Cdd:pfam13304 222 ILLENGGGGELPAFELSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHP---KLLRRLLELLkeLSRNGAQLILTTH 297
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
268-433 |
3.06e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 45.75 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 268 VSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVT-------------GDHPQGYSNDltlfgrrrgsgetiwDI 334
Cdd:PRK10253 15 LGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahghvwldGEHIQHYASK---------------EV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 335 KKHIGYVSSSLHLDYRVstTVRNVILSGYFDSIGIYQAVSDRQQKLVQQWLDILGIdKRTADAPFHSLSWGQQRLALIVR 414
Cdd:PRK10253 80 ARRIGLLAQNATTPGDI--TVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAM 156
|
170
....*....|....*....
gi 16128728 415 ALVKHPTLLILDEPLQGLD 433
Cdd:PRK10253 157 VLAQETAIMLLDEPTTWLD 175
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
10-191 |
3.11e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 46.34 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 10 TFRLSDTKTL-QLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGerqsqfsHITRLSFEQL----QKLvsdewq 84
Cdd:COG4178 369 TLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG-------RIARPAGARVlflpQRP------ 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 85 rnntdMLGPGeddTGR-------TTAEIIQDEVKDAPRCMQL---AQQFGITALLDRRfkyLSTGETRKTLLCQALMSEP 154
Cdd:COG4178 436 -----YLPLG---TLReallypaTAEAFSDAELREALEAVGLghlAERLDEEADWDQV---LSLGEQQRLAFARLLLHKP 504
|
170 180 190
....*....|....*....|....*....|....*..
gi 16128728 155 DLLILDEPFDGLDVASRQQLAERLASlHQSGITLVLV 191
Cdd:COG4178 505 DWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISV 540
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-192 |
3.12e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 45.19 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 16 TKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAG-ELP-----LLKGERQSQFSHITR-------LSF-EQLQKLVSD 81
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGlDTPtsgdvIFNGQPMSKLSSAAKaelrnqkLGFiYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 82 EWQRNNTDM-LGPGeddtGRTTAEIIQdevkdapRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
Cdd:PRK11629 102 FTALENVAMpLLIG----KKKPAEINS-------RALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190
....*....|....*....|....*....|..
gi 16128728 161 EPFDGLDVASRQQLAERLASLHQSGITLVLVL 192
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNRLQGTAFLVV 202
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
276-460 |
3.28e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.73 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRR--RGSGETIWDIKKHIGYV----SSSLHLD 348
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMiETPT--GGELYYQGQDllKADPEAQKLLRQKIQIVfqnpYGSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 349 YRVSTTVR-----NVILSGyfdsigiyqavSDRQQKlVQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTL 422
Cdd:PRK11308 109 KKVGQILEeplliNTSLSA-----------AERREK-ALAMMAKVGLRPEHYDRYPHMFSGGQrQRIA-IARALMLDPDV 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 16128728 423 LILDEPLQGLD-PLNRQLIRRFVDvLISEGETQLLFVSH 460
Cdd:PRK11308 176 VVADEPVSALDvSVQAQVLNLMMD-LQQELGLSYVFISH 213
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-190 |
3.34e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.85 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGelpLL---KGE----------RQSQF-SHI-------TRL--------SFEQ 74
Cdd:COG4586 43 FTIEPGEIVGFIGPNGAGKSTTIKMLTG---ILvptSGEvrvlgyvpfkRRKEFaRRIgvvfgqrSQLwwdlpaidSFRL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 75 LQKL--VSDEWQRNNTDMLgpgeddtgrttaeiiqdevkdaprcmqlAQQFGITALLDRRFKYLSTGETRKTLLCQALMS 152
Cdd:COG4586 120 LKAIyrIPDAEYKKRLDEL----------------------------VELLDLGELLDTPVRQLSLGQRMRCELAAALLH 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 16128728 153 EPDLLILDEPFDGLDVASRQQLAERLASLHQS-GITLVL 190
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILL 210
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
15-220 |
4.11e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.02 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 15 DTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGElP---LLKGERQSQFSHITRLSFEQLQKL-VSDEWQR----- 85
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PaykILEGDILFKGESILDLEPEERAHLgIFLAFQYpieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 86 --NNTDML-----------GPGEDDTgRTTAEIIQDEVKdaprCMQLAQQFgitalLDRRFKY-LSTGETRKTLLCQALM 151
Cdd:CHL00131 98 gvSNADFLrlaynskrkfqGLPELDP-LEFLEIINEKLK----LVGMDPSF-----LSRNVNEgFSGGEKKRNEILQMAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128728 152 SEPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLN--RFDE--IPEFVQfagVLADCTLAETGAKE 220
Cdd:CHL00131 168 LDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqRLLDyiKPDYVH---VMQNGKIIKTGDAE 237
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
388-480 |
4.54e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 388 LGIDKRTADAPFHSLSWGQ-QRLALIVRAL--VKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETqLLFVSHHAED 464
Cdd:PRK00635 796 LGLDYLPLGRPLSSLSGGEiQRLKLAYELLapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHT-VVIIEHNMHV 874
|
90
....*....|....*.
gi 16128728 465 APACiTHRLEFVPDGG 480
Cdd:PRK00635 875 VKVA-DYVLELGPEGG 889
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
123-200 |
5.15e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 5.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 123 FGI-TALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLNrfdEIPE 200
Cdd:PRK10762 382 FNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSS---EMPE 457
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
10-245 |
5.82e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 44.78 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 10 TFRLSDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALagelpllkGERQSQFSHITRLSFEQLQKLVSDEWQRNNT- 88
Cdd:PRK10575 18 SFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML--------GRHQPPSEGEILLDAQPLESWSSKAFARKVAy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 89 --DMLGPGEddtGRTTAEII------------QDEVKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEP 154
Cdd:PRK10575 90 lpQQLPAAE---GMTVRELVaigrypwhgalgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 155 DLLILDEPFDGLDVASRQQ---LAERLAslHQSGITLVLVLNRfdeipefVQFAGVLADCTLAETGAkeELLQQALVAQL 231
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDvlaLVHRLS--QERGLTVIAVLHD-------INMAARYCDYLVALRGG--EMIAQGTPAEL 235
|
250 260
....*....|....*....|
gi 16128728 232 AHSEQLEGVQ------LPEP 245
Cdd:PRK10575 236 MRGETLEQIYgipmgiLPHP 255
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
291-462 |
6.00e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 291 IVGPNGAGKSTLLSLVTgdhpqgysndLTLFGRRRGSGETIWDIkKHIGYVSSSLHLD-------YRV------------ 351
Cdd:COG0419 28 IVGPNGAGKSTILEAIR----------YALYGKARSRSKLRSDL-INVGSEEASVELEfehggkrYRIerrqgefaefle 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 352 -STTVRNVILSGYFDsIGIYQAVSDRQQKL-------VQQWLDILGIDKR-----TADAPFHSLSWGQQ-RLAL--IVRa 415
Cdd:COG0419 97 aKPSERKEALKRLLG-LEIYEELKERLKELeealesaLEELAELQKLKQEilaqlSGLDPIETLSGGERlRLALadLLS- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128728 416 lvkhptlLILDepLQGLDPLNRqliRRFVDVLISegetqLLFVSHHA 462
Cdd:COG0419 175 -------LILD--FGSLDEERL---ERLLDALEE-----LAIITHVI 204
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
136-189 |
6.19e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 45.64 E-value: 6.19e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 16128728 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLV 189
Cdd:PLN03211 207 ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIV 260
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
244-433 |
6.75e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 45.71 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 244 EPDEPSARHALPANEPRIVLNNGVVSY--NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG--DHPQGYSNdlt 319
Cdd:TIGR00957 620 EPDSIERRTIKPGEGNSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAemDKVEGHVH--- 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 320 lfgrrrgsgetiwdIKKHIGYVSSSLHLDyrvSTTVRNVILSGYFDSIGIYQAVSDRQQKLVQqwLDIL-GIDKRTADAP 398
Cdd:TIGR00957 697 --------------MKGSVAYVPQQAWIQ---NDSLRENILFGKALNEKYYQQVLEACALLPD--LEILpSGDRTEIGEK 757
|
170 180 190
....*....|....*....|....*....|....*
gi 16128728 399 FHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:TIGR00957 758 GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
291-442 |
7.27e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 291 IVGPNGAGKSTLLSLVTG-------------------DH-----------PQGYSNDL--TL--------FGRRRGsget 330
Cdd:NF033858 32 LIGPDGVGKSSLLSLIAGarkiqqgrvevlggdmadaRHrravcpriaymPQGLGKNLypTLsvfenldfFGRLFG---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 331 iwdikkhigyvssslhldyrvsttvrnvilsgyfdsigiyQAVSDRQQKlvqqwldilgID---KRTADAPFHS-----L 402
Cdd:NF033858 108 ----------------------------------------QDAAERRRR----------IDellRATGLAPFADrpagkL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16128728 403 SWG-QQRLALIVrALVKHPTLLILDEPLQGLDPLNR----QLIRR 442
Cdd:NF033858 138 SGGmKQKLGLCC-ALIHDPDLLILDEPTTGVDPLSRrqfwELIDR 181
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
33-191 |
8.13e-05 |
|
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: 44.09 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 33 AFVGSNGSGKSALARALAGELPLLKGERQSQfshiTRLSFEQ--LQKLVSDEWQRNNTDM-----------------LGP 93
Cdd:cd03260 30 ALIGPSGCGKSTLLRLLNRLNDLIPGAPDEG----EVLLDGKdiYDLDVDVLELRRRVGMvfqkpnpfpgsiydnvaYGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 94 geDDTGRTTAEIIQDEVKDAPRcmqlaqqfgiTALLDRRFK------YLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
Cdd:cd03260 106 --RLHGIKLKEELDERVEEALR----------KAALWDEVKdrlhalGLSGGQQQRLCLARALANEPEVLLLDEPTSALD 173
|
170 180
....*....|....*....|....
gi 16128728 168 VASRQQLAERLASLHQSgITLVLV 191
Cdd:cd03260 174 PISTAKIEELIAELKKE-YTIVIV 196
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
129-222 |
1.07e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.07 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 129 LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVL 208
Cdd:PRK13631 170 LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVM 249
|
90
....*....|....
gi 16128728 209 ADCTLAETGAKEEL 222
Cdd:PRK13631 250 DKGKILKTGTPYEI 263
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
253-434 |
1.25e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 43.49 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 253 ALPANEPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLL-SL-----------VTGDhpqgysndLTL 320
Cdd:COG1117 4 PASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrCLnrmndlipgarVEGE--------ILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 321 FG-------------RRR------------GSgetIWD-----IKKHiGYVSSSlHLDYRVSTTVRNVilsgyfdsiGIY 370
Cdd:COG1117 76 DGediydpdvdvvelRRRvgmvfqkpnpfpKS---IYDnvaygLRLH-GIKSKS-ELDEIVEESLRKA---------ALW 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 371 QAVSDRqqklvqqwldiLgidkrtaDAPFHSLSWGQQ-RLAlIVRALVKHPTLLILDEPLQGLDP 434
Cdd:COG1117 142 DEVKDR-----------L-------KKSALGLSGGQQqRLC-IARALAVEPEVLLMDEPTSALDP 187
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
283-445 |
1.48e-04 |
|
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: 43.55 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 283 VNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQGysndltlfgrrrgsGETIWDIKKhIGYVSSSLHLDYrvSTTVRNvILS 361
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVlKPDE--------------GDIEIELDT-VSYKPQYIKADY--EGTVRD-LLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 362 GYFDSIGIYqavsdrqqklvQQW----LDILGIDkRTADAPFHSLSWGQ-QRLALIVrALVKHPTLLILDEPLQGLDPLN 436
Cdd:cd03237 84 SITKDFYTH-----------PYFkteiAKPLQIE-QILDREVPELSGGElQRVAIAA-CLSKDADIYLLDEPSAYLDVEQ 150
|
170
....*....|...
gi 16128728 437 R----QLIRRFVD 445
Cdd:cd03237 151 RlmasKVIRRFAE 163
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
268-323 |
1.62e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 43.28 E-value: 1.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128728 268 VSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGY-------SNDLTLFGR 323
Cdd:PRK13547 9 VARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvTGDVTLNGE 71
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
24-238 |
1.74e-04 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 44.00 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshIT-------RLSFEQLQK---LVSDEWQ------RNN 87
Cdd:COG1132 361 LTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR-------ILidgvdirDLTLESLRRqigVVPQDTFlfsgtiREN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 88 TDMLGPGEDDtgrttaeiiqDEVKDAprcMQLAQ--QFgITAL-------LDRRFKYLSTGEtrKTLLC--QALMSEPDL 156
Cdd:COG1132 434 IRYGRPDATD----------EEVEEA---AKAAQahEF-IEALpdgydtvVGERGVNLSGGQ--RQRIAiaRALLKDPPI 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 157 LILDEPFDGLDVASRQQLAERLASLHQsGITLVLVLNRF------DEIpefVqfagVLADCTLAETGAKEELLQQ-ALVA 229
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLstirnaDRI---L----VLDDGRIVEQGTHEELLARgGLYA 569
|
....*....
gi 16128728 230 QLAHSEQLE 238
Cdd:COG1132 570 RLYRLQFGE 578
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-223 |
1.83e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.87 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQklvsdEWQRNNTDM------LGPGE-- 95
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELR-----EVRRKKIAMvfqsfaLMPHMtv 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 96 -DDT--GRTTAEIIQDEVKDapRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ 172
Cdd:PRK10070 124 lDNTafGMELAGINAEERRE--KALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16128728 173 QLAERLASL---HQSgiTLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELL 223
Cdd:PRK10070 202 EMQDELVKLqakHQR--TIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
124-206 |
2.13e-04 |
|
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: 41.92 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 124 GITAL-LDRRFKYLSTGETRKTLLCQALMSEPD--LLILDEPFDGLDVASRQQLAERLASLHQSGITLVL------VLNR 194
Cdd:cd03238 75 GLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILiehnldVLSS 154
|
90
....*....|..
gi 16128728 195 FDEIPEFVQFAG 206
Cdd:cd03238 155 ADWIIDFGPGSG 166
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
24-183 |
2.39e-04 |
|
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: 43.52 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALageLPLLKGERQSQF--SHITRLSFEQLQKLVSdewqrnntDM----------L 91
Cdd:COG4172 307 LTLRRGETLGLVGESGSGKSTLGLAL---LRLIPSEGEIRFdgQDLDGLSRRALRPLRR--------RMqvvfqdpfgsL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 92 GPgeddtgR-TTAEII-------QDEVKDAPRcMQLAQQfgitAL----LDR--RFKY---LSTGETRKTLLCQALMSEP 154
Cdd:COG4172 376 SP------RmTVGQIIaeglrvhGPGLSAAER-RARVAE----ALeevgLDPaaRHRYpheFSGGQRQRIAIARALILEP 444
|
170 180
....*....|....*....|....*....
gi 16128728 155 DLLILDEPFDGLDVASRQQLAERLASLHQ 183
Cdd:COG4172 445 KLLVLDEPTSALDVSVQAQILDLLRDLQR 473
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
251-460 |
2.55e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.69 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 251 RHALPANEPRIVLNNGVVSYNDR---PILNNLSWQVNPGEHWQIVGPNGAGKS----TLLSLVTGDHPQGYSNDLTLFGR 323
Cdd:PRK10261 4 SDELDARDVLAVENLNIAFMQEQqkiAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLLRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 324 RRGSGETIWDIKKHIGYV-SSSLHLDYRVSTTVRNVILS---GYFDSIGIYQAVSdRQQKLVQ--QWLDILGI-DKRTAD 396
Cdd:PRK10261 84 SRQVIELSEQSAAQMRHVrGADMAMIFQEPMTSLNPVFTvgeQIAESIRLHQGAS-REEAMVEakRMLDQVRIpEAQTIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 397 APF-HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSH 460
Cdd:PRK10261 163 SRYpHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITH 227
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
24-170 |
2.87e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGE-RQSQFSHI------TRLSFEQLQKLVsdEWQRNNTDmlgPGED 96
Cdd:PRK15064 340 LLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTvKWSENANIgyyaqdHAYDFENDLTLF--DWMSQWRQ---EGDD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 97 DT------GRTTaeIIQDEVKdaprcmqlaqqfgitalldRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
Cdd:PRK15064 415 EQavrgtlGRLL--FSQDDIK-------------------KSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES 473
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-161 |
3.10e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 42.38 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 24 LTLNAGDswaFV---GSNGSGKSALARALAGELP------LLKGERqsqfshITRLSFEQLQKLVS-------------- 80
Cdd:COG1101 27 LTIEEGD---FVtviGSNGAGKSTLLNAIAGSLPpdsgsiLIDGKD------VTKLPEYKRAKYIGrvfqdpmmgtapsm 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 81 --DE-----WQRNNTDMLGPGEDDTGRttaEIIQDEVKDaprcMQLaqqfGITALLDRRFKYLSTGEtRKTL-LCQALMS 152
Cdd:COG1101 98 tiEEnlalaYRRGKRRGLRRGLTKKRR---ELFRELLAT----LGL----GLENRLDTKVGLLSGGQ-RQALsLLMATLT 165
|
....*....
gi 16128728 153 EPDLLILDE 161
Cdd:COG1101 166 KPKLLLLDE 174
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-197 |
4.08e-04 |
|
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: 43.08 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 29 GDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshiTRLSFEQLQKLVSDEWQRNNTDMLGPGEDD--TGRT----T 102
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGD--------ATVAGKSILTNISDVHQNMGYCPQFDAIDDllTGREhlylY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 103 AEIIQDEVKDAPRCMQLA-QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASL 181
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVANWSiQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
|
170
....*....|....*.
gi 16128728 182 HQSGITLVLVLNRFDE 197
Cdd:TIGR01257 2117 IREGRAVVLTSHSMEE 2132
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
261-433 |
4.60e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.52 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 261 IVLNNGVVSY-NDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgysndLtlfgrrrgsgETIwdikkhig 339
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG---------L----------ERI-------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 340 yVSSSLHLDYRVSTTV----RNVILsgYFDSIGIYQAVSDRQ----------------QKLVQQWLDILGIDKRTADAPf 399
Cdd:PRK11650 57 -TSGEIWIGGRVVNELepadRDIAM--VFQNYALYPHMSVREnmayglkirgmpkaeiEERVAEAARILELEPLLDRKP- 132
|
170 180 190
....*....|....*....|....*....|....*
gi 16128728 400 HSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLD 433
Cdd:PRK11650 133 RELSGGQrQRVAM-GRAIVREPAVFLFDEPLSNLD 166
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
25-249 |
5.81e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.04 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 25 TLNAGDSWAFVGSNGSGKSALARALAG--ELPLLKGERQSQF--SHITRLSFEQLQKLVSDE----WQRNNTDmLGPGed 96
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVSSLAIMGliDYPGRVMAEKLEFngQDLQRISEKERRNLVGAEvamiFQDPMTS-LNPC-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 97 dtgRTTAEIIQDEVK---------DAPRCMQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFD 164
Cdd:PRK11022 106 ---YTVGFQIMEAIKvhqggnkktRRQRAIDLLNQVGIPDPASRLDVYphqLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 165 GLDVASRQQLAERLASLHQ-SGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQ-------QALVAQL----- 231
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRaprhpytQALLRALpefaq 262
|
250 260
....*....|....*....|
gi 16128728 232 --AHSEQLEGVQLPEPDEPS 249
Cdd:PRK11022 263 dkARLASLPGVVPGKYDRPN 282
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
29-198 |
7.03e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 41.64 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 29 GDSWAFVGSNGSGKSALARALAGelpLLKGERQSQFSHITRLSFE---QLQKLVSDEWQRNNTDMLGPG-EDDT--GRTT 102
Cdd:PRK13650 33 GEWLSIIGHNGSGKSTTVRLIDG---LLEAESGQIIIDGDLLTEEnvwDIRHKIGMVFQNPDNQFVGATvEDDVafGLEN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 103 AEIIQDEVKDapRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLH 182
Cdd:PRK13650 110 KGIPHEEMKE--RVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIR 187
|
170
....*....|....*..
gi 16128728 183 QS-GITLVLVLNRFDEI 198
Cdd:PRK13650 188 DDyQMTVISITHDLDEV 204
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-191 |
7.71e-04 |
|
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: 41.20 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 35 VGSNGSGKSALARALAGEL-PLLkGERQSQFSHITRLSF-------EQLQKLVSDEWQ---------------RNNTDML 91
Cdd:cd03236 32 VGPNGIGKSTALKILAGKLkPNL-GKFDDPPDWDEILDEfrgselqNYFTKLLEGDVKvivkpqyvdlipkavKGKVGEL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 92 GPGEDDTGRttaeiiQDEVKDaprcmqlaqQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
Cdd:cd03236 111 LKKKDERGK------LDELVD---------QLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180
....*....|....*....|
gi 16128728 172 QQLAERLASLHQSGITLVLV 191
Cdd:cd03236 176 LNAARLIRELAEDDNYVLVV 195
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
385-460 |
8.15e-04 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 41.32 E-value: 8.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 385 LDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLIRRFVDV---LISEGETQLLfVSH 460
Cdd:COG4598 139 LAKVGLADKRDAYPAH-LSGGQQQRAAIARALAMEPEVMLFDEPTSALDP---ELVGEVLKVmrdLAEEGRTMLV-VTH 212
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
136-176 |
8.45e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 8.45e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 16128728 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR-------QQLAE 176
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKyeiytiiNELAA 452
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
258-460 |
9.34e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 41.69 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 258 EPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRrrgsgetiwdikkh 337
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT-KGTITINNI-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 338 igyvsSSLHLDYRVSTTVrnvilsgyfdSIG-IYQAVS-----------------------------DRQQKLVQQWLDI 387
Cdd:PRK09700 68 -----NYNKLDHKLAAQL----------GIGiIYQELSvideltvlenlyigrhltkkvcgvniidwREMRVRAAMMLLR 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128728 388 LGIdKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDplNRQLIRRF--VDVLISEGeTQLLFVSH 460
Cdd:PRK09700 133 VGL-KVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT--NKEVDYLFliMNQLRKEG-TAIVYISH 203
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
14-197 |
1.02e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 40.85 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 14 SDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVSDEWQRNNTDMLGP 93
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 94 G-EDDT--GRTTAEIIQDEVkdAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
Cdd:PRK13642 98 TvEDDVafGMENQGIPREEM--IKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180
....*....|....*....|....*...
gi 16128728 171 RQQLAERLASLH-QSGITLVLVLNRFDE 197
Cdd:PRK13642 176 RQEIMRVIHEIKeKYQLTVLSITHDLDE 203
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-198 |
1.27e-03 |
|
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: 39.28 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 29 GDSWAFVGSNGSGKSALARALAGELPLLKGErqsqfshitrlsfeqlQKLVSDEWQRNNTDMLGPGEDDTGRTTAEIIQD 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGG----------------VIYIDGEDILEEVLDQLLLIIVGGKKASGSGEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 109 EVKDAprcMQLAQQFGitalldrrfkylstgetrktllcqalmsePDLLILDEPFDGLDVASRQQL------AERLASLH 182
Cdd:smart00382 66 RLRLA---LALARKLK-----------------------------PDVLILDEITSLLDAEQEALLllleelRLLLLLKS 113
|
170
....*....|....*.
gi 16128728 183 QSGITLVLVLNRFDEI 198
Cdd:smart00382 114 EKNLTVILTTNDEKDL 129
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
292-459 |
1.52e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.54 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 292 VGPNGAGKSTLLSLVTgdhpqgYSNDLTLFGRRRGS----GETIWD-------IKKHIGYV-------SSSLH------- 346
Cdd:PRK14243 42 IGPSGCGKSTILRCFN------RLNDLIPGFRVEGKvtfhGKNLYApdvdpveVRRRIGMVfqkpnpfPKSIYdniayga 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 347 --------LDYRVSTTVRNVILsgyfdsigiYQAVSDrqqKLVQQWLdilgidkrtadapfhSLSWGQQRLALIVRALVK 418
Cdd:PRK14243 116 ringykgdMDELVERSLRQAAL---------WDEVKD---KLKQSGL---------------SLSGGQQQRLCIARAIAV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16128728 419 HPTLLILDEPLQGLDP--------LNRQLIRRFVDVLISEGETQLLFVS 459
Cdd:PRK14243 169 QPEVILMDEPCSALDPistlrieeLMHELKEQYTIIIVTHNMQQAARVS 217
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
115-191 |
1.68e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 40.36 E-value: 1.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128728 115 RCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASL-HQSGITLVLV 191
Cdd:PRK11300 133 RAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLI 210
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
129-256 |
1.87e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 129 LDRRFKYLSTGETRKTLLCQALMS---EPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLVL------VLNRFDEIP 199
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIiehnmhVVKVADYVL 882
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128728 200 EFVQFAGVLADCTLAETgAKEELLQQALVAQLAHSEQLEGVQ-LPE-PDEPSARHALPA 256
Cdd:PRK00635 883 ELGPEGGNLGGYLLASC-SPEELIHLHTPTAKALRPYLSSPQeLPYlPDPSPKPPVPAD 940
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
276-308 |
1.96e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.64 E-value: 1.96e-03
10 20 30
....*....|....*....|....*....|...
gi 16128728 276 LNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTG 308
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAG 72
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
260-442 |
2.47e-03 |
|
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: 39.84 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 260 RIVLNNGVVSYND--RPILNNLSWQVNPGEHWQIVGPNGAGKSTLLS-LVTGDHPQGysnDLTLFGRRRGSgETIWDIKK 336
Cdd:cd03289 2 QMTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLNTEG---DIQIDGVSWNS-VPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 337 HIGYVSSSLHLdyrVSTTVR-NVILSGYFDSIGIYQAVSDRQQKLV-QQWLDILgiDKRTADAPFhSLSWGQQRLALIVR 414
Cdd:cd03289 78 AFGVIPQKVFI---FSGTFRkNLDPYGKWSDEEIWKVAEEVGLKSViEQFPGQL--DFVLVDGGC-VLSHGHKQLMCLAR 151
|
170 180
....*....|....*....|....*...
gi 16128728 415 ALVKHPTLLILDEPLQGLDPLNRQLIRR 442
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIRK 179
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
274-433 |
2.53e-03 |
|
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: 39.84 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 274 PILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHpqgysndltlfgrrrgsgETIWDIKKHIGYVSSSLHLDYRVST 353
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGEL------------------EPSEGKIKHSGRISFSSQFSWIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 354 TVRNVILSGYFDSIGIYQAVSdrqqKLVQQWLDILGI---DKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQ 430
Cdd:cd03291 113 TIKENIIFGVSYDEYRYKSVV----KACQLEEDITKFpekDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
...
gi 16128728 431 GLD 433
Cdd:cd03291 189 YLD 191
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-303 |
3.52e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 129 LDRRFKYLSTGETRKTLLCQALMSEPD--LLILDEPFDGLDVASRQQLAERLASLHQSGITLVLV------LNRFDEIPE 200
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVehdedtIRAADYVID 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 201 FVQFAGVLADCTLAEtGAKEELLQ--QALVAQ-LAHSEQLEgvqlpepdEPSARHalPANEPRIVLNnGVVSYNdrpiLN 277
Cdd:TIGR00630 562 IGPGAGEHGGEVVAS-GTPEEILAnpDSLTGQyLSGRKKIE--------VPAERR--PGNGKFLTLK-GARENN----LK 625
|
170 180
....*....|....*....|....*.
gi 16128728 278 NLSWQVNPGEHWQIVGPNGAGKSTLL 303
Cdd:TIGR00630 626 NITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-226 |
3.62e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 134 KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ------------------QLAERLASLHQSgiTLVLVLNRF 195
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKliektivdikdkadktiiTIAHRIASIKRS--DKIVVFNNP 1434
|
90 100 110
....*....|....*....|....*....|.
gi 16128728 196 DEIPEFVQFAGVLADCTLAETGAKEELLQQA 226
Cdd:PTZ00265 1435 DRTGSFVQAHGTHEELLSVQDGVYKKYVKLA 1465
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
403-479 |
3.77e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 39.33 E-value: 3.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128728 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLfVSHHAEDAPAcITHRLEFVPDG 479
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLL-TTQYMEEAEQ-LAHELTVIDRG 220
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
122-207 |
3.78e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 38.74 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 122 QFGITALLDRRFKYLSTGEtrKTLLC--------QALMSEPDLLILDEPFDGLDVASR-QQLAERLASLHQSGITLVLVL 192
Cdd:cd03240 102 QGESNWPLLDMRGRCSGGE--KVLASliirlalaETFGSNCGILALDEPTTNLDEENIeESLAEIIEERKSQKNFQLIVI 179
|
90
....*....|....*
gi 16128728 193 NRfDEipEFVQFAGV 207
Cdd:cd03240 180 TH-DE--ELVDAADH 191
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
34-181 |
4.87e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.72 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 34 FVGSNGSGKSALARALAGELPLLKGE---------------RQ-----SQ-FSHITRLSFEQ-------LQKLVSDEWqr 85
Cdd:NF033858 297 FLGSNGCGKSTTMKMLTGLLPASEGEawlfgqpvdagdiatRRrvgymSQaFSLYGELTVRQnlelharLFHLPAAEI-- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 86 nntdmlgpgeddtgrttaeiiqdevkdAPRCMQLAQQFGITALLDRRFKYLSTGeTRKTL-LCQALMSEPDLLILDEPFD 164
Cdd:NF033858 375 ---------------------------AARVAEMLERFDLADVADALPDSLPLG-IRQRLsLAVAVIHKPELLILDEPTS 426
|
170
....*....|....*..
gi 16128728 165 GLDVASRQQLAERLASL 181
Cdd:NF033858 427 GVDPVARDMFWRLLIEL 443
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
372-465 |
6.80e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 38.86 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 372 AVSDRQQKLVQQwLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEG 451
Cdd:PRK10070 137 NAEERREKALDA-LRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKH 214
|
90
....*....|....
gi 16128728 452 ETQLLFVSHHAEDA 465
Cdd:PRK10070 215 QRTIVFISHDLDEA 228
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
400-460 |
8.51e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 38.35 E-value: 8.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128728 400 HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSH 460
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISH 217
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
134-204 |
8.81e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 38.22 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 134 KYLSTGETrKTLLC----------QALMSEPDLLILDEPFDGLDVASRQQLAERLASLH-QSGITLVlVLNRFDEIPEFV 202
Cdd:PRK00064 272 DFGSTGQQ-KLLLLalklaeaellKEETGEAPILLLDDVASELDDGRRAALLERLKGLGaQVFITTT-DLEDLADLLENA 349
|
..
gi 16128728 203 QF 204
Cdd:PRK00064 350 KI 351
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
285-460 |
9.26e-03 |
|
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: 37.73 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 285 PGEHWQIVGPNGAGKSTLLSLVTGD-HPQgysndltlFGRRRGSGEtiWD-IKKHigYVSSSLHlDY---RVSTTVRNVI 359
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKlKPN--------LGKFDDPPD--WDeILDE--FRGSELQ-NYftkLLEGDVKVIV 91
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128728 360 LSGYFDSI---------GIYQAVSDRQQK--LVQQwLDILGIDKRTADapfhSLSWGQ-QRLAlIVRALVKHPTLLILDE 427
Cdd:cd03236 92 KPQYVDLIpkavkgkvgELLKKKDERGKLdeLVDQ-LELRHVLDRNID----QLSGGElQRVA-IAAALARDADFYFFDE 165
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170 180 190
....*....|....*....|....*....|....*..
gi 16128728 428 PLQGLDPLNR----QLIRRfvdvlISEGETQLLFVSH 460
Cdd:cd03236 166 PSSYLDIKQRlnaaRLIRE-----LAEDDNYVLVVEH 197
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