|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-490 |
0e+00 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 1036.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 1 MSSLQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLVS 80
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 81 DEWQRNNTDLLSPGEEDTGRTTAEIIQDEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILD 160
Cdd:PRK10938 81 DEWQRNNTDMLSPGEDDTGRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 161 EPFDGLDVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLLQQALVAQLAHSEKLDGI 240
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQLAHSEQLEGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 241 TLPEPDVPPARHALADSAPRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYSNDLTL 320
Cdd:PRK10938 241 QLPEPDEPSARHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 321 FGRRRGSGETIWDIKKHIGYVSSSLHLDYRVSTNVRNVILSGYFDSIGIYQAVSDKQHKLVQQWLDILGIDKRTADAPFH 400
Cdd:PRK10938 321 FGRRRGSGETIWDIKKHIGYVSSSLHLDYRVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPFH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDAPDCITHRLAFVPSGD 480
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPACITHRLEFVPDGD 480
|
490
....*....|
gi 488984360 481 GYTYQLGPVA 490
Cdd:PRK10938 481 IYRYVQTKLN 490
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
259-490 |
2.64e-118 |
|
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: 347.07 E-value: 2.64e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 259 PRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYSNDLTLFGRRRGsGETIWDIKKHI 338
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRG-GEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 339 GYVSSSLHLDYRVSTNVRNVILSGYFDSIGIYQAVSDKQHKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVK 418
Cdd:COG1119 81 GLVSPALQLRFPRDETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHL-ADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984360 419 HPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDAPDCITHRLAFVpsgDGYTYQLGPVA 490
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLK---DGRVVAAGPKE 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-460 |
7.73e-47 |
|
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: 169.70 E-value: 7.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 10 TFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLP---LLSGQRESHFSRVTRLSFEQLQKLVSDEWQRN 86
Cdd:COG1123 13 RYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLELSEALRGRRIGMVFQDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 87 NTDL--LSPGEEdtgrtTAEIIQDEVKDP----ARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILD 160
Cdd:COG1123 93 MTQLnpVTVGDQ-----IAEALENLGLSRaearARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 161 EPFDGLDVNSRQQLAALLADLHSA-GITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLlqqalvaqLAHSEKLDG 239
Cdd:COG1123 168 EPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI--------LAAPQALAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 240 ITLPEPDVPPARHALADSAPRIVLNDGVVSYNDR-----PVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQg 313
Cdd:COG1123 240 VPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGlLRPT- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 314 ySNDLTLFGR--RRGSGETIWDIKKHIGYV----SSSlhLDYRVStnVRNVILsgyfDSIGIYQAVSDKQ-HKLVQQWLD 386
Cdd:COG1123 319 -SGSILFDGKdlTKLSRRSLRELRRRVQMVfqdpYSS--LNPRMT--VGDIIA----EPLRLHGLLSRAErRERVAELLE 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984360 387 ILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNR-QLVRRFVDVLIGEGATqLLFVSH 460
Cdd:COG1123 390 RVGLPPDLADRYPHELSGGQrQRVA-IARALALEPKLLILDEPTSALDVSVQaQILNLLRDLQRELGLT-YLFISH 463
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
256-471 |
1.21e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.40 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 256 DSAPRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRRGSGetiwdiK 335
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP-TSGTVRLFGKPPRRA------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 336 KHIGYVSSSLHLDYRVSTNVRNVILSGYFDSIGIYQAVSDKQHKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRA 415
Cdd:COG1121 75 RRIGYVPQRAEVDWDFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDL-ADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488984360 416 LVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSHHAEDAPDCITH 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 |
4.90e-40 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 143.44 E-value: 4.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 263 LNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRrgsgetIWDIKKHIGYVS 342
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP-TSGSIRVFGKP------LEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 343 SSLHLDYRVSTNVRNVILSGYFDSIGIYQAVSDKQHKLVQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPTL 422
Cdd:cd03235 75 QRRSIDRDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSE-LADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984360 423 LILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSH 460
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMT-ILVVTH 190
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-460 |
2.67e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 137.89 E-value: 2.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQResHFSRVTRLSF-EQLQKLVSDE----------------WQRN 86
Cdd:COG0488 19 LSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--SIPKGLRIGYlPQEPPLDDDLtvldtvldgdaelralEAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 87 NTDLLSPGEEDTGRTTAEIIQDEVKD------PARCARLAEQFGIS-ALLDRRFKYLSTGETRKTLLCQALMTDPQLLIL 159
Cdd:COG0488 97 EELEAKLAEPDEDLERLAELQEEFEAlggweaEARAEEILSGLGFPeEDLDRPVSELSGGWRRRVALARALLSEPDLLLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 160 DEPFDGLDVNSRQQLAALLADLHSagiTLVLV------LNRF-DEIPEfvqfagvLADCTLSE-TG------EKSSLL-- 223
Cdd:COG0488 177 DEPTNHLDLESIEWLEEFLKNYPG---TVLVVshdryfLDRVaTRILE-------LDRGKLTLyPGnysaylEQRAERle 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 224 --------QQALVAQL----------------AHS-----EKLDGITLPEPDVPPA-RHALADSAPRIVLN-DGV-VSYN 271
Cdd:COG0488 247 qeaaayakQQKKIAKEeefirrfrakarkakqAQSrikalEKLEREEPPRRDKTVEiRFPPPERLGKKVLElEGLsKSYG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 272 DRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQGysndltlfGRRRgSGETIwdikkHIGYVS---SSLHL 347
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELePDS--------GTVK-LGETV-----KIGYFDqhqEELDP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 348 DYRVSTNVRnvilsgyfdsigiyQAVSDKQHKLVQQWLDILGIDKRTADAPFHSLSWGQQ-RLALIvRALVKHPTLLILD 426
Cdd:COG0488 393 DKTVLDELR--------------DGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKaRLALA-KLLLSPPNVLLLD 457
|
490 500 510
....*....|....*....|....*....|....*
gi 488984360 427 EPLQGLDPLNRQLVrrfVDVLIG-EGAtqLLFVSH 460
Cdd:COG0488 458 EPTNHLDIETLEAL---EEALDDfPGT--VLLVSH 487
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
269-465 |
1.31e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 129.41 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPqgYSNDLTLFGRRRGSGETiwDIKKHIGYV--SSSL 345
Cdd:COG1131 9 RYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGlLRP--TSGEVRVLGEDVARDPA--EVRRRIGYVpqEPAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 346 HLDYRVSTNVRnvilsgYFDsiGIYQAVSDKQHKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTLLIL 425
Cdd:COG1131 85 YPDLTVRENLR------FFA--RLYGLPRKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488984360 426 DEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSHHAEDA 465
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKT-VLLSTHYLEEA 194
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
276-428 |
1.58e-33 |
|
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: 123.91 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 276 INHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGdHPQGYSNDLTLFGRRRgSGETIWDIKKHIGYVSSSLHLDYRvSTNV 355
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG-LLSPTEGTILLDGQDL-TDDERKSLRKEIGYVFQDPQLFPR-LTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984360 356 RNVILSGYFDsiGIYQAVSDKQHKLVQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEP 428
Cdd:pfam00005 78 ENLRLGLLLK--GLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-231 |
9.70e-33 |
|
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: 124.81 E-value: 9.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVT-RLSFEQLQK---LV 79
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRgGEDVWELRKrigLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 80 SDEWQRNNTDLLSPgeED---TGRTTAEIIQDEVKDP--ARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDP 154
Cdd:COG1119 84 SPALQLRFPRDETV--LDvvlSGFFDSIGLYREPTDEqrERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984360 155 QLLILDEPFDGLDVNSRQQLAALLADLHSAG-ITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLLQQALVAQL 231
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEA 239
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
260-461 |
7.66e-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: 117.07 E-value: 7.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 260 RIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRrgsgetIWDIK---- 335
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKP-SSGEVLLDGRD------LASLSrrel 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 336 -KHIGYVSSSLHLDYRVStnVRNVILSGYFDSIGIYQAVSDKQHKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVR 414
Cdd:COG1120 74 aRRIAYVPQEPPAPFGLT--VRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHL-ADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984360 415 ALVKHPTLLILDEPLQGLDPLNR----QLVRRFVDvliGEGATqLLFVSHH 461
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQlevlELLRRLAR---ERGRT-VVMVLHD 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
261-465 |
9.56e-29 |
|
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: 113.80 E-value: 9.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQgysndltlfgrrrgSGETIWD------ 333
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLlKPD--------------SGSILIDgedvrk 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 334 ----IKKHIGYVSSSLHLDYRVStnVRNVILsgYFdsIGIYQAVSDKQHKLVQQWLDILGIDKrTADAPFHSLSWGQQRL 409
Cdd:COG4555 68 epreARRQIGVLPDERGLYDRLT--VRENIR--YF--AELYGLFDEELKKRIEELIELLGLEE-FLDRRVGELSTGMKKK 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488984360 410 ALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSHHAEDA 465
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKT-VLFSSHIMQEV 195
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
261-479 |
3.44e-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: 110.18 E-value: 3.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGrrRGSGETIWDIKKHIGY 340
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKP-DSGEIKVLG--KDIKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 341 V--SSSLHLDYRVSTNVRnviLSGyfdsigiyqavsdkqhklvqqwldilgidkrtadapfhslswGQQRLALIVRALVK 418
Cdd:cd03230 78 LpeEPSLYENLTVRENLK---LSG------------------------------------------GMKQRLALAQALLH 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984360 419 HPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSHHAEDAPDcITHRLAFVPSG 479
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRELKKEGKT-ILLSSHILEEAER-LCDRVAILNNG 171
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-202 |
1.03e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 110.95 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 1 MSSLQISQGTFRLSDTKTLK-IDhLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGqreshfsRVTRLSfeqlqKLV 79
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEdVS-LTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSG-------TVRLFG-----KPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 80 SDEW-------QRNNTDLLSPgeedtgrTTAEiiqdEV-----------------KDPARCARLAEQFGISALLDRRFKY 135
Cdd:COG1121 71 RRARrrigyvpQRAEVDWDFP-------ITVR----DVvlmgrygrrglfrrpsrADREAVDEALERVGLEDLADRPIGE 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 136 LSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFV 202
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYF 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
261-467 |
1.63e-27 |
|
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: 109.73 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYND-RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRRRgSGETIWDIKKHI 338
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGlLKPT--SGEVLVDGKDI-TKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 339 GYV----SSSLhldyrVSTNV--------RNvilsgyfdsigiyQAVSDKQ-HKLVQQWLDILGIDKRtADAPFHSLSWG 405
Cdd:COG1122 78 GLVfqnpDDQL-----FAPTVeedvafgpEN-------------LGLPREEiRERVEEALELVGLEHL-ADRPPHELSGG 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984360 406 QQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSHHAEDAPD 467
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKT-VIIVTHDLDLVAE 199
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
259-474 |
3.57e-27 |
|
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: 108.34 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 259 PRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPqgYSNDLTLFGRRRGSGETiwDIKKH 337
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGlLPP--SAGEVLWNGEPIRDARE--DYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 338 IGYVS--SSLHLDYRVSTNVRnvilsgyfdsigIYQAVS--DKQHKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIV 413
Cdd:COG4133 77 LAYLGhaDGLKPELTVRENLR------------FWAALYglRADREAIDEALEAVGLAGL-ADLPVRQLSAGQKRRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984360 414 RALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSHHAEDAPDCITHRLA 474
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQPLELAAARVLDLG 203
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-210 |
4.89e-27 |
|
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: 107.94 E-value: 4.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 10 TFRLSDTKTLKIDH--LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLVSDEWQRNN 87
Cdd:cd03225 6 SFSYPDGARPALDDisLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 88 TDLLSPgeedtgRTTAEII-------QDEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILD 160
Cdd:cd03225 86 DQFFGP------TVEEEVAfglenlgLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984360 161 EPFDGLDVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLAD 210
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-198 |
9.46e-27 |
|
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: 107.23 E-value: 9.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 5 QISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQreshfSRVTRLSFEQLQKLVSDEWQ 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGS-----IRVFGKPLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 85 RNNTDLLSP--GEE--DTGRTTAEIIQDEVKDPARCARLA--EQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLI 158
Cdd:cd03235 76 RRSIDRDFPisVRDvvLMGLYGHKGLFRRLSKADKAKVDEalERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984360 159 LDEPFDGLDVNSRQQLAALLADLHSAGITLV-------LVLNRFDEI 198
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILvvthdlgLVLEYFDRV 202
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
262-475 |
9.71e-27 |
|
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: 107.17 E-value: 9.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 262 VLNDGVVSYND--RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRRGSgETIWDIKKHIG 339
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP-TSGEVLVDGKDLTK-LSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 340 YV----SSSLhldyrVSTNVRNVILSGyFDSIGIYQavsDKQHKLVQQWLDILGIDKRtADAPFHSLSWGQ-QRLALIVr 414
Cdd:cd03225 79 LVfqnpDDQF-----FGPTVEEEVAFG-LENLGLPE---EEIEERVEEALELVGLEGL-RDRSPFTLSGGQkQRVAIAG- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984360 415 ALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSHHAEDAPDCITHRLAF 475
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKT-IIIVTHDLDLLLELADRVIVL 207
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
269-465 |
9.98e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.55 E-value: 9.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgysndltLFGRRRGSGetiwdiKKHIGYVSSSLHLD 348
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRP-------TSGTVRRAG------GARVAYVPQRSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 349 YRVSTNVRNVILSGYFDSIGIYQAVSDKQHKLVQQWLDILGIDkRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEP 428
Cdd:NF040873 68 DSLPLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984360 429 LQGLDPLNRQLVRRFVDVLIGEGATqLLFVSHHAEDA 465
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGAT-VVVVTHDLELV 182
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
263-475 |
1.69e-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: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 263 LNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRRGSGEtIWDIKKHIGYVS 342
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP-TSGEILIDGKDIAKLP-LEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 343 SslhldyrvstnvrnviLSGyfdsigiyqavsdkqhklvqqwldilgidkrtadapfhslswGQQRLALIVRALVKHPTL 422
Cdd:cd00267 80 Q----------------LSG------------------------------------------GQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984360 423 LILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSHHAEDAPDCITHRLAF 475
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRT-VIIVTHDPELAELAADRVIVL 153
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
268-463 |
2.71e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.05 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 268 VSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRRRgSGETIWDIKKHIGYVSSSLH 346
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADlDPPT--SGEIYLDGKPL-SAMPPPEWRRQVAYVPQEPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 347 L-DYRVSTNvrnvilsgyFDSIGIYQAVSDKQHKLvQQWLDILGIDKRTADAPFHSLSWGQ-QRLALIvRALVKHPTLLI 424
Cdd:COG4619 85 LwGGTVRDN---------LPFPFQLRERKFDRERA-LELLERLGLPPDILDKPVERLSGGErQRLALI-RALLLQPDVLL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984360 425 LDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAE 463
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPE 192
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-190 |
3.44e-26 |
|
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: 106.48 E-value: 3.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKL--VSD 81
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIgvLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 82 E---WQRNntdllspgeedTGRttaEIIQ--------DEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQAL 150
Cdd:COG4555 82 ErglYDRL-----------TVR---ENIRyfaelyglFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARAL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488984360 151 MTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVL 190
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLF 187
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-210 |
1.11e-25 |
|
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: 102.71 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 5 QISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLVSDEWQ 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 85 rnntdllspgeedtgrttaeiiqdevkdparcarlaeqfgisalldrrfkyLSTGETRKTLLCQALMTDPQLLILDEPFD 164
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984360 165 GLDVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLAD 210
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
10-190 |
4.00e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 100.52 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 10 TFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKL--VSDEwqrnn 87
Cdd:COG1131 7 TKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIgyVPQE----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 88 tdlLSPGEEDTGRTTAEIIQ-----DEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEP 162
Cdd:COG1131 82 ---PALYPDLTVRENLRFFArlyglPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180
....*....|....*....|....*...
gi 488984360 163 FDGLDVNSRQQLAALLADLHSAGITLVL 190
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLL 186
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
225-468 |
5.01e-24 |
|
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: 105.23 E-value: 5.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 225 QALVAQLAHSEKLDGITLPEPDVP-PARHALADSAPRIVLNDGVVSY--NDRPVINHLSWTVNPGEHWQIVGPNGAGKST 301
Cdd:COG4987 297 QHLGRVRAAARRLNELLDAPPAVTePAEPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKST 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 302 LLSLVTGDHP--QGysnDLTLFGR--RRGSGETIWdikKHIGYVSSSLHLdyrVSTNVRNVILSGYfdsigiyQAVSDKQ 377
Cdd:COG4987 377 LLALLLRFLDpqSG---SITLGGVdlRDLDEDDLR---RRIAVVPQRPHL---FDTTLRENLRLAR-------PDATDEE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 378 hklVQQWLDILGIDKRTADAPF----------HSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLN-RQLVRRFVD 445
Cdd:COG4987 441 ---LWAALERVGLGDWLAALPDgldtwlgeggRRLSGGErRRLAL-ARALLRDAPILLLDEPTEGLDAATeQALLADLLE 516
|
250 260
....*....|....*....|...
gi 488984360 446 VLigEGATqLLFVSHHAEDAPDC 468
Cdd:COG4987 517 AL--AGRT-VLLITHRLAGLERM 536
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
24-190 |
6.56e-24 |
|
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: 99.09 E-value: 6.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQreshfsrVTRlsFEQLQKLVSDEWQRnntDLLSPGEED---TGR 100
Cdd:COG4133 23 FTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGE-------VLW--NGEPIRDAREDYRR---RLAYLGHADglkPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 101 TTAEIIQ------DEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQL 174
Cdd:COG4133 91 TVRENLRfwaalyGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
|
170
....*....|....*.
gi 488984360 175 AALLADLHSAGITLVL 190
Cdd:COG4133 171 AELIAAHLARGGAVLL 186
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
269-460 |
4.21e-23 |
|
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: 96.90 E-value: 4.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRRRGSGETIWdikKHIGyvssSLhL 347
Cdd:cd03268 9 TYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGlIKPD--SGEITFDGKSYQKNIEAL---RRIG----AL-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 348 DYRvstnvrnvILSGY---FDSIGIYQAVSDKQHKLVQQWLDILGIdKRTADAPFHSLSWG-QQRLAlIVRALVKHPTLL 423
Cdd:cd03268 79 EAP--------GFYPNltaRENLRLLARLLGIRKKRIDEVLDVVGL-KDSAKKKVKGFSLGmKQRLG-IALALLGNPDLL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984360 424 ILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSH 460
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQGIT-VLISSH 184
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
268-445 |
4.28e-23 |
|
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: 95.97 E-value: 4.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 268 VSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqGYSNDLTLFGRrrgsgeTIWDIK-----KHIGYVS 342
Cdd:cd03214 7 VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK-PSSGEILLDGK------DLASLSpkelaRKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 343 sslhldyrvstnvrnvilsgyfdsigiyqavsdkqhklvqQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPTL 422
Cdd:cd03214 80 ----------------------------------------QALELLGLAH-LADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180
....*....|....*....|....*..
gi 488984360 423 LILDEPLQGLDPLNR----QLVRRFVD 445
Cdd:cd03214 119 LLLDEPTSHLDIAHQiellELLRRLAR 145
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
261-479 |
4.61e-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: 97.06 E-value: 4.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGR--RRGSGEtiwdIKKH 337
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTlLKPT--SGRATVAGHdvVREPRE----VRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 338 IGYVSSSLHLDyRVSTNVRNVILSGyfdsiGIYQAVSDKQHKLVQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALV 417
Cdd:cd03265 75 IGIVFQDLSVD-DELTGWENLYIHA-----RLYGVPGAERRERIDELLDFVGLLE-AADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984360 418 KHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDApDCITHRLAFVPSG 479
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEA-EQLCDRVAIIDHG 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-192 |
4.72e-23 |
|
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: 98.19 E-value: 4.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ-----REshfsrVTRLSFEQLQKL 78
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvlldgRD-----LASLSRRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 79 VSdewqrnntdLLSPGEEDTGRTT-AEII------------QDEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTL 145
Cdd:COG1120 77 IA---------YVPQEPPAPFGLTvRELValgryphlglfgRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488984360 146 LCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADL-HSAGITLVLVL 192
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVL 195
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
261-474 |
4.34e-22 |
|
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: 92.83 E-value: 4.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDR--PVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHpQGYSNDLTLFGrRRGSGETIWDIKKHI 338
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLY-DPTSGEILIDG-VDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 339 GYVSSSLHLdyrVSTNVRNVILSGyfdsigiyqavsdkqhklvqqwldilgidkrtadapfhslswGQ-QRLAlIVRALV 417
Cdd:cd03228 79 AYVPQDPFL---FSGTIRENILSG------------------------------------------GQrQRIA-IARALL 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 418 KHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGeGATQLLfvshhaedapdcITHRLA 474
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALAK-GKTVIV------------IAHRLS 156
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
24-210 |
5.82e-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: 94.32 E-value: 5.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ-----REshfsrVTRLSFEQLQKLV------SDEwQrnntdLLS 92
Cdd:COG1122 22 LSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEvlvdgKD-----ITKKNLRELRRKVglvfqnPDD-Q-----LFA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 93 PG-EED-------TGRTTAEIIQdevkdpaRCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFD 164
Cdd:COG1122 91 PTvEEDvafgpenLGLPREEIRE-------RVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984360 165 GLDVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLAD 210
Cdd:COG1122 164 GLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
269-479 |
1.07e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 95.26 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETIWDIKKH----IGYVSS 343
Cdd:PRK13537 16 RYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGlTHPDA--------GSISLCGEPVPSRARHarqrVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 344 --SLHLDYRVSTNVRnvILSGYFdsiGIYQAVSdkqHKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPT 421
Cdd:PRK13537 88 fdNLDPDFTVRENLL--VFGRYF---GLSAAAA---RALVPPLLEFAKLENK-ADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984360 422 LLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLfVSHHAEDApDCITHRLAFVPSG 479
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILL-TTHFMEEA-ERLCDRLCVIEEG 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-459 |
1.64e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.43 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 19 LKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQK----LVSDEwqrnntDLLSPG 94
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlgiyLVPQE------PLLFPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 95 EedtgrTTAEII----QDEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNS 170
Cdd:PRK15439 101 L-----SVKENIlfglPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 171 RQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEkssllqqalVAQLAHSEKLDGITlpepdvPPA 250
Cdd:PRK15439 176 TERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK---------TADLSTDDIIQAIT------PAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 251 RHALADSAPRIVL---NDGVVSYNDRPVIN----------HLSWTVNPGEHWQIVGPNGAGKSTLLSlvtgdhpqgysnd 317
Cdd:PRK15439 241 REKSLSASQKLWLelpGNRRQQAAGAPVLTvedltgegfrNISLEVRAGEILGLAGVVGAGRTELAE------------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 318 lTLFGRRRGSGETIW----DIKK-------HIGYV-------SSSLHLDYRVSTNVRNVIlsgyFDSIGIYQAVSdKQHK 379
Cdd:PRK15439 308 -TLYGLRPARGGRIMlngkEINAlstaqrlARGLVylpedrqSSGLYLDAPLAWNVCALT----HNRRGFWIKPA-RENA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 380 LVQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR----QLVRRfvdvlIGEGATQL 455
Cdd:PRK15439 382 VLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARndiyQLIRS-----IAAQNVAV 456
|
....
gi 488984360 456 LFVS 459
Cdd:PRK15439 457 LFIS 460
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
265-463 |
1.69e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.41 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 265 DGVV-SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG--DHPQGYsndLTLFGRRRGSgetiwDIKKHIGYV 341
Cdd:COG4152 5 KGLTkRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGilAPDSGE---VLWDGEPLDP-----EDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 342 --SSSLhldYRvSTNVRNVILsgYFDSI-GIYQAVSDKQhklVQQWLDILGIDKRtADAPFHSLSWG-QQRLALIVrALV 417
Cdd:COG4152 77 peERGL---YP-KMKVGEQLV--YLARLkGLSKAEAKRR---ADEWLERLGLGDR-ANKKVEELSKGnQQKVQLIA-ALL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984360 418 KHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSH---HAE 463
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTT-VIFSSHqmeLVE 193
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
261-447 |
2.22e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 92.42 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSY-NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQgySNDLTLFGR--RRGSGETIWDIKK 336
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEeRPT--SGQVLVNGQdlSRLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 337 HIGYVssslHLDYRVSTNvRNVilsgyFDSIGIYQAVSDKQHK----LVQQWLDILGIDKRtADAPFHSLSWG-QQRLAl 411
Cdd:COG2884 80 RIGVV----FQDFRLLPD-RTV-----YENVALPLRVTGKSRKeirrRVREVLDLVGLSDK-AKALPHELSGGeQQRVA- 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 488984360 412 IVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVL 447
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDP---ETSWEIMELL 180
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
258-460 |
3.66e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.03 E-value: 3.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 258 APRIVLNDGVVSY----NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQG-------------YSNDLT 319
Cdd:COG1136 2 SPLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGlDRPTSgevlidgqdisslSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 320 LFgRRRgsgetiwdikkHIGYVSSSLHLdyrVST-NVR-NVILSGYFDSIGIYQAvsdkqHKLVQQWLDILGIDKRtADA 397
Cdd:COG1136 82 RL-RRR-----------HIGFVFQFFNL---LPElTALeNVALPLLLAGVSRKER-----RERARELLERVGLGDR-LDH 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984360 398 PFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNR----QLVRRFVDvliGEGATqLLFVSH 460
Cdd:COG1136 141 RPSQLSGGQqQRVA-IARALVNRPKLILADEPTGNLDSKTGeevlELLRELNR---ELGTT-IVMVTH 203
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
269-465 |
5.21e-21 |
|
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: 91.19 E-value: 5.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgysndLTLfgrrRGSGETIWD-------IKKHIGYV 341
Cdd:cd03269 9 RFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG---------IIL----PDSGEVLFDgkpldiaARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 342 SSS--LHLDYRVSTNVRnvilsgYFDSI---GIYQAVSDkqhklVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRAL 416
Cdd:cd03269 76 PEErgLYPKMKVIDQLV------YLAQLkglKKEEARRR-----IDEWLERLELSEY-ANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984360 417 VKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSHHAEDA 465
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKT-VILSTHQMELV 191
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
240-480 |
5.61e-21 |
|
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: 95.98 E-value: 5.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 240 ITLPEPDVPPARHAL-ADSAPRIVLNDGVVSY-NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSND 317
Cdd:COG4988 315 LDAPEPAAPAGTAPLpAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP-YSGS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 318 LTLFGRRRgSGETIWDIKKHIGYVSSSLHLdyrVSTNVRNVILSGYFDsigiyqaVSDKQhklVQQWLDILGIDKRTADA 397
Cdd:COG4988 394 ILINGVDL-SDLDPASWRRQIAWVPQNPYL---FAGTIRENLRLGRPD-------ASDEE---LEAALEAAGLDEFVAAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 398 PF----------HSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLiGEGATQLLfvshhaedap 466
Cdd:COG4988 460 PDgldtplgeggRGLSGGQaQRLAL-ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVIL---------- 527
|
250
....*....|....
gi 488984360 467 dcITHRLAFVPSGD 480
Cdd:COG4988 528 --ITHRLALLAQAD 539
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-192 |
5.78e-21 |
|
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: 90.19 E-value: 5.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 5 QISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLVSDEWQ 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 85 rnntdllspgeedtgrttaeiiqdevkdparcarLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFD 164
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180
....*....|....*....|....*....
gi 488984360 165 GLDVNSRQQLAALLADL-HSAGITLVLVL 192
Cdd:cd03214 127 HLDIAHQIELLELLRRLaRERGKTVVMVL 155
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
274-460 |
6.19e-21 |
|
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: 91.01 E-value: 6.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 274 PVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRR-RGSGETIWD--IKKHIGYVSSSLHL-D 348
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGlDRPT--SGEVRVDGTDiSKLSEKELAafRRRHIGFVFQSFNLlP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 349 YRvsTNVRNVILSGYFDSIGiyqavSDKQHKLVQQWLDILGIDKRtADAPFHSLSWG-QQRLAlIVRALVKHPTLLILDE 427
Cdd:cd03255 96 DL--TALENVELPLLLAGVP-----KKERRERAEELLERVGLGDR-LNHYPSELSGGqQQRVA-IARALANDPKIILADE 166
|
170 180 190
....*....|....*....|....*....|....
gi 488984360 428 PLQGLDPLNRQLVRR-FVDVLIGEGATqLLFVSH 460
Cdd:cd03255 167 PTGNLDSETGKEVMElLRELNKEAGTT-IVVVTH 199
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
269-479 |
2.06e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.20 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYSNdLTLFG-----RRRGSgetiwdiKKHIGYVSS 343
Cdd:PRK13536 50 SYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGK-ITVLGvpvpaRARLA-------RARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 344 --SLHLDYRVSTNVrnVILSGYFdsigiyQAVSDKQHKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPT 421
Cdd:PRK13536 122 fdNLDLEFTVRENL--LVFGRYF------GMSTREIEAVIPSLLEFARLESK-ADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984360 422 LLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLfVSHHAEDApDCITHRLAFVPSG 479
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILL-TTHFMEEA-ERLCDRLCVLEAG 248
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
114-461 |
2.40e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 94.42 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 114 ARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADL--HSAGITlVLV 191
Cdd:NF033858 115 RRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIraERPGMS-VLV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 192 LNRFDEipEFVQF-------AG-VLADCT----LSETGEKSslLQQALVAQLAHSEKLDgitlPEPDVPPARHALADSAP 259
Cdd:NF033858 194 ATAYME--EAERFdwlvamdAGrVLATGTpaelLARTGADT--LEAAFIALLPEEKRRG----HQPVVIPPRPADDDDEP 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 260 RIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRGSGETiwDIKKHIG 339
Cdd:NF033858 266 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAS-EGEAWLFGQPVDAGDI--ATRRRVG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 340 YVSSSLHLdYRVSTnVR-NVILSGYfdsigIYQAVSDKQHKLVQQWLDILGIdKRTADAPFHSLSWGQ-QRLALIVrALV 417
Cdd:NF033858 343 YMSQAFSL-YGELT-VRqNLELHAR-----LFHLPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIrQRLSLAV-AVI 413
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 488984360 418 KHPTLLILDEPLQGLDPLNRQlvrRFVDVLIG----EGATqlLFVSHH 461
Cdd:NF033858 414 HKPELLILDEPTSGVDPVARD---MFWRLLIElsreDGVT--IFISTH 456
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
258-465 |
3.21e-20 |
|
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: 93.43 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 258 APRIVLNDGVVSY--NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGysndLTLFGRRRGSGETIWDIK 335
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHG----GRISGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 336 -----KHIGYV----SSSLhldyrVSTNVRNVILsgyfDSIGIYQAVSDKQHKLVQQWLDILGIDKRtADAPFHSLSWGQ 406
Cdd:COG1123 78 ealrgRRIGMVfqdpMTQL-----NPVTVGDQIA----EALENLGLSRAEARARVLELLEAVGLERR-LDRYPHQLSGGQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 407 QRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDA 465
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVV 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-433 |
3.22e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.16 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLP------LLSGQReshfsrVTRLSFEQLQKL-VSDEWQRNNtdlLSP--- 93
Cdd:COG1129 25 LELRPGEVHALLGENGAGKSTLMKILSGVYQpdsgeiLLDGEP------VRFRSPRDAQAAgIAIIHQELN---LVPnls 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 94 -------GEEDTGRTT---AEIIqdevkdpARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPF 163
Cdd:COG1129 96 vaeniflGREPRRGGLidwRAMR-------RRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 164 DGLDVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLLQQALVAQLAhSEKLDGITlP 243
Cdd:COG1129 169 ASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMV-GRELEDLF-P 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 244 EPDVPPARHALAdsaprivlndgVVSYNDRPVINHLSWTVNPGEhwqIV---GPNGAGKSTLLSLVTGDHPQgYSNDLTL 320
Cdd:COG1129 247 KRAAAPGEVVLE-----------VEGLSVGGVVRDVSFSVRAGE---ILgiaGLVGAGRTELARALFGADPA-DSGEIRL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 321 FGRRRGSGeTIWD-IKKHIGYVS-----SSLHLDYRVSTNVrnvilsgyfdSIGIYQAVSD-------KQHKLVQQWLDI 387
Cdd:COG1129 312 DGKPVRIR-SPRDaIRAGIAYVPedrkgEGLVLDLSIRENI----------TLASLDRLSRgglldrrRERALAEEYIKR 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 488984360 388 LGIDKRTADAPFHSLSWG-QQRlALIVRALVKHPTLLILDEPLQGLD 433
Cdd:COG1129 381 LRIKTPSPEQPVGNLSGGnQQK-VVLAKWLATDPKVLILDEPTRGID 426
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
255-460 |
3.48e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 89.76 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 255 ADSAPRIVLNDGVVSY----NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGE 329
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGlEKPTS--------GEVLVDGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 330 TIWDIKKHIGYV--SSSLhLDYRvsTNVRNVILSgyFDSIGIYQAvsdKQHKLVQQWLDILGIDKRtADA-PfHSLSWG- 405
Cdd:COG1116 74 PVTGPGPDRGVVfqEPAL-LPWL--TVLDNVALG--LELRGVPKA---ERRERARELLELVGLAGF-EDAyP-HQLSGGm 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488984360 406 QQRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFV-DVLIGEGATqLLFVSH 460
Cdd:COG1116 144 RQRVA-IARALANDPEVLLMDEPFGALDALTRERLQDELlRLWQETGKT-VLFVTH 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-191 |
4.93e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.67 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRvtRLSFEQLQKLVSDEWQRNNTDLLSPG----EEDTG 99
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA--RVAYVPQRSEVPDSLPLTVRDLVAMGrwarRGLWR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 100 RTTAEiiqdevkDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLA 179
Cdd:NF040873 91 RLTRD-------DRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLA 163
|
170
....*....|..
gi 488984360 180 DLHSAGITLVLV 191
Cdd:NF040873 164 EEHARGATVVVV 175
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-433 |
1.45e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.38 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 19 LKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ---RESHFSRVT-RLSFEQ-----LQKL-VSDEW--QRN 86
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTitiNNINYNKLDhKLAAQLgigiiYQELsVIDELtvLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 87 ntdlLSPGEEDTGRTTAEIIQDEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGL 166
Cdd:PRK09700 101 ----LYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 167 DVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLLQQALVAQLAHSEKldgitlpEPD 246
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGREL-------QNR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 247 VPPARHALADSAPRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRG 326
Cdd:PRK09700 250 FNAMKENVSNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRA-GGEIRLNGKDIS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 327 SGETIWDIKKHIGYVSSS-----LHLDYRVSTNV---RNVILSGYFDSIGIYQavSDKQHKLVQQWLDILGIDKRTADAP 398
Cdd:PRK09700 329 PRSPLDAVKKGMAYITESrrdngFFPNFSIAQNMaisRSLKDGGYKGAMGLFH--EVDEQRTAENQRELLALKCHSVNQN 406
|
410 420 430
....*....|....*....|....*....|....*
gi 488984360 399 FHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:PRK09700 407 ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGID 441
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
223-476 |
1.88e-19 |
|
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: 91.43 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 223 LQQALVAqlahSEKLDGITLPEPDVPPARHA--LADSAPRIVLNDgvVSY----NDRPVINHLSWTVNPGEHWQIVGPNG 296
Cdd:COG2274 438 FQDAKIA----LERLDDILDLPPEREEGRSKlsLPRLKGDIELEN--VSFrypgDSPPVLDNISLTIKPGERVAIVGRSG 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 297 AGKSTLLSLVTG-DHPQ-------GYsnDLTLFGRRrgsgetiwDIKKHIGYVSSSLHLdyrVSTNVRNVILSGYFDsig 368
Cdd:COG2274 512 SGKSTLLKLLLGlYEPTsgrilidGI--DLRQIDPA--------SLRRQIGVVLQDVFL---FSGTIRENITLGDPD--- 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 369 iyqaVSDKQhklVQQWLDILGIDKRTADAP--FH--------SLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNR 437
Cdd:COG2274 576 ----ATDEE---IIEAARLAGLHDFIEALPmgYDtvvgeggsNLSGGQrQRLA-IARALLRNPRILILDEATSALDAETE 647
|
250 260 270
....*....|....*....|....*....|....*....
gi 488984360 438 QLVRRFVDVLIGeGATQLLfvshhaedapdcITHRLAFV 476
Cdd:COG2274 648 AIILENLRRLLK-GRTVII------------IAHRLSTI 673
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
263-460 |
3.25e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 263 LNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgysndltlfgrrrgSGETIWDIKKHIGYV 341
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGeLEPD--------------SGEVSIPKGLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 342 SSSLHLDyrVSTNVRNVILSGY---------------------------------FDSIGIYQAVSDkqhklVQQWLDIL 388
Cdd:COG0488 67 PQEPPLD--DDLTVLDTVLDGDaelraleaeleeleaklaepdedlerlaelqeeFEALGGWEAEAR-----AEEILSGL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 389 GIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEP-----LQGLDPLNRQLVRRfvdvligEGAtqLLFVSH 460
Cdd:COG0488 140 GFPEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPtnhldLESIEWLEEFLKNY-------PGT--VLVVSH 207
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
261-461 |
3.84e-19 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 86.65 E-value: 3.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSY-NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqGYSNDLTLFGRR--RGSGETIWDIKKH 337
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVE-PTSGEILVDGQDvtALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 338 IGYVSSSLHLDYRVS--TNVrnviLSGYFDSIGIYQAV----SDKQHKLVQQWLDILGIDKRtADAPFHSLSWGQ-QRLA 410
Cdd:COG3638 82 IGMIFQQFNLVPRLSvlTNV----LAGRLGRTSTWRSLlglfPPEDRERALEALERVGLADK-AYQRADQLSGGQqQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984360 411 lIVRALVKHPTLLILDEPLQGLDPLN-RQLVRRFVDVLIGEGATqLLFVSHH 461
Cdd:COG3638 157 -IARALVQEPKLILADEPVASLDPKTaRQVMDLLRRIAREDGIT-VVVNLHQ 206
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
257-465 |
5.77e-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: 88.23 E-value: 5.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 257 SAPRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRrrgsgetiwDI- 334
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfETPD--SGRILLDGR---------DVt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 335 -----KKHIGYVSSSL----HLdyrvstNVR-NVilsGYfdsiGI-YQAVS-DKQHKLVQQWLDILGIDKRtADAPFHSL 402
Cdd:COG3842 71 glppeKRNVGMVFQDYalfpHL------TVAeNV---AF----GLrMRGVPkAEIRARVAELLELVGLEGL-ADRYPHQL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984360 403 SWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGE-GATqLLFVSHHAEDA 465
Cdd:COG3842 137 SGGQqQRVAL-ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElGIT-FIYVTHDQEEA 199
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
261-460 |
6.66e-19 |
|
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: 86.01 E-value: 6.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSY----NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRRGSGETIWdIKK 336
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP-WSGEVTFDGRPVTRRRRKA-FRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 337 HIGYVS----SSLHLDYRVSTnvrnvILSGYFDSIGIYQAVSDkqhklVQQWLDILGIDKRTADAPFHSLSWGQ-QRLAl 411
Cdd:COG1124 80 RVQMVFqdpyASLHPRHTVDR-----ILAEPLRIHGLPDREER-----IAELLEQVGLPPSFLDRYPHQLSGGQrQRVA- 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984360 412 IVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSH 460
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSH 197
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
261-465 |
6.71e-19 |
|
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: 85.81 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSY-NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLL----SLVTGDhpqgySNDLTLFGR--RRGSGETIWD 333
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLrcinRLVEPS-----SGSILLEGTdiTKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 334 IKKHIGYVSSSLHLDYRvSTNVRNViLSGYFDSI----GIYQAVSDKQHKLVQQWLDILGIDKRtADAPFHSLSWGQQRL 409
Cdd:TIGR02315 77 LRRRIGMIFQHYNLIER-LTVLENV-LHGRLGYKptwrSLLGRFSEEDKERALSALERVGLADK-AYQRADQLSGGQQQR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 410 ALIVRALVKHPTLLILDEPLQGLDPLN-RQLVRRFVDVLIGEGATQLLFVsHHAEDA 465
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTsKQVMDYLKRINKEDGITVIINL-HQVDLA 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
261-465 |
9.95e-19 |
|
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: 84.49 E-value: 9.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGYSndlTLFGRRRGSGETIWdiKKHIG 339
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlERPDSGE---ILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 340 YV--SSSL--HLdyRVSTNVRnvilsgyfdsIGIYQAVSDKQH--KLVQQWLDILGIDkRTADAPFHSLSWGQQRLALIV 413
Cdd:cd03259 76 MVfqDYALfpHL--TVAENIA----------FGLKLRGVPKAEirARVRELLELVGLE-GLLNRYPHELSGGQQQRVALA 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984360 414 RALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDA 465
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEA 194
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
237-468 |
1.23e-18 |
|
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: 88.50 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 237 LDGITLPEPDVPPArhaLADSAPRIVLNDGVVSYNDR-PVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYs 315
Cdd:TIGR02857 301 LDAAPRPLAGKAPV---TAAPASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTE- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 316 ndltlfGRRRGSGETIWDIK-----KHIGYVSSSLHLdyrVSTNVRnvilsgyfDSIGIYQAVSDKQhkLVQQWLDILGI 390
Cdd:TIGR02857 377 ------GSIAVNGVPLADADadswrDQIAWVPQHPFL---FAGTIA--------ENIRLARPDASDA--EIREALERAGL 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 391 DKRTADAPF----------HSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIgEGATqLLFVS 459
Cdd:TIGR02857 438 DEFVAALPQgldtpigeggAGLSGGQaQRLAL-ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRT-VLLVT 514
|
....*....
gi 488984360 460 HHAEDAPDC 468
Cdd:TIGR02857 515 HRLALAALA 523
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-190 |
1.25e-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: 83.22 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSDTKTLK-IDhLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGqreshfsRVTRLSFEqlqklvsde 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDdIS-LTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSG-------EIKVLGKD--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 83 wqrnntdllspgeedtgrttaeIIQDEVKDPARCARLAEQFG-ISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDE 161
Cdd:cd03230 64 ----------------------IKKEPEEVKRRIGYLPEEPSlYENLTVRENLKLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180
....*....|....*....|....*....
gi 488984360 162 PFDGLDVNSRQQLAALLADLHSAGITLVL 190
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKEGKTILL 150
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-163 |
1.25e-18 |
|
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: 82.70 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 19 LKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLVSDEWQRNNTDLLSPGEEDT 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 99 GRTTAEIIQDEVKDPARCARLAEQFGISALLDRRFKY----LSTGETRKTLLCQALMTDPQLLILDEPF 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
10-210 |
1.90e-18 |
|
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: 83.96 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 10 TFRLSDTKTLKIDHLS--VAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLvsdewqrnn 87
Cdd:cd03266 10 RFRDVKKTVQAVDGVSftVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 88 tDLLSPGEEDTGRTTA-EIIQ----------DEVKdpARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQL 156
Cdd:cd03266 81 -GFVSDSTGLYDRLTArENLEyfaglyglkgDELT--ARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488984360 157 LILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLAD 210
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHR 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
274-460 |
3.33e-18 |
|
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: 83.29 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 274 PVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETIWDIKKHIGYV--SSSLhLDYR 350
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGlERPTS--------GEVLVDGEPVTGPGPDRGYVfqQDAL-LPWL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 351 vsTNVRNVILsgyfdsiGI-YQAVSDKQ-HKLVQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEP 428
Cdd:cd03293 89 --TVLDNVAL-------GLeLQGVPKAEaRERAEELLELVGLSG-FENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190
....*....|....*....|....*....|...
gi 488984360 429 LQGLDPLNRQLVRR-FVDVLIGEGATqLLFVSH 460
Cdd:cd03293 159 FSALDALTREQLQEeLLDIWRETGKT-VLLVTH 190
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
274-464 |
4.04e-18 |
|
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: 83.25 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 274 PVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVtgdhpqgYSNDLTLFGR---RRGSGE---------TIWDIKKH-IGY 340
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCI-------YGNYLPDSGSilvRHDGGWvdlaqasprEILALRRRtIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 341 VSSSLHLDYRVSTnvRNVILSGYFDsigiyQAVSDKQ-HKLVQQWLDILGIDKRTADAPFHSLSWG-QQRLAlIVRALVK 418
Cdd:COG4778 98 VSQFLRVIPRVSA--LDVVAEPLLE-----RGVDREEaRARARELLARLNLPERLWDLPPATFSGGeQQRVN-IARGFIA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984360 419 HPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSHHAED 464
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIEEAKARGTA-IIGIFHDEEV 214
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
270-479 |
4.41e-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: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 270 YNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGetiWDI-------KKHIGYV 341
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTlLRPTS--------GTARVAG---YDVvreprkvRRSIGIV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 342 SSSLHLDyRVSTNVRNVILSGyfdsiGIYQAVSDKQHKLVQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRALVKHPT 421
Cdd:TIGR01188 72 PQYASVD-EDLTGRENLEMMG-----RLYGLPKDEAEERAEELLELFEL-GEAADRPVGTYSGGMRRRLDIAASLIHQPD 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984360 422 LLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLfVSHHAEDApDCITHRLAFVPSG 479
Cdd:TIGR01188 145 VLFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILL-TTHYMEEA-DKLCDRIAIIDHG 200
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
201-474 |
7.70e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 86.37 E-value: 7.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 201 FVQFAGVLADcTLSETGEKSSLLQQALVAqlahSEKLDGI--TLPEPDVPPARHALADSAPRIVLNDgvVSY---NDRPV 275
Cdd:COG1132 283 FILYLLRLFG-PLRQLANVLNQLQRALAS----AERIFELldEPPEIPDPPGAVPLPPVRGEIEFEN--VSFsypGDRPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 276 INHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG--DHPQGysnDLTLFGRrrgsgetiwDIK--------KHIGYVSSSL 345
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfyDPTSG---RILIDGV---------DIRdltleslrRQIGVVPQDT 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 346 HLdyrVSTNVRNVILSGYFDsigiyqaVSDKQhklVQQWLDILGIDKRTADAPF----------HSLSWGQ-QRLAlIVR 414
Cdd:COG1132 424 FL---FSGTIRENIRYGRPD-------ATDEE---VEEAAKAAQAHEFIEALPDgydtvvgergVNLSGGQrQRIA-IAR 489
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 415 ALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIgEGATqlLFVshhaedapdcITHRLA 474
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLM-KGRT--TIV----------IAHRLS 536
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
261-461 |
1.32e-17 |
|
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: 81.47 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGeHWQIVGPNGAGKSTLLSLVTGDHPQGYSNdLTLFGRRRGSGETiwDIKKHIGY 340
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGT-IRIDGQDVLKQPQ--KLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 341 vsssLHLDYRVSTNVRnviLSGYFDSIGIYQAVSDKQ-HKLVQQWLDILGIDKRtADAPFHSLSWGQ-QRLAlIVRALVK 418
Cdd:cd03264 77 ----LPQEFGVYPNFT---VREFLDYIAWLKGIPSKEvKARVDEVLELVNLGDR-AKKKIGSLSGGMrRRVG-IAQALVG 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984360 419 HPTLLILDEPLQGLDPLNRQlvrRFVDVLIGEGATQLLFVSHH 461
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERI---RFRNLLSELGEDRIVILSTH 187
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
275-461 |
1.53e-17 |
|
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: 82.01 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 275 VINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHP--QGysnDLTLFGR-----------RRG-----------SGET 330
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRptSG---RILFDGRditglpphriaRLGiartfqnprlfPELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 331 IWD-------IKKHIGYVSSSLHLDYRVSTnvrnvilsgyfdsigiYQAVSDKqhklVQQWLDILGIDKRtADAPFHSLS 403
Cdd:COG0411 96 VLEnvlvaahARLGRGLLAALLRLPRARRE----------------EREARER----AEELLERVGLADR-ADEPAGNLS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984360 404 WGQQRLALIVRALVKHPTLLILDEPLQGldpLNRQLVRRFVDVLI----GEGATqLLFVSHH 461
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAG---LNPEETEELAELIRrlrdERGIT-ILLIEHD 212
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
273-460 |
1.63e-17 |
|
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: 81.40 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 273 RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQG-----YSNDLTLFGRRRGSgetiwDIKKHIGYV----S 342
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGlLKPTSgsiifDGKDLLKLSRRLRK-----IRRKEIQMVfqdpM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 343 SSLHLDYRVSTNVRNVILsgyfdsigIYQAVSDKQHKLVQQWLDI--LGIDKRTADAPFHSLSWGQQRLALIVRALVKHP 420
Cdd:cd03257 93 SSLNPRMTIGEQIAEPLR--------IHGKLSKKEARKEAVLLLLvgVGLPEEVLNRYPHELSGGQRQRVAIARALALNP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488984360 421 TLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSH 460
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITH 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
21-201 |
1.73e-17 |
|
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: 80.79 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 21 IDHLS--VAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLvsdewqrnntdllsPgeEDT 98
Cdd:cd03269 16 LDDISfsVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYL--------------P--EER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 99 GRTTAEIIQDEVKDPARCA------------RLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGL 166
Cdd:cd03269 80 GLYPKMKVIDQLVYLAQLKglkkeearrridEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190
....*....|....*....|....*....|....*
gi 488984360 167 DVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEF 201
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQMELVEEL 194
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
268-456 |
1.83e-17 |
|
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: 81.46 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 268 VSY-NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLS----LVTGDHPQGYSNDLtlfGRRRGSGETIWDIKKHIGYVS 342
Cdd:cd03256 8 KTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRclngLVEPTSGSVLIDGT---DINKLKGKALRQLRRQIGMIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 343 SSLHLDYRVS--TNVrnviLSGYFDSIGIYQA------VSDKQHKLvqQWLDILGIDKRtADAPFHSLSWGQQRLALIVR 414
Cdd:cd03256 85 QQFNLIERLSvlENV----LSGRLGRRSTWRSlfglfpKEEKQRAL--AALERVGLLDK-AYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984360 415 ALVKHPTLLILDEPLQGLDPLN-RQLVRRFVDVLIGEGATQLL 456
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASsRQVMDLLKRINREEGITVIV 200
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
275-460 |
1.83e-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: 81.26 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 275 VINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgysndltLFGRRRGSGETI--------WDIKKHIGYVSSSLH 346
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAG-----------LLEPDAGFATVDgfdvvkepAEARRRLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 347 LDYRVStnVRNVIlsGYFDsiGIYQAVSDKQHKLVQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILD 426
Cdd:cd03266 89 LYDRLT--ARENL--EYFA--GLYGLKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190
....*....|....*....|....*....|....
gi 488984360 427 EPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSH 460
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKC-ILFSTH 194
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
263-467 |
2.13e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.60 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 263 LNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQG--YSNDLTLFGRRRGSGETiwdIKKHIGY 340
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsASGEVLLNGRRLTALPA---EQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 341 vsssL--------HLDyrVSTNVRnvilsgyfdsIGIYQAVSDKQ-HKLVQQWLDILGIDKRtADAPFHSLSWGQQ-RLA 410
Cdd:COG4136 81 ----LfqddllfpHLS--VGENLA----------FALPPTIGRAQrRARVEQALEEAGLAGF-ADRDPATLSGGQRaRVA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 411 LiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDAPD 467
Cdd:COG4136 144 L-LRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA 199
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
261-465 |
2.33e-17 |
|
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: 81.01 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFG--RRRGSGETIWDIKKH 337
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGlLRPD--SGEVLIDGedISGLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 338 IGYV--SSSLhldyrvstnvrnvilsgyFDSIGIYQAVSD--KQH---------KLVQQWLDILGI----DKRTADapfh 400
Cdd:cd03261 79 MGMLfqSGAL------------------FDSLTVFENVAFplREHtrlseeeirEIVLEKLEAVGLrgaeDLYPAE---- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 401 sLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR----QLVRRFVDVLigeGATQLLfVSHHAEDA 465
Cdd:cd03261 137 -LSGGMKKRVALARALALDPELLLYDEPTAGLDPIASgvidDLIRSLKKEL---GLTSIM-VTHDLDTA 200
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-191 |
2.40e-17 |
|
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: 80.98 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 10 TFRLSDTKTLKIDH--LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQ---LQKLVSDEWq 84
Cdd:cd03293 9 TYGGGGGAVTALEDisLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRgyvFQQDALLPW- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 85 RNNTDLLSPGEEDTGRTTAEIIqdevkdpARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFD 164
Cdd:cd03293 88 LTVLDNVALGLELQGVPKAEAR-------ERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180
....*....|....*....|....*...
gi 488984360 165 GLDVNSRQQLAALLADL-HSAGITLVLV 191
Cdd:cd03293 161 ALDALTREQLQEELLDIwRETGKTVLLV 188
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
261-490 |
2.69e-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: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVinHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgysndltlfgrrrgSGETIWDIKKHIG 339
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGfLPPD--------------SGRILWNGQDLTA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 340 YVS-----SSL--------HLDyrVSTNVrnvilsgyfdSIGIYQA--VSDKQHKLVQQWLDILGID---KRTADApfhs 401
Cdd:COG3840 66 LPPaerpvSMLfqennlfpHLT--VAQNI----------GLGLRPGlkLTAEQRAQVEQALERVGLAgllDRLPGQ---- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 402 LSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGE-GATqLLFVSHHAEDApDCITHRLAFVpsG 479
Cdd:COG3840 130 LSGGQrQRVAL-ARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLT-VLMVTHDPEDA-ARIADRVLLV--A 204
|
250
....*....|.
gi 488984360 480 DGYTYQLGPVA 490
Cdd:COG3840 205 DGRIAADGPTA 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
268-443 |
2.95e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.36 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 268 VSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqGYSNDLTLFGRRRGSGETiWDIKKHIGyV---SSS 344
Cdd:PRK13548 10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS-PDSGEVRLNGRPLADWSP-AELARRRA-VlpqHSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 345 LHLDYRvstnVRNVILSGyfdsIGIYQAVSDKQHKLVQQWLDILGIDKrTADAPFHSLSWG-QQRLALiVRALV------ 417
Cdd:PRK13548 87 LSFPFT----VEEVVAMG----RAPHGLSRAEDDALVAAALAQVDLAH-LAGRDYPQLSGGeQQRVQL-ARVLAqlwepd 156
|
170 180 190
....*....|....*....|....*....|
gi 488984360 418 KHPTLLILDEPLQGLDPLNRQ----LVRRF 443
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHhvlrLARQL 186
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
268-445 |
3.60e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 81.32 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 268 VSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqGYSNDLTLFGRRRGSgETIWDIKKHIGyV---SSS 344
Cdd:COG4559 9 VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELT-PSSGEVRLNGRPLAA-WSPWELARRRA-VlpqHSS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 345 LHLDYRVSTNVRnvilsgyfdsIGIYQAVSDKQH--KLVQQWLDILGIDkRTADAPFHSLSWG-QQR------LALIVRA 415
Cdd:COG4559 86 LAFPFTVEEVVA----------LGRAPHGSSAAQdrQIVREALALVGLA-HLAGRSYQTLSGGeQQRvqlarvLAQLWEP 154
|
170 180 190
....*....|....*....|....*....|....
gi 488984360 416 LVKHPTLLILDEPLQGLDPLNRQ----LVRRFVD 445
Cdd:COG4559 155 VDGGPRWLFLDEPTSALDLAHQHavlrLARQLAR 188
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
269-472 |
3.79e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 80.66 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEhwqIV---GPNGAGKSTLLSLVTG----DHPQGY--SNDLT---LFGR-RRGsgetiwdik 335
Cdd:cd03218 9 RYGKRKVVNGVSLSVKQGE---IVgllGPNGAGKTTTFYMIVGlvkpDSGKILldGQDITklpMHKRaRLG--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 336 khIGYV--SSSLHLDYRVSTNVRNVILSGYFDSigiyqavsDKQHKLVQQWLDILGIDKrTADAPFHSLSWGQQRLALIV 413
Cdd:cd03218 77 --IGYLpqEASIFRKLTVEENILAVLEIRGLSK--------KEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984360 414 RALVKHPTLLILDEPLQGLDPLN----RQLVRRFVDVLIGegatqLLFVSHHAEDAPDcITHR 472
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDPIAvqdiQKIIKILKDRGIG-----VLITDHNVRETLS-ITDR 202
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
271-465 |
4.60e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 81.21 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 271 NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRRRgSGETIWDIKKHIGYVSSSLHLDY 349
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGlLLPE--AGTITVGGMVL-SEETVWDVRRQVGMVFQNPDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 350 rVSTNVRNVILSGyFDSIGIYQavsDKQHKLVQQWLDILGIDKRTADAPfHSLSWGQ-QRLAlIVRALVKHPTLLILDEP 428
Cdd:PRK13635 95 -VGATVQDDVAFG-LENIGVPR---EEMVERVDQALRQVGMEDFLNREP-HRLSGGQkQRVA-IAGVLALQPDIIILDEA 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984360 429 LQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDA 465
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA 204
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-463 |
4.98e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 83.34 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSrvtrlsfeqlqklvsdew 83
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWS------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 84 qrnNTDLLSPGEEDTGRTTAEIIQDE---VKDPA-------------------------RCARLAEQFGISALLD-RRFK 134
Cdd:TIGR02633 64 ---GSPLKASNIRDTERAGIVIIHQEltlVPELSvaeniflgneitlpggrmaynamylRAKNLLRELQLDADNVtRPVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 135 YLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLS 214
Cdd:TIGR02633 141 DYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 215 ETGEKSSLLQQALVAQLAHSEkldgITLPEPDVPparHALADSAPRIvlnDGVVSYN----DRPVINHLSWTVNPGEHWQ 290
Cdd:TIGR02633 221 ATKDMSTMSEDDIITMMVGRE----ITSLYPHEP---HEIGDVILEA---RNLTCWDvinpHRKRVDDVSFSLRRGEILG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 291 IVGPNGAGKSTLLSLVTGDHPQGYSNDLTLFGR-----------RRGSGETIWDIKKHiGYVSsslhlDYRVSTNVRNVI 359
Cdd:TIGR02633 291 VAGLVGAGRTELVQALFGAYPGKFEGNVFINGKpvdirnpaqaiRAGIAMVPEDRKRH-GIVP-----ILGVGKNITLSV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 360 LSGYfdsIGIYQAVSDKQHKLVQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQL 439
Cdd:TIGR02633 365 LKSF---CFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYE 441
|
490 500
....*....|....*....|....
gi 488984360 440 VRRFVDVLIGEGATQLLFVSHHAE 463
Cdd:TIGR02633 442 IYKLINQLAQEGVAIIVVSSELAE 465
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
275-461 |
7.78e-17 |
|
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: 79.79 E-value: 7.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 275 VINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQGysndltlfGRRRGSGETIWDIKKH------IGyvssslhl 347
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLrPTS--------GSVLFDGEDITGLPPHeiarlgIG-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 348 dyRVSTNVR---------NVILSGYFDSIGIYQAVSDKQHKL-----VQQWLDILGIDKRtADAPFHSLSWGQQRLALIV 413
Cdd:cd03219 79 --RTFQIPRlfpeltvleNVMVAAQARTGSGLLLARARREERearerAEELLERVGLADL-ADRPAGELSYGQQRRLEIA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488984360 414 RALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSHH 461
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGIT-VLLVEHD 202
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
261-461 |
1.07e-16 |
|
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: 77.74 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSY--NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQgySNDLTLFGRRRGSGETiwDIKKH 337
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDlKPQ--QGEITLDGVPVSDLEK--ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 338 IGYVSSSLHLdyrVSTNVRNvilsgyfdSIGIyqavsdkqhklvqqwldilgidkrtadapfhSLSWG-QQRLALiVRAL 416
Cdd:cd03247 77 ISVLNQRPYL---FDTTLRN--------NLGR-------------------------------RFSGGeRQRLAL-ARIL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984360 417 VKHPTLLILDEPLQGLDPLN-RQLVRRFVDVLigEGATqLLFVSHH 461
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITeRQLLSLIFEVL--KDKT-LIWITHH 156
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
24-191 |
1.68e-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: 78.63 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLP------LLSGQRESHFS--RVTRL----SFeQLQKLVSDEWQRNNtdLL 91
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRptsgsvLFDGEDITGLPphEIARLgigrTF-QIPRLFPELTVLEN--VM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 92 SPGEEDTGRTT--AEIIQDEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVN 169
Cdd:cd03219 98 VAAQARTGSGLllARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPE 177
|
170 180
....*....|....*....|..
gi 488984360 170 SRQQLAALLADLHSAGITLVLV 191
Cdd:cd03219 178 ETEELAELIRELRERGITVLLV 199
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-433 |
3.07e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLP-----------LLSGQRESHFS-------RVTRLS--FEQ----LQKLV 79
Cdd:PRK15134 30 LQIEAGETLALVGESGSGKSVTALSILRLLPsppvvypsgdiRFHGESLLHASeqtlrgvRGNKIAmiFQEpmvsLNPLH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 80 SDEWQRNNTDLLSPG-EEDTGRttAEIIQdevkdparCArlaEQFGISALLDRRFKY---LSTGETRKTLLCQALMTDPQ 155
Cdd:PRK15134 110 TLEKQLYEVLSLHRGmRREAAR--GEILN--------CL---DRVGIRQAAKRLTDYphqLSGGERQRVMIAMALLTRPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 156 LLILDEPFDGLDVNSRQQLAALLADLHSA-GITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLL---QQALVAQL 231
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFsapTHPYTQKL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 232 AHSEkldgitlPEPDVPPARhalADSAPRIVLNDGVVSYNDRP-----------VINHLSWTVNPGEHWQIVGPNGAGKS 300
Cdd:PRK15134 257 LNSE-------PSGDPVPLP---EPASPLLDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 301 T----LLSLVTGDHPQGYSND-LTLFGRRRgsgetIWDIKKHIGYV----SSSLHldyrVSTNVRNVILSGyfdsIGIYQ 371
Cdd:PRK15134 327 TtglaLLRLINSQGEIWFDGQpLHNLNRRQ-----LLPVRHRIQVVfqdpNSSLN----PRLNVLQIIEEG----LRVHQ 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984360 372 AV--SDKQHKLVQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433
Cdd:PRK15134 394 PTlsAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQrQRIA-IARALILKPSLIILDEPTSSLD 457
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
270-465 |
3.23e-16 |
|
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: 76.69 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 270 YNDRP-VINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQgySNDLTLFGR-----RRGsgetIWDIKKHIGYVS 342
Cdd:TIGR01166 1 YPGGPeVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLlRPQ--SGAVLIDGEpldysRKG----LLERRQRVGLVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 343 S-------SLHLDYRVSTNVRNVILSGyfdsigiyqavsDKQHKLVQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRA 415
Cdd:TIGR01166 75 QdpddqlfAADVDQDVAFGPLNLGLSE------------AEVERRVREALTAVGASG-LRERPTHCLSGGEKKRVAIAGA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984360 416 LVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSHHAEDA 465
Cdd:TIGR01166 142 VAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMT-VVISTHDVDLA 190
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
291-465 |
3.39e-16 |
|
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: 77.34 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 291 IVGPNGAGKSTLLSLVTG----DHPQGYSNDLTLFGRRRGSgetiwDI---KKHIGYVSSSL----HLdyrvstNVRNVI 359
Cdd:cd03297 28 IFGASGAGKSTLLRCIAGlekpDGGTIVLNGTVLFDSRKKI-----NLppqQRKIGLVFQQYalfpHL------NVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 360 LSGYfdsigiyQAVSDKQHK-LVQQWLDILGIDKrTADAPFHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNR 437
Cdd:cd03297 97 AFGL-------KRKRNREDRiSVDELLDLLGLDH-LLNRYPAQLSGGEkQRVAL-ARALAAQPELLLLDEPFSALDRALR 167
|
170 180
....*....|....*....|....*...
gi 488984360 438 QLVRRFVDVLIGEGATQLLFVSHHAEDA 465
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEA 195
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
260-475 |
4.09e-16 |
|
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: 77.24 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 260 RIVLNDGVVSYND--RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgysndltLFGRRRGS----GETIW- 332
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAG-----------LYKPTSGSvlldGTDIRq 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 333 ----DIKKHIGYVSSSLHLdyrVSTNVRNVILSGyfdsigiYQAVSDKQhklVQQWLDILGIDKRTADAPF--------- 399
Cdd:cd03245 71 ldpaDLRRNIGYVPQDVTL---FYGTLRDNITLG-------APLADDER---ILRAAELAGVTDFVNKHPNgldlqiger 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 400 -HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDplnRQLVRRFVDVLIGEGATQLLFVshhaedapdcITHRLAF 475
Cdd:cd03245 138 gRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD---MNSEERLKERLRQLLGDKTLII----------ITHRPSL 201
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
261-460 |
5.56e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.46 E-value: 5.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgysndltlfgrrrgSGETIWDIKKHIG 339
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGlVAPD--------------EGVIKRNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 340 YVSSSLHLDYRVSTNVRNVILsgyfdsigIYQAVSDKqhklvqqwlDILGIDKRTA-----DAPFHSLSWGQQRLALIVR 414
Cdd:PRK09544 71 YVPQKLYLDTTLPLTVNRFLR--------LRPGTKKE---------DILPALKRVQaghliDAPMQKLSGGETQRVLLAR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984360 415 ALVKHPTLLILDEPLQGLDpLNRQL-VRRFVDVLIGEGATQLLFVSH 460
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVD-VNGQVaLYDLIDQLRRELDCAVLMVSH 179
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
269-479 |
6.86e-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: 76.39 E-value: 6.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHP--QGysnDLTLFGRRRGSgeTIWDIKKHIGYVSSSlh 346
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRptSG---TAYINGYSIRT--DRKAARQSLGYCPQF-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 347 ldyrvstnvrNVI---LSGYfDSIGIY---QAVSDKQHKLVQQW-LDILGIDKRtADAPFHSLSWGQQR-LALIVrALVK 418
Cdd:cd03263 84 ----------DALfdeLTVR-EHLRFYarlKGLPKSEIKEEVELlLRVLGLTDK-ANKRARTLSGGMKRkLSLAI-ALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984360 419 HPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGAtqLLFVSHHAEDApDCITHRLAFVPSG 479
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRS--IILTTHSMDEA-EALCDRIAIMSDG 208
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
17-197 |
9.32e-16 |
|
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: 77.82 E-value: 9.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 17 KTLKIDHLS--VAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSfEQLQKLVSDEWQRNNTDllspg 94
Cdd:TIGR01188 5 DFKAVDGVNfkVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREP-RKVRRSIGIVPQYASVD----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 95 EEDTGRTTAEII-------QDEVKdpARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLD 167
Cdd:TIGR01188 79 EDLTGRENLEMMgrlyglpKDEAE--ERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190
....*....|....*....|....*....|
gi 488984360 168 VNSRQQLAALLADLHSAGITLVLVLNRFDE 197
Cdd:TIGR01188 157 PRTRRAIWDYIRALKEEGVTILLTTHYMEE 186
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-191 |
1.03e-15 |
|
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: 75.76 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 16 TKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGdlpLLSGQRESHFSRVTRLSFEQLQKLVSDEWQRNNTDLLSPGE 95
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG---LIKESSGSILLNGKPIKAKERRKSIGYVMQDVDYQLFTDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 96 EDTGRTTAEIIQDevkDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLA 175
Cdd:cd03226 90 REELLLGLKELDA---GNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVG 166
|
170
....*....|....*.
gi 488984360 176 ALLADLHSAGITLVLV 191
Cdd:cd03226 167 ELIRELAAQGKAVIVI 182
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
261-479 |
1.11e-15 |
|
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: 75.99 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVinHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRRRGSGETIwDIKKHIG 339
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQ--SGRVLINGVDVTAAPPA-DRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 340 YVSSSL--HLDyrVSTNVrnvilsGYFDSIGIYQAVSDKQ--HKLVQQwLDILGIDKRTADApfhsLSWGQ-QRLALiVR 414
Cdd:cd03298 76 FQENNLfaHLT--VEQNV------GLGLSPGLKLTAEDRQaiEVALAR-VGLAGLEKRLPGE----LSGGErQRVAL-AR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984360 415 ALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDAPDcITHRLAFVPSG 479
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKR-LAQRVVFLDNG 205
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
269-479 |
1.18e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 76.28 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLL----SLVTGDhpqgySNDLTLFGRR-RGSGETIWDIKKHIGYVSS 343
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrcinKLEEIT-----SGDLIVDGLKvNDPKVDERLIRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 344 SLHLdYRVSTNVRNVIlsgyFDSIGIYQAVSDKQHKLVQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLL 423
Cdd:PRK09493 85 QFYL-FPHLTALENVM----FGPLRVRGASKEEAEKQARELLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488984360 424 ILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSHHAEDAPDCIThRLAFVPSG 479
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMT-MVIVTHEIGFAEKVAS-RLIFIDKG 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-217 |
1.29e-15 |
|
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: 75.61 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLsfEQLQKLVSDEWQRN----------NTDL-LS 92
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA--PPADRPVSMLFQENnlfahltveqNVGLgLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 93 PGEedtgRTTAEiiqdevkDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQ 172
Cdd:cd03298 97 PGL----KLTAE-------DRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984360 173 QLAALLADLHS-AGITLVLVLNRFDEIPEFVQFAGVLADCTLSETG 217
Cdd:cd03298 166 EMLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-223 |
2.26e-15 |
|
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: 75.45 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 19 LKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGqreshfsrvtRLSFeqlqklvsdewqrNNTDL--LSPGEE 96
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSG----------KILL-------------NGKDItnLPPEKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 97 DTG-----------RTTAEIIQ--------DEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLL 157
Cdd:cd03299 72 DISyvpqnyalfphMTVYKNIAyglkkrkvDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 158 ILDEPFDGLDVNSRQQLAALLADLH-SAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLL 223
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
269-460 |
2.77e-15 |
|
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: 74.74 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDhpqgysndltlfgRRRGSGETIWDIK-------KHIGYV 341
Cdd:TIGR03740 9 RFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGI-------------LRPTSGEIIFDGHpwtrkdlHKIGSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 342 SSSL----HLDYRVSTNVRNVILSgyfdsigiyqaVSDKQHKLVQQWLDILGIDKRTADapfhSLSWG-QQRLAlIVRAL 416
Cdd:TIGR03740 76 IESPplyeNLTARENLKVHTTLLG-----------LPDSRIDEVLNIVDLTNTGKKKAK----QFSLGmKQRLG-IAIAL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488984360 417 VKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLfVSH 460
Cdd:TIGR03740 140 LNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVIL-SSH 182
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
261-460 |
3.72e-15 |
|
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: 72.48 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDhpqgysndltlfgRRRGSGETIWDIKKHIGY 340
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGE-------------LEPDEGIVTWGSTVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 341 vssslhldyrvstnvrnvilsgyfdsigiyqavsdkqhklvqqwldilgidkrtadapFHSLSWGQQRLALIVRALVKHP 420
Cdd:cd03221 68 ----------------------------------------------------------FEQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984360 421 TLLILDEPLQGLDPLNRQLVRRFvdvLIG-EGAtqLLFVSH 460
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEA---LKEyPGT--VILVSH 125
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
268-434 |
4.60e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.55 E-value: 4.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 268 VSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgysndltlfgrrrgSGETIWDiKKHIGYVSSSLH 346
Cdd:TIGR01189 8 CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGlLRPD--------------SGEVRWN-GTPLAEQRDEPH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 347 ldyrvstnvRNVILSGYFDSIG----------IYQAVSDKQHKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRAL 416
Cdd:TIGR01189 73 ---------ENILYLGHLPGLKpelsalenlhFWAAIHGGAQRTIEDALAAVGLTGF-EDLPAAQLSAGQQRRLALARLW 142
|
170
....*....|....*...
gi 488984360 417 VKHPTLLILDEPLQGLDP 434
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDK 160
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
256-460 |
4.71e-15 |
|
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: 74.63 E-value: 4.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 256 DSAPRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRR--RGSGETIW 332
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGlLRPD--SGEILVDGQDitGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 333 DIKKHIGYV--SSSLhldyrvstnvrnvilsgyFDSIGIYQAV----------SDKQ-HKLVQQWLDILG----IDKRTA 395
Cdd:COG1127 79 ELRRRIGMLfqGGAL------------------FDSLTVFENVafplrehtdlSEAEiRELVLEKLELVGlpgaADKMPS 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 396 DapfhsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR----QLVRRFVDVLigeGATQLLfVSH 460
Cdd:COG1127 141 E-----LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSavidELIRELRDEL---GLTSVV-VTH 200
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
271-472 |
5.14e-15 |
|
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: 73.98 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 271 NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVtgdhpqgYSNDLTLFGRRRGSGETIWDIKK--------HIGYVS 342
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLI-------YKEELPTSGTIRVNGQDVSDLRGraipylrrKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 343 SslhlDYRVSTNvRNVilsgyFDSIGIYQAVSDKQHKLVQQ----WLDILGIDKRTADAPfHSLSWG-QQRLAlIVRALV 417
Cdd:cd03292 85 Q----DFRLLPD-RNV-----YENVAFALEVTGVPPREIRKrvpaALELVGLSHKHRALP-AELSGGeQQRVA-IARAIV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984360 418 KHPTLLILDEPLQGLDPLNrqlVRRFVDVLIG---EGATqlLFVSHHAEDAPDCITHR 472
Cdd:cd03292 153 NSPTILIADEPTGNLDPDT---TWEIMNLLKKinkAGTT--VVVATHAKELVDTTRHR 205
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
16-217 |
5.99e-15 |
|
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: 73.41 E-value: 5.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 16 TKTLK----IDHLS--VAAGESWAFVGSNGSGKSALARALAGDLPLLSGQreshfsrVTrlsfeQLQKLVSDE---WQRN 86
Cdd:cd03268 7 TKTYGkkrvLDDISlhVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGE-------IT-----FDGKSYQKNieaLRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 87 NTDLLSPG--EEDTGR----TTAEIIQdevKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILD 160
Cdd:cd03268 75 GALIEAPGfyPNLTARenlrLLARLLG---IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 161 EPFDGLDVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETG 217
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
270-464 |
6.23e-15 |
|
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: 74.29 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 270 YNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQGysndltlfGRRRGSGETIWDIKK----HIGYV--- 341
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLlQPTS--------GEVRVAGLVPWKRRKkflrRIGVVfgq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 342 SSSLHLDYRVstnvrnviLSGYFDSIGIYQAVSDKQHKLVQQWLDILGIDkRTADAPFHSLSWGQQRLALIVRALVKHPT 421
Cdd:cd03267 103 KTQLWWDLPV--------IDSFYLLAAIYDLPPARFKKRLDELSELLDLE-ELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984360 422 LLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAED 464
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKD 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
225-461 |
8.89e-15 |
|
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: 76.63 E-value: 8.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 225 QALVAQLAHSEKLDGITLPEPDVP----PARHALADSAPRIVLNDGVVSY-NDRPVINHLSWTVNPGEHWQIVGPNGAGK 299
Cdd:TIGR02868 295 QQLTRVRAAAERIVEVLDAAGPVAegsaPAAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 300 STLLSLVTG--DHPQGysnDLTLFGRRRGSGETIwDIKKHIGYVSSSLHLdyrVSTNVRNVILSGYFDSIG--IYQAVSD 375
Cdd:TIGR02868 375 STLLATLAGllDPLQG---EVTLDGVPVSSLDQD-EVRRRVSVCAQDAHL---FDTTVRENLRLARPDATDeeLWAALER 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 376 KQhklVQQWLDIL--GIDKR-TADAPfhSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLN-RQLVRRFVDVLigE 450
Cdd:TIGR02868 448 VG---LADWLRALpdGLDTVlGEGGA--RLSGGErQRLAL-ARALLADAPILLLDEPTEHLDAETaDELLEDLLAAL--S 519
|
250
....*....|.
gi 488984360 451 GATQLLfVSHH 461
Cdd:TIGR02868 520 GRTVVL-ITHH 529
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-190 |
1.13e-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: 72.53 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGqreshfsrvtRLSFEQLQ-KLVSDEWQRNntdLLSPGEEDTGRTT 102
Cdd:cd03231 21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG----------RVLLNGGPlDFQRDSIARG---LLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 103 AEIIQD-----EVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAAL 177
Cdd:cd03231 88 LSVLENlrfwhADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|...
gi 488984360 178 LADLHSAGITLVL 190
Cdd:cd03231 168 MAGHCARGGMVVL 180
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
261-460 |
1.19e-14 |
|
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: 72.95 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRR-RGSGETIWDIKKHI 338
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLlEEPD--SGTIIIDGLKlTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 339 GYVSSSLHLdYRVSTNVRNVILSgyfdsIGIYQAVSDKQ-HKLVQQWLDILGIDKRtADAPFHSLSWGQ-QRLAlIVRAL 416
Cdd:cd03262 79 GMVFQQFNL-FPHLTVLENITLA-----PIKVKGMSKAEaEERALELLEKVGLADK-ADAYPAQLSGGQqQRVA-IARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984360 417 VKHPTLLILDEPLQGLDPlnrQLVRRFVDV---LIGEGATQLLfVSH 460
Cdd:cd03262 151 AMNPKVMLFDEPTSALDP---ELVGEVLDVmkdLAEEGMTMVV-VTH 193
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
168-480 |
1.21e-14 |
|
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: 76.28 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 168 VNSRQQLAALLADLHSAGITLVLVLNRFD---------EIPEFVQFAGVLADC--TLSET-GEksslLQQALVAqlahSE 235
Cdd:TIGR02204 238 IRTRALLTAIVIVLVFGAIVGVLWVGAHDviagkmsagTLGQFVFYAVMVAGSigTLSEVwGE----LQRAAGA----AE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 236 KLDGITLPEPDVPPARHALADSAP---RIVLNDGVVSY---NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGD 309
Cdd:TIGR02204 310 RLIELLQAEPDIKAPAHPKTLPVPlrgEIEFEQVNFAYparPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRF 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 310 H-PQGysndltlfGRRRGSGETIW-----DIKKHIGYVSSSLHLdyrVSTNVRNVILSGYFDSIG---IYQAVSDKQHKL 380
Cdd:TIGR02204 390 YdPQS--------GRILLDGVDLRqldpaELRARMALVPQDPVL---FAASVMENIRYGRPDATDeevEAAARAAHAHEF 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 381 VQQWLDilGIDKRTADAPFhSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIgEGATQLLfvs 459
Cdd:TIGR02204 459 ISALPE--GYDTYLGERGV-TLSGGQrQRIA-IARAILKDAPILLLDEATSALDAESEQLVQQALETLM-KGRTTLI--- 530
|
330 340
....*....|....*....|.
gi 488984360 460 hhaedapdcITHRLAFVPSGD 480
Cdd:TIGR02204 531 ---------IAHRLATVLKAD 542
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
279-465 |
1.26e-14 |
|
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: 73.14 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 279 LSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQGysndltlfGRRRGSGETIWD---IKKHIGYVSSslhlDYRVSTN 354
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIkPDS--------GKILLNGKDITNlppEKRDISYVPQ----NYALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 355 VrNVilsgyFDSI--GIYQAVSDKQ--HKLVQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQ 430
Cdd:cd03299 86 M-TV-----YKNIayGLKKRKVDKKeiERKVLEIAEMLGIDHLLNRKP-ETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190
....*....|....*....|....*....|....*
gi 488984360 431 GLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDA 465
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEA 193
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
33-226 |
1.26e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.07 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 33 AFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLVSDEWQRNNTDLLSPG-EEDTGRTTAEIIQDEVK 111
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIFSPTvEQDIAFGPINLGLDEET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 112 DPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADL-HSAGITLVL 190
Cdd:PRK13652 114 VAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984360 191 VLNRFDEIPEFVQFAGVL------ADCTLSETGEKSSLLQQA 226
Cdd:PRK13652 194 STHQLDLVPEMADYIYVMdkgrivAYGTVEEIFLQPDLLARV 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-433 |
1.56e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.74 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLP--------LLSGQrESHFSRVtRLSFE-------QLQKLVSDEWQRNNT 88
Cdd:PRK13549 26 LKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtyegeiIFEGE-ELQASNI-RDTERagiaiihQELALVKELSVLENI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 89 DLlspGEEDT--GRTtaeiiqDEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGL 166
Cdd:PRK13549 104 FL---GNEITpgGIM------DYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 167 DVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLLQQALVAQLAHSEkldgITLPEPD 246
Cdd:PRK13549 175 TESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVGRE----LTALYPR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 247 VPparHALADsaprIVLN-DGVVSYN----DRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYSNDLTLF 321
Cdd:PRK13549 251 EP---HTIGE----VILEvRNLTAWDpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFID 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 322 GRR---RGSGETIwdiKKHIGYVSSSLHLDYRVST-NV-RNVILSGYFDSIGIYQAVSDKQHKLVQQWLDILGIDKRTAD 396
Cdd:PRK13549 324 GKPvkiRNPQQAI---AQGIAMVPEDRKRDGIVPVmGVgKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPE 400
|
410 420 430
....*....|....*....|....*....|....*..
gi 488984360 397 APFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:PRK13549 401 LAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
278-465 |
1.75e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 72.69 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 278 HLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFG---------RRRGSgetiwdikkhIGYVSSSL--H 346
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPA-SGSLTLNGqdhtttppsRRPVS----------MLFQENNLfsH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 347 LdyrvstNVRNVIlsgyfdSIGIYQAV--SDKQHKLVQQWLDILGIDKRTADAPfHSLSWGQ-QRLALiVRALVKHPTLL 423
Cdd:PRK10771 86 L------TVAQNI------GLGLNPGLklNAAQREKLHAIARQMGIEDLLARLP-GQLSGGQrQRVAL-ARCLVREQPIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984360 424 ILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDA 465
Cdd:PRK10771 152 LLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDA 193
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
24-191 |
2.10e-14 |
|
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: 72.54 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLqklvsdEWQRNNTDL--------LSPGE 95
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR------KIRRKEIQMvfqdpmssLNPRM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 96 edT-GRTTAEIIQDEVKDPARCAR------LAEQFGISALLDRRFKY-LSTGETRKTLLCQALMTDPQLLILDEPFDGLD 167
Cdd:cd03257 100 --TiGEQIAEPLRIHGKLSKKEARkeavllLLVGVGLPEEVLNRYPHeLSGGQRQRVAIARALALNPKLLIADEPTSALD 177
|
170 180
....*....|....*....|....*
gi 488984360 168 VNSRQQLAALLADLHSA-GITLVLV 191
Cdd:cd03257 178 VSVQAQILDLLKKLQEElGLTLLFI 202
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
258-445 |
2.52e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.49 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 258 APRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRGSGETIwDIKKH 337
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT-AGTVLVAGDDVEALSAR-AASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 338 IGYV--SSSLHLDYRVstnvRNVILSGYFDSIGIYQAVSDKQHKLVQQWLDILGIDkRTADAPFHSLSWGQQRLALIVRA 415
Cdd:PRK09536 79 VASVpqDTSLSFEFDV----RQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVA-QFADRPVTSLSGGERQRVLLARA 153
|
170 180 190
....*....|....*....|....*....|....*
gi 488984360 416 LVKHPTLLILDEPLQGLDpLNRQ-----LVRRFVD 445
Cdd:PRK09536 154 LAQATPVLLLDEPTASLD-INHQvrtleLVRRLVD 187
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
267-448 |
2.52e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 72.37 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 267 VVSYNDRPVINHLSWTVNPGEhwqIV---GPNGAGKSTLLSLVTG----DHPQGYSND-----LTLFGR-RRGsgetiwd 333
Cdd:COG1137 10 VKSYGKRTVVKDVSLEVNQGE---IVgllGPNGAGKTTTFYMIVGlvkpDSGRIFLDGedithLPMHKRaRLG------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 334 ikkhIGYVS--SSLhldYR---VSTNVRNVILSGYFDsigiyqavSDKQHKLVQQWLDILGIDKRtADAPFHSLSWGQQR 408
Cdd:COG1137 80 ----IGYLPqeASI---FRkltVEDNILAVLELRKLS--------KKEREERLEELLEEFGITHL-RKSKAYSLSGGERR 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488984360 409 LALIVRALVKHPTLLILDEPLQGLDPLN----RQLVRRFVD----VLI 448
Cdd:COG1137 144 RVEIARALATNPKFILLDEPFAGVDPIAvadiQKIIRHLKErgigVLI 191
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
276-460 |
3.41e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 72.33 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 276 INHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQGysndltlfGRRRGSGETIWDIKKH----IGYVSSSLHLD-Y 349
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkPTG--------GTILLRGQHIEGLPGHqiarMGVVRTFQHVRlF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 350 RVSTNVRNV-----------ILSGYFDSIGIYQAVSDKQHKlVQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRALVK 418
Cdd:PRK11300 93 REMTVIENLlvaqhqqlktgLFSGLLKTPAFRRAESEALDR-AATWLERVGL-LEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984360 419 HPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSH 460
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEH 212
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-191 |
3.80e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 73.57 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 1 MSSLQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGqreshfsrvtRLSFEQlqKLVS 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSG----------EILIGG--RDVT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 81 DewqrnntdlLSPGEEDTG-----------RTTAEII----------QDEVKdpARCARLAEQFGISALLDRRFKYLSTG 139
Cdd:COG3839 69 D---------LPPKDRNIAmvfqsyalyphMTVYENIafplklrkvpKAEID--RRVREAAELLGLEDLLDRKPKQLSGG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984360 140 ETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSA-GITLVLV 191
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYV 190
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
267-468 |
3.82e-14 |
|
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: 71.13 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 267 VVSYNDRP-VINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgysndltLFGRRRGS----GETI--WDIKKHIG 339
Cdd:cd03226 6 SFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG-----------LIKESSGSillnGKPIkaKERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 340 YVSSslHLDYRVSTN-VRNVILSGYfdsigiyQAVSDKQHKlVQQWLDILGIDKRTADAPfHSLSWGQ-QRLALIVrALV 417
Cdd:cd03226 75 YVMQ--DVDYQLFTDsVREELLLGL-------KELDAGNEQ-AETVLKDLDLYALKERHP-LSLSGGQkQRLAIAA-ALL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984360 418 KHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLfVSHHAEDAPDC 468
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIV-ITHDYEFLAKV 192
|
|
| 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 488984360 268 VSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRGSGETIWdiKKHIGYVSSSLHL 347
Cdd:cd03231 8 CERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPL-AGRVLLNGGPLDFQRDSI--ARGLLYLGHAPGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 348 DYRVSTNVRNVILSGYFDSIGIYQAVSDkqhklvqqwLDILGIDkrtaDAPFHSLSWGQQRLALIVRALVKHPTLLILDE 427
Cdd:cd03231 85 KTTLSVLENLRFWHADHSDEQVEEALAR---------VGLNGFE----DRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
....*.
gi 488984360 428 PLQGLD 433
Cdd:cd03231 152 PTTALD 157
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
260-465 |
4.99e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 73.18 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 260 RIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgysndltlfgrrrgSGEtiwdikkhi 338
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDPT--------------SGE--------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 339 gyvsssLHLDYRVSTNV----RNVilsGY-FDSIGIYQAVS----------------DKQHKLVQQWLDILGID---KRT 394
Cdd:COG3839 60 ------ILIGGRDVTDLppkdRNI---AMvFQSYALYPHMTvyeniafplklrkvpkAEIDRRVREAAELLGLEdllDRK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 395 ADApfhsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNR--------QLVRRFvdvligeGATqLLFVSHHAEDA 465
Cdd:COG3839 131 PKQ----LSGGQrQRVA-LGRALVREPKVFLLDEPLSNLDAKLRvemraeikRLHRRL-------GTT-TIYVTHDQVEA 197
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-190 |
5.50e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.80 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLP-----LLSGQRESHFS----RVTR--LSFEQLQKLVSDEWQRnnTDLLS 92
Cdd:COG4138 17 AQVNAGELIHLIGPNGAGKSTLLARMAGLLPgqgeiLLNGRPLSDWSaaelARHRayLSQQQSPPFAMPVFQY--LALHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 93 PGEEDTGRTTAEIiqdevkdparcARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMT-------DPQLLILDEPFDG 165
Cdd:COG4138 95 PAGASSEAVEQLL-----------AQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNS 163
|
170 180
....*....|....*....|....*..
gi 488984360 166 LDVnsRQQLA--ALLADLHSAGITLVL 190
Cdd:COG4138 164 LDV--AQQAAldRLLRELCQQGITVVM 188
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
254-442 |
5.75e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.09 E-value: 5.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 254 LADSAPRIVLNDGVVSYN-DRP-VINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGdhPQGYSNDLTLFGRRRGSGETI 331
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQsDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG--IEKVKSGEIFYNNQAITDDNF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 332 WDIKKHIG---------YVSSSLHLDyrVSTNVRNvilsgyfdsigiyQAVS-DKQHKLVQQWLDILGIDKRTADAPfHS 401
Cdd:PRK13648 79 EKLRKHIGivfqnpdnqFVGSIVKYD--VAFGLEN-------------HAVPyDEMHRRVSEALKQVDMLERADYEP-NA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984360 402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQ----LVRR 442
Cdd:PRK13648 143 LSGGQkQRVA-IAGVLALNPSVIILDEATSMLDPDARQnlldLVRK 187
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
261-479 |
6.04e-14 |
|
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: 69.91 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRRRGSGE-TIWDIKKHI 338
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEPD--SGSILIDGEDLTDLEdELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 339 GYVssslhldyrvstnvrnvilsgyFDSIGIYQavsdkqHKLVqqwLDILGidkrtadapfHSLSWGQ-QRLAlIVRALV 417
Cdd:cd03229 79 GMV----------------------FQDFALFP------HLTV---LENIA----------LGLSGGQqQRVA-LARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984360 418 KHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDApDCITHRLAFVPSG 479
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEA-ARLADRVVVLRDG 177
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
24-190 |
6.88e-14 |
|
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: 71.21 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSG-----------QRESHFSRVTrLSFEQLQKLVSDewqrnntdlLS 92
Cdd:cd03267 42 FTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGevrvaglvpwkRRKKFLRRIG-VVFGQKTQLWWD---------LP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 93 PGeeDTGRTTAEIIQ-DEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSR 171
Cdd:cd03267 112 VI--DSFYLLAAIYDlPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180
....*....|....*....|
gi 488984360 172 QQLAALLADLHSA-GITLVL 190
Cdd:cd03267 190 ENIRNFLKEYNRErGTTVLL 209
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-191 |
6.91e-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: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHfSRVTRLSFEQLqklvsdew 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-STVKIGYFEQL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 84 qrnntdllspgeedtgrttaeiiqdevkdparcarlaeqfgisalldrrfkylSTGETRKTLLCQALMTDPQLLILDEPF 163
Cdd:cd03221 72 -----------------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180
....*....|....*....|....*...
gi 488984360 164 DGLDVNSRQQLAALLADLHSagiTLVLV 191
Cdd:cd03221 99 NHLDLESIEALEEALKEYPG---TVILV 123
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-210 |
9.94e-14 |
|
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: 68.99 E-value: 9.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGdlpllsgqreshfsrvtrlsfeqlqklvsdewqrnntdLLSPgeeDTGrtta 103
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMKILSG--------------------------------------LYKP---DSG---- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 104 EIIQDEVKDPARCARLAEQFGISALldrrfkY-LSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLH 182
Cdd:cd03216 56 EILVDGKEVSFASPRDARRAGIAMV------YqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLR 129
|
170 180
....*....|....*....|....*...
gi 488984360 183 SAGITLVLVLNRFDEIPEFVQFAGVLAD 210
Cdd:cd03216 130 AQGVAVIFISHRLDEVFEIADRVTVLRD 157
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
24-208 |
1.12e-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: 70.16 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQK----LVSDEwqRNNTDLLSPgeEDTG 99
Cdd:cd03224 21 LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARagigYVPEG--RRIFPELTV--EENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 100 RTTAEIIQDEVKDparcARLAEQFGISALLDRRFK----YLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLA 175
Cdd:cd03224 97 LLGAYARRRAKRK----ARLERVYELFPRLKERRKqlagTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190
....*....|....*....|....*....|...
gi 488984360 176 ALLADLHSAGITLVLVLNRFDEIPEFVQFAGVL 208
Cdd:cd03224 173 EAIRELRDEGVTILLVEQNARFALEIADRAYVL 205
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-191 |
1.46e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.87 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 7 SQGTFRLSDTKT-LKIDHLSVAAGESWAFVGSNGSGKSALARALAG--------------DLPLLSGQRESHFSRVTRLS 71
Cdd:PRK10419 15 HGGLSGKHQHQTvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlespsqgnvswrgePLAKLNRAQRKAFRRDIQMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 72 FEQlqklvsdewqrnntdllSPGEEDTGRTTAEIIQ---------DEVKDPARCARLAEQFGISA-LLDRRFKYLSTGET 141
Cdd:PRK10419 95 FQD-----------------SISAVNPRKTVREIIReplrhllslDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984360 142 RKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADL-HSAGITLVLV 191
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFI 208
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
268-463 |
1.92e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.60 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 268 VSYND--RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHpqgysndltlfgrRRGSGETIWDIKKHIGYVSSSL 345
Cdd:COG2401 36 VELRVveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL-------------KGTPVAGCVDVPDNQFGREASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 346 --HLDYRVSTNvrnvilsgyfDSIGIYQAV--SDkqhklVQQWLdilgidkrtadAPFHSLSWGQQRLALIVRALVKHPT 421
Cdd:COG2401 103 idAIGRKGDFK----------DAVELLNAVglSD-----AVLWL-----------RRFKELSTGQKFRFRLALLLAERPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984360 422 LLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAE 463
Cdd:COG2401 157 LLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
23-188 |
1.95e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 68.92 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 23 HLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGqreshfsrVTRLSFEQLQKlVSDEWQRNntdLLSPGEEDTGRTT 102
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSG--------EVRWNGTPLAE-QRDEPHEN---ILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 103 ----------AEIIQDEVKDparCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQ 172
Cdd:TIGR01189 88 lsalenlhfwAAIHGGAQRT---IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170
....*....|....*..
gi 488984360 173 QLAALLAD-LHSAGITL 188
Cdd:TIGR01189 165 LLAGLLRAhLARGGIVL 181
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
269-465 |
1.95e-13 |
|
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: 69.57 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRRrgsgetIWDI---KKHIGYVSSS 344
Cdd:cd03300 9 FYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfETPT--SGEILLDGKD------ITNLpphKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 345 L----HLDyrVSTNVrnvilsgyfdSIGIYQAVSDKQ--HKLVQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVK 418
Cdd:cd03300 81 YalfpHLT--VFENI----------AFGLRLKKLPKAeiKERVAEALDLVQLEGYANRKP-SQLSGGQQQRVAIARALVN 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984360 419 HPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDA 465
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEA 194
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-185 |
2.11e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.13 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 25 SVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ-----RESHFSRVtrlsFEQLQKL-----------VSDE---WQR 85
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTikldgGDIDDPDV----AEACHYLghrnamkpaltVAENlefWAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 86 -NNTDLLSPgeedtgrttaeiiqdevkDPARCArlaeqFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFD 164
Cdd:PRK13539 100 fLGGEELDI------------------AAALEA-----VGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180
....*....|....*....|.
gi 488984360 165 GLDVNSRQQLAALLADlHSAG 185
Cdd:PRK13539 157 ALDAAAVALFAELIRA-HLAQ 176
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
136-433 |
2.16e-13 |
|
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: 72.28 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 136 LSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITL-------------VLVLNRFDEIPEFV 202
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVthdryfldnvagwILELDRGRGIPWEG 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 203 QFAGVL--ADCTLSETGEKSSLLQQALV------------------AQLAHSEKLDGITLPEPD------VPPArhalad 256
Cdd:TIGR03719 242 NYSSWLeqKQKRLEQEEKEESARQKTLKrelewvrqspkgrqakskARLARYEELLSQEFQKRNetaeiyIPPG------ 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 257 saPRivLNDGVV-------SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHpQGYSNDLTLfgrrrgsGE 329
Cdd:TIGR03719 316 --PR--LGDKVIeaenltkAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQE-QPDSGTIEI-------GE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 330 TIwdikkHIGYVSSSL-HLDyrvstnvrnvilsgyfDSIGIYQAVSDKqhklvqqwLDILGIDKRTADA----------- 397
Cdd:TIGR03719 384 TV-----KLAYVDQSRdALD----------------PNKTVWEEISGG--------LDIIKLGKREIPSrayvgrfnfkg 434
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 488984360 398 -----PFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:TIGR03719 435 sdqqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-199 |
2.49e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 70.26 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSD-TKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ--RESHFSRVTRLSFEQLQKLVS 80
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRilFDGKPIDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 81 DEWQRNNTDLLSPG-EEDT--GRTTAEIIQDEVKDpaRCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLL 157
Cdd:PRK13636 86 MVFQDPDNQLFSASvYQDVsfGAVNLKLPEDEVRK--RVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984360 158 ILDEPFDGLDVNSRQQLAALLADLHSA-GITLVLVLNRFDEIP 199
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVP 206
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-190 |
3.03e-13 |
|
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: 68.22 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 15 DTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ-----RESHFSRVTRLSFEQLQKLVsdeWQRNNTD 89
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAvlidgEPLDYSRKGLLERRQRVGLV---FQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 90 LLSP--------GEEDTGRTTAEIiqdevkdPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDE 161
Cdd:TIGR01166 81 LFAAdvdqdvafGPLNLGLSEAEV-------ERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDE 153
|
170 180
....*....|....*....|....*....
gi 488984360 162 PFDGLDVNSRQQLAALLADLHSAGITLVL 190
Cdd:TIGR01166 154 PTAGLDPAGREQMLAILRRLRAEGMTVVI 182
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
261-433 |
3.32e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.91 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHP--QG---YSNDLTLfgRR------RGSGE 329
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLldDGriiYEQDLIV--ARlqqdppRNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 330 TIWDikkhigYVSSSL-----------HLDYRVSTNVRNVILSgyfdSIGIYQAVSDKQH-----KLVQQWLDILGIDkr 393
Cdd:PRK11147 82 TVYD------FVAEGIeeqaeylkryhDISHLVETDPSEKNLN----ELAKLQEQLDHHNlwqleNRINEVLAQLGLD-- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488984360 394 tADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:PRK11147 150 -PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
23-191 |
3.68e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.63 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 23 HLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHfSRVTRLSFEQLQklvsDEWQRNNT--DLLSPGEEDTGR 100
Cdd:COG0488 335 SLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG-ETVKIGYFDQHQ----EELDPDKTvlDELRDGAPGGTE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 101 TTAeiiqdevkdparcARLAEQFGISAllDRRFKY---LSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAAL 177
Cdd:COG0488 410 QEV-------------RGYLGRFLFSG--DDAFKPvgvLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA 474
|
170
....*....|....
gi 488984360 178 LADLhsAGiTLVLV 191
Cdd:COG0488 475 LDDF--PG-TVLLV 485
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-440 |
4.02e-13 |
|
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: 71.37 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 10 TFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAG--DLPLLSGQRESHFSR------VTRLSF--------- 72
Cdd:TIGR03269 7 TKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVALcekcgyVERPSKvgepcpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 73 EQLQKLVSDEWqrnntDLLSPGEEDTGRTTAEIIQ-------------------DEVKDPA-----RCARLAEQFGISAL 128
Cdd:TIGR03269 87 GTLEPEEVDFW-----NLSDKLRRRIRKRIAIMLQrtfalygddtvldnvlealEEIGYEGkeavgRAVDLIEMVQLSHR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 129 LDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQL-AALLADLHSAGITLVLVLNRFDEIPEFVQFAGV 207
Cdd:TIGR03269 162 ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhNALEEAVKASGISMVLTSHWPEVIEDLSDKAIW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 208 LADCTLSETGEKSSLLQQALvAQLAHSEKLDGITLPEPDVpparhALADSAPR-IVLNDGVVSyndrpVINHLSWTVNPG 286
Cdd:TIGR03269 242 LENGEIKEEGTPDEVVAVFM-EGVSEVEKECEVEVGEPII-----KVRNVSKRyISVDRGVVK-----AVDNVSLEVKEG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 287 EHWQIVGPNGAGKSTLLSLVTGDHP--QGYSN--------DLT---LFGRRRgsgetiwdIKKHIGYvsssLHLDYRVST 353
Cdd:TIGR03269 311 EIFGIVGTSGAGKTTLSKIIAGVLEptSGEVNvrvgdewvDMTkpgPDGRGR--------AKRYIGI----LHQEYDLYP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 354 NvrNVILSGYFDSIGIYQAVSDKQHKLVQQwLDILGIDKRTA----DAPFHSLSWGQQ-RLALiVRALVKHPTLLILDEP 428
Cdd:TIGR03269 379 H--RTVLDNLTEAIGLELPDELARMKAVIT-LKMVGFDEEKAeeilDKYPDELSEGERhRVAL-AQVLIKEPRIVILDEP 454
|
490
....*....|..
gi 488984360 429 LQGLDPLNRQLV 440
Cdd:TIGR03269 455 TGTMDPITKVDV 466
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
268-465 |
5.09e-13 |
|
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: 69.40 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 268 VSY-------NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGR--RRGSGETIWDIKKH 337
Cdd:TIGR04521 6 VSYiyqpgtpFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGlLKPT--SGTVTIDGRdiTAKKKKKLKDLRKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 338 IGYV----SSSLhldyrVSTNV--------RNVILSGyfdsigiyqavsDKQHKLVQQWLDILGIDKRTAD-APFHsLSW 404
Cdd:TIGR04521 84 VGLVfqfpEHQL-----FEETVykdiafgpKNLGLSE------------EEAEERVKEALELVGLDEEYLErSPFE-LSG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984360 405 GQQRLALIVRALVKHPTLLILDEPLQGLDPLNR-QLVRRFVDVLIGEGATqLLFVSHHAEDA 465
Cdd:TIGR04521 146 GQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRkEILDLFKRLHKEKGLT-VILVTHSMEDV 206
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
269-465 |
5.47e-13 |
|
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: 68.48 E-value: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYND-RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVtgdhpqgysNDLT--LFGRRRGSGETI--WD---IKKHIGY 340
Cdd:cd03295 9 RYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI---------NRLIepTSGEIFIDGEDIreQDpveLRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 341 VSSSLHL--DYRVSTNVRNVI-LSGYfdsigiyqaVSDKQHKLVQQWLDILGIDKRT-ADAPFHSLSWGQQRLALIVRAL 416
Cdd:cd03295 80 VIQQIGLfpHMTVEENIALVPkLLKW---------PKEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984360 417 VKHPTLLILDEPLQGLDPLNR-QLVRRFVDVLIGEGATqLLFVSHHAEDA 465
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRdQLQEEFKRLQQELGKT-IVFVTHDIDEA 199
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-275 |
5.63e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 69.38 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQ----LQKLVSDEWQRNNTDLLspgEEDTG 99
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQFPESQLF---EETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 100 RTTA------EIIQDEVKDPArcARLAEQFGISALLDRRFKY-LSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQ 172
Cdd:PRK13643 104 KDVAfgpqnfGIPKEKAEKIA--AEKLEMVGLADEFWEKSPFeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 173 QLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLLQQalvaqlahsekLDGITLPEPDVPPARH 252
Cdd:PRK13643 182 EMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE-----------VDFLKAHELGVPKATH 250
|
250 260
....*....|....*....|...
gi 488984360 253 aLADSAPRIvlndGVVSYNDRPV 275
Cdd:PRK13643 251 -FADQLQKT----GAVTFEKLPI 268
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-225 |
5.63e-13 |
|
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: 70.95 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 3 SLQISQGTFRLSDTKTLKIDHLS--VAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ-----REshfsrVTRLSFEQL 75
Cdd:COG4987 333 SLELEDVSFRYPGAGRPVLDGLSltLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSitlggVD-----LRDLDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 76 QKLVS---------DEWQRNNtdLLspgeedTGRTTAeiiqdevkDPARCARLAEQFGISALLDRRFKYLST-------- 138
Cdd:COG4987 408 RRRIAvvpqrphlfDTTLREN--LR------LARPDA--------TDEELWAALERVGLGDWLAALPDGLDTwlgeggrr 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 139 ---GETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADlHSAGITLVLV------LNRFDEIPefvqfagVLA 209
Cdd:COG4987 472 lsgGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLIthrlagLERMDRIL-------VLE 543
|
250
....*....|....*.
gi 488984360 210 DCTLSETGEKSSLLQQ 225
Cdd:COG4987 544 DGRIVEQGTHEELLAQ 559
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-194 |
5.76e-13 |
|
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: 66.86 E-value: 5.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSDTKTLKID--HLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQreshfsrvTRLSFEQLQKLVSD 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRnvSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGR--------VRLDGADISQWDPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 82 EWQRN-----NTDLLSPGeedtgrTTAEIIqdevkdparcarlaeqfgisalldrrfkyLSTGETRKTLLCQALMTDPQL 156
Cdd:cd03246 73 ELGDHvgylpQDDELFSG------SIAENI-----------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984360 157 LILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNR 194
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR 155
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-433 |
5.86e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.80 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 17 KTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ-----RESHFSRvTRLSFE-------QLQKLVSDEWQ 84
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSilylgKEVTFNG-PKSSQEagigiihQELNLIPQLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 85 RNNTDLlspGEEDTGRTTAeIIQDEVKDPArcARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFD 164
Cdd:PRK10762 97 AENIFL---GREFVNRFGR-IDWKKMYAEA--DKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 165 GLDVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLAD------CTLSETGEKSslLQQALVAQlahseKLD 238
Cdd:PRK10762 171 ALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDgqfiaeREVADLTEDS--LIEMMVGR-----KLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 239 gitlpepdvpparhalaDSAPRIVLNDGVVSYNDR----PVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGy 314
Cdd:PRK10762 244 -----------------DQYPRLDKAPGEVRLKVDnlsgPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRT- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 315 SNDLTLFGRRRGSGETIWDIKKHIGYVSSS-----LHLDYRVSTNVRNVILsGYFDSIGIyQAVSDKQHKLVQQWLDILG 389
Cdd:PRK10762 306 SGYVTLDGHEVVTRSPQDGLANGIVYISEDrkrdgLVLGMSVKENMSLTAL-RYFSRAGG-SLKHADEQQAVSDFIRLFN 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 488984360 390 IDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:PRK10762 384 IKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-192 |
5.90e-13 |
|
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: 68.36 E-value: 5.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 14 SDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLVSDE---WQRNN--- 87
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIgmiFQQFNlie 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 88 -----TDLLSP--GEEDTGRTTAEIIQDEvkDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILD 160
Cdd:cd03256 92 rlsvlENVLSGrlGRRSTWRSLFGLFPKE--EKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILAD 169
|
170 180 190
....*....|....*....|....*....|...
gi 488984360 161 EPFDGLDVNSRQQLAALLADLHSA-GITLVLVL 192
Cdd:cd03256 170 EPVASLDPASSRQVMDLLKRINREeGITVIVSL 202
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-225 |
5.91e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.00 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLS----FEQLQKLVSDEWQRNNTDLLspgEEDTG 99
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQIRKKVGLVFQFPESQLF---EETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 100 RTTAEIIQDEVKDPARCARLAEQ----FGIS-ALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQL 174
Cdd:PRK13649 105 KDVAFGPQNFGVSQEEAEALAREklalVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKEL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984360 175 AALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLLQQ 225
Cdd:PRK13649 185 MTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
24-191 |
6.13e-13 |
|
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: 68.23 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAG-DLP-----LLSGQRESHFSRVTRL------------SFEQLQKLVSDEwqr 85
Cdd:COG4181 33 LEVEAGESVAIVGASGSGKSTLLGLLAGlDRPtsgtvRLAGQDLFALDEDARArlrarhvgfvfqSFQLLPTLTALE--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 86 nNTDLlsPGEEdTGRTTAEiiqdevkdpARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDG 165
Cdd:COG4181 110 -NVML--PLEL-AGRRDAR---------ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGN 176
|
170 180
....*....|....*....|....*..
gi 488984360 166 LDVNSRQQLAALLADLHS-AGITLVLV 191
Cdd:COG4181 177 LDAATGEQIIDLLFELNReRGTTLVLV 203
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
24-230 |
7.05e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.50 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLVSDEWQRnntdLLSPgeedTGRTTA 103
Cdd:PRK11231 23 LSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQH----HLTP----EGITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 104 EII------------QDEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSR 171
Cdd:PRK11231 95 ELVaygrspwlslwgRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 172 QQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLLQQALVAQ 230
Cdd:PRK11231 175 VELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRT 233
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-460 |
7.50e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.75 E-value: 7.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 1 MSSLQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSG--QRESHFsRVTRL-------- 70
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGriIYEQDL-IVARLqqdpprnv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 71 --------------------SFEQLQKLVSDEWQRNNTDLLSPGEEDTGRTTAEIIQDEVKDparcarLAEQFGISAllD 130
Cdd:PRK11147 80 egtvydfvaegieeqaeylkRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINE------VLAQLGLDP--D 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 131 RRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGI-------------TLVLVLNRfde 197
Cdd:PRK11147 152 AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIfishdrsfirnmaTRIVDLDR--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 198 ipefvqfaGVLA----DCTLSETGEKSSL----LQQALV-AQLAHSEKL--DGI----TLPEPDVPP------------- 249
Cdd:PRK11147 229 --------GKLVsypgNYDQYLLEKEEALrveeLQNAEFdRKLAQEEVWirQGIkarrTRNEGRVRAlkalrrerserre 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 250 ----ARHALADSAP--RIVLNDGVVSYN--DRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQgysndltl 320
Cdd:PRK11147 301 vmgtAKMQVEEASRsgKIVFEMENVNYQidGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQlQAD-------- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 321 fgrrrgSGETIWDIKKHIGYVS---SSLHLDYRVSTNV----RNVILSGyfdsigiyqavsDKQHKL--VQqwlDILGID 391
Cdd:PRK11147 373 ------SGRIHCGTKLEVAYFDqhrAELDPEKTVMDNLaegkQEVMVNG------------RPRHVLgyLQ---DFLFHP 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 392 KRtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGegatQLLFVSH 460
Cdd:PRK11147 432 KR-AMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQG----TVLLVSH 495
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-191 |
7.74e-13 |
|
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: 66.83 E-value: 7.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQklvsdew 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 84 QRnntdllspgeedtgRTTAEIIQDEVKDPARCARLAEQFGisalldrrfkyLSTGETRKTLLCQALMTDPQLLILDEPF 163
Cdd:cd03229 74 LR--------------RRIGMVFQDFALFPHLTVLENIALG-----------LSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180
....*....|....*....|....*....
gi 488984360 164 DGLDVNSRQQLAALLADLH-SAGITLVLV 191
Cdd:cd03229 129 SALDPITRREVRALLKSLQaQLGITVVLV 157
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
272-488 |
8.64e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 8.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 272 DRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgysndLTlfgrRRGSGETIW---DIKKHIGYVSSSL--- 345
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG---------LA----RPDAGEVLWqgePIRRQRDEYHQDLlyl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 346 -HLD--YRVSTNVRNVIlsgyfdsigIYQAVSDKQHK-LVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPT 421
Cdd:PRK13538 80 gHQPgiKTELTALENLR---------FYQRLHGPGDDeALWEALAQVGLAGF-EDVPVRQLSAGQQRRVALARLWLTRAP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 422 LLILDEPLQGLDplnRQLVRRFvdvligegaTQLLfvSHHAEDAPDCI--THRLAFVPSGDGYTYQLGP 488
Cdd:PRK13538 150 LWILDEPFTAID---KQGVARL---------EALL--AQHAEQGGMVIltTHQDLPVASDKVRKLRLGQ 204
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
225-460 |
9.83e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 70.24 E-value: 9.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 225 QALVAQLAHSEKLDGITLPEPDVP-PARHALADSAPRIVLNDGVVSYNDR--PVINHLSWTVNPGEHWQIVGPNGAGKST 301
Cdd:PRK11160 302 QHLGQVIASARRINEITEQKPEVTfPTTSTAAADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKST 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 302 LLSLVTG--DHPQGysnDLTLFGRR-RGSGETiwDIKKHIGYVSSSLHLdyrVSTNVRNVILsgyfdsIGIYQAvSDKQ- 377
Cdd:PRK11160 382 LLQLLTRawDPQQG---EILLNGQPiADYSEA--ALRQAISVVSQRVHL---FSATLRDNLL------LAAPNA-SDEAl 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 378 ---------HKLVQQ------WLDILGidkRTadapfhsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDplnRQLVRR 442
Cdd:PRK11160 447 ievlqqvglEKLLEDdkglnaWLGEGG---RQ-------LSGGEQRRLGIARALLHDAPLLLLDEPTEGLD---AETERQ 513
|
250 260
....*....|....*....|
gi 488984360 443 FVDVL--IGEGATqLLFVSH 460
Cdd:PRK11160 514 ILELLaeHAQNKT-VLMITH 532
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-191 |
1.27e-12 |
|
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: 67.13 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 10 TFRLSDTKT--LKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLVSDE----W 83
Cdd:cd03255 9 TYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRRHigfvF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 84 QRNNtdLLSpgeedtgRTTA--------EIIQDEVKD-PARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDP 154
Cdd:cd03255 89 QSFN--LLP-------DLTAlenvelplLLAGVPKKErRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984360 155 QLLILDEPFDGLDVNSRQQLAALLADL-HSAGITLVLV 191
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVV 197
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
12-191 |
1.40e-12 |
|
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: 66.89 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 12 RLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGqreshfsrvtRLSFEQlqKLVSDewqrnntdlL 91
Cdd:cd03301 9 RFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSG----------RIYIGG--RDVTD---------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 92 SPGEEDTG-----------RTTAEII----------QDEVKdpARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQAL 150
Cdd:cd03301 68 PPKDRDIAmvfqnyalyphMTVYDNIafglklrkvpKDEID--ERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984360 151 MTDPQLLILDEPFDGLDVNSRQQLAALLADLHSA-GITLVLV 191
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYV 187
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
24-213 |
1.49e-12 |
|
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: 66.76 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRE-SHFSRVTRLsfEQLQKLVSDEWQRN-NTDLLSPGE------ 95
Cdd:cd03263 23 LNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYiNGYSIRTDR--KAARQSLGYCPQFDaLFDELTVREhlrfya 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 96 EDTGRTTAEIIQDevkdparCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLA 175
Cdd:cd03263 101 RLKGLPKSEIKEE-------VELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIW 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984360 176 ALLADLhSAGITLVLVLNRFDEIPEFVQFAGVLADCTL 213
Cdd:cd03263 174 DLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-198 |
1.66e-12 |
|
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: 66.55 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 18 TLKIDHlsVAAGESWAFVGSNGSGKSALARALAG------------DLPLLSGQRESHFS---RVTRLSFEQLQkLVSDE 82
Cdd:cd03297 14 TLKIDF--DLNEEVTGIFGASGAGKSTLLRCIAGlekpdggtivlnGTVLFDSRKKINLPpqqRKIGLVFQQYA-LFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 83 WQRNNTDLLSPGEEDTgrttaeiiqdevKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEP 162
Cdd:cd03297 91 NVRENLAFGLKRKRNR------------EDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984360 163 FDGLDVNSRQQLAALLADLHSA-GITLVLVLNRFDEI 198
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEA 195
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
270-465 |
1.93e-12 |
|
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: 66.98 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 270 YNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGYSndlTLFGRRRGSGETIWDikKHIGYVSSSLHLd 348
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERPDSGT---ILFGGEDATDVPVQE--RNVGFVFQHYAL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 349 YRVSTNVRNVILsGYFDSIGIYQAVSDKQHKLVQQWLDILGIDKRTADAPfHSLSWGQ-QRLALiVRALVKHPTLLILDE 427
Cdd:cd03296 86 FRHMTVFDNVAF-GLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYP-AQLSGGQrQRVAL-ARALAVEPKVLLLDE 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984360 428 PLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDA 465
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEA 200
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
269-460 |
2.30e-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: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETIWD-------IKKHIGY 340
Cdd:COG1126 10 SFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLlEEPDS--------GTITVDGEDLTDskkdinkLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 341 V--SSSL--HLdyrvsTNVRNVILsgyfdsigiyqA------VSDKQ-HKLVQQWLDILGI-DKrtADA-PfHSLSWGQ- 406
Cdd:COG1126 82 VfqQFNLfpHL-----TVLENVTL-----------ApikvkkMSKAEaEERAMELLERVGLaDK--ADAyP-AQLSGGQq 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 407 QRLAlIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVLIG---EGATQLLfVSH 460
Cdd:COG1126 143 QRVA-IARALAMEPKVMLFDEPTSALDP---ELVGEVLDVMRDlakEGMTMVV-VTH 194
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-460 |
2.62e-12 |
|
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: 68.94 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 10 TFRLSDTKTLKIDHLS--VAAGESWAFVGSNGSGKSALARALAGDLP----------LLSGQReshfsrVTRLSFEQLQK 77
Cdd:COG4172 15 AFGQGGGTVEAVKGVSfdIAAGETLALVGESGSGKSVTALSILRLLPdpaahpsgsiLFDGQD------LLGLSERELRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 78 LvsdewqRNN----------TDL--LSPgeedTGRTTAEIIQ-------DEVKdpARCARLAEQFGISALLDRRFKY--- 135
Cdd:COG4172 89 I------RGNriamifqepmTSLnpLHT----IGKQIAEVLRlhrglsgAAAR--ARALELLERVGIPDPERRLDAYphq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 136 LSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADL-HSAGITLVLV---LN---RF-DEIpeFVQFAGV 207
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLIthdLGvvrRFaDRV--AVMRQGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 208 LAdctlsETGEKSSLL---QQALVAQLAHSEkldgitlPEPDVPPARhalADSAPRIVLNDGVVSYNDR----------- 273
Cdd:COG4172 235 IV-----EQGPTAELFaapQHPYTRKLLAAE-------PRGDPRPVP---PDAPPLLEARDLKVWFPIKrglfrrtvghv 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 274 PVINHLSWTVNPGEHWQIVGPNGAGKSTL----LSLVtgdhpqGYSNDLTLFGRR--RGSGETIWDIKKHIGYV-----S 342
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI------PSEGEIRFDGQDldGLSRRALRPLRRRMQVVfqdpfG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 343 SslhLDYRVStnVRNVILSGyfdsIGIYQ-AVSDKQH-KLVQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKH 419
Cdd:COG4172 374 S---LSPRMT--VGQIIAEG----LRVHGpGLSAAERrARVAEALEEVGLDPAARHRYPHEFSGGQrQRIA-IARALILE 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 488984360 420 PTLLILDEPLQGLD--------PLNRQLVRRFvdvligegatQL--LFVSH 460
Cdd:COG4172 444 PKLLVLDEPTSALDvsvqaqilDLLRDLQREH----------GLayLFISH 484
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-225 |
2.81e-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: 69.09 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 3 SLQISQGTFRLSDTKTLKIDHLS--VAAGESWAFVGSNGSGKSALARALAGDLPLLSGqreshfsrvtRLSFEQ--LQKL 78
Cdd:COG2274 473 DIELENVSFRYPGDSPPVLDNISltIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG----------RILIDGidLRQI 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 79 VSDEWQRN------NTDLLSpG--EE-----DTGRTTAEIIqdevkdpaRCARLA--EQFgISAL---LDRRF----KYL 136
Cdd:COG2274 543 DPASLRRQigvvlqDVFLFS-GtiREnitlgDPDATDEEII--------EAARLAglHDF-IEALpmgYDTVVgeggSNL 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 137 STGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLhSAGITLVLVLNRfdeiPEFVQFAG---VLADCTL 213
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHR----LSTIRLADriiVLDKGRI 687
|
250
....*....|..
gi 488984360 214 SETGEKSSLLQQ 225
Cdd:COG2274 688 VEDGTHEELLAR 699
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
263-456 |
2.95e-12 |
|
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: 65.92 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 263 LNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGR--RRGSGETIwdIKKHIGY 340
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPP-RSGSIRFDGRdiTGLPPHER--ARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 341 VSSSlhldyrvstnvRNVilsgyFDS--------IGIYQAVSDKQHKLVQQWLDILGIDKRTADAPFHSLSWGQQRLALI 412
Cdd:cd03224 80 VPEG-----------RRI-----FPEltveenllLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAI 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488984360 413 VRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLL 456
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILL 187
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
10-224 |
3.28e-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: 65.99 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 10 TFRLSDTKTLK-IDhLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLvsdewqRNNT 88
Cdd:cd03261 7 TKSFGGRTVLKgVD-LDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRL------RRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 89 ----------DLLSPGE------EDTGRTTAEIIQDEVKDparcaRLaEQFGISALLDRRFKYLSTGETRKTLLCQALMT 152
Cdd:cd03261 80 gmlfqsgalfDSLTVFEnvafplREHTRLSEEEIREIVLE-----KL-EAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984360 153 DPQLLILDEPFDGLD-VNSRqQLAALLADLHSA-GITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLLQ 224
Cdd:cd03261 154 DPELLLYDEPTAGLDpIASG-VIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-198 |
3.36e-12 |
|
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: 64.76 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQK----LVSDEwqrnntdllspgeedtg 99
Cdd:cd03215 21 FEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRagiaYVPED----------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 100 RTTAEIIQDEvkdparcaRLAEQFGISALLdrrfkylSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLA 179
Cdd:cd03215 84 RKREGLVLDL--------SVAENIALSSLL-------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIR 148
|
170
....*....|....*....
gi 488984360 180 DLHSAGITLVLVLNRFDEI 198
Cdd:cd03215 149 ELADAGKAVLLISSELDEL 167
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
261-474 |
3.50e-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: 66.02 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRP---VINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVtgdhpQGY---SNDLTLFGRRRGSGETIWDI 334
Cdd:cd03249 1 IEFKNVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL-----ERFydpTSGEILLDGVDIRDLNLRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 335 KKHIGYVSSSLHLdyrVSTNVRNVILSGYFDSIGIYQAVSDKQ---HKLVQQWLDilGIDKRTADAPFhSLSWGQ-QRLA 410
Cdd:cd03249 76 RSQIGLVSQEPVL---FDGTIAENIRYGKPDATDEEVEEAAKKaniHDFIMSLPD--GYDTLVGERGS-QLSGGQkQRIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984360 411 lIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIgEGATQLLfvshhaedapdcITHRLA 474
Cdd:cd03249 150 -IARALLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIV------------IAHRLS 199
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
274-463 |
4.56e-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: 65.68 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 274 PVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRR--RGSGETIWDIKKHIGYVSSSLHLdyr 350
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERPT--SGSVLVDGTDltLLSGKELRKARRRIGMIFQHFNL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 351 vstnvrnvilsgyFDSIGIYQAVS----------DKQHKLVQQWLDILGI-DKrtADAPFHSLSWGQ-QRLAlIVRALVK 418
Cdd:cd03258 94 -------------LSSRTVFENVAlpleiagvpkAEIEERVLELLELVGLeDK--ADAYPAQLSGGQkQRVG-IARALAN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984360 419 HPTLLILDEPLQGLDP--------LNRQLVRRFvdvligeGATqLLFVSHHAE 463
Cdd:cd03258 158 NPKVLLCDEATSALDPettqsilaLLRDINREL-------GLT-IVLITHEME 202
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
261-480 |
5.93e-12 |
|
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: 65.33 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYND--RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVtgdhPQGYsnDLTLfGRRRGSGETIWDIK--- 335
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI----PRFY--DVDS-GRILIDGHDVRDYTlas 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 336 --KHIGYVSSSLHLdyrVSTNVRNVILSGYFDsigiyqaVSDKQ----------HKLVQQWLDilGIDKRTADAPFhSLS 403
Cdd:cd03251 74 lrRQIGLVSQDVFL---FNDTVAENIAYGRPG-------ATREEveeaaraanaHEFIMELPE--GYDTVIGERGV-KLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984360 404 WGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIgEGATQLLfvshhaedapdcITHRLAFVPSGD 480
Cdd:cd03251 141 GGQrQRIA-IARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFV------------IAHRLSTIENAD 204
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
269-474 |
6.86e-12 |
|
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: 64.94 E-value: 6.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYN-DRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG--DHPQGYsndlTLFGRRRGSGETIWDIKKHIGYVSSSL 345
Cdd:cd03254 11 SYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfyDPQKGQ----ILIDGIDIRDISRKSLRSMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 346 HLdyrVSTNVR-NVILSGyfdsigiyqavSDKQHKLVQQWLDILGIDKRTADAP----------FHSLSWGQQRLALIVR 414
Cdd:cd03254 87 FL---FSGTIMeNIRLGR-----------PNATDEEVIEAAKEAGAHDFIMKLPngydtvlgenGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 415 ALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIgEGATQLLfvshhaedapdcITHRLA 474
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLM-KGRTSII------------IAHRLS 199
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
259-465 |
7.12e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.29 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 259 PRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDhPQGYSNDLTLFGRRRGSGETIWDIKKHI 338
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 339 GYVSSSLHLDYRVSTNvRNVILSGYFDSIGIYQAVSDKQHKLVQQWLDilgidKRTADApfHSLSWGQQRLALIVRALVK 418
Cdd:PRK11614 83 AIVPEGRRVFSRMTVE-ENLAMGGFFAERDQFQERIKWVYELFPRLHE-----RRIQRA--GTMSGGEQQMLAIGRALMS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984360 419 HPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLfVSHHAEDA 465
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFL-VEQNANQA 200
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-225 |
7.88e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.54 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 3 SLQISQGTFRLSDTKTLKIDHLS--VAAGESWAFVGSNGSGKSAL----ARAL---AGDLpLLSGQRESHFSRvtrlsfE 73
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSlqIKAGEKVALLGRTGCGKSTLlqllTRAWdpqQGEI-LLNGQPIADYSE------A 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 74 QLQKLVSDEWQRnnTDLLSpgeeDTGRTTAEIIQDEVKDPARCARLaEQFGISALLD-------------RRfkyLSTGE 140
Cdd:PRK11160 411 ALRQAISVVSQR--VHLFS----ATLRDNLLLAAPNASDEALIEVL-QQVGLEKLLEddkglnawlgeggRQ---LSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 141 TRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADlHSAGITLVLVLNRFDEIPEFVQFAgVLADCTLSETGEKS 220
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE-HAQNKTVLMITHRLTGLEQFDRIC-VMDNGQIIEQGTHQ 558
|
....*
gi 488984360 221 SLLQQ 225
Cdd:PRK11160 559 ELLAQ 563
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
261-470 |
8.37e-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: 63.22 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqgysndltlfgrrRGSGETIWDIKKhigy 340
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK-------------PDSGEILVDGKE---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 341 vssslhldyrvstnvrnVILSGYFDSI--GIYqavsdkqhkLVQQwldilgidkrtadapfhsLSWGQQRLALIVRALVK 418
Cdd:cd03216 64 -----------------VSFASPRDARraGIA---------MVYQ------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488984360 419 HPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSHHAEDAP---DCIT 470
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLRAQGVA-VIFISHRLDEVFeiaDRVT 153
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
269-440 |
9.15e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.42 E-value: 9.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLL----SLVTGDHPQGysNDLTLFGRR-RGSGETIWDIKK---HIGY 340
Cdd:PRK09984 13 TFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAG--SHIELLGRTvQREGRLARDIRKsraNTGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 341 VSSSLHLDYRVSTnVRNVILsGYFDSIGIYQAV------SDKQHKLvqQWLDILGIdKRTADAPFHSLSWGQQRLALIVR 414
Cdd:PRK09984 91 IFQQFNLVNRLSV-LENVLI-GALGSTPFWRTCfswftrEQKQRAL--QALTRVGM-VHFAHQRVSTLSGGQQQRVAIAR 165
|
170 180
....*....|....*....|....*.
gi 488984360 415 ALVKHPTLLILDEPLQGLDPLNRQLV 440
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIV 191
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-233 |
1.17e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGdlpllsgqreshFSRVTRLSFEQLQKLVSDEWQRNNTDLLsPGEEDTGRTTA 103
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMG------------FVRLASGKISILGQPTRQALQKNLVAYV-PQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 104 EIIQDEV----------------KDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLD 167
Cdd:PRK15056 95 VLVEDVVmmgryghmgwlrrakkRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 168 VNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTL----SETGEKSSLLQQALVAQLAH 233
Cdd:PRK15056 175 VKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLasgpTETTFTAENLELAFSGVLRH 244
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
271-480 |
1.20e-11 |
|
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: 63.00 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 271 NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQGysndltlfGRRRGSGETI--WD---IKKHIGYVSSS 344
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLlRPTS--------GRVRLDGADIsqWDpneLGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 345 LHLdyrVSTNVRNVILSGyfdsigiyqavsdkqhklvqqwldilgidkrtadapfhslswGQ-QRLALiVRALVKHPTLL 423
Cdd:cd03246 85 DEL---FSGSIAENILSG------------------------------------------GQrQRLGL-ARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 424 ILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLfvshhaedapdcITHRLAFVPSGD 480
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIV------------IAHRPETLASAD 163
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
271-435 |
1.28e-11 |
|
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: 64.21 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 271 NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGY--SNDLTLFGRRRGSGETiwdiKKHIGYVSSSlhlD 348
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttSGQILFNGQPRKPDQF----QKCVAYVRQD---D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 349 YRVST-NVRNVIlsgYFDSIGIYQAVSDK--QHKLVQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLIL 425
Cdd:cd03234 91 ILLPGlTVRETL---TYTAILRLPRKSSDaiRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170
....*....|
gi 488984360 426 DEPLQGLDPL 435
Cdd:cd03234 168 DEPTSGLDSF 177
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
224-440 |
1.39e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.79 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 224 QQALVAQLAHSEKLDgitLPEPDVPPARHALADSAP-RIVLNDGVV-SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKST 301
Cdd:PRK11174 315 AQAVGAAESLVTFLE---TPLAHPQQGEKELASNDPvTIEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTS 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 302 LLSLVTGDHPqgYSNDLTLFGRR-RGSGETIWdiKKHIGYVSSSLHLdyrVSTNVRNVILSGYFDS--IGIYQAVSDKQh 378
Cdd:PRK11174 392 LLNALLGFLP--YQGSLKINGIElRELDPESW--RKHLSWVGQNPQL---PHGTLRDNVLLGNPDAsdEQLQQALENAW- 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984360 379 klVQQWLDIL--GIDKRTADAPFhSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLV 440
Cdd:PRK11174 464 --VSEFLPLLpqGLDTPIGDQAA-GLSVGQaQRLAL-ARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
269-465 |
1.41e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 65.74 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETIWDI---KKHIGYVSSS 344
Cdd:PRK09452 23 SFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfETPDS--------GRIMLDGQDITHVpaeNRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 345 LHLdyrvstnvrnvilsgyFDSIGIYQAVSdkqHKLVQQWLDILGIDKRTADA-------------PfHSLSWGQQRLAL 411
Cdd:PRK09452 95 YAL----------------FPHMTVFENVA---FGLRMQKTPAAEITPRVMEAlrmvqleefaqrkP-HQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984360 412 IVRALVKHPTLLILDEPLQGLD------------PLNRQLVRRFVdvligegatqllFVSHHAEDA 465
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDyklrkqmqnelkALQRKLGITFV------------FVTHDQEEA 208
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
267-479 |
2.04e-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: 66.96 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 267 VVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRGSgeTIWDIKKHIGYVSSSLH 346
Cdd:TIGR01257 1946 VYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVT-SGDATVAGKSILT--NISDVHQNMGYCPQFDA 2022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 347 LDYrvstnvrnvILSGYfDSIGIY---QAVSDKQHKLVQQW-LDILGIdKRTADAPFHSLSWGQQRLALIVRALVKHPTL 422
Cdd:TIGR01257 2023 IDD---------LLTGR-EHLYLYarlRGVPAEEIEKVANWsIQSLGL-SLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 423 LILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLfVSHHAEDApDCITHRLAFVPSG 479
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL-TSHSMEEC-EALCTRLAIMVKG 2146
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
24-197 |
2.25e-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: 63.54 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEqLQKLVSDEWQRNNTDllspgEEDTGRTTA 103
Cdd:cd03265 21 FRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLSVD-----DELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 104 EII-------QDEVKDpaRCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAA 176
Cdd:cd03265 95 YIHarlygvpGAERRE--RIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWE 172
|
170 180
....*....|....*....|..
gi 488984360 177 LLADLHSA-GITLVLVLNRFDE 197
Cdd:cd03265 173 YIEKLKEEfGMTILLTTHYMEE 194
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
242-465 |
2.69e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 65.24 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 242 LPEPDvPPARHALAdsaPRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgysndltl 320
Cdd:PRK11607 5 IPRPQ-AKTRKALT---PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPT-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 321 fgrrrgSGETIWDikkhigYVSSSLHLDYRVSTNVrnvILSGY--FDSIGIYQ--AVSDKQHKL--------VQQWLDIL 388
Cdd:PRK11607 73 ------AGQIMLD------GVDLSHVPPYQRPINM---MFQSYalFPHMTVEQniAFGLKQDKLpkaeiasrVNEMLGLV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 389 GIDKRTADAPfHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLD-PLNRQLVRRFVDVLIGEGATQLLfVSHHAEDA 465
Cdd:PRK11607 138 HMQEFAKRKP-HQLSGGQrQRVAL-ARSLAKRPKLLLLDEPMGALDkKLRDRMQLEVVDILERVGVTCVM-VTHDQEEA 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-183 |
2.96e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 64.72 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 3 SLQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQ------ 76
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKvgfvfq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 77 -------KLVSDEWQRNNTDLlsPGEEdtgRTTAEIIQDEVkdparcARLAEQFGISALLDRRFKYLSTGETRKTLLCQA 149
Cdd:PRK10851 82 hyalfrhMTVFDNIAFGLTVL--PRRE---RPNAAAIKAKV------TQLLEMVQLAHLADRYPAQLSGGQKQRVALARA 150
|
170 180 190
....*....|....*....|....*....|....
gi 488984360 150 LMTDPQLLILDEPFDGLDVNSRQQLAALLADLHS 183
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHE 184
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-230 |
3.01e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.99 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSD-TKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGdlpLLSGQReshfSRVTRLSFEQLQKlvSDE 82
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNG---IYLPQR----GRVKVMGREVNAE--NEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 83 WQRNNTDLL----------SPGEEDT--GRTTAEIIQDEVKDPARCARLAeqFGISALLDRRFKYLSTGETRKTLLCQAL 150
Cdd:PRK13647 76 WVRSKVGLVfqdpddqvfsSTVWDDVafGPVNMGLDKDEVERRVEEALKA--VRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 151 MTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLLQQALVAQ 230
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-223 |
3.63e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.86 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 1 MSSLQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLVS 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 81 DEWQRNNTDLLSPGEE--DTGRT--TAEIIQDEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQL 156
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQvvEMGRTphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 157 LILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLL 223
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
268-438 |
3.92e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.11 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 268 VSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLL-SLVTGDHPQG-----YSNDLTLFGRRRgsgetiwdIKKHIGYV 341
Cdd:PRK11231 10 VGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLkCFARLLTPQSgtvflGDKPISMLSSRQ--------LARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 342 SSSLHLDYRVStnVRNVILSGYFDSIGIYQAVSDKQHKLVQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPT 421
Cdd:PRK11231 82 PQHHLTPEGIT--VRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINH-LADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170
....*....|....*..
gi 488984360 422 LLILDEPLQGLDpLNRQ 438
Cdd:PRK11231 159 VVLLDEPTTYLD-INHQ 174
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
276-464 |
4.00e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 63.65 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 276 INHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYS----NDLTLFGRRRGsgETIWDIKKHIGYV----SSSLHL 347
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGtvtvDDITITHKTKD--KYIRPVRKRIGMVfqfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 348 DyrvstNVRNVILSGYFDSIGIYQAVSDKQHKLVQQwldiLGIDKRT-ADAPFHsLSWGQQRLALIVRALVKHPTLLILD 426
Cdd:PRK13646 101 D-----TVEREIIFGPKNFKMNLDEVKNYAHRLLMD----LGFSRDVmSQSPFQ-MSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984360 427 EPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAED 464
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNE 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
268-472 |
4.99e-11 |
|
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: 62.69 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 268 VSYNDRPVINHLSWTVNPGEhwqIV---GPNGAGKSTLLSLVTGDHPqgysndltlfgRRRGS----GETIWDIKKH--- 337
Cdd:COG0410 11 AGYGGIHVLHGVSLEVEEGE---IVallGRNGAGKTTLLKAISGLLP-----------PRSGSirfdGEDITGLPPHria 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 338 ---IGYVS------SSLhldyrvstNVR-NVILSGYFdsigiyQAVSDKQHKLVQQWLD---ILGiDKRTADApfHSLSW 404
Cdd:COG0410 77 rlgIGYVPegrrifPSL--------TVEeNLLLGAYA------RRDRAEVRADLERVYElfpRLK-ERRRQRA--GTLSG 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 405 GQQR-LAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLfVSHHAEDAPDcITHR 472
Cdd:COG0410 140 GEQQmLA-IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILL-VEQNARFALE-IADR 205
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
279-456 |
5.33e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.22 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 279 LSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQGYSndLTLFGRRRgSGETIWDIKKHIGYV---------SSSLHLD 348
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYlPQRGR--VKVMGREV-NAENEKWVRSKVGLVfqdpddqvfSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 349 yrVSTNVRNVILSGyfdsigiyqavsDKQHKLVQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEP 428
Cdd:PRK13647 101 --VAFGPVNMGLDK------------DEVERRVEEALKAVRMWDFRDKPPYH-LSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180
....*....|....*....|....*...
gi 488984360 429 LQGLDPLNRQLVRRFVDVLIGEGATQLL 456
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLHNQGKTVIV 193
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
279-468 |
5.53e-11 |
|
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: 62.45 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 279 LSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFG------------RRRGsgetiwdikKHIGYVSSSL 345
Cdd:COG4181 31 ISLEVEAGESVAIVGASGSGKSTLLGLLAGlDRPT--SGTVRLAGqdlfaldedaraRLRA---------RHVGFVFQSF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 346 HLdyrVS--TNVRNVI----LSGYFDSigiyqavsdkqHKLVQQWLDILGIDKRTADAPfHSLSWG-QQRLAlIVRALVK 418
Cdd:COG4181 100 QL---LPtlTALENVMlpleLAGRRDA-----------RARARALLERVGLGHRLDHYP-AQLSGGeQQRVA-LARAFAT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984360 419 HPTLLILDEPLQGLDPLNRQLVrrfVDVLIG---EGATQLLFVSHHAEDAPDC 468
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQI---IDLLFElnrERGTTLVLVTHDPALAARC 213
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-225 |
7.82e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.87 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 23 HLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLS----FEQLQKLVSDEWQRNNTDLLspgeEDT 98
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRPVRKRIGMVFQFPESQLF----EDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 99 grTTAEII---------QDEVKDpaRCARLAEQFGISA-LLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDV 168
Cdd:PRK13646 103 --VEREIIfgpknfkmnLDEVKN--YAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984360 169 NSRQQLAALLADLH-SAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLLQQ 225
Cdd:PRK13646 179 QSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
269-451 |
8.01e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.22 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYSN------DLTLFG----RRRGsgetiwdikkhI 338
Cdd:PRK10895 12 AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddeDISLLPlharARRG-----------I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 339 GYVSSSLHLDYRVStnvrnvILSGYFDSIGIYQAVSDKQHK-LVQQWLDILGIDkRTADAPFHSLSWGQQRLALIVRALV 417
Cdd:PRK10895 81 GYLPQEASIFRRLS------VYDNLMAVLQIRDDLSAEQREdRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190
....*....|....*....|....*....|....
gi 488984360 418 KHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEG 451
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSG 187
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
24-191 |
8.20e-11 |
|
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: 61.92 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGqreshfsrvtRLSFEqlqklvsdewqrnntdllspGEEDTGRTTA 103
Cdd:COG0410 24 LEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSG----------SIRFD--------------------GEDITGLPPH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 104 EIIQ------------------------------DEVKDPARCARLAEQFGIsaLLDRRFK---YLSTGEtRKTL-LCQA 149
Cdd:COG0410 74 RIARlgigyvpegrrifpsltveenlllgayarrDRAEVRADLERVYELFPR--LKERRRQragTLSGGE-QQMLaIGRA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984360 150 LMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLV 191
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLV 192
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
275-460 |
8.67e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 61.76 E-value: 8.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 275 VINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGR--RRGSGETIWDIKKH-IGYVSSSLHL--D 348
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGlDTPT--SGDVIFNGQpmSKLSSAAKAELRNQkLGFIYQFHHLlpD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 349 YRVSTNVRNVILSGyfdsigiyQAVSDKQHKLVQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEP 428
Cdd:PRK11629 102 FTALENVAMPLLIG--------KKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|..
gi 488984360 429 LQGLDPLNRQLVRRFVDVLIGEGATQLLFVSH 460
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTH 204
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
273-434 |
8.71e-11 |
|
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: 61.03 E-value: 8.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 273 RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQGYSNDLTLFGRRRGSGEtiwdIKKHIGYVssslhldyrv 351
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrTGLGVSGEVLINGRPLDKRS----FRKIIGYV---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 352 stnVRNVILSGYFDsigiyqavsdkqhklVQQWLDIlgidkrtaDAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQG 431
Cdd:cd03213 88 ---PQDDILHPTLT---------------VRETLMF--------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
...
gi 488984360 432 LDP 434
Cdd:cd03213 142 LDS 144
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
261-460 |
8.94e-11 |
|
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: 61.81 E-value: 8.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgySNDLTLFGRRRGS----GETIWDIKK 336
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNR------LNDLIPGAPDEGEvlldGKDIYDLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 337 HIgyvsssLHLDYRVSTnVR---NVILSGYFDSIGI---YQAVSDKQ--HKLVQQWLDILGIDKRTAD-APFHSLSWGQ- 406
Cdd:cd03260 75 DV------LELRRRVGM-VFqkpNPFPGSIYDNVAYglrLHGIKLKEelDERVEEALRKAALWDEVKDrLHALGLSGGQq 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488984360 407 QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRfvdvLIGEGATQL--LFVSH 460
Cdd:cd03260 148 QRLC-LARALANEPEVLLLDEPTSALDPISTAKIEE----LIAELKKEYtiVIVTH 198
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
271-465 |
9.44e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 62.41 E-value: 9.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 271 NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHP--QGY----SNDLTlfgrrrgsGETIWDIKKHIGYV--- 341
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPpdSGSilidGKDVT--------KLPEYKRAKYIGRVfqd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 342 -----SSS------LHLDYRvstnvRNvilsgyfDSIGIYQAVSDKQHKLVQQWLDIL--GIDKRTaDAPFHSLSWGQ-Q 407
Cdd:COG1101 89 pmmgtAPSmtieenLALAYR-----RG-------KRRGLRRGLTKKRRELFRELLATLglGLENRL-DTKVGLLSGGQrQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984360 408 RLALIVrALVKHPTLLILDEPLQGLDP--------LNRQLVRRFvdvligegatQL--LFVSHHAEDA 465
Cdd:COG1101 156 ALSLLM-ATLTKPKLLLLDEHTAALDPktaalvleLTEKIVEEN----------NLttLMVTHNMEQA 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
276-466 |
1.10e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.56 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 276 INHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG------------DHPQGYSndltlfgrRRGsgetIWDIKKHIGYV-- 341
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGilkpssgrilfdGKPIDYS--------RKG----LMKLRESVGMVfq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 342 -------SSSLHLDyrVSTNVRNVILSgyfdsigiyqavSDKQHKLVQQWLDILGIDkRTADAPFHSLSWGQQRLALIVR 414
Cdd:PRK13636 90 dpdnqlfSASVYQD--VSFGAVNLKLP------------EDEVRKRVDNALKRTGIE-HLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984360 415 ALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDAP 466
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVP 206
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-474 |
1.21e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARAL-------AGDL---PLLSGQRESHFSRVTRLSFEQLQKLVSDE----WQRNNTD 89
Cdd:PRK10261 37 FSLQRGETLAIVGESGSGKSVTALALmrlleqaGGLVqcdKMLLRRRSRQVIELSEQSAAQMRHVRGADmamiFQEPMTS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 90 L---LSPGEE--DTGRTTAEIIQDEVKDPARcaRLAEQFGI---SALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDE 161
Cdd:PRK10261 117 LnpvFTVGEQiaESIRLHQGASREEAMVEAK--RMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 162 PFDGLDVNSRQQLAALLADLH---SAGITLV-----LVLNRFDEIPEFVQFAGVladctlsETGEKSSLLQ-------QA 226
Cdd:PRK10261 195 PTTALDVTIQAQILQLIKVLQkemSMGVIFIthdmgVVAEIADRVLVMYQGEAV-------ETGSVEQIFHapqhpytRA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 227 LVAQLAHSEKLDGITLP-----------EPDVPPA-RHALADSAP---------RIVLNDGVVSYNDRPV--INHLSWTV 283
Cdd:PRK10261 268 LLAAVPQLGAMKGLDYPrrfplislehpAKQEPPIeQDTVVDGEPilqvrnlvtRFPLRSGLLNRVTREVhaVEKVSFDL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 284 NPGEHWQIVGPNGAGKST----LLSLVtgdhpQGYSNDLTLFGRRRG--SGETIWDIKKHIGYVSSslhlDYRVSTNVRN 357
Cdd:PRK10261 348 WPGETLSLVGESGSGKSTtgraLLRLV-----ESQGGEIIFNGQRIDtlSPGKLQALRRDIQFIFQ----DPYASLDPRQ 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 358 VILSGYFDSIGIYQAVS-DKQHKLVQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLN 436
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
490 500 510
....*....|....*....|....*....|....*....
gi 488984360 437 R-QLVRRFVDvLIGEGATQLLFVSHHAEdAPDCITHRLA 474
Cdd:PRK10261 499 RgQIINLLLD-LQRDFGIAYLFISHDMA-VVERISHRVA 535
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-224 |
1.30e-10 |
|
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: 60.62 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDlpllsgqresHFSRVTR----LSFEQLQKLV 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH----------PKYEVTEgeilFKGEDITDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 80 SDE---------WQrnntdllSPgEEDTGRTTAEIIQDevkdparcarLAEQFgisalldrrfkylSTGETRKTLLCQAL 150
Cdd:cd03217 71 PEErarlgiflaFQ-------YP-PEIPGVKNADFLRY----------VNEGF-------------SGGEKKRNEILQLL 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984360 151 MTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNRfDEIPEFVQ--FAGVLADCTLSETGEKSSLLQ 224
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY-QRLLDYIKpdRVHVLYDGRIVKSGDKELALE 194
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
256-470 |
1.36e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.27 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 256 DSAPRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTgdhpqgysndlTLFGRRRGS----GETI 331
Cdd:PRK10247 3 ENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVA-----------SLISPTSGTllfeGEDI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 332 WDIKKHIgyvssslhldYR--VSTNVRNVILSG---YFDSIGIYQAVSDK-QHKLVQQWLDILGIDKRTADAPFHSLSWG 405
Cdd:PRK10247 72 STLKPEI----------YRqqVSYCAQTPTLFGdtvYDNLIFPWQIRNQQpDPAIFLDDLERFALPDTILTKNIAELSGG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 406 Q-QRLALIvRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAED---APDCIT 470
Cdd:PRK10247 142 EkQRISLI-RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEinhADKVIT 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
261-465 |
1.68e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 62.47 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETiWDI----- 334
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETPDS--------GRIVLNGRD-LFTnlppr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 335 KKHIGYVSSS--L--HLDyrVSTNVrnvilsgyfdSIGIYQAVSDKQ--HKLVQQWLDILGID---KRTadaPfHSLSWG 405
Cdd:COG1118 74 ERRVGFVFQHyaLfpHMT--VAENI----------AFGLRVRPPSKAeiRARVEELLELVQLEglaDRY---P-SQLSGG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984360 406 Q-QRLALIvRALVKHPTLLILDEPLQGLD----PLNRQLVRRFVDVLigEGATqlLFVSHHAEDA 465
Cdd:COG1118 138 QrQRVALA-RALAVEPEVLLLDEPFGALDakvrKELRRWLRRLHDEL--GGTT--VFVTHDQEEA 197
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
291-474 |
1.75e-10 |
|
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: 62.43 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 291 IVGPNGAGKSTLLSLVTG-DHP-QGY--SNDLTLFGRRRGsgetIWdIKKH---IGYV--SSSLHLDYRVSTNVRnvils 361
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAGlERPdSGRirLGGEVLQDSARG----IF-LPPHrrrIGYVfqEARLFPHLSVRGNLL----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 362 gYfdsiGIYQAVSDKQHKLVQQWLDILGI----DKRTadapfHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLN 436
Cdd:COG4148 100 -Y----GRKRAPRAERRISFDEVVELLGIghllDRRP-----ATLSGGErQRVA-IGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984360 437 RQLVRRFVDVLIGEGATQLLFVSHhaedAPDCIThRLA 474
Cdd:COG4148 169 KAEILPYLERLRDELDIPILYVSH----SLDEVA-RLA 201
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
256-465 |
1.88e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 61.55 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 256 DSAPRIVLNDGVVSYND--RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQgySNDLTLFGRRRgSGETIW 332
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLlKPQ--SGEIKIDGITI-SKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 333 DIKKHIG---------YVSSSLHLDYRVSTNVRNVilsgyfdsigiyqaVSDKQHKLVQQWLDILGIDKRTADAPfHSLS 403
Cdd:PRK13632 80 EIRKKIGiifqnpdnqFIGATVEDDIAFGLENKKV--------------PPKKMKDIIDDLAKKVGMEDYLDKEP-QNLS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984360 404 WGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDA 465
Cdd:PRK13632 145 GGQkQRVA-IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA 206
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-197 |
1.88e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.16 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 1 MSSLQISQGTFRLSDTKTLKIDHLS--VAAGESWAFVGSNGSGKSALARAL-------AGDLPLLSGQ--RESHFSRVTR 69
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSftVASGECFGLLGPNGAGKSTIARMIlgmtspdAGKITVLGVPvpARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 70 LSFEQLQKLVSDEWQRNNtdLLSPGEedTGRTTAEIIQDEVKDPARCARLAEQfgisalLDRRFKYLSTGETRKTLLCQA 149
Cdd:PRK13536 117 GVVPQFDNLDLEFTVREN--LLVFGR--YFGMSTREIEAVIPSLLEFARLESK------ADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488984360 150 LMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNRFDE 197
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEE 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
257-488 |
2.01e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.65 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 257 SAPRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVT--GDHPQGY--SNDLTLFGRRRGSGETIW 332
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmNDKVSGYrySGDVLLGGRSIFNYRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 333 DIKKHIGYVssslhldYRVSTNVRNVILSGYFDSIGIYQAVSDKQHK-LVQQWLDILG----IDKRTADAPFHsLSWGQQ 407
Cdd:PRK14271 98 EFRRRVGML-------FQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRgVAQARLTEVGlwdaVKDRLSDSPFR-LSGGQQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 408 RLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEgaTQLLFVSHHAEDAPDcITHRLAFVpsGDGYTYQLG 487
Cdd:PRK14271 170 QLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAAR-ISDRAALF--FDGRLVEEG 244
|
.
gi 488984360 488 P 488
Cdd:PRK14271 245 P 245
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
261-480 |
2.23e-10 |
|
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: 60.71 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYND-RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLvtgdhpqgysndltLF-------GRRRGSGETIW 332
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRL--------------LFrfydvssGSILIDGQDIR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 333 DIK-----KHIGYVSSSLHLdyrVSTNVRNVILSGYFDS--IGIYQAVSDKQ-HKLVQQWLD----ILGidKRTAdapfh 400
Cdd:cd03253 67 EVTldslrRAIGVVPQDTVL---FNDTIGYNIRYGRPDAtdEEVIEAAKAAQiHDKIMRFPDgydtIVG--ERGL----- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 401 SLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLN-RQLVRRFVDVLigEGATQLLfvshhaedapdcITHRLAFVPS 478
Cdd:cd03253 137 KLSGGEkQRVA-IARAILKNPPILLLDEATSALDTHTeREIQAALRDVS--KGRTTIV------------IAHRLSTIVN 201
|
..
gi 488984360 479 GD 480
Cdd:cd03253 202 AD 203
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
263-481 |
2.27e-10 |
|
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: 60.62 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 263 LNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRGSGETIWDIKKHIGYVS 342
Cdd:TIGR03410 3 VSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVK-SGSIRLDGEDITKLPPHERARAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 343 ------SSLhldyrvstNVRNVILSGYfdsigiyQAVSDKQHKLVQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRA 415
Cdd:TIGR03410 82 qgreifPRL--------TVEENLLTGL-------AALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQqQQLA-IARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984360 416 LVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHH---AEDAPD--CITHRLAFVPSGDG 481
Cdd:TIGR03410 146 LVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYldfARELADryYVMERGRVVASGAG 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
261-465 |
2.63e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.85 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfgrrrgsGETIWDikkhig 339
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGlETPSA--------------GELLAG------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 340 yvSSSLHlDYRVSTNV----------RNVIlsgyfDSIGIyqAVSDKQHKLVQQWLDILGIDKRTADAPfHSLSWGQ-QR 408
Cdd:PRK11247 73 --TAPLA-EAREDTRLmfqdarllpwKKVI-----DNVGL--GLKGQWRDAALQALAAVGLADRANEWP-AALSGGQkQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 409 LALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDA 465
Cdd:PRK11247 142 VAL-ARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEA 197
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-190 |
3.14e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 61.28 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRE---SHFSRVTRLSF----------------EQLQKLVSdewq 84
Cdd:COG4152 22 FTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgEPLDPEDRRRIgylpeerglypkmkvgEQLVYLAR---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 85 rnntdlLspgeedTGRTTAEIIQdevkdpaRCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFD 164
Cdd:COG4152 98 ------L------KGLSKAEAKR-------RADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180
....*....|....*....|....*..
gi 488984360 165 GLD-VNsRQQLAALLADLHSAGITLVL 190
Cdd:COG4152 159 GLDpVN-VELLKDVIRELAAKGTTVIF 184
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
282-461 |
3.29e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.96 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 282 TVNPGE-HwQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRgSGETIWDIKKH-IGYVSSSLHL--DYRVSTNV-- 355
Cdd:COG1129 26 ELRPGEvH-ALLGENGAGKSTLMKILSGVYQPD-SGEILLDGEPV-RFRSPRDAQAAgIAIIHQELNLvpNLSVAENIfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 356 -RNVILSGYFDsigiyqavSDKQHKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
Cdd:COG1129 103 gREPRRGGLID--------WRAMRRRARELLARLGLDID-PDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTE 173
|
170 180 190
....*....|....*....|....*....|..
gi 488984360 435 -----LNRqLVRRFVDvligEGATqLLFVSHH 461
Cdd:COG1129 174 reverLFR-IIRRLKA----QGVA-IIYISHR 199
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
145-463 |
3.43e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.22 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 145 LLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSagiTLVLV------LNR---------FDEI---P----EFV 202
Cdd:PRK15064 165 LLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNS---TMIIIshdrhfLNSvcthmadldYGELrvyPgnydEYM 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 203 QFAGVLADCTLSETGEKSSLLQ--QALV---------AQLAHS--EKLDGITLPEpdVPPA----------------RHA 253
Cdd:PRK15064 242 TAATQARERLLADNAKKKAQIAelQSFVsrfsanaskAKQATSraKQIDKIKLEE--VKPSsrqnpfirfeqdkklhRNA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 254 LadsapriVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgysndltlfgrrrGSGETIWD 333
Cdd:PRK15064 320 L-------EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEP-------------DSGTVKWS 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 334 IKKHIGYVSSSLHLDYRVSTNVrnvilsgyFDSIGIYQAVSDKQhklvQQWLDILG--------IDKrtadaPFHSLSWG 405
Cdd:PRK15064 380 ENANIGYYAQDHAYDFENDLTL--------FDWMSQWRQEGDDE----QAVRGTLGrllfsqddIKK-----SVKVLSGG 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984360 406 QQRLALIVRALVKHPTLLILDEPLQGLD-----PLNRQLvRRFvdvligEGAtqLLFVSHHAE 463
Cdd:PRK15064 443 EKGRMLFGKLMMQKPNVLVMDEPTNHMDmesieSLNMAL-EKY------EGT--LIFVSHDRE 496
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
261-434 |
3.57e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 60.53 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLL-SLVTGDHPQGYS---NDLTLFGRRRGSGET--IWDI 334
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLrCINLLEQPEAGTirvGDITIDTARSLSQQKglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 335 KKHIGYVSSSLHLdYRVSTNVRNVILSgyfdSIGIYQAVSDKQHKLVQQWLDILGIDKRTADAPfHSLSWGQQRLALIVR 414
Cdd:PRK11264 84 RQHVGFVFQNFNL-FPHRTVLENIIEG----PVIVKGEPKEEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIAR 157
|
170 180
....*....|....*....|
gi 488984360 415 ALVKHPTLLILDEPLQGLDP 434
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDP 177
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
19-190 |
3.85e-10 |
|
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: 59.51 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 19 LKIDHLSVAAGESWAF--------------VGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRlSFEQLQKLVSDEWQ 84
Cdd:cd03264 1 LQLENLTKRYGKKRALdgvsltlgpgmyglLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 85 RNNTDLLSPGEE--DTGRTTAEIIQDEVKdpARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEP 162
Cdd:cd03264 80 EFGVYPNFTVREflDYIAWLKGIPSKEVK--ARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180
....*....|....*....|....*...
gi 488984360 163 FDGLDVNSRQQLAALLADLhSAGITLVL 190
Cdd:cd03264 158 TAGLDPEERIRFRNLLSEL-GEDRIVIL 184
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-225 |
4.40e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 60.08 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSDTKTLK-IDhLSVAAGESWAFVGSNGSGKSALARALAGdlpllsgqRESHfsRVT----RLSFEQLQKL 78
Cdd:COG0396 1 LEIKNLHVSVEGKEILKgVN-LTIKPGEVHAIMGPNGSGKSTLAKVLMG--------HPKY--EVTsgsiLLDGEDILEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 79 VSDE---------WQR-------NNTDLLspgeedtgRTTAEIIQDEVKDPA----RCARLAEQFGISA-LLDRrfkYL- 136
Cdd:COG0396 70 SPDEraragiflaFQYpveipgvSVSNFL--------RTALNARRGEELSAReflkLLKEKMKELGLDEdFLDR---YVn 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 137 ---STGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLV--LNRF-DEI-PEFVQfagVLA 209
Cdd:COG0396 139 egfSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIIthYQRIlDYIkPDFVH---VLV 215
|
250
....*....|....*.
gi 488984360 210 DCTLSETGEKsSLLQQ 225
Cdd:COG0396 216 DGRIVKSGGK-ELALE 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
270-471 |
5.08e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.98 E-value: 5.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 270 YNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHP-QG--YSNDLTLFGRRRGSGETIWDIKKHIGYVSSSL 345
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFlEKPsEGsiVVNGQTINLVRDKDGQLKVADKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 346 -----HLDYRVSTNVRNVILSGYFDSIGIYQAVSDKQhklVQQWLDILGIDKRTADA-PFHsLSWGQQRLALIVRALVKH 419
Cdd:PRK10619 95 tmvfqHFNLWSHMTVLENVMEAPIQVLGLSKQEARER---AVKYLAKVGIDERAQGKyPVH-LSGGQQQRVSIARALAME 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984360 420 PTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSHHAEDAPDCITH 471
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFARHVSSH 221
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
279-433 |
5.50e-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: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 279 LSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqgYSNDLTLFGRRRGSgetiWDIK---KHIGYVSSslhldyrvstNV 355
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP--GQGEILLNGRPLSD----WSAAelaRHRAYLSQ----------QQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 356 RNVILSGYFDSIGIYQ---AVSDKQHKLVQQWLDILGIDKRTAdAPFHSLSWG-QQRLALIVRALVKHPT------LLIL 425
Cdd:COG4138 79 SPPFAMPVFQYLALHQpagASSEAVEQLLAQLAEALGLEDKLS-RPLTQLSGGeWQRVRLAAVLLQVWPTinpegqLLLL 157
|
....*...
gi 488984360 426 DEPLQGLD 433
Cdd:COG4138 158 DEPMNSLD 165
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
291-460 |
5.57e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 60.66 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 291 IVGPNGAGKSTLLSLVTG-DHPQ-GYS--NDLTLFGRRRGsgetIW--DIKKHIGYV--SSSLHLDYRVSTNVR---NVI 359
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGlTRPQkGRIvlNGRVLFDAEKG----IClpPEKRRIGYVfqDARLFPHYKVRGNLRygmAKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 360 LSGYFDSIgiyqavsdkqhklvqqwLDILGIDKRTADAPfHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD-PLNR 437
Cdd:PRK11144 105 MVAQFDKI-----------------VALLGIEPLLDRYP-GSLSGGEkQRVA-IGRALLTAPELLLMDEPLASLDlPRKR 165
|
170 180
....*....|....*....|...
gi 488984360 438 QLVrRFVDVLIGEGATQLLFVSH 460
Cdd:PRK11144 166 ELL-PYLERLAREINIPILYVSH 187
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
261-465 |
5.64e-10 |
|
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: 59.19 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETIWDI---KK 336
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGlEEPTS--------GRIYIGGRDVTDLppkDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 337 HIGYV--SSSLHLDYRVSTNVrnvilsgyfdSIGIYQAVSDKQH--KLVQQWLDILGIDKRTADAPfHSLSWGQ-QRLAL 411
Cdd:cd03301 73 DIAMVfqNYALYPHMTVYDNI----------AFGLKLRKVPKDEidERVREVAELLQIEHLLDRKP-KQLSGGQrQRVAL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488984360 412 iVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDA 465
Cdd:cd03301 142 -GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEA 194
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-191 |
5.69e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.49 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 17 KTLK-IDHLSVA--AGESWAFVGSNGSGKSALARALAGDLPLLSGqreshfsRVTRLSfEQLQKLVSDEWQRNNTDL--- 90
Cdd:PRK15079 32 KTLKaVDGVTLRlyEGETLGVVGESGCGKSTFARAIIGLVKATDG-------EVAWLG-KDLLGMKDDEWRAVRSDIqmi 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 91 -------LSPgeedtgR-TTAEII------------QDEVKDPARcARLAEQFGISALLDRRFKYLSTGETRKTLLCQAL 150
Cdd:PRK15079 104 fqdplasLNP------RmTIGEIIaeplrtyhpklsRQEVKDRVK-AMMLKVGLLPNLINRYPHEFSGGQCQRIGIARAL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984360 151 MTDPQLLILDEPFDGLDVNSRQQLAALLADLH-SAGITLVLV 191
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIFI 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
257-480 |
5.92e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.79 E-value: 5.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 257 SAPRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTgdhpqgYSNDL----TLFGRRRGSGETIW 332
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN------RMNDLnpevTITGSIVYNGHNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 333 -------DIKKHIGYVSSSLH-LDYRVSTNV-RNVILSGYFDSIGIYQAVsDKQHKLVQQWLDIlgiDKRTADAPFhSLS 403
Cdd:PRK14239 76 sprtdtvDLRKEIGMVFQQPNpFPMSIYENVvYGLRLKGIKDKQVLDEAV-EKSLKGASIWDEV---KDRLHDSAL-GLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984360 404 WGQQRLALIVRALVKHPTLLILDEPLQGLDPLNrqlVRRFVDVLIG-EGATQLLFVSHHAEDAPDcITHRLAFVPSGD 480
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPIS---AGKIEETLLGlKDDYTMLLVTRSMQQASR-ISDRTGFFLDGD 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
272-467 |
6.12e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.20 E-value: 6.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 272 DRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYSNDLTlfgrrRG---SGETIWDIKKHIGYVSSSLHlD 348
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLI-----RGepiTKENIREVRKFVGLVFQNPD-D 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 349 YRVSTNVRNVILSGYFDsIGIYQAVSdkQHKlVQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEP 428
Cdd:PRK13652 90 QIFSPTVEQDIAFGPIN-LGLDEETV--AHR-VSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984360 429 LQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDAPD 467
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPE 203
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
259-465 |
6.32e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 59.88 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 259 PRIVLNDGVVSY----NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRR-RGSG-ETI 331
Cdd:COG4525 2 SMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGfLAPS--SGEITLDGVPvTGPGaDRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 332 WDIKKHigyvssSLhLDYRvstNVR-NVILSGYFdsigiyQAVSDKQ-HKLVQQWLDILGIDKrTADAPFHSLSWGQQRL 409
Cdd:COG4525 80 VVFQKD------AL-LPWL---NVLdNVAFGLRL------RGVPKAErRARAEELLALVGLAD-FARRRIWQLSGGMRQR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488984360 410 ALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDA 465
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
24-196 |
6.37e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 6.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGdlpLLSGQRESHFSRVTRLSFEQLQKLVSDEWQRNNTDllspgeedtgrTTA 103
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTLLRLLAG---ALKGTPVAGCVDVPDNQFGREASLIDAIGRKGDFK-----------DAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 104 EIIqdevkdpARCarlaeqfGIS--ALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADL 181
Cdd:COG2401 117 ELL-------NAV-------GLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKL 182
|
170
....*....|....*.
gi 488984360 182 -HSAGITLVLVLNRFD 196
Cdd:COG2401 183 aRRAGITLVVATHHYD 198
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
274-460 |
6.51e-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: 60.45 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 274 PVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGysndltlfGRRRGS----GETIWDIK---------KHIGY 340
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPP--------GITSGEilfdGEDLLKLSekelrkirgREIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 341 V----SSSLHLDYRVSTNVRNVILsgyfdsigIYQAVSDKQ-HKLVQQWLDILGID--KRTADA-PfHSLSWGQ-QRlAL 411
Cdd:COG0444 91 IfqdpMTSLNPVMTVGDQIAEPLR--------IHGGLSKAEaRERAIELLERVGLPdpERRLDRyP-HELSGGMrQR-VM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 412 IVRALVKHPTLLILDEPLQGLDP------LN--RQLVRRFvdvligeGATqLLFVSH 460
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVtiqaqiLNllKDLQREL-------GLA-ILFITH 209
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
249-460 |
6.62e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 59.32 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 249 PARHALADSAPRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgysndltlfgrrrgS 327
Cdd:COG1134 15 RLYHEPSRSLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEPT--------------S 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 328 GEtiwdIKKHiGYVSS------SLHLDYrvsTNVRNVILSGYfdsigiyqavsdkqhklvqqwldILG-----IDKRTA- 395
Cdd:COG1134 81 GR----VEVN-GRVSAllelgaGFHPEL---TGRENIYLNGR-----------------------LLGlsrkeIDEKFDe 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 396 -----------DAPFHSLSWGQQ-RLALIVrALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATqLLFVSH 460
Cdd:COG1134 130 ivefaelgdfiDQPVKTYSSGMRaRLAFAV-ATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRT-VIFVSH 204
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
271-480 |
6.65e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.68 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 271 NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSlVTGDHPQGYSNDLTLFGRRRGSGETIWDI-----KKHIGYVSSSL 345
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLK-VLNRLIEIYDSKIKVDGKVLYFGKDIFQIdaiklRKEVGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 346 HLDYRVSTnvrnvilsgyFDSIGI---YQAVSDKQH--KLVQQWLDILGIDKRTAD---APFHSLSWGQQRLALIVRALV 417
Cdd:PRK14246 100 NPFPHLSI----------YDNIAYplkSHGIKEKREikKIVEECLRKVGLWKEVYDrlnSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984360 418 KHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGAtqLLFVSHHAEDAPDcITHRLAFVPSGD 480
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIA--IVIVSHNPQQVAR-VADYVAFLYNGE 229
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
269-433 |
6.66e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.81 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG--DHPQGysnDLtLFGRRRGSgetiwDI---KKHIGYVSS 343
Cdd:PRK11000 12 AYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleDITSG---DL-FIGEKRMN-----DVppaERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 344 SL----HLDyrVSTNVrnvilsgyfdSIGIYQAVSDKQH--KLVQQWLDILGIDKRTADAPfHSLSWGQ-QRLAlIVRAL 416
Cdd:PRK11000 83 SYalypHLS--VAENM----------SFGLKLAGAKKEEinQRVNQVAEVLQLAHLLDRKP-KALSGGQrQRVA-IGRTL 148
|
170
....*....|....*..
gi 488984360 417 VKHPTLLILDEPLQGLD 433
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLD 165
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-196 |
1.04e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 59.26 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 12 RLSDT----KTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGdlpLLSG---------------QRESHFSRVTRLS- 71
Cdd:PRK09984 9 KLAKTfnqhQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSG---LITGdksagshiellgrtvQREGRLARDIRKSr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 72 ------FEQLQkLVSDEWQRNNTDLLSPGEEDTGRTTAEIIQDEVKDpaRCARLAEQFGISALLDRRFKYLSTGETRKTL 145
Cdd:PRK09984 86 antgyiFQQFN-LVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQ--RALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984360 146 LCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLH-SAGITLVLVLNRFD 196
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINqNDGITVVVTLHQVD 214
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
238-481 |
1.06e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.59 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 238 DGITLPEPDVPPARHALADSAPRIVLND-GVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-------- 308
Cdd:COG4178 340 EALEAADALPEAASRIETSEDGALALEDlTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwpygsgr 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 309 -DHPQGYSndlTLFGRRRgsgetiwdikkhiGYV-SSSLhldyrvstnvRNVILsgYFDSIGiyqAVSDKQhklVQQWLD 386
Cdd:COG4178 420 iARPAGAR---VLFLPQR-------------PYLpLGTL----------REALL--YPATAE---AFSDAE---LREALE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 387 ILG----IDKRTADAPF-HSLSWG-QQRLAlIVRALVKHPTLLILDEPLQGLDPLN-RQLVRRFVDVLigEGATqLLFVS 459
Cdd:COG4178 466 AVGlghlAERLDEEADWdQVLSLGeQQRLA-FARLLLHKPDWLFLDEATSALDEENeAALYQLLREEL--PGTT-VISVG 541
|
250 260
....*....|....*....|..
gi 488984360 460 HHAEDAPDCiTHRLAFVPSGDG 481
Cdd:COG4178 542 HRSTLAAFH-DRVLELTGDGSW 562
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
273-482 |
1.11e-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: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 273 RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgySNDLTLFGRRrgsgetiwDIKKHIGYVSSSLHLDYRVS 352
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP--TSGTVLVGGK--------DIETNLDAVRQSLGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 353 TNVRNVILSgyfDSIGIYQAVSDKQHKLVQQWLDILGID-----KRTADApfHSLSWGQQRLALIVRALVKHPTLLILDE 427
Cdd:TIGR01257 1013 ILFHHLTVA---EHILFYAQLKGRSWEEAQLEMEAMLEDtglhhKRNEEA--QDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488984360 428 PLQGLDPLNRqlvRRFVDVLIGEGATQLLFVSHHAEDAPDCITHRLAFVPSGDGY 482
Cdd:TIGR01257 1088 PTSGVDPYSR---RSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLY 1139
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
257-465 |
1.29e-09 |
|
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: 59.67 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 257 SAPRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHP------QGySNDLT-LFGRRRGSG 328
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGlERQtagtiyQG-GRDITrLPPQKRDYG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 329 etiwdikkhIGYVSSSLHLDYRVSTNVrnvilsGYfdsiGIYQAVSDKQ--HKLVQQWLDILGIDKRTADAPfHSLSWGQ 406
Cdd:TIGR03265 80 ---------IVFQSYALFPNLTVADNI------AY----GLKNRGMGRAevAERVAELLDLVGLPGSERKYP-GQLSGGQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984360 407 Q-RLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGE-GATQLLfVSHHAEDA 465
Cdd:TIGR03265 140 QqRVAL-ARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIM-VTHDQEEA 198
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
268-465 |
1.40e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.56 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 268 VSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRR-RGSGETIWDIKKHIGYvssslh 346
Cdd:PRK11248 9 ADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGKPvEGPGAERGVVFQNEGL------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 347 LDYRvstNVR-NVILSGYFDSIGIYQAVSDKQHKLVQqwLDILGIDKRtadaPFHSLSWGQQRLALIVRALVKHPTLLIL 425
Cdd:PRK11248 82 LPWR---NVQdNVAFGLQLAGVEKMQRLEIAHQMLKK--VGLEGAEKR----YIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488984360 426 DEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDA 465
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
248-480 |
1.71e-09 |
|
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: 60.15 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 248 PPARHALADSAPRIVLnDGVV---SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgysndltlfgrR 324
Cdd:COG4618 318 EPERMPLPRPKGRLSV-ENLTvvpPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP-----------T 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 325 RGS----GETI--WD---IKKHIGYVSSSLHL-DYRVSTNV-RnvilSGYFDSIGIYQA-----VsdkqHKLVQQWLDil 388
Cdd:COG4618 386 AGSvrldGADLsqWDreeLGRHIGYLPQDVELfDGTIAENIaR----FGDADPEKVVAAaklagV----HEMILRLPD-- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 389 GIDKRTADAPfHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLfvshhaedapd 467
Cdd:COG4618 456 GYDTRIGEGG-ARLSGGQrQRIGL-ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVV----------- 522
|
250
....*....|...
gi 488984360 468 cITHRLAFVPSGD 480
Cdd:COG4618 523 -ITHRPSLLAAVD 534
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-190 |
1.77e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.95 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGdlpLL---SG----------QRESHFSR----V----TRL--------SFEQ 74
Cdd:COG4586 43 FTIEPGEIVGFIGPNGAGKSTTIKMLTG---ILvptSGevrvlgyvpfKRRKEFARrigvVfgqrSQLwwdlpaidSFRL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 75 LQKL--VSDEWQRNNTDllspgeedtgrttaeiiqdevkdparcaRLAEQFGISALLDRRFKYLSTGETRKTLLCQALMT 152
Cdd:COG4586 120 LKAIyrIPDAEYKKRLD----------------------------ELVELLDLGELLDTPVRQLSLGQRMRCELAAALLH 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984360 153 DPQLLILDEPFDGLDVNSRQQLAALLADLH-SAGITLVL 190
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEYNrERGTTILL 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
245-480 |
1.82e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 59.97 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 245 PDV--PPARHALADSAPRIVLNDGVVSY-NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQgysndltl 320
Cdd:PRK13657 317 PDVrdPPGAIDLGRVKGAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFdPQ-------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 321 FGRRRGSGETIWDI-----KKHIGYV-SSSLHLDYRVSTNVRnvilsgyfdsIGIYQAVSDKQHKLVQ--QWLDIlgIDK 392
Cdd:PRK13657 389 SGRILIDGTDIRTVtraslRRNIAVVfQDAGLFNRSIEDNIR----------VGRPDATDEEMRAAAEraQAHDF--IER 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 393 RTADAPFH------SLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIgEGATQllFVshhaeda 465
Cdd:PRK13657 457 KPDGYDTVvgergrQLSGGErQRLA-IARALLKDPPILILDEATSALDVETEAKVKAALDELM-KGRTT--FI------- 525
|
250
....*....|....*
gi 488984360 466 pdcITHRLAFVPSGD 480
Cdd:PRK13657 526 ---IAHRLSTVRNAD 537
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-191 |
2.02e-09 |
|
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: 58.91 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLP---------LLSGQReshfsrVTRLSFEQLQKLvsdewqRnntdllspg 94
Cdd:COG0444 26 FDVRRGETLGLVGESGSGKSTLARAILGLLPppgitsgeiLFDGED------LLKLSEKELRKI------R--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 95 eedtGRTTAEIIQD----------------------------EVKdpARCARLAEQFGISALLDRRFKY---LSTGETRK 143
Cdd:COG0444 85 ----GREIQMIFQDpmtslnpvmtvgdqiaeplrihgglskaEAR--ERAIELLERVGLPDPERRLDRYpheLSGGMRQR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984360 144 TLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSA-GITLVLV 191
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFI 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-198 |
2.05e-09 |
|
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: 56.94 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSDTKTLKIDHLS--VAAGESWAFVGSNGSGKSALARALAGDLPLLSGqrESHFSRVTRLSFE-QLQKLVS 80
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSleLKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQG--EITLDGVPVSDLEkALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 81 DEWQRN---NTDLLSPgeedtgrttaeiiqdevkdparcarlaeqfgisalLDRRFkylSTGETRKTLLCQALMTDPQLL 157
Cdd:cd03247 79 VLNQRPylfDTTLRNN-----------------------------------LGRRF---SGGERQRLALARILLQDAPIV 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984360 158 ILDEPFDGLDVNSRQQLAALLADlHSAGITLVLV------LNRFDEI 198
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFE-VLKDKTLIWIthhltgIEHMDKI 166
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
269-465 |
2.34e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 58.94 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYsndltlfGRRRGSGETIWDI---KKHIGYVSSSL 345
Cdd:PRK10851 11 SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTS-------GHIRFHGTDVSRLharDRKVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 346 HLdYRVSTnvrnvilsgYFDSIGIYQAV--------SDKQHKLVQQWLDILGIDkRTADAPFHSLSWGQ-QRLALiVRAL 416
Cdd:PRK10851 84 AL-FRHMT---------VFDNIAFGLTVlprrerpnAAAIKAKVTQLLEMVQLA-HLADRYPAQLSGGQkQRVAL-ARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984360 417 VKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDA 465
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEA 200
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-191 |
2.35e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.44 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 2 SSLQISQGTFRLSDTKTL-KIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGqreshfsRVTRLSFEQL----Q 76
Cdd:COG4178 361 GALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG-------RIARPAGARVlflpQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 77 K-------LvsdewqRNNtdLLSPGEEDTgRTTAEIIqdEVKDPARCARLAEQFGISALLDRRfkyLSTGETRKTLLCQA 149
Cdd:COG4178 434 RpylplgtL------REA--LLYPATAEA-FSDAELR--EALEAVGLGHLAERLDEEADWDQV---LSLGEQQRLAFARL 499
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984360 150 LMTDPQLLILDEPFDGLDVNSRQQLAALLADlHSAGITLVLV 191
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISV 540
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
291-465 |
2.40e-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: 58.66 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 291 IVGPNGAGKSTLLSLVTG-DHPQgysndltlFGRRRGSGETIWDIKKHIGYVssslhldyrvstnvrNVILSGY--FDSI 367
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGfEQPD--------SGSIMLDGEDVTNVPPHLRHI---------------NMVFQSYalFPHM 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 368 GIYQAVSD--KQHKL--------VQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD-PLN 436
Cdd:TIGR01187 58 TVEENVAFglKMRKVpraeikprVLEALRLVQLEEFADRKP-HQLSGGQQQRVALARALVFKPKILLLDEPLSALDkKLR 136
|
170 180
....*....|....*....|....*....
gi 488984360 437 RQLVRRFVDVLIGEGATqLLFVSHHAEDA 465
Cdd:TIGR01187 137 DQMQLELKTIQEQLGIT-FVFVTHDQEEA 164
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-181 |
2.41e-09 |
|
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: 57.67 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAG---DLPLLSGQ---RESHFSRvtrlsfEQLQKLVSDEWQrnnTDLLSPG--E 95
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQilfNGQPRKP------DQFQKCVAYVRQ---DDILLPGltV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 96 EDTGRTTAEIIQDEVKDPARCARLAEQFGISALLDRR-----FKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNS 170
Cdd:cd03234 99 RETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRiggnlVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170
....*....|.
gi 488984360 171 RQQLAALLADL 181
Cdd:cd03234 179 ALNLVSTLSQL 189
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
283-468 |
2.57e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.48 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 283 VNPGEHWQIVGPNGAGKSTLLSLVTGdHPQGYSNDLTLFGR--RRGSGETIWDIK-KHIGYVSSSLHLDYRVSTnVRNVI 359
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAG-LDDGSSGEVSLVGQplHQMDEEARAKLRaKHVGFVFQSFMLIPTLNA-LENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 360 LSgyfdsiGIYQAVSDKQ-HKLVQQWLDILGIDKRTADAPfHSLSWG-QQRLALiVRALVKHPTLLILDEPLQGLDplnR 437
Cdd:PRK10584 111 LP------ALLRGESSRQsRNGAKALLEQLGLGKRLDHLP-AQLSGGeQQRVAL-ARAFNGRPDVLFADEPTGNLD---R 179
|
170 180 190
....*....|....*....|....*....|....
gi 488984360 438 QLVRRFVDVLIG---EGATQLLFVSHHAEDAPDC 468
Cdd:PRK10584 180 QTGDKIADLLFSlnrEHGTTLILVTHDLQLAARC 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
15-256 |
2.92e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 57.78 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 15 DTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ-----RESHFSRVTRLSFEQLQKLVsdeWQRNNTD 89
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEvlikgEPIKYDKKSLLEVRKTVGIV---FQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 90 LLSPG-EEDT--GRTTAEIIQDEVKDpaRCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGL 166
Cdd:PRK13639 91 LFAPTvEEDVafGPLNLGLSKEEVEK--RVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 167 DVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGE-----------KSSLLQQALVAQLAHS- 234
Cdd:PRK13639 169 DPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTpkevfsdietiRKANLRLPRVAHLIEIl 248
|
250 260
....*....|....*....|...
gi 488984360 235 EKLDGITLPEP-DVPPARHALAD 256
Cdd:PRK13639 249 NKEDNLPIKMGyTIGEARRNIKE 271
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-191 |
2.93e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 57.28 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 23 HLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ----RESHfsRVTRLSfeqlQKLVSDEWQRNN--TDL------ 90
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSltlnGQDH--TTTPPS----RRPVSMLFQENNlfSHLtvaqni 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 91 ---LSPGEedtgRTTAEIiQDEVKDparcarLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLD 167
Cdd:PRK10771 93 glgLNPGL----KLNAAQ-REKLHA------IARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180
....*....|....*....|....*
gi 488984360 168 VNSRQQLAALLADL-HSAGITLVLV 191
Cdd:PRK10771 162 PALRQEMLTLVSQVcQERQLTLLMV 186
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
268-461 |
3.06e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 57.38 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 268 VSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGdHPqGY---SNDLTLFGRrrgsgetiwDI---------K 335
Cdd:COG0396 8 VSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HP-KYevtSGSILLDGE---------DIlelspderaR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 336 KHIGY----------VSSSLHLdyRVSTNVRNVILSGYFDSigiyqavsdkqHKLVQQWLDILGIDKRTADAPFH-SLSW 404
Cdd:COG0396 77 AGIFLafqypveipgVSVSNFL--RTALNARRGEELSAREF-----------LKLLKEKMKELGLDEDFLDRYVNeGFSG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 405 GQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLfVSHH 461
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILI-ITHY 199
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
10-198 |
3.26e-09 |
|
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: 55.85 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 10 TFRLSDTKTLKIDHLS--VAAGESWAFVGSNGSGKSALARALAGDLPLLSGqreshfsrvtRLSFeqlqklvsdewqrNN 87
Cdd:cd03228 7 SFSYPGRPKPVLKDVSltIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSG----------EILI-------------DG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 88 TDLLSPGEEDTGRTTAEIIQDevkdparcarlaeqfgiSALLDR--RFKYLSTGETRKTLLCQALMTDPQLLILDEPFDG 165
Cdd:cd03228 64 VDLRDLDLESLRKNIAYVPQD-----------------PFLFSGtiRENILSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984360 166 LDVNSRQQLAALLADLhSAGITLVLV------LNRFDEI 198
Cdd:cd03228 127 LDPETEALILEALRAL-AKGKTVIVIahrlstIRDADRI 164
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
259-473 |
5.30e-09 |
|
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: 56.35 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 259 PRIVLNDGVVSYND--RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLslvtgdhpqgysndLTLFGRRRGSGETIW---- 332
Cdd:cd03244 1 GDIEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLL--------------LALFRLVELSSGSILidgv 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 333 DIKKhIGyvsssLHlDYRVSTNV---RNVILSG----------YFDSIGIYQAVSDKQHK-LVQQWLDilGIDKRTADAP 398
Cdd:cd03244 67 DISK-IG-----LH-DLRSRISIipqDPVLFSGtirsnldpfgEYSDEELWQALERVGLKeFVESLPG--GLDTVVEEGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984360 399 FHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRfvdvLIGE---GATQLlfvshhaedapdCITHRL 473
Cdd:cd03244 138 EN-LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQK----TIREafkDCTVL------------TIAHRL 198
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
276-443 |
5.31e-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: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 276 INHLSWTVNPGEhwqIV---GPNGAGKSTLLSLVTGD-HPQGYS---NDLTLFGRRRgsgetiwDIKKHIGYVS---SSL 345
Cdd:COG4586 38 VDDISFTIEPGE---IVgfiGPNGAGKSTTIKMLTGIlVPTSGEvrvLGYVPFKRRK-------EFARRIGVVFgqrSQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 346 HLDYRVStnvrnvilsgyfDSIGIYQA---VSDKQHKlvqQWLD----ILGIDKrTADAPFHSLSWGQQRLALIVRALVK 418
Cdd:COG4586 108 WWDLPAI------------DSFRLLKAiyrIPDAEYK---KRLDelveLLDLGE-LLDTPVRQLSLGQRMRCELAAALLH 171
|
170 180
....*....|....*....|....*
gi 488984360 419 HPTLLILDEPLQGLDPLNRQLVRRF 443
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREF 196
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-252 |
5.52e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 57.61 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSDTKTLKIDhlsvaAGESWAFVGSNGSGKSALARALAGdlplLSGQReshfSRVT--RLSFeqlqklvsd 81
Cdd:COG4170 13 IDTPQGRVKAVDRVSLTLN-----EGEIRGLVGESGSGKSLIAKAICG----ITKDN----WHVTadRFRW--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 82 ewqrNNTDLL--SPGE--EDTGRTTAEIIQDevkdPARC----ARLAEQFgISALLDRRFK------------------- 134
Cdd:COG4170 71 ----NGIDLLklSPRErrKIIGREIAMIFQE----PSSCldpsAKIGDQL-IEAIPSWTFKgkwwqrfkwrkkraiellh 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 135 -------------Y---LSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLH-SAGITLVLVLNRFDE 197
Cdd:COG4170 142 rvgikdhkdimnsYpheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNqLQGTSILLISHDLES 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 198 IPEFVQFAGVLADCTLSETGEKSSLLQ-------QALVA-------QLAHSEKLDgiTLPEpDVPPARH 252
Cdd:COG4170 222 ISQWADTITVLYCGQTVESGPTEQILKsphhpytKALLRsmpdfrqPLPHKSRLN--TLPG-SIPPLQH 287
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
33-201 |
5.82e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.15 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 33 AFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVT----RLSFEQLQKLVSDEWQRNNTDLLspgeEDT-------GRT 101
Cdd:PRK13641 37 ALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRKKVSLVFQFPEAQLF----ENTvlkdvefGPK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 102 TAEIIQDEVKDPARcaRLAEQFGIS-ALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLAD 180
Cdd:PRK13641 113 NFGFSEDEAKEKAL--KWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKD 190
|
170 180
....*....|....*....|.
gi 488984360 181 LHSAGITLVLVLNRFDEIPEF 201
Cdd:PRK13641 191 YQKAGHTVILVTHNMDDVAEY 211
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-171 |
5.85e-09 |
|
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: 56.65 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 18 TLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVtrlSFEQlQKLVSDeWQRNNTDLLSpgEED 97
Cdd:cd03237 14 TLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV---SYKP-QYIKAD-YEGTVRDLLS--SIT 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984360 98 TGRTTAEIIQDEVKDParcarlaeqFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSR 171
Cdd:cd03237 87 KDFYTHPYFKTEIAKP---------LQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
283-467 |
6.14e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.05 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 283 VNPGEHWQIVGPNGAGKSTLLSLVTG--DHPQGYSNDLTLFGRRRGSGETIWDIKKHIGYVSSSLHLDYRVSTNVRNVIL 360
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEETVLKDVAF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 361 SGyfDSIGIYQavsDKQHKLVQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLV 440
Cdd:PRK13643 109 GP--QNFGIPK---EKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEM 183
|
170 180
....*....|....*....|....*..
gi 488984360 441 RRFVDVLIGEGATQLLfVSHHAEDAPD 467
Cdd:PRK13643 184 MQLFESIHQSGQTVVL-VTHLMDDVAD 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
271-433 |
6.28e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.04 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 271 NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqgysndlTLFGRRRGSGETIwdikkHIGYVSSSLHldYR 350
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP-------PAAGTIKLDGGDI-----DDPDVAEACH--YL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 351 VSTNVRNVILSgyfdsigiyqaVSDKqhklVQQWLDILGIDKRTADA-------------PFHSLSWGQQRLALIVRALV 417
Cdd:PRK13539 79 GHRNAMKPALT-----------VAEN----LEFWAAFLGGEELDIAAaleavglaplahlPFGYLSAGQKRRVALARLLV 143
|
170
....*....|....*.
gi 488984360 418 KHPTLLILDEPLQGLD 433
Cdd:PRK13539 144 SNRPIWILDEPTAALD 159
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
276-464 |
6.84e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 56.98 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 276 INHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgysndltLFGRRRGS----GETIWD-------IKKHIGYV--- 341
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNG-----------LLKPTSGKiiidGVDITDkkvklsdIRKKVGLVfqy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 342 ------SSSLHLDyrVSTNVRNVILSgyfdsigiyqavSDKQHKLVQQWLDILGIDKRT-AD-APFhSLSWGQQRLALIV 413
Cdd:PRK13637 92 peyqlfEETIEKD--IAFGPINLGLS------------EEEIENRVKRAMNIVGLDYEDyKDkSPF-ELSGGQKRRVAIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984360 414 RALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAED 464
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMED 207
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
257-461 |
7.15e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.81 E-value: 7.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 257 SAPRIVLNDGVVSY-NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGdHPQGYSNDLTLFGRrrgsgETIWDIK 335
Cdd:PRK15056 3 QQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMG-FVRLASGKISILGQ-----PTRQALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 336 KH-IGYVSSSLHLDYRVSTNVRNVILSGYFDSIGIYQAVSDKQHKLVQQWL---DILGIDKRTadapFHSLSWGQQRLAL 411
Cdd:PRK15056 77 KNlVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALarvDMVEFRHRQ----IGELSGGQKKRVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984360 412 IVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLlfVSHH 461
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTML--VSTH 200
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
201-442 |
7.18e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.19 E-value: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 201 FVQFAGVLADcTLSETGEKSSLLQQALVAQLAHSEKLDGitlpepdvpPARHALADSAP----RIVLNDGVVSY-NDRPV 275
Cdd:PRK10790 287 FISYLGRLNE-PLIELTTQQSMLQQAVVAGERVFELMDG---------PRQQYGNDDRPlqsgRIDIDNVSFAYrDDNLV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 276 INHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHP--QGysnDLTLFGRRRGS-GETIwdIKKHIGYVSSslhlDYRV- 351
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPltEG---EIRLDGRPLSSlSHSV--LRQGVAMVQQ----DPVVl 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 352 -STNVRNVILSGYFDSIGIYQAVSDKQ-HKLVQQWLDilGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPL 429
Cdd:PRK10790 428 aDTFLANVTLGRDISEEQVWQALETVQlAELARSLPD--GLYTPLGEQG-NNLSVGQKQLLALARVLVQTPQILILDEAT 504
|
250
....*....|...
gi 488984360 430 QGLDPLNRQLVRR 442
Cdd:PRK10790 505 ANIDSGTEQAIQQ 517
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-194 |
8.62e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.09 E-value: 8.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 25 SVAAGESWAFVGSNGSGKSALARALAGDLP-----LLSGQRESHFSRVT----RLSFEQLQKLVS--DEWQRNNTDLLSP 93
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLPgsgsiQFAGQPLEAWSAAElarhRAYLSQQQTPPFamPVFQYLTLHQPDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 94 GEEDTGRTTAEiiqdevkdparcaRLAEQFGISALLDRRFKYLSTGETRKTLLCQA-LMTDP------QLLILDEPFDGL 166
Cdd:PRK03695 98 TRTEAVASALN-------------EVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPdinpagQLLLLDEPMNSL 164
|
170 180 190
....*....|....*....|....*....|.
gi 488984360 167 DVNSRQQLAALLADLHSAGITLVLV---LNR 194
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGIAVVMSshdLNH 195
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
260-436 |
9.53e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.07 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 260 RIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLvtgdhpqgYSNDLTLFGRRRGSGETIWD----IK 335
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRV--------FNRLIELYPEARVSGEVYLDgqdiFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 336 KHIGYVSSSLHLDYRVSTNVRNVILsgyFDSIgiyqAVSDKQHKLV-----------------QQWLDIlgidKRTADAP 398
Cdd:PRK14247 75 MDVIELRRRVQMVFQIPNPIPNLSI---FENV----ALGLKLNRLVkskkelqervrwalekaQLWDEV----KDRLDAP 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984360 399 FHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLN 436
Cdd:PRK14247 144 AGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPEN 181
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
119-186 |
9.81e-09 |
|
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: 9.81e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984360 119 LAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGI 186
Cdd:cd03218 117 LLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGI 184
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-433 |
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 488984360 23 HLSVAAGESWAFVGSNGSGKSALARALAGDLP------LLSGQRES-----------------HFSRVTRLS-------- 71
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQpdsgeiLIDGKPVRirsprdaialgigmvhqHFMLVPNLTvaenivlg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 72 FEQLQKLVSDewqrnntdllspgeedtgRTTAEiiqdevkdpARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALM 151
Cdd:COG3845 105 LEPTKGGRLD------------------RKAAR---------ARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 152 TDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVL------ADCTLSETGEKSslLQQ 225
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLrrgkvvGTVDTAETSEEE--LAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 226 ALVAQlahsekldgitlpEPDVPPARHALADSAPRIVLND-GVVSYNDRPVINHLSWTVNPGEhwqIV---GPNGAGKST 301
Cdd:COG3845 236 LMVGR-------------EVLLRVEKAPAEPGEVVLEVENlSVRDDRGVPALKDVSLEVRAGE---ILgiaGVAGNGQSE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 302 LLSLVTG-DHPQgySNDLTLFGRRRGsGETIWDIKKH-IGYVSSSLH-----LDYRVstnVRNVILSGY----FDSIGI- 369
Cdd:COG3845 300 LAEALAGlRPPA--SGSIRLDGEDIT-GLSPRERRRLgVAYIPEDRLgrglvPDMSV---AENLILGRYrrppFSRGGFl 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984360 370 -YQAVSDKQHKLVQQWlDIlgidkRTA--DAPFHSLSWG-QQRLaLIVRALVKHPTLLILDEPLQGLD 433
Cdd:COG3845 374 dRKAIRAFAEELIEEF-DV-----RTPgpDTPARSLSGGnQQKV-ILARELSRDPKLLIAAQPTRGLD 434
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-433 |
1.09e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.56 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALA----GDLP----LLSGQRESHFSRVTRLS------FEQLQkLVSDEWQRNNTD 89
Cdd:PLN03073 198 VTLAFGRHYGLVGRNGTGKTTFLRYMAmhaiDGIPkncqILHVEQEVVGDDTTALQcvlntdIERTQ-LLEEEAQLVAQQ 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 90 LLSPGEEDTGRTTAEIIQDEVKDPARcARLAEQFGISALLD-----------------------RRFKYLSTGETRKTLL 146
Cdd:PLN03073 277 RELEFETETGKGKGANKDGVDKDAVS-QRLEEIYKRLELIDaytaearaasilaglsftpemqvKATKTFSGGWRMRIAL 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 147 CQALMTDPQLLILDEPFDGLDVNS---------------------RQQLAALLAD-LHSAGITLVLVLNRFDEIpEFVQF 204
Cdd:PLN03073 356 ARALFIEPDLLLLDEPTNHLDLHAvlwletyllkwpktfivvshaREFLNTVVTDiLHLHGQKLVTYKGDYDTF-ERTRE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 205 AGVLADCTLSETGEKSSLLQQALVAQLAHSEK-----------LDGI--------------TLPEPDVPParhaladSAP 259
Cdd:PLN03073 435 EQLKNQQKAFESNERSRSHMQAFIDKFRYNAKraslvqsrikaLDRLghvdavvndpdykfEFPTPDDRP-------GPP 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 260 RIVLNDGVVSYNDRPVI-NHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQgysndltlfgrrrgSGETIWDIKKH 337
Cdd:PLN03073 508 IISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGElQPS--------------SGTVFRSAKVR 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 338 IGyVSSSLHLD-YRVSTNVRNVILSgyfdsigIYQAVSDKQhklVQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRAL 416
Cdd:PLN03073 574 MA-VFSQHHVDgLDLSSNPLLYMMR-------CFPGVPEQK---LRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKIT 642
|
490
....*....|....*..
gi 488984360 417 VKHPTLLILDEPLQGLD 433
Cdd:PLN03073 643 FKKPHILLLDEPSNHLD 659
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-243 |
1.26e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 56.15 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 16 TKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLP------LLSGQRESHFSRVtrlsfEQLQKLVSDEWQRNNTD 89
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRpqkgkvLVSGIDTGDFSKL-----QGIRKLVGIVFQNPETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 90 LLSPG-EEDTGRTTAEIIQDEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDV 168
Cdd:PRK13644 90 FVGRTvEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 169 NSRQQLAALLADLHSAGITLVLVLNRFDEI-------------------PEfvqfaGVLADCTLSETGekssLLQQALVa 229
Cdd:PRK13644 170 DSGIAVLERIKKLHEKGKTIVYITHNLEELhdadriivmdrgkivlegePE-----NVLSDVSLQTLG----LTPPSLI- 239
|
250
....*....|....
gi 488984360 230 QLAHSEKLDGITLP 243
Cdd:PRK13644 240 ELAENLKMHGVVIP 253
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
261-480 |
1.30e-08 |
|
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: 54.78 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDR-----PVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgysndltLFGRRRGSGetiwdik 335
Cdd:cd03250 1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEK-------LSGSVSVPG------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 336 kHIGYVSSSLHLdyrVSTNVRNVILSGY-FDSiGIYQAV-------SDkqhklvqqwLDIL-----------GIdkrtad 396
Cdd:cd03250 67 -SIAYVSQEPWI---QNGTIRENILFGKpFDE-ERYEKVikacalePD---------LEILpdgdlteigekGI------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 397 apfhSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDP-LNRQLVRrfvDVLIGEGA---TQLLfvshhaedapdcITH 471
Cdd:cd03250 127 ----NLSGGQkQRISL-ARAVYSDADIYLLDDPLSAVDAhVGRHIFE---NCILGLLLnnkTRIL------------VTH 186
|
....*....
gi 488984360 472 RLAFVPSGD 480
Cdd:cd03250 187 QLQLLPHAD 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-225 |
1.32e-08 |
|
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: 57.12 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 6 ISQGTFRLSDTKTLKIDHlsvaaGESWAFVGSNGSGKSALARALAGDLPLLSGQreshfsrvtrlsfeqLQKLVSDEWqr 85
Cdd:TIGR03269 292 VDRGVVKAVDNVSLEVKE-----GEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE---------------VNVRVGDEW-- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 86 nnTDLLSPGEEDTGRTTAEI---IQDEVKDPARCA--RLAEQFGIS-------------------------ALLDRRFKY 135
Cdd:TIGR03269 350 --VDMTKPGPDGRGRAKRYIgilHQEYDLYPHRTVldNLTEAIGLElpdelarmkavitlkmvgfdeekaeEILDKYPDE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 136 LSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLA-ALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLS 214
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVThSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
250
....*....|.
gi 488984360 215 ETGEKSSLLQQ 225
Cdd:TIGR03269 508 KIGDPEEIVEE 518
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
10-210 |
1.38e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.77 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 10 TFRLSDTKTLKIDHLS--VAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLVSDEWQR-N 86
Cdd:PRK13632 14 SFSYPNSENNALKNVSfeINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNpD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 87 NTDLLSPGEEDTG------RTTAEIIQDEVKDparcarLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILD 160
Cdd:PRK13632 94 NQFIGATVEDDIAfglenkKVPPKKMKDIIDD------LAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984360 161 EPFDGLDVNSRQQLAALLADLHSAGI-TLVLVLNRFDEIpefvqfagVLAD 210
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA--------ILAD 210
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
272-440 |
1.62e-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: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 272 DRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHpQGYSNDLTLFGRRRGSGETIWdIKKHIGYVSSSLHLdyrV 351
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLY-QPTGGQVLLDGVPLVQYDHHY-LHRQVALVGQEPVL---F 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 352 STNVRNVILSG---YFDSIGIYQAVSDKQHKLVQQWLDilGIDKRTADAPfHSLSWGQ-QRLAlIVRALVKHPTLLILDE 427
Cdd:TIGR00958 568 SGSVRENIAYGltdTPDEEIMAAAKAANAHDFIMEFPN--GYDTEVGEKG-SQLSGGQkQRIA-IARALVRKPRVLILDE 643
|
170
....*....|...
gi 488984360 428 PLQGLDPLNRQLV 440
Cdd:TIGR00958 644 ATSALDAECEQLL 656
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-200 |
1.64e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.95 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ-----RESHFSRVT-----RLSF--E--QLQKLVSDEWQRNNTD 89
Cdd:COG1129 273 FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEirldgKPVRIRSPRdairaGIAYvpEdrKGEGLVLDLSIRENIT 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 90 L-----------LSPGEEDtgrttaeiiqdevkdpARCARLAEQFGI-SALLDRRFKYLSTGETRKTLLCQALMTDPQLL 157
Cdd:COG1129 353 LasldrlsrgglLDRRRER----------------ALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984360 158 ILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLnrfDEIPE 200
Cdd:COG1129 417 ILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVIS---SELPE 456
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
272-438 |
1.72e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.51 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 272 DRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGdHPQGYSNDLTLFGRRRgSGETIWDIKKHIGYVSSSLHLDYrV 351
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDG-LLEAESGQIIIDGDLL-TEENVWDIRHKIGMVFQNPDNQF-V 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 352 STNVRNVILSGyFDSIGI-YQAVSDKqhklVQQWLDILGIDKRTADAPfHSLSWGQ-QRLAlIVRALVKHPTLLILDEPL 429
Cdd:PRK13650 96 GATVEDDVAFG-LENKGIpHEEMKER----VNEALELVGMQDFKEREP-ARLSGGQkQRVA-IAGAVAMRPKIIILDEAT 168
|
....*....
gi 488984360 430 QGLDPLNRQ 438
Cdd:PRK13650 169 SMLDPEGRL 177
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
276-428 |
1.73e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 276 INHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQG-YsndltlfgrrrgSGETIWD--------IK----KHIGYVS 342
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtY------------EGEIIFEgeelqasnIRdterAGIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 343 SSLHL--DYRVSTNV---RNVILSGYFDsigiYQAVSDKQHKLVQQwldiLGIDKrTADAPFHSLSWGQQRLALIVRALV 417
Cdd:PRK13549 89 QELALvkELSVLENIflgNEITPGGIMD----YDAMYLRAQKLLAQ----LKLDI-NPATPVGNLGLGQQQLVEIAKALN 159
|
170
....*....|.
gi 488984360 418 KHPTLLILDEP 428
Cdd:PRK13549 160 KQARLLILDEP 170
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
273-443 |
1.86e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 54.88 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 273 RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPqgySNDLTLFG----RRRGSGETIWdIKKHIGYVSSSLHL 347
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGiERP---SAGKIWFSghdiTRLKNREVPF-LRRQIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 348 --DYRVSTNVR-NVILSGyfdsigiyqAVSDKQHKLVQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLI 424
Cdd:PRK10908 91 lmDRTVYDNVAiPLIIAG---------ASGDDIRRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLL 160
|
170 180
....*....|....*....|
gi 488984360 425 LDEPLQGLD-PLNRQLVRRF 443
Cdd:PRK10908 161 ADEPTGNLDdALSEGILRLF 180
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
263-461 |
1.96e-08 |
|
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: 54.96 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 263 LNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYSNDLTLFGrrrgsGETIWDIK------- 335
Cdd:TIGR01978 3 IKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILFK-----GQDLLELEpderara 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 336 ---------KHIGYVSSSLHLdyRVSTNVRNvilsgyfdSIGIYQAVSDKQ-HKLVQQWLDILGID----KRTADAPFhs 401
Cdd:TIGR01978 78 glflafqypEEIPGVSNLEFL--RSALNARR--------SARGEEPLDLLDfEKLLKEKLALLDMDeeflNRSVNEGF-- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 402 lSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGaTQLLFVSHH 461
Cdd:TIGR01978 146 -SGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPD-RSFLIITHY 203
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
114-186 |
1.99e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 55.04 E-value: 1.99e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984360 114 ARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLD---VNSRQQlaaLLADLHSAGI 186
Cdd:COG1137 115 ERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiaVADIQK---IIRHLKERGI 187
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
269-465 |
2.00e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 55.02 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLV-------TGD-HPQGYSNDLTlfgrRRGSGETIWDIKKHIGY 340
Cdd:COG4161 11 FYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQlNIAGHQFDFS----QKPSEKAIRLLRQKVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 341 VSSSLHLdYRVSTNVRNVI-----LSGYFDSIGIYQAvsdkqhklvQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRA 415
Cdd:COG4161 87 VFQQYNL-WPHLTVMENLIeapckVLGLSKEQAREKA---------MKLLARLRLTDKADRFPLH-LSGGQQQRVAIARA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984360 416 LVKHPTLLILDEPLQGLDP-LNRQLVrRFVDVLIGEGATQLLfVSHHAEDA 465
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPeITAQVV-EIIRELSQTGITQVI-VTHEVEFA 204
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
119-445 |
2.08e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 119 LAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLhSAGITLVLV---LNRF 195
Cdd:PRK13409 196 VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIREL-AEGKYVLVVehdLAVL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 196 DEIPEFVQFA-------GVLadctlseTGEKSsllqqalvAQLAHSEKLDGItLPEPDV---PPA----RHALADSAPRI 261
Cdd:PRK13409 275 DYLADNVHIAygepgayGVV-------SKPKG--------VRVGINEYLKGY-LPEENMrirPEPiefeERPPRDESERE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 262 VL---NDGVVSYNDrpvinhLSWTVNPGEHWQ-----IVGPNGAGKSTLLSLVTGD-HPQgysndltlfgrrrgSGETIW 332
Cdd:PRK13409 339 TLveyPDLTKKLGD------FSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVlKPD--------------EGEVDP 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 333 DIKkhIGYVSSSLHLDY--RVSTNVRNV---ILSGYFdsigiyqavsdkQHKLVQQwldiLGIDkRTADAPFHSLSWGQ- 406
Cdd:PRK13409 399 ELK--ISYKPQYIKPDYdgTVEDLLRSItddLGSSYY------------KSEIIKP----LQLE-RLLDKNVKDLSGGEl 459
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 488984360 407 QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLV----RRFVD 445
Cdd:PRK13409 460 QRVA-IAACLSRDADLYLLDEPSAHLDVEQRLAVakaiRRIAE 501
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
119-445 |
2.31e-08 |
|
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: 56.33 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 119 LAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLV---LNRF 195
Cdd:COG1245 196 LAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVehdLAIL 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 196 DEIPEFVQFA-------GVLadctlseTGEKSsllqqalvAQLAHSEKLDGItLPEP-----------DVPPARhALADS 257
Cdd:COG1245 276 DYLADYVHILygepgvyGVV-------SKPKS--------VRVGINQYLDGY-LPEEnvrirdepiefEVHAPR-REKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 258 APRIVLNDGVVSYNDrpvinhLSWTVNPGEHWQ-----IVGPNGAGKSTLLSLVTG-DHPQgysndltlfgrrrgSGETI 331
Cdd:COG1245 339 ETLVEYPDLTKSYGG------FSLEVEGGEIREgevlgIVGPNGIGKTTFAKILAGvLKPD--------------EGEVD 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 332 WDIKkhIGY----VSSSlhLDYRVSTNVRNVILSGYFDSIGiyqavsdkQHKLVQQwldiLGIDkRTADAPFHSLSWGQ- 406
Cdd:COG1245 399 EDLK--ISYkpqyISPD--YDGTVEEFLRSANTDDFGSSYY--------KTEIIKP----LGLE-KLLDKNVKDLSGGEl 461
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 488984360 407 QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLV----RRFVD 445
Cdd:COG1245 462 QRVA-IAACLSRDADLYLLDEPSAHLDVEQRLAVakaiRRFAE 503
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-214 |
2.48e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQ--LQKLV--SDEWQRNNTDLLSPGEEDTG 99
Cdd:PRK15439 284 LEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlARGLVylPEDRQSSGLYLDAPLAWNVC 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 100 RTTAE---IIQDEVKDPARCARLAEQFGIS-ALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLA 175
Cdd:PRK15439 364 ALTHNrrgFWIKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIY 443
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984360 176 ALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLS 214
Cdd:PRK15439 444 QLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-260 |
2.75e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.20 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 1 MSSLQISQGTFRLSDTKTLKIDHLS--VAAGESWAFVGSNGSGKSALARAL-------AGDLpLLSGQ---RESHFSRVT 68
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSfhVQRGECFGLLGPNGAGKTTTLRMLlglthpdAGSI-SLCGEpvpSRARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 69 RLSFEQLQKLVSDEWQRNNtdLLSPGEEdTGRTTAEIiqdevkdPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQ 148
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVREN--LLVFGRY-FGLSAAAA-------RALVPPLLEFAKLENKADAKVGELSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 149 ALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNrfdeipeFVQFAGVLAD--CTLsETGEKssLLQQA 226
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH-------FMEEAERLCDrlCVI-EEGRK--IAEGA 221
|
250 260 270
....*....|....*....|....*....|....
gi 488984360 227 LVAQLAHSEKLDGITLPEPDVPPARHALADSAPR 260
Cdd:PRK13537 222 PHALIESEIGCDVIEIYGPDPVALRDELAPLAER 255
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
269-465 |
3.06e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 54.81 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYND--RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-----DHPQgysNDLTLFGRRRGSgETIWDIKKHIGYV 341
Cdd:PRK13640 14 TYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpdDNPN---SKITVDGITLTA-KTVWDIREKVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 342 SSSLHLDYrVSTNVRNVILSGYFDSigiyQAVSDKQHKLVQQWLDILGIdKRTADAPFHSLSWGQ-QRLAlIVRALVKHP 420
Cdd:PRK13640 90 FQNPDNQF-VGATVGDDVAFGLENR----AVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQkQRVA-IAGILAVEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984360 421 TLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDA 465
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-192 |
3.19e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.78 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 3 SLQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQK----L 78
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARrravL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 79 vsdewqRNNTDLLSPgeedtgRTTAEII--------QDEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQAL 150
Cdd:PRK13548 82 ------PQHSSLSFP------FTVEEVVamgraphgLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984360 151 M------TDPQLLILDEPFDGLDVNSRQQLAALLADL-HSAGITLVLVL 192
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVL 198
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
271-467 |
4.04e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 54.71 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 271 NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLL----SLVTGDHPQGYSNDLTlfgrrRGSGETIWDIKKHIGYVSSSLH 346
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAkhmnALLIPSEGKVYVDGLD-----TSDEENLWDIRNKAGMVFQNPD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 347 lDYRVSTNVRNVILSGYfDSIGIYQavsDKQHKLVQQWLDILGIDKRTADAPfHSLSWGQ-QRLAlIVRALVKHPTLLIL 425
Cdd:PRK13633 96 -NQIVATIVEEDVAFGP-ENLGIPP---EEIRERVDESLKKVGMYEYRRHAP-HLLSGGQkQRVA-IAGILAMRPECIIF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984360 426 DEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAEDAPD 467
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
24-210 |
4.06e-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: 54.22 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLP------LLSGQReshfsrVTRLSFEQLQKL------------------V 79
Cdd:COG1127 26 LDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpdsgeiLVDGQD------ITGLSEKELYELrrrigmlfqggalfdsltV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 80 sdeWQ------RNNTDLlspgeedtgrtTAEIIQDEVKDparcaRLaEQFGisaLLDRRFKY---LSTGETRKTLLCQAL 150
Cdd:COG1127 100 ---FEnvafplREHTDL-----------SEAEIRELVLE-----KL-ELVG---LPGAADKMpseLSGGMRKRVALARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984360 151 MTDPQLLILDEPFDGLDVNSRQQLAALLADLHSA-GITLVLVLNRFDEIPEFVQFAGVLAD 210
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLAD 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-180 |
4.26e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 53.27 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 23 HLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQreshfsrvTRLSFEQLQKLvSDEWQRNNT---------DLLSP 93
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGE--------VLWQGEPIRRQ-RDEYHQDLLylghqpgikTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 94 GE------EDTGRTTAEIIQDEVkdparcarlaEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLD 167
Cdd:PRK13538 92 LEnlrfyqRLHGPGDDEALWEAL----------AQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170
....*....|...
gi 488984360 168 VNSRQQLAALLAD 180
Cdd:PRK13538 162 KQGVARLEALLAQ 174
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
276-465 |
4.50e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 54.33 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 276 INHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRRgSGETIWDIKKHIGYVSSSLHLDYrVSTNV 355
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE-FEGKVKIDGELL-TAENVWNLRRKIGMVFQNPDNQF-VGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 356 RNVILSGyFDSIGIYQAVSDKqhKLVQQWLDILGIDKRTADAPfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPL 435
Cdd:PRK13642 100 EDDVAFG-MENQGIPREEMIK--RVDEALLAVNMLDFKTREPA--RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190
....*....|....*....|....*....|
gi 488984360 436 NRQLVRRFVDVLIGEGATQLLFVSHHAEDA 465
Cdd:PRK13642 175 GRQEIMRVIHEIKEKYQLTVLSITHDLDEA 204
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
272-440 |
4.91e-08 |
|
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: 53.63 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 272 DRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQGysndltlfgrrrgsGETIWDIKKHIGYVSSSLHLDYR 350
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYqPQG--------------GQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 351 V--------STNVRNVILSGYFD-SIGIYQAVSDKQHKLVQQWLDILGIDKRTADAPfHSLSWGQ-QRLAlIVRALVKHP 420
Cdd:cd03248 92 LvgqepvlfARSLQDNIAYGLQScSFECVKEAAQKAHAHSFISELASGYDTEVGEKG-SQLSGGQkQRVA-IARALIRNP 169
|
170 180
....*....|....*....|
gi 488984360 421 TLLILDEPLQGLDPLNRQLV 440
Cdd:cd03248 170 QVLILDEATSALDAESEQQV 189
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
264-464 |
5.29e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 54.31 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 264 NDGVVSYND-RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHpqgysndltlfgrRRGSGETIWDIKKhIGYVS 342
Cdd:PRK13639 5 RDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGIL-------------KPTSGEVLIKGEP-IKYDK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 343 SSLhldyrvsTNVRNvilsgyfdSIGIYQAVSDKQ--HKLVQQwlDI------LG-----IDKRTADA------------ 397
Cdd:PRK13639 71 KSL-------LEVRK--------TVGIVFQNPDDQlfAPTVEE--DVafgplnLGlskeeVEKRVKEAlkavgmegfenk 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 398 PFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATqlLFVSHHAED 464
Cdd:PRK13639 134 PPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGIT--IIISTHDVD 198
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
259-461 |
5.41e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.89 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 259 PRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVtgDHPQGYSNDLTLFGRRRGSGETIWDIKKHI 338
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL--NRMNELESEVRVEGRVEFFNQNIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 339 GYVSSSLHLDY--------RVSTNVR-NVILSGYFDSIGIyQAVSDKQHKLVQQWLDILG-IDKRTADapfhsLSWGQQR 408
Cdd:PRK14258 84 NRLRRQVSMVHpkpnlfpmSVYDNVAyGVKIVGWRPKLEI-DDIVESALKDADLWDEIKHkIHKSALD-----LSGGQQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984360 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHH 461
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
24-231 |
6.41e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 6.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQreshfsrvTRLSFEQLQKLVSDEWQRNnTDLLSPGEEDTGRTTa 103
Cdd:PRK10253 28 VEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGH--------VWLDGEHIQHYASKEVARR-IGLLAQNATTPGDIT- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 104 eiIQDEV----------------KDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLD 167
Cdd:PRK10253 98 --VQELVargryphqplftrwrkEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984360 168 VNSRQQLAALLADLH-SAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLLQQALVAQL 231
Cdd:PRK10253 176 ISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERI 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
5-181 |
6.46e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.20 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 5 QISQGTFRlsDTKTLK-IDHLS--VAAGESWAFVGSNGSGKSALARAL-------AGDLpLLSGQRESHFSRVTRlsfEQ 74
Cdd:PRK11308 16 PVKRGLFK--PERLVKaLDGVSftLERGKTLAVVGESGCGKSTLARLLtmietptGGEL-YYQGQDLLKADPEAQ---KL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 75 LQKLVSDEWQrNNTDLLSPgEEDTGRTTAE--IIQDEVKDPARCARLAEQFGISAL----LDRRFKYLSTGETRKTLLCQ 148
Cdd:PRK11308 90 LRQKIQIVFQ-NPYGSLNP-RKKVGQILEEplLINTSLSAAERREKALAMMAKVGLrpehYDRYPHMFSGGQRQRIAIAR 167
|
170 180 190
....*....|....*....|....*....|...
gi 488984360 149 ALMTDPQLLILDEPFDGLDVNSRQQLAALLADL 181
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMDL 200
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
270-460 |
6.75e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.86 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 270 YNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG------------DHPQGYSNDlTLFGRRRGSGETIWDIKKH 337
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGllrpqkgavlwqGKPLDYSKR-GLLALRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 338 IGYVSsslhLDYRVSTNVRNvilsgyfdsIGIYQAVSDKQhklVQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRALV 417
Cdd:PRK13638 90 IFYTD----IDSDIAFSLRN---------LGVPEAEITRR---VDEALTLVDA-QHFRHQPIQCLSHGQKKRVAIAGALV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984360 418 KHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGaTQLLFVSH 460
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQG-NHVIISSH 194
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
24-191 |
7.64e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.46 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAG-DLP-----LLSGQRESH---FSRVTRLSFEQLQklvsdewqrnntdlLSPG 94
Cdd:PRK11607 40 LTIYKGEIFALLGASGCGKSTLLRMLAGfEQPtagqiMLDGVDLSHvppYQRPINMMFQSYA--------------LFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 95 EEDTGRTTAEIIQDEVKDPARCARLAEQFGISALLD---RRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSR 171
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
|
170 180
....*....|....*....|.
gi 488984360 172 QQLAALLAD-LHSAGITLVLV 191
Cdd:PRK11607 186 DRMQLEVVDiLERVGVTCVMV 206
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
254-473 |
7.85e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 254 LADSAPRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGYSNDLTLFGRRRGsgetiw 332
Cdd:PRK13543 5 LHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGlLHVESGQIQIDGKTATRG------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 333 DIKKHIGYVS--SSLHLDYRVSTNVRNVI-LSGYfdsigiyqavsdKQHKLVQQWLDILGIDKRtADAPFHSLSWGQQRL 409
Cdd:PRK13543 79 DRSRFMAYLGhlPGLKADLSTLENLHFLCgLHGR------------RAKQMPGSALAIVGLAGY-EDTLVRQLSAGQKKR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984360 410 ALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDV-LIGEGATqlLFVSHHAEDAPDCITHRL 473
Cdd:PRK13543 146 LALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAhLRGGGAA--LVTTHGAYAAPPVRTRML 208
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
279-433 |
1.01e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.01 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 279 LSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPqgysndltlfgrrrGSGETIWDIKKHIGYVSSSLHLdYR--VSTNVR 356
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP--------------GSGSIQFAGQPLEAWSAAELAR-HRayLSQQQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 357 NVILSGYFDSIGIYQ---AVSDKQHKLVQQWLDILGIDKRTAdAPFHSLSWGQ-QRLAL------IVRALVKHPTLLILD 426
Cdd:PRK03695 80 PPFAMPVFQYLTLHQpdkTRTEAVASALNEVAEALGLDDKLG-RSVNQLSGGEwQRVRLaavvlqVWPDINPAGQLLLLD 158
|
....*..
gi 488984360 427 EPLQGLD 433
Cdd:PRK03695 159 EPMNSLD 165
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
10-245 |
1.54e-07 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 52.82 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 10 TFRLSDTKTLKIDH--LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGqreshfsRVT-----RLSFEQLqklvsde 82
Cdd:TIGR04520 7 SFSYPESEKPALKNvsLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSG-------KVTvdgldTLDEENL------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 83 WQ-RN-------NTD--LLSP--------GEEDTGRTTAEIIQdevkdpaRCARLAEQFGISALLDRRFKYLSTGETRKT 144
Cdd:TIGR04520 73 WEiRKkvgmvfqNPDnqFVGAtveddvafGLENLGVPREEMRK-------RVDEALKLVGMEDFRDREPHLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 145 LLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHS-AGITLVLVLNRFDEIPE----FVQFAG-VLADCTLSETGE 218
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDMEEAVLadrvIVMNKGkIVAEGTPREIFS 225
|
250 260 270
....*....|....*....|....*....|..
gi 488984360 219 KSSLLQQA-----LVAQLAHSEKLDGITLPEP 245
Cdd:TIGR04520 226 QVELLKEIgldvpFITELAKALKKRGIPLPPD 257
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
24-191 |
1.61e-07 |
|
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: 52.24 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLsfeqlqklvsDEWQRN-NTDL----LSPG---E 95
Cdd:cd03300 21 LDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL----------PPHKRPvNTVFqnyaLFPHltvF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 96 EDT--GRTTAEIIQDEVKdpARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQ 173
Cdd:cd03300 91 ENIafGLRLKKLPKAEIK--ERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKD 168
|
170
....*....|....*....
gi 488984360 174 LAALLADLH-SAGITLVLV 191
Cdd:cd03300 169 MQLELKRLQkELGITFVFV 187
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-194 |
1.75e-07 |
|
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: 51.82 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 14 SDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ----------------RE--SHFSRVTRLSFEQL 75
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSvlldgtdirqldpadlRRniGYVPQDVTLFYGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 76 qklvsdewqRNNTDLLSPGEEDtgrttAEIIqdevkdpaRCARLAeqfGISALLDR-----------RFKYLSTGETRKT 144
Cdd:cd03245 95 ---------RDNITLGAPLADD-----ERIL--------RAAELA---GVTDFVNKhpngldlqigeRGRGLSGGQRQAV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984360 145 LLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLhSAGITLVLVLNR 194
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHR 198
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
275-484 |
1.78e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.78 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 275 VINHLSWTVNPGEHWQIVGPNGAGKST-------LLSLVTG---------------DHPQGYSNDLTLFGRRRGSGETIW 332
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTfiehlnaLLLPDTGtiewifkdeknkkktKEKEKVLEKLVIQKTRFKKIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 333 DIKKHIGYVSSSLHLDYRVSTNVRNVILSGYfdSIGIyqavsDKQH--KLVQQWLDILGIDKRTAD-APFhSLSWGQQRL 409
Cdd:PRK13651 102 EIRRRVGVVFQFAEYQLFEQTIEKDIIFGPV--SMGV-----SKEEakKRAAKYIELVGLDESYLQrSPF-ELSGGQKRR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 410 ALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLfVSHHAEDAPDcITHRLAFVPSG----DGYTY 484
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIIL-VTHDLDNVLE-WTKRTIFFKDGkiikDGDTY 250
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
261-445 |
1.85e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 52.39 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgysndltLFGRRRGS----GETIWDIK- 335
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISR-----------LLPPDSGEvlvdGLDVATTPs 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 336 ----KHIGYVSSSLHLDYRVStnVRNVILSGYFD-SIGiyqAVSDKQHKLVQQWLDILGIDKrTADAPFHSLSWGQQRLA 410
Cdd:COG4604 71 relaKRLAILRQENHINSRLT--VRELVAFGRFPySKG---RLTAEDREIIDEAIAYLDLED-LADRYLDELSGGQRQRA 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984360 411 LIVRALVKHPTLLILDEPLQGLDPLN-RQ---LVRRFVD 445
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHsVQmmkLLRRLAD 183
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
136-200 |
1.88e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 1.88e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984360 136 LSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNrfdEIPE 200
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISS---ELPE 467
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-247 |
1.95e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 52.36 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 15 DTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVT--RLSFEQLQKLVSDEWQRNNTDLLs 92
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPEYQLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 93 pgeEDT-------GRTTAEIIQDEVKDpaRCARLAEQFGIS--ALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPF 163
Cdd:PRK13637 98 ---EETiekdiafGPINLGLSEEEIEN--RVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 164 DGLDVNSRQQLAALLADLHSA-GITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLLQQAlvaqlahsEKLDGITL 242
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEV--------ETLESIGL 244
|
....*
gi 488984360 243 PEPDV 247
Cdd:PRK13637 245 AVPQV 249
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-181 |
2.15e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 3 SLQISQGTF-RLSDTKT-LKIDHLSVAAGESWAFVGSNGSGKSALARALagdLPLLSGQRE--------SHFSRVTRLSF 72
Cdd:PRK15134 284 AFPIRKGILkRTVDHNVvVKNISFTLRPGETLGLVGESGSGKSTTGLAL---LRLINSQGEiwfdgqplHNLNRRQLLPV 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 73 E-QLQKLVSDEWQRNNTDLlspgeedtgrTTAEIIQD--EVKDPARCARLAEQFGISAL----LD--RRFKY---LSTGE 140
Cdd:PRK15134 361 RhRIQVVFQDPNSSLNPRL----------NVLQIIEEglRVHQPTLSAAQREQQVIAVMeevgLDpeTRHRYpaeFSGGQ 430
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984360 141 TRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADL 181
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSL 471
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
24-191 |
2.17e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.80 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDlpllsgqreshfSRVTRLSFEQLQKLVSDeWQ-----RNNTDLLSPGEEDT 98
Cdd:PRK11614 26 LHINQGEIVTLIGANGAGKTTLLGTLCGD------------PRATSGRIVFDGKDITD-WQtakimREAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 99 GRTTAE-------IIQDEVKDPARCARLAEQFgiSALLDRRFK---YLSTGETRKTLLCQALMTDPQLLILDEPFDGLDV 168
Cdd:PRK11614 93 SRMTVEenlamggFFAERDQFQERIKWVYELF--PRLHERRIQragTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180
....*....|....*....|...
gi 488984360 169 NSRQQLAALLADLHSAGITLVLV 191
Cdd:PRK11614 171 IIIQQIFDTIEQLREQGMTIFLV 193
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
269-465 |
2.21e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 51.94 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLL-SLVTGDHPQgySNDLTLFGRR-----RGSGETIWDIKKHIGYVS 342
Cdd:PRK11124 11 FYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLrVLNLLEMPR--SGTLNIAGNHfdfskTPSDKAIRELRRNVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 343 SSLHLdYRVSTNVRNVI-----LSGYFDSIGIYQAvsdkqhklvQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALV 417
Cdd:PRK11124 89 QQYNL-WPHLTVQQNLIeapcrVLGLSKDQALARA---------EKLLERLRLKPYADRFPLH-LSGGQQQRVAIARALM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984360 418 KHPTLLILDEPLQGLDP-LNRQLVrRFVDVLIGEGATQLLfVSHHAEDA 465
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPeITAQIV-SIIRELAETGITQVI-VTHEVEVA 204
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-433 |
2.23e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ-----RESHFSRvTRLSFEQLQKLVSDEWQrnntdlLSPGeedt 98
Cdd:PRK11288 25 FDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSilidgQEMRFAS-TTAALAAGVAIIYQELH------LVPE---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 99 gRTTAEIIQ-----------DEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLD 167
Cdd:PRK11288 94 -MTVAENLYlgqlphkggivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 168 VNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEK-SSLLQQALVAQLAHSEkLDGITLPEPd 246
Cdd:PRK11288 173 AREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDmAQVDRDQLVQAMVGRE-IGDIYGYRP- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 247 vpparHALADSAPRI--VLNDGVVSyndrPVinhlSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysNDLTLFGR 323
Cdd:PRK11288 251 -----RPLGEVRLRLdgLKGPGLRE----PI----SFSVRAGEIVGLFGLVGAGRSELMKLLYGaTRRTA--GQVYLDGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 324 R---RGSGETIW--------DIKK----HIGYVSSSLHLDYRvstnvRNVILSGYFdsigiyqaVSDKQH-KLVQQWLDI 387
Cdd:PRK11288 316 PidiRSPRDAIRagimlcpeDRKAegiiPVHSVADNINISAR-----RHHLRAGCL--------INNRWEaENADRFIRS 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 488984360 388 LGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:PRK11288 383 LNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
249-311 |
2.25e-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: 51.76 E-value: 2.25e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984360 249 PARHALADSAPRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHP 311
Cdd:cd03220 11 PTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiYPP 74
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-190 |
2.43e-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: 51.70 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 14 SDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQK---LVSDE---WQRNN 87
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSkvsLVGQEpvlFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 88 TDLLSPGEedTGRTTAEIIQDEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLD 167
Cdd:cd03248 105 QDNIAYGL--QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180
....*....|....*....|...
gi 488984360 168 VNSRQQLAALLADLHSAGITLVL 190
Cdd:cd03248 183 AESEQQVQQALYDWPERRTVLVI 205
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
23-191 |
2.54e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 51.55 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 23 HLSVAAGESWAFVGSNGSGKSALARALAgdlpLL----SGQ---RESHFSRVTRLSFEQLQKL---VSDEWQRNNtdlLS 92
Cdd:COG4161 22 NLECPSGETLVLLGPSGAGKSSLLRVLN----LLetpdSGQlniAGHQFDFSQKPSEKAIRLLrqkVGMVFQQYN---LW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 93 PG---EEDTgrTTAEI-IQDEVKDPA--RCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGL 166
Cdd:COG4161 95 PHltvMENL--IEAPCkVLGLSKEQAreKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180
....*....|....*....|....*
gi 488984360 167 DVNSRQQLAALLADLHSAGITLVLV 191
Cdd:COG4161 173 DPEITAQVVEIIRELSQTGITQVIV 197
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
128-198 |
2.84e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.65 E-value: 2.84e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 128 LLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHS---AGITLV-----LVLNRFDEI 198
Cdd:PRK09544 113 LIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRReldCAVLMVshdlhLVMAKTDEV 191
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
12-192 |
2.89e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 53.13 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 12 RLSDTKTLKIDHLSVA-AGESWAFVGSNGSGKSALARALAGDLP---LLSGQRESHFSRVTRlsfeQLQKLVSDEWQRNn 87
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAkPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDA----KEMRAISAYVQQD- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 88 tDLLSPGeedtgRTTAE--IIQDEVKDPARCARLAEQFGISALLDR---------------RFKYLSTGETRKTLLCQAL 150
Cdd:TIGR00955 108 -DLFIPT-----LTVREhlMFQAHLRMPRRVTKKEKRERVDEVLQAlglrkcantrigvpgRVKGLSGGERKRLAFASEL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984360 151 MTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVL 192
Cdd:TIGR00955 182 LTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTI 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-191 |
3.02e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 51.55 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 3 SLQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAgdlpLL----SGQRE---SHFSRVTRLSFEQL 75
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLN----LLemprSGTLNiagNHFDFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 76 QKL---VSDEWQRNNtdlLSPgeedtgrtTAEIIQDEVKDPARCARLAEQFGIS---ALLDR--------RFK-YLSTGE 140
Cdd:PRK11124 78 RELrrnVGMVFQQYN---LWP--------HLTVQQNLIEAPCRVLGLSKDQALAraeKLLERlrlkpyadRFPlHLSGGQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984360 141 TRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLV 191
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIV 197
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
271-460 |
3.10e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 271 NDRPVINHLSWTVNPGEHWQIVGPNGAGKS-TLLSLV------TGDHPQG----------YSNDLTLFGRRRGSGETIW- 332
Cdd:PRK15134 20 TVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpspPVVYPSGdirfhgesllHASEQTLRGVRGNKIAMIFq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 333 ----------DIKKHIgYVSSSLHLDYRVSTnVRNVILSGyFDSIGIYQAVsdkqhklvqqwldilgidKRTADAPfHSL 402
Cdd:PRK15134 100 epmvslnplhTLEKQL-YEVLSLHRGMRREA-ARGEILNC-LDRVGIRQAA------------------KRLTDYP-HQL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984360 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSH 460
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITH 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
12-191 |
3.36e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.60 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 12 RLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAG-DLP----LLSGQRESHFSRV-TRLSFEQLQKLvsdEWQR 85
Cdd:PRK11247 21 RYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGlETPsageLLAGTAPLAEAREdTRLMFQDARLL---PWKK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 86 --NNTDLlspGEEDTGRTTAEIIQDEVkdparcarlaeqfgisALLDRRFKY---LSTGETRKTLLCQALMTDPQLLILD 160
Cdd:PRK11247 98 viDNVGL---GLKGQWRDAALQALAAV----------------GLADRANEWpaaLSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190
....*....|....*....|....*....|....
gi 488984360 161 EPFDGLDVNSR---QQLAALLADLHsaGITLVLV 191
Cdd:PRK11247 159 EPLGALDALTRiemQDLIESLWQQH--GFTVLLV 190
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-460 |
3.56e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 2 SSLQISQGTFRLSDTKTLKIDhlsvaAGESWAFVGSNGSGKSALARALAGDL----------------------PLLS-- 57
Cdd:PRK10636 5 SSLQIRRGVRVLLDNATATIN-----PGQKVGLVGKNGCGKSTLLALLKNEIsadggsytfpgnwqlawvnqetPALPqp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 58 -------GQREshfsrvtrlsFEQLQKLVSDEWQRNNTDLLSP--GEEDTgrTTAEIIQdevkdpARCARLAEQFGIS-A 127
Cdd:PRK10636 80 aleyvidGDRE----------YRQLEAQLHDANERNDGHAIATihGKLDA--IDAWTIR------SRAASLLHGLGFSnE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 128 LLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSagiTLVLVLNRFDEIPEFVQFAGV 207
Cdd:PRK10636 142 QLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 208 LADCTLSE-TGEKSSL---------LQQAL-------VAQLAHS---------------------EKLDGITLPEPDVPP 249
Cdd:PRK10636 219 IEQQSLFEyTGNYSSFevqratrlaQQQAMyesqqerVAHLQSYidrfrakatkakqaqsrikmlERMELIAPAHVDNPF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 250 ARHALA-DSAPRIVLNDGVVS--YNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQgysndltlfgrrr 325
Cdd:PRK10636 299 HFSFRApESLPNPLLKMEKVSagYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGElAPV------------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 326 gSGETIWDIKKHIGYVSSSlHLDYRVStnvrnvilsgyfDSIGIYQAVSDKQHKLVQQWLDILGI-----DKRTadAPFH 400
Cdd:PRK10636 366 -SGEIGLAKGIKLGYFAQH-QLEFLRA------------DESPLQHLARLAPQELEQKLRDYLGGfgfqgDKVT--EETR 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984360 401 SLSWGQQR---LALIVRalvKHPTLLILDEPLQGLDPLNRQ-LVRRFVDVligEGAtqLLFVSH 460
Cdd:PRK10636 430 RFSGGEKArlvLALIVW---QRPNLLLLDEPTNHLDLDMRQaLTEALIDF---EGA--LVVVSH 485
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-245 |
3.65e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 51.56 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 23 HLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQreshfsrvTRLSFEQLQKlvsdewQRNNTDLlSPGEEDTG--- 99
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGT--------VTIGERVITA------GKKNKKL-KPLRKKVGivf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 100 ---------RTTAEII----------QDEVKDPARcaRLAEQFGIS-ALLDRRFKYLSTGETRKTLLCQALMTDPQLLIL 159
Cdd:PRK13634 92 qfpehqlfeETVEKDIcfgpmnfgvsEEDAKQKAR--EMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 160 DEPFDGLDVNSRQQLAALLADLH-SAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGE-------------------K 219
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLHkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTpreifadpdeleaigldlpE 249
|
250 260
....*....|....*....|....*.
gi 488984360 220 SSLLQQALVAQLahsekldGITLPEP 245
Cdd:PRK13634 250 TVKFKRALEEKF-------GISFPKP 268
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
259-460 |
4.64e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.34 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 259 PRIVLNDGVvsyndrpvinhlSWTVNPGE-HwQIVGPNGAGKSTLLSLVTGdhpqGYSNDltlfgrrrgSGETIWD---- 333
Cdd:COG3845 16 GGVVANDDV------------SLTVRPGEiH-ALLGENGAGKSTLMKILYG----LYQPD---------SGEILIDgkpv 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 334 --------IKKHIGYVssslH---LDYRVSTNVRNVILsGYFDSIGIY----------QAVSDKQHklvqqwldiLGIDk 392
Cdd:COG3845 70 rirsprdaIALGIGMV----HqhfMLVPNLTVAENIVL-GLEPTKGGRldrkaarariRELSERYG---------LDVD- 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984360 393 rtADAPFHSLSWG-QQRLAlIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDV---LIGEGATqLLFVSH 460
Cdd:COG3845 135 --PDAKVEDLSVGeQQRVE-ILKALYRGARILILDEPTAVLTP---QEADELFEIlrrLAAEGKS-IIFITH 199
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
24-231 |
4.74e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.05 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGqreshfsRVTrLSFEQLQKLVSDEWQRNNTDLLsPGEEDTGRTTA 103
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAG-------NII-IDDEDISLLPLHARARRGIGYL-PQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 104 ---------EIIQDEVKD--PARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQ 172
Cdd:PRK10895 95 vydnlmavlQIRDDLSAEqrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 173 QLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLLQQALVAQL 231
Cdd:PRK10895 175 DIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRV 233
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-208 |
4.77e-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: 50.61 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHfSRVTRL-----SFeqlqklvsdewqrnNTDLlsPGEEDT 98
Cdd:cd03220 43 FEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR-GRVSSLlglggGF--------------NPEL--TGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 99 -------GRTTAEIiqDEVKDpaRCARLAEqfgISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSR 171
Cdd:cd03220 106 ylngrllGLSRKEI--DEKID--EIIEFSE---LGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984360 172 QQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVL 208
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVL 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
10-244 |
5.00e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.34 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 10 TFRLSDTKTLKIDHLSVAAGE-SW-AFVGSNGSGKSALARALAGDLPLLSGQReshfSRVTRLSFEQLQKLVSDEWQRNN 87
Cdd:PRK13640 12 SFTYPDSKKPALNDISFSIPRgSWtALIGHNGSGKSTISKLINGLLLPDDNPN----SKITVDGITLTAKTVWDIREKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 88 TDLLSPGEEDTGRTtaeiIQDEV------------KDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQ 155
Cdd:PRK13640 88 IVFQNPDNQFVGAT----VGDDVafglenravprpEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 156 LLILDEPFDGLDVNSRQQLAALLADLH-SAGITLVLVLNRFDEIPEFVQF-----AGVLADCTLSETGEKSSLLQQA--- 226
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEANMADQVlvlddGKLLAQGSPVEIFSKVEMLKEIgld 243
|
250 260
....*....|....*....|
gi 488984360 227 --LVAQLAHSEKLDGITLPE 244
Cdd:PRK13640 244 ipFVYKLKNKLKEKGISVPQ 263
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
276-467 |
5.53e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.98 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 276 INHLSWTVNPGEHWQIVGPNGAGKSTLLSlvtgdHPQGY----SNDLTLFGRR---RGSGETIWDIKKHIGYVssslhLD 348
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQ-----HFNALlkpsSGTITIAGYHitpETGNKNLKKLRKKVSLV-----FQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 349 YRVSTNVRNVILSGYFDSIGIYQAVSDKQHKLVQQWLDILGIDKRTAD-APFhSLSWGQQRLALIVRALVKHPTLLILDE 427
Cdd:PRK13641 93 FPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISkSPF-ELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984360 428 PLQGLDPLNR-QLVRRFVDVLiGEGATQLLfVSHHAEDAPD 467
Cdd:PRK13641 172 PAAGLDPEGRkEMMQLFKDYQ-KAGHTVIL-VTHNMDDVAE 210
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
268-433 |
5.73e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.80 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 268 VSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGdHPqGYSndlTLFGRRRGSGETIWDI----KKHIG---- 339
Cdd:CHL00131 15 ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HP-AYK---ILEGDILFKGESILDLepeeRAHLGifla 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 340 --Y------VSSSLHLdyRVSTNVRNVILS-GYFDSIGIYQAVSDKqhklvqqwLDILGIDK----RTADAPFhslSWGQ 406
Cdd:CHL00131 90 fqYpieipgVSNADFL--RLAYNSKRKFQGlPELDPLEFLEIINEK--------LKLVGMDPsflsRNVNEGF---SGGE 156
|
170 180
....*....|....*....|....*..
gi 488984360 407 QRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLD 183
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-178 |
5.74e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.85 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFE-----QLQKLVSdeWqRNNTDLLSPGEEDT 98
Cdd:PRK11248 22 LTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAErgvvfQNEGLLP--W-RNVQDNVAFGLQLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 99 GRTTAEIIQdevkdpaRCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALL 178
Cdd:PRK11248 99 GVEKMQRLE-------IAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLL 171
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
276-433 |
5.79e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.97 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 276 INHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQG--YSNDLTLFGRRRGSgetiWDIKKHIGYVSSSlhlDYRVST 353
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkGSGSVLLNGMPIDA----KEMRAISAYVQQD---DLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 354 -NVRNVIlsgyfdsigIYQA-------VSDKQHKL-VQQWLDILGI----DKRTADAPFH-SLSWGQ-QRLALIVRALvK 418
Cdd:TIGR00955 114 lTVREHL---------MFQAhlrmprrVTKKEKRErVDEVLQALGLrkcaNTRIGVPGRVkGLSGGErKRLAFASELL-T 183
|
170
....*....|....*
gi 488984360 419 HPTLLILDEPLQGLD 433
Cdd:TIGR00955 184 DPPLLFCDEPTSGLD 198
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
267-463 |
5.90e-07 |
|
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: 49.46 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 267 VVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgysndltlfgrrrGSGETIWDIKKHIGYVSsslH 346
Cdd:cd03223 8 LATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPW-------------GSGRIGMPEGEDLLFLP---Q 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 347 LDYRVSTNVRNVIlsgyfdsigIYqavsdkqhklvqQWLDILGIDKrtadapfhslswgQQRLALIvRALVKHPTLLILD 426
Cdd:cd03223 72 RPYLPLGTLREQL---------IY------------PWDDVLSGGE-------------QQRLAFA-RLLLHKPKFVFLD 116
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984360 427 EPLQGLDPlnrQLVRRFVDVLIGEGATqLLFVSHHAE 463
Cdd:cd03223 117 EATSALDE---ESEDRLYQLLKELGIT-VISVGHRPS 149
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
243-305 |
6.16e-07 |
|
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: 52.13 E-value: 6.16e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984360 243 PEPDVPPARHALADSAPRIVLNDGVVSYN-DRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSL 305
Cdd:COG5265 340 PEVADAPDAPPLVVGGGEVRFENVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARL 403
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-63 |
6.28e-07 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 49.78 E-value: 6.28e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984360 4 LQISQGTFR-----LSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESH 63
Cdd:cd03250 1 ISVEDASFTwdsgeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP 65
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-197 |
6.49e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 50.78 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 10 TFRLSDTKTLKIDHLS--VAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLVSDEWQRNN 87
Cdd:PRK13635 12 SFRYPDAATYALKDVSfsVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 88 T--------DLLSPGEEDTGRTTAEIIQdevkdpaRCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLIL 159
Cdd:PRK13635 92 NqfvgatvqDDVAFGLENIGVPREEMVE-------RVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984360 160 DEPFDGLDVNSRQQLAALLADL-HSAGITLVLVLNRFDE 197
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDE 203
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-240 |
6.87e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.53 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ---RESHFSRVTRLSFEQLQKLVSDEWQRNN--TDL------LS 92
Cdd:PRK11831 28 LTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEilfDGENIPAMSRSRLYTVRKRMSMLFQSGAlfTDMnvfdnvAY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 93 PGEEDTgRTTAEIIQDEV--KDPARCARLAEQFGISALldrrfkylSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNS 170
Cdd:PRK11831 108 PLREHT-QLPAPLLHSTVmmKLEAVGLRGAAKLMPSEL--------SGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984360 171 RQQLAALLADL-HSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLL--QQALVAQLahsekLDGI 240
Cdd:PRK11831 179 MGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQanPDPRVRQF-----LDGI 246
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
33-198 |
6.97e-07 |
|
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: 49.86 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 33 AFVGSNGSGKSALARALAGdlpllsgqreshfsRVTRLSfeqlqklVSDEWQRNNTDLlspGEEDTGRTTAEIIQDEVKD 112
Cdd:cd03213 39 AIMGPSGAGKSTLLNALAG--------------RRTGLG-------VSGEVLINGRPL---DKRSFRKIIGYVPQDDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 113 PARCARlaEQFGISALLdrrfKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVL 192
Cdd:cd03213 95 PTLTVR--ETLMFAAKL----RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSI 168
|
170
....*....|....
gi 488984360 193 --------NRFDEI 198
Cdd:cd03213 169 hqpsseifELFDKL 182
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
271-434 |
7.07e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.00 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 271 NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG--DHPQG-------YSNDLTLFGRRRGSGET--IWDIKKHIG 339
Cdd:PRK13631 37 NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGliKSKYGtiqvgdiYIGDKKNNHELITNPYSkkIKNFKELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 340 YVSSSLHL-DYRV-STNVRNVILsgyFDSIGIYQAVSDKqHKLVQQWLDILGIDKRTAD-APFhSLSWGQQRLALIVRAL 416
Cdd:PRK13631 117 RVSMVFQFpEYQLfKDTIEKDIM---FGPVALGVKKSEA-KKLAKFYLNKMGLDDSYLErSPF-GLSGGQKRRVAIAGIL 191
|
170
....*....|....*...
gi 488984360 417 VKHPTLLILDEPLQGLDP 434
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDP 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-171 |
1.01e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 2 SSLQISQGTFRLsdtktlKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQreshFSRVTRLSFEQlQKLVSD 81
Cdd:PRK13409 344 PDLTKKLGDFSL------EVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE----VDPELKISYKP-QYIKPD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 82 ------EWQRNNTDLLSpgeedtgrttAEIIQDEVKDParcarlaeqFGISALLDRRFKYLSTGETRKTLLCQALMTDPQ 155
Cdd:PRK13409 413 ydgtveDLLRSITDDLG----------SSYYKSEIIKP---------LQLERLLDKNVKDLSGGELQRVAIAACLSRDAD 473
|
170
....*....|....*.
gi 488984360 156 LLILDEPFDGLDVNSR 171
Cdd:PRK13409 474 LYLLDEPSAHLDVEQR 489
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
24-182 |
1.08e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.80 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAG-------DLpLLSGQRESHFSRVTR---LSFeQLQKLVSdewQRNNTDLLSP 93
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGleditsgDL-FIGEKRMNDVPPAERgvgMVF-QSYALYP---HLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 94 GEEDTGRTTAEIIQdevkdpaRCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQ 173
Cdd:PRK11000 99 GLKLAGAKKEEINQ-------RVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQ 171
|
....*....
gi 488984360 174 LAALLADLH 182
Cdd:PRK11000 172 MRIEISRLH 180
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
268-445 |
1.10e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 268 VSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGY--SNDLTLFGRRRGSgetiwDIKKHIGYVSSS- 344
Cdd:TIGR00956 771 IKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVitGGDRLVNGRPLDS-----SFQRSIGYVQQQd 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 345 LHLDyrvSTNVR-NVILSGYFDSigiYQAVSDKQ-HKLVQQWLDILGIDKrTADA----PFHSLSWGQQRLALIVRALVK 418
Cdd:TIGR00956 846 LHLP---TSTVReSLRFSAYLRQ---PKSVSKSEkMEYVEEVIKLLEMES-YADAvvgvPGEGLNVEQRKRLTIGVELVA 918
|
170 180 190
....*....|....*....|....*....|..
gi 488984360 419 HPTLLI-LDEPLQGLDPLNR----QLVRRFVD 445
Cdd:TIGR00956 919 KPKLLLfLDEPTSGLDSQTAwsicKLMRKLAD 950
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
282-467 |
1.11e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 50.13 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 282 TVNPGEHWQIVGPNGAGKSTLLSLVTGDH-PQgySNDLTLFGRRRGSGETIWDIK---KHIGYVSSSLHLDYRVSTNVRN 357
Cdd:PRK13649 29 TIEDGSYTAFIGHTGSGKSTIMQLLNGLHvPT--QGSVRVDDTLITSTSKNKDIKqirKKVGLVFQFPESQLFEETVLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 358 VILSGyfDSIGIYQavsDKQHKLVQQWLDILGIDKRTAD-APFhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLN 436
Cdd:PRK13649 107 VAFGP--QNFGVSQ---EEAEALAREKLALVGISESLFEkNPF-ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190
....*....|....*....|....*....|.
gi 488984360 437 RQLVRRFVDVLIGEGATQLLfVSHHAEDAPD 467
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVL-VTHLMDDVAN 210
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
257-442 |
1.21e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.45 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 257 SAPRIVLNDGVVSYND--RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSlvtgdhpqgysndlTLFGRRRGSGETIWDi 334
Cdd:TIGR01271 1214 SGGQMDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLS--------------ALLRLLSTEGEIQID- 1278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 335 kkHIGYVSSSLHlDYRVSTNV---RNVILSGYF-DSIGIYQAVSDKQ----------HKLVQQWLDILgiDKRTADAPFh 400
Cdd:TIGR01271 1279 --GVSWNSVTLQ-TWRKAFGVipqKVFIFSGTFrKNLDPYEQWSDEEiwkvaeevglKSVIEQFPDKL--DFVLVDGGY- 1352
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984360 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRR 442
Cdd:TIGR01271 1353 VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRK 1394
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
9-191 |
1.38e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.79 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 9 GTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ-----RESHF------SRVTRLSFE---- 73
Cdd:PRK15112 19 GWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGElliddHPLHFgdysyrSQRIRMIFQdpst 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 74 -----QLQKLVSDEWQRNNTDLLSPGEEDtgrttaEIIQDevkdparcarlAEQFGIsaLLDRRFKY---LSTGETRKTL 145
Cdd:PRK15112 99 slnprQRISQILDFPLRLNTDLEPEQREK------QIIET-----------LRQVGL--LPDHASYYphmLAPGQKQRLG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984360 146 LCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSA-GITLVLV 191
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYV 206
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
136-341 |
1.62e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 136 LSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLhsAGiTLVLV----------------LNRFDEIP 199
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY--PG-TVVAVthdryfldnvagwileLDRGRGIP 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 200 -EfvqfagvladctlsetGEKSSLLQQ--ALVAQLAHSEK---------LDGITLPepdvPPARHA-----------LAD 256
Cdd:PRK11819 241 wE----------------GNYSSWLEQkaKRLAQEEKQEAarqkalkreLEWVRQS----PKARQAkskarlaryeeLLS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 257 SA---------------PRivLNDGVV-------SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHpQGY 314
Cdd:PRK11819 301 EEyqkrnetneifippgPR--LGDKVIeaenlskSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQE-QPD 377
|
250 260
....*....|....*....|....*..
gi 488984360 315 SNDLTLfgrrrgsGETIwdikkHIGYV 341
Cdd:PRK11819 378 SGTIKI-------GETV-----KLAYV 392
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-230 |
1.65e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPllsGQRESHFSRVT---RLSFEQLQKLVSDEWQRNNTDLLSPGEEDTGR 100
Cdd:PRK13547 22 LRIEPGRVTALLGRNGAGKSTLLKALAGDLT---GGGAPRGARVTgdvTLNGEPLAAIDAPRLARLRAVLPQAAQPAFAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 101 TTAEII------------QDEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQAL---------MTDPQLLIL 159
Cdd:PRK13547 99 SAREIVllgrypharragALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 160 DEPFDGLDVNSRQQL----AALLADLHSAGITLV----LVLNRFDEIpefvqfaGVLADCTLSETGEKSSLLQQALVAQ 230
Cdd:PRK13547 179 DEPTAALDLAHQHRLldtvRRLARDWNLGVLAIVhdpnLAARHADRI-------AMLADGAIVAHGAPADVLTPAHIAR 250
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
268-463 |
1.65e-06 |
|
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: 48.68 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 268 VSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGdHPqgysndltlfgrrrgsgetiwdikkhigyvssslhl 347
Cdd:cd03217 8 VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HP------------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 348 DYRVstnVRNVILsgyFDSIGIYQAVSDKQHKL-----VQQWLDILGIdkRTADapF-----HSLSWGQQRLALIVRALV 417
Cdd:cd03217 51 KYEV---TEGEIL---FKGEDITDLPPEERARLgiflaFQYPPEIPGV--KNAD--FlryvnEGFSGGEKKRNEILQLLL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984360 418 KHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGaTQLLFVSHHAE 463
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKLREEG-KSVLIITHYQR 165
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
265-433 |
1.72e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.65 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 265 DGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQGYSNDLTLFGRRRGSgetiwDIKKHIGYVSS 343
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiQGNNFTGTILANNRKPTK-----QILKRTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 344 S----LHLdyrvstNVRNVILsgyFDSIGIYQAVSDKQHKL--VQQWLDILGIDK----RTADAPFHSLSWGQQRLALIV 413
Cdd:PLN03211 148 DdilyPHL------TVRETLV---FCSLLRLPKSLTKQEKIlvAESVISELGLTKcentIIGNSFIRGISGGERKRVSIA 218
|
170 180
....*....|....*....|
gi 488984360 414 RALVKHPTLLILDEPLQGLD 433
Cdd:PLN03211 219 HEMLINPSLLILDEPTSGLD 238
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
280-443 |
2.96e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.77 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 280 SWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHP-----------QGYSNDLTLFG--RRRGSGETIWdikkhiGYVssslH 346
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLApdagevhyrmrDGQLRDLYALSeaERRRLLRTEW------GFV----H 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 347 LDYR------VST--NVRNVILSgyfdsIGI--YQAVSDKqhklVQQWLDILGID-KRTADAPfHSLSWG-QQRLAlIVR 414
Cdd:PRK11701 96 QHPRdglrmqVSAggNIGERLMA-----VGArhYGDIRAT----AGDWLERVEIDaARIDDLP-TTFSGGmQQRLQ-IAR 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984360 415 ALVKHPTLLILDEPLQGLD--------PLNRQLVRRF 443
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDvsvqarllDLLRGLVREL 201
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-225 |
3.03e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.84 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 23 HLSVAAGESWAFVGSNGSGKSALARALAGDLP-----LLSGQReshfsrVTRLSFEQLQKLVSdeWQRNNTDLLSPGEED 97
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslKINGIE------LRELDPESWRKHLS--WVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 98 TGRTTAEIIQDEVKDPARCARLAEQFgISAL---LDRRFK----YLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNS 170
Cdd:PRK11174 442 NVLLGNPDASDEQLQQALENAWVSEF-LPLLpqgLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488984360 171 RQQLAALLADLhSAGITLVLVLNRFDEIPEFVQFAgVLADCTLSETGEKSSLLQQ 225
Cdd:PRK11174 521 EQLVMQALNAA-SRRQTTLMVTHQLEDLAQWDQIW-VMQDGQIVQQGDYAELSQA 573
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
10-193 |
3.08e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.03 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 10 TFRLSDTKTLKIDHLSV--AAGESWAFVGSNGSGKSALARALAGdlpllsgqreshfsrVTRLSFeqlqKLVSDEWQRNN 87
Cdd:PRK15093 12 EFKTSDGWVKAVDRVSMtlTEGEIRGLVGESGSGKSLIAKAICG---------------VTKDNW----RVTADRMRFDD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 88 TDLL--SPGEED--TGRTTAEIIQD--EVKDPA-----------------------------RCARLAEQFGISALLD-- 130
Cdd:PRK15093 73 IDLLrlSPRERRklVGHNVSMIFQEpqSCLDPServgrqlmqnipgwtykgrwwqrfgwrkrRAIELLHRVGIKDHKDam 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984360 131 RRFKY-LSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLN 193
Cdd:PRK15093 153 RSFPYeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLIS 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-202 |
3.32e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.40 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 15 DTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVT-RLSFEQLQK---LVSDEWQRN---- 86
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKgmaYITESRRDNgffp 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 87 NTDL-----LSPGEEDTGRTTAEIIQDEVKDparcARLAEQ----FGIS-ALLDRRFKYLSTGETRKTLLCQALMTDPQL 156
Cdd:PRK09700 355 NFSIaqnmaISRSLKDGGYKGAMGLFHEVDE----QRTAENqrelLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984360 157 LILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNrfdEIPEFV 202
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSS---ELPEII 473
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
269-460 |
3.90e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.28 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 269 SYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRGSGETIWDIKKHIGYVSSSLHLD 348
Cdd:PRK15439 20 QYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD-SGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 349 YRVStnVRNVILSGYFDSIGIYQAVSDKQHKLVQQwLDIlgidkrtaDAPFHSLSWGQQRLALIVRALVKHPTLLILDEP 428
Cdd:PRK15439 99 PNLS--VKENILFGLPKRQASMQKMKQLLAALGCQ-LDL--------DSSAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190
....*....|....*....|....*....|..
gi 488984360 429 LQGLDPLNRQLVRRFVDVLIGEGATqLLFVSH 460
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQGVG-IVFISH 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-197 |
4.07e-06 |
|
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: 49.63 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSDTKTLKIDHLSVAA--GESWAFVGSNGSGKSALARALAGDLPLLSGQRE-SHFSRVTRLSfeQLQKLVS 80
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVrpGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATvAGKSILTNIS--DVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 81 DEWQRNNTDLLSPGEEDTgRTTAEIIQDEVKDPARCARLAEQ-FGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLIL 159
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGREHL-YLYARLRGVPAEEIEKVANWSIQsLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984360 160 DEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNRFDE 197
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEE 2132
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
379-465 |
4.27e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 48.48 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 379 KLVQQWLDILGIDKRTAD-APFhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLF 457
Cdd:PRK13634 123 QKAREMIELVGLPEELLArSPF-ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVL 201
|
....*...
gi 488984360 458 VSHHAEDA 465
Cdd:PRK13634 202 VTHSMEDA 209
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-198 |
4.33e-06 |
|
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: 47.87 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLVSDEWQRNNtdLLSpgeedtgRTTA 103
Cdd:cd03252 23 LRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENV--LFN-------RSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 104 EII--------QDEVKDPARCARlAEQF------GISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVN 169
Cdd:cd03252 94 DNIaladpgmsMERVIEAAKLAG-AHDFiselpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180
....*....|....*....|....*....
gi 488984360 170 SRQQLAALLADLhSAGITLVLVLNRFDEI 198
Cdd:cd03252 173 SEHAIMRNMHDI-CAGRTVIIIAHRLSTV 200
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
261-465 |
6.33e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 48.18 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETIWD--IKKH 337
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKPTE--------GQIFIDGEDVTHrsIQQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 338 ---IGYVSSSLHLDYRVSTNVrnvilsGY-FDSIGIYQAVSDKQHKLVQQWLDILGIDKRTADapfhSLSWGQQ-RLALi 412
Cdd:PRK11432 79 dicMVFQSYALFPHMSLGENV------GYgLKMLGVPKEERKQRVKEALELVDLAGFEDRYVD----QISGGQQqRVAL- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 413 VRALVKHPTLLILDEPLQGLDPlNrqlVRRFVDVLIGEGATQL----LFVSHHAEDA 465
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDA-N---LRRSMREKIRELQQQFnitsLYVTHDQSEA 200
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
282-434 |
6.39e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 48.15 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 282 TVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGYS-----NDLTLFGRRRgsgetIWDIKKHIGYV--SSSLhLDYRvst 353
Cdd:COG1135 27 TIEKGEIFGIIGYSGAGKSTLIRCINLlERPTSGSvlvdgVDLTALSERE-----LRAARRKIGMIfqHFNL-LSSR--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 354 NVR-NV----ILSGYfdsigiyqavsDKQ--HKLVQQWLDILGIDKRtADAPFHSLSWGQ-QRLAlIVRALVKHPTLLIL 425
Cdd:COG1135 98 TVAeNValplEIAGV-----------PKAeiRKRVAELLELVGLSDK-ADAYPSQLSGGQkQRVG-IARALANNPKVLLC 164
|
....*....
gi 488984360 426 DEPLQGLDP 434
Cdd:COG1135 165 DEATSALDP 173
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-433 |
6.44e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 17 KTLKIDHLSVAAGESWAFVGSNGSGKSALARAL-------AGDLpLLSGQrESHFSRvTRLSFEQLQKLVSDEW----QR 85
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLfgiyqkdSGSI-LFQGK-EIDFKS-SKEALENGISMVHQELnlvlQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 86 NNTDLLSPGEedtgRTTAEIIQDEVKDPARCARLAEQFGISalLDRRFKY--LSTGETRKTLLCQALMTDPQLLILDEPF 163
Cdd:PRK10982 89 SVMDNMWLGR----YPTKGMFVDQDKMYRDTKAIFDELDID--IDPRAKVatLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 164 DGLDVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETGEKSSLLQQALVAQLAHSEKLDgiTLP 243
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQ--RFP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 244 EPDVPPARhaladsaprIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSlvtgdhpqgysndlTLFGR 323
Cdd:PRK10982 241 DKENKPGE---------VILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVE--------------TLFGI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 324 RRGSGETIWDIKKHIGYVSS--------SLHLDYRVSTNVR-------NVILSG---YFDSIGIyqaVSDKQHKLVQQWL 385
Cdd:PRK10982 298 REKSAGTITLHGKKINNHNAneainhgfALVTEERRSTGIYayldigfNSLISNirnYKNKVGL---LDNSRMKSDTQWV 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 488984360 386 dilgIDKRTADAPFH-----SLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:PRK10982 375 ----IDSMRVKTPGHrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
24-191 |
7.54e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.08 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKL----VSDEWQ----------RNNTD 89
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhVGFVFQsfmliptlnaLENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 90 L--LSPGEEDTgrttaeiiqdevKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLD 167
Cdd:PRK10584 111 LpaLLRGESSR------------QSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180
....*....|....*....|....*
gi 488984360 168 VNSRQQLAALLADL-HSAGITLVLV 191
Cdd:PRK10584 179 RQTGDKIADLLFSLnREHGTTLILV 203
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
229-427 |
7.72e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 48.26 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 229 AQLAHsEKLDGITLPEPDVPPARHALADSAP-----RIVLNDgvVSYN------DRP-VINHLSWTVNPGEHWQIVGPNG 296
Cdd:COG4615 292 ANVAL-RKIEELELALAAAEPAAADAAAPPApadfqTLELRG--VTYRypgedgDEGfTLGPIDLTIRRGELVFIVGGNG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 297 AGKSTLLSLVTG-DHPQgysndltlfgrrrgSGETIWDIKKhigyVSSSLHLDYR--VStnvrnVILSGY--FDS-IGIY 370
Cdd:COG4615 369 SGKSTLAKLLTGlYRPE--------------SGEILLDGQP----VTADNREAYRqlFS-----AVFSDFhlFDRlLGLD 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984360 371 QAVSDKQhklVQQWLDILGIDKRTA--DAPFHS--LSWGQQ-RLALIVrALVKHPTLLILDE 427
Cdd:COG4615 426 GEADPAR---ARELLERLELDHKVSveDGRFSTtdLSQGQRkRLALLV-ALLEDRPILVFDE 483
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
268-461 |
8.34e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.09 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 268 VSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSL--------VTGDHPQGYSNDLTLFGRRRGSGETIWDIKKH-- 337
Cdd:PRK09580 9 VSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATlagredyeVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYpv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 338 -IGYVSSSLHLDYRVSTnVRNVILSGYFDSIGIYQAVSDKQhKLVQQWLDILgidKRTADAPFhslSWGQQRLALIVRAL 416
Cdd:PRK09580 89 eIPGVSNQFFLQTALNA-VRSYRGQEPLDRFDFQDLMEEKI-ALLKMPEDLL---TRSVNVGF---SGGEKKRNDILQMA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984360 417 VKHPTLLILDEPLQGLDPLNRQLVRRFVDVLiGEGATQLLFVSHH 461
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHY 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
128-210 |
8.41e-06 |
|
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: 47.30 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 128 LLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSA-GITLVLVLNRFDEipefvqfAG 206
Cdd:cd03295 128 FADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDE-------AF 200
|
....
gi 488984360 207 VLAD 210
Cdd:cd03295 201 RLAD 204
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
24-191 |
8.97e-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: 8.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGqreshfsRVT---RLSFeqlqklvsdewqrnntdLLSPG----EE 96
Cdd:COG1134 47 FEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG-------RVEvngRVSA-----------------LLELGagfhPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 97 DTGR------------TTAEIIQ--DEVKDparcarlaeqF-GISALLDRRFKYLSTGE-TRktlLCQALMT--DPQLLI 158
Cdd:COG1134 103 LTGReniylngrllglSRKEIDEkfDEIVE----------FaELGDFIDQPVKTYSSGMrAR---LAFAVATavDPDILL 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 488984360 159 LDEpfdGL---DVNSRQQLAALLADLHSAGITLVLV 191
Cdd:COG1134 170 VDE---VLavgDAAFQKKCLARIRELRESGRTVIFV 202
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
10-181 |
9.04e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.80 E-value: 9.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 10 TFRLSDTKTLKIDHL--SVAAGESWAFVGSNGSGKSALARALAGDLP---LLSGQRESHFSRVTRLSFEQLQKLVSDE-- 82
Cdd:PRK09473 21 TFSTPDGDVTAVNDLnfSLRAGETLGIVGESGSGKSQTAFALMGLLAangRIGGSATFNGREILNLPEKELNKLRAEQis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 83 --WQRNNTDL---LSPGEEDT-------GRTTAEIIQ------DEVKDPArcARlaeqfgisalldRRFKY----LSTGE 140
Cdd:PRK09473 101 miFQDPMTSLnpyMRVGEQLMevlmlhkGMSKAEAFEesvrmlDAVKMPE--AR------------KRMKMypheFSGGM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984360 141 TRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADL 181
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNEL 207
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-230 |
9.07e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 47.31 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 11 FRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ-----RESHFSRVTRLSF-EQLQKLVSD-EW 83
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAvlwqgKPLDYSKRGLLALrQQVATVFQDpEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 84 QRNNTDLLSP---GEEDTGRTTAEIiqdevkdpARcaRLAEQFgisALLD-RRFKY-----LSTGETRKTLLCQALMTDP 154
Cdd:PRK13638 89 QIFYTDIDSDiafSLRNLGVPEAEI--------TR--RVDEAL---TLVDaQHFRHqpiqcLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 155 QLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNRFDEIPE-----FVQFAG-VLADCTLSETGEKSSLLQQALV 228
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEisdavYVLRQGqILTHGAPGEVFACTEAMEQAGL 235
|
..
gi 488984360 229 AQ 230
Cdd:PRK13638 236 TQ 237
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
270-461 |
9.37e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.48 E-value: 9.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 270 YNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRrrgsgetiwDIKKHIgyvssslhld 348
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGlLNPE--KGEILFERQ---------SIKKDL---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 349 yrvSTNVRNVILSGYFDSIGIYQAVSDKQHKLVQQWLDILGIDK--------RTADAPFHSLSWGQQRLALIVRALVKHP 420
Cdd:PRK13540 70 ---CTYQKQLCFVGHRSGINPYLTLRENCLYDIHFSPGAVGITElcrlfsleHLIDYPCGLLSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984360 421 TLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLfVSHH 461
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLL-TSHQ 186
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
129-200 |
1.04e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 1.04e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984360 129 LDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNrfdEIPE 200
Cdd:PRK10762 389 MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSS---EMPE 457
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-181 |
1.10e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.43 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 1 MSSLQISQGTFRLSDTKT--LKIDHLS--VAAGESWAFVGSNGSGKSALARALAG--DLP--LLSGQRESHFSRVTRLSF 72
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApfRAVDRISysVKQGEVVGIVGESGSGKSVSSLAIMGliDYPgrVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 73 EQLQKLVSDE----WQRNNTDLlspgeeDTGRTTAEIIQDEVK---------DPARCARLAEQFGISALLDRRFKY---L 136
Cdd:PRK11022 81 KERRNLVGAEvamiFQDPMTSL------NPCYTVGFQIMEAIKvhqggnkktRRQRAIDLLNQVGIPDPASRLDVYphqL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984360 137 STGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADL 181
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLEL 199
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
223-460 |
1.10e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 223 LQQALVAQlahseklDGITLPEPDVPParhaladSAPRIVLNDGVVSY---NDRPVINHLSWTVNPGEHWQIVGPNGAGK 299
Cdd:PLN03130 591 LEELLLAE-------ERVLLPNPPLEP-------GLPAISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGK 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 300 STLLSLVTGDHPQGYSNDLTLfgrrRGSgetiwdikkhIGYVSsslHLDYRVSTNVRNVILSGY-FDSIGIYQA--VSDK 376
Cdd:PLN03130 657 TSLISAMLGELPPRSDASVVI----RGT----------VAYVP---QVSWIFNATVRDNILFGSpFDPERYERAidVTAL 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 377 QHKLvqQWL---DILGIDKRTADapfhsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP-LNRQL--------VRRFV 444
Cdd:PLN03130 720 QHDL--DLLpggDLTEIGERGVN-----ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVfdkcikdeLRGKT 792
|
250
....*....|....*.
gi 488984360 445 DVLIgegATQLLFVSH 460
Cdd:PLN03130 793 RVLV---TNQLHFLSQ 805
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
276-487 |
1.11e-05 |
|
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: 46.87 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 276 INHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG----DHPQGYSN--DLTLFGRRRgsgetIWDIKKH-IGYVSSSLHL- 347
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRliepTSGKVLIDgqDIAAMSRKE-----LRELRRKkISMVFQSFALl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 348 DYRvsTNVRNVILsgyfdsiGI-YQAVSDKQ-HKLVQQWLDILGIDKRTADAPfHSLSWG-QQRLALiVRALVKHPTLLI 424
Cdd:cd03294 115 PHR--TVLENVAF-------GLeVQGVPRAErEERAAEALELVGLEGWEHKYP-DELSGGmQQRVGL-ARALAVDPDILL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984360 425 LDEPLQGLDPLNR-----QLVRrfvdvLIGEGATQLLFVSHHAEDAPDcITHRLAFVPsgDGYTYQLG 487
Cdd:cd03294 184 MDEAFSALDPLIRremqdELLR-----LQAELQKTIVFITHDLDEALR-LGDRIAIMK--DGRLVQVG 243
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
272-433 |
1.16e-05 |
|
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: 46.71 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 272 DRPVINH-LSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGySNDLTLFGRRRGSGETIWdIKKHIGYV-SSSLHLDY 349
Cdd:cd03252 13 DGPVILDnISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE-NGRVLVDGHDLALADPAW-LRRQVGVVlQENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 350 RVSTNV---------RNVI----LSGYFDSIgiyqavsdkqHKLVQQWLDILGidKRTAdapfhSLSWGQ-QRLAlIVRA 415
Cdd:cd03252 91 SIRDNIaladpgmsmERVIeaakLAGAHDFI----------SELPEGYDTIVG--EQGA-----GLSGGQrQRIA-IARA 152
|
170
....*....|....*...
gi 488984360 416 LVKHPTLLILDEPLQGLD 433
Cdd:cd03252 153 LIHNPRILIFDEATSALD 170
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
261-433 |
1.17e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.53 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSY-NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGdhpqgysndLtlfgrrrgsgETIwdikkhig 339
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG---------L----------ERI-------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 340 yVSSSLHLDYRVSTNV----RNVILsgYFDSIGIYqavsdkQHKLVQQ----WLDILG-----IDKRTADA-------PF 399
Cdd:PRK11650 57 -TSGEIWIGGRVVNELepadRDIAM--VFQNYALY------PHMSVREnmayGLKIRGmpkaeIEERVAEAarilelePL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488984360 400 -----HSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLD 433
Cdd:PRK11650 128 ldrkpRELSGGQrQRVAM-GRAIVREPAVFLFDEPLSNLD 166
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-175 |
1.22e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.86 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 2 SSLQISQGTFRLSdtktlkIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQreshFSRVTRLSFEQlQKLVSD 81
Cdd:COG1245 345 PDLTKSYGGFSLE------VEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE----VDEDLKISYKP-QYISPD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 82 ewqRNNT--DLLSpgEEDTGRTTAEIIQDEVKDParcarlaeqFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLIL 159
Cdd:COG1245 414 ---YDGTveEFLR--SANTDDFGSSYYKTEIIKP---------LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 479
|
170
....*....|....*.
gi 488984360 160 DEPFDGLDVNSRQQLA 175
Cdd:COG1245 480 DEPSAHLDVEQRLAVA 495
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
275-433 |
1.28e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.80 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 275 VINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQGysndltlfGRRRGSGETIWDI---------KKHIGYVSSS 344
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGClDKPTS--------GTYRVAGQDVATLdadalaqlrREHFGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 345 LHLDYRVSTnVRNVILSgyfdsiGIYQAVSDKQHKL-VQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLL 423
Cdd:PRK10535 95 YHLLSHLTA-AQNVEVP------AVYAGLERKQRLLrAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVI 166
|
170
....*....|
gi 488984360 424 ILDEPLQGLD 433
Cdd:PRK10535 167 LADEPTGALD 176
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
273-463 |
1.47e-05 |
|
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: 45.50 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 273 RPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQgYSNDLTLFGRRRGSGETIWDIKKHIGYVS-----SSLHL 347
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPP-ASGEITLDGKPVTRRSPRDAIRAGIAYVPedrkrEGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 348 DYRVStnvRNVILSgyfdsigiyqavsdkqhklvqqwldilgidkrtadapfHSLSWG-QQRLaLIVRALVKHPTLLILD 426
Cdd:cd03215 92 DLSVA---ENIALS--------------------------------------SLLSGGnQQKV-VLARWLARDPRVLILD 129
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984360 427 EPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAE 463
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDE 166
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
15-191 |
1.51e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.41 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 15 DTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAG-DLPLlSGQRESHFSRVTRLSFEQLQKLVSDEW----QRNNtd 89
Cdd:PRK10535 20 QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGClDKPT-SGTYRVAGQDVATLDADALAQLRREHFgfifQRYH-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 90 LLSpgeEDTGRTTAEI--IQDEVKDPARCAR---LAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFD 164
Cdd:PRK10535 97 LLS---HLTAAQNVEVpaVYAGLERKQRLLRaqeLLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180
....*....|....*....|....*..
gi 488984360 165 GLDVNSRQQLAALLADLHSAGITLVLV 191
Cdd:PRK10535 174 ALDSHSGEEVMAILHQLRDRGHTVIIV 200
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-181 |
1.89e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 46.65 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLvsdewqRNNTDL--------LSPGe 95
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPL------RRRMQMvfqdpyasLNPR- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 96 edtgRTTAEIIQD-----EVKDPA----RCARLAEQFGISALLDRRFKY-LSTGETRKTLLCQALMTDPQLLILDEPFDG 165
Cdd:COG4608 112 ----MTVGDIIAEplrihGLASKAerreRVAELLELVGLRPEHADRYPHeFSGGQRQRIGIARALALNPKLIVCDEPVSA 187
|
170
....*....|....*.
gi 488984360 166 LDVNSRQQLAALLADL 181
Cdd:COG4608 188 LDVSIQAQVLNLLEDL 203
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-191 |
2.07e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 47.08 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 15 DTKTLK-IDhLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGqreshfsRVT-------RLSFEQLQKLVS----De 82
Cdd:COG1132 352 DRPVLKdIS-LTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSG-------RILidgvdirDLTLESLRRQIGvvpqD- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 83 wqrnnTDLLSpgeeDT-------GRTTAEiiQDEVKDPARCARLAEqF------GISALLDRRFKYLSTGEtrKTLLC-- 147
Cdd:COG1132 423 -----TFLFS----GTireniryGRPDAT--DEEVEEAAKAAQAHE-FiealpdGYDTVVGERGVNLSGGQ--RQRIAia 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488984360 148 QALMTDPQLLILDEPFDGLDVNSRQQLAALLADLhSAGITLVLV 191
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVI 531
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
14-197 |
2.16e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 46.24 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 14 SDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVTRLSFEQLQKLVSDEWQRNNTDLLSP 93
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 94 GEEDT---GRTTAEIIQDEVkdparCARLAEQFGISALLD---RRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLD 167
Cdd:PRK13642 98 TVEDDvafGMENQGIPREEM-----IKRVDEALLAVNMLDfktREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190
....*....|....*....|....*....|.
gi 488984360 168 VNSRQQLAALLADLHSA-GITLVLVLNRFDE 197
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKyQLTVLSITHDLDE 203
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
201-468 |
2.28e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 201 FVQFAGVLADCTLSETGEKSSLLQQALVAQ--LAHSEKLDG-ITLP-------EPDVPPARHALADSaprIVLNDGVVSY 270
Cdd:PLN03232 1168 FASTMGLLLSYTLNITTLLSGVLRQASKAEnsLNSVERVGNyIDLPseataiiENNRPVSGWPSRGS---IKFEDVHLRY 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 271 NDR--PVINHLSWTVNPGEHWQIVGPNGAGKSTLLS----LVTGDHPQ----GYsnDLTLFGrrrgsgetIWDIKKHIGY 340
Cdd:PLN03232 1245 RPGlpPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNalfrIVELEKGRimidDC--DVAKFG--------LTDLRRVLSI 1314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 341 VSSSLHLdyrVSTNVR-NVILSGYFDSIGIYQAVSDKQHKLVQQwLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKH 419
Cdd:PLN03232 1315 IPQSPVL---FSGTVRfNIDPFSEHNDADLWEALERAHIKDVID-RNPFGLDAEVSEGG-ENFSVGQRQLLSLARALLRR 1389
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 488984360 420 PTLLILDEPLQGLDPLNRQLVRRfvdvLIGE--GATQLLFVSHHAEDAPDC 468
Cdd:PLN03232 1390 SKILVLDEATASVDVRTDSLIQR----TIREefKSCTMLVIAHRLNTIIDC 1436
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-167 |
2.37e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 45.90 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 1 MSSLQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARAL------------AGDLPLLSGQRESHFSRVT 68
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 69 RlsfeQLQKLVSDEWQRNNtdlLSPgeedtGRTTAE-------IIQDEVKDPA--RCARLAEQFGISALLDRRFKYLSTG 139
Cdd:PRK11264 81 R----QLRQHVGFVFQNFN---LFP-----HRTVLEniiegpvIVKGEPKEEAtaRARELLAKVGLAGKETSYPRRLSGG 148
|
170 180
....*....|....*....|....*...
gi 488984360 140 ETRKTLLCQALMTDPQLLILDEPFDGLD 167
Cdd:PRK11264 149 QQQRVAIARALAMRPEVILFDEPTSALD 176
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
111-198 |
2.54e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.41 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 111 KDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADL-HSAGITLV 189
Cdd:PRK11144 104 SMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLaREINIPIL 183
|
....*....
gi 488984360 190 LVLNRFDEI 198
Cdd:PRK11144 184 YVSHSLDEI 192
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
261-463 |
3.26e-05 |
|
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: 46.33 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 261 IVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTG--DHPQ---------------GYSNDLTLFGR 323
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPtsgriiyhvalcekcGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 324 R-RGSGETI-------WD--------IKKHIGYV---SSSLHLDYRVSTNVRNVILS-GYFDSIGIYQAVsdKQHKLVQQ 383
Cdd:TIGR03269 81 PcPVCGGTLepeevdfWNlsdklrrrIRKRIAIMlqrTFALYGDDTVLDNVLEALEEiGYEGKEAVGRAV--DLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 384 WLDILGIDKrtadapfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSHHAE 463
Cdd:TIGR03269 159 SHRITHIAR--------DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-200 |
3.30e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 46.25 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 14 SDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ---------RESHfsRVTRLSFEQLQK---LVSD 81
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEirldgrplsSLSH--SVLRQGVAMVQQdpvVLAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 82 EWQRNNTdllspgeedTGRTTAEIIQDEVKDPARCARLAEQF--GISALLDRRFKYLSTGETRKTLLCQALMTDPQLLIL 159
Cdd:PRK10790 430 TFLANVT---------LGRDISEEQVWQALETVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILIL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984360 160 DEPFDGLDVNSRQQLAALLADLHSAgITLVLVLNRFDEIPE 200
Cdd:PRK10790 501 DEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLSTIVE 540
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
291-463 |
3.48e-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: 44.27 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 291 IVGPNGAGKSTLL---SLVTGDHpqgysndlTLFGRRRGSGetiwdikkHIGYVSSSLHLDYRVStnvrnvilsgyfdsi 367
Cdd:cd03227 26 ITGPNGSGKSTILdaiGLALGGA--------QSATRRRSGV--------KAGCIVAAVSAELIFT--------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 368 giyqavsdkqhklvqqwldilgidkrtadapFHSLSWGQQ---RLALIVR-ALVKHPTLLILDEPLQGLDPLNRQLVRRF 443
Cdd:cd03227 75 -------------------------------RLQLSGGEKelsALALILAlASLKPRPLYILDEIDRGLDPRDGQALAEA 123
|
170 180
....*....|....*....|
gi 488984360 444 VDVLIGEGAtQLLFVSHHAE 463
Cdd:cd03227 124 ILEHLVKGA-QVIVITHLPE 142
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
221-480 |
3.56e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.51 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 221 SLLQQALVAQLAhSEKLDGITLPEPDVPPARHALADSAPRIVLNDGVVSYN---DRPVINHLSWTVNPGEHWQIVGPNGA 297
Cdd:PLN03232 576 NLLSQVVNANVS-LQRIEELLLSEERILAQNPPLQPGAPAISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGE 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 298 GKSTLLSLVTGDHPQGYSNDLtlfgrrrgsgetiwDIKKHIGYVSsslHLDYRVSTNVRNVILSGY-FDSIGIYQA--VS 374
Cdd:PLN03232 655 GKTSLISAMLGELSHAETSSV--------------VIRGSVAYVP---QVSWIFNATVRENILFGSdFESERYWRAidVT 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 375 DKQHKLvqqwlDIL-GIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVLIGE--- 450
Cdd:PLN03232 718 ALQHDL-----DLLpGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA---HVAHQVFDSCMKDelk 789
|
250 260 270
....*....|....*....|....*....|
gi 488984360 451 GATQLLfvshhaedapdcITHRLAFVPSGD 480
Cdd:PLN03232 790 GKTRVL------------VTNQLHFLPLMD 807
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
282-438 |
4.95e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.73 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 282 TVNPGEHWQIVGPNGAGKSTLLSLVTG-DHPQgySNDLTLFGRRRgSGETIWDIKKHIGYVSSSLHLdyrvstnvrnvil 360
Cdd:PRK10522 345 TIKRGELLFLIGGNGSGKSTLAMLLTGlYQPQ--SGEILLDGKPV-TAEQPEDYRKLFSAVFTDFHL------------- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 361 sgyFDSIgIYQAVSDKQHKLVQQWLDILGI-------DKRTADApfhSLSWGQ-QRLALIVrALVKHPTLLILDEPLQGL 432
Cdd:PRK10522 409 ---FDQL-LGPEGKPANPALVEKWLERLKMahkleleDGRISNL---KLSKGQkKRLALLL-ALAEERDILLLDEWAADQ 480
|
....*.
gi 488984360 433 DPLNRQ 438
Cdd:PRK10522 481 DPHFRR 486
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
291-462 |
5.63e-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: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 291 IVGPNGAGKSTLLSLVTgdhpqgysndLTLFGRRRGSGETIWDIkKHIGYVSSSLHLD-------YRV------------ 351
Cdd:COG0419 28 IVGPNGAGKSTILEAIR----------YALYGKARSRSKLRSDL-INVGSEEASVELEfehggkrYRIerrqgefaefle 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 352 -STNVRNVILSGYFDsIGIYQAVSDKQHKL-------VQQWLDILGIDKR-----TADAPFHSLSWGQQ-RLAL--IVRa 415
Cdd:COG0419 97 aKPSERKEALKRLLG-LEIYEELKERLKELeealesaLEELAELQKLKQEilaqlSGLDPIETLSGGERlRLALadLLS- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984360 416 lvkhptlLILDepLQGLDPLNRqlvRRFVDVLigegaTQLLFVSHHA 462
Cdd:COG0419 175 -------LILD--FGSLDEERL---ERLLDAL-----EELAIITHVI 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
274-480 |
5.87e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 274 PVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLV------TGDH----PQGYSNDLTLFGRRRGSGETIWDIKKHIGYVSS 343
Cdd:PTZ00265 1182 PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlKNDHhivfKNEHTNDMTNEQDYQGDEEQNVGMKNVNEFSLT 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 344 ---SLHLDYRVSTNVRNVILSG----------------------YFDSIGIYQAV----SDKQHKLVQQWLDILGIDK-- 392
Cdd:PTZ00265 1262 kegGSGEDSTVFKNSGKILLDGvdicdynlkdlrnlfsivsqepMLFNMSIYENIkfgkEDATREDVKRACKFAAIDEfi 1341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 393 -------RTADAPF-HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVdVLIGEGATQLLFVshhaed 464
Cdd:PTZ00265 1342 eslpnkyDTNVGPYgKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI-VDIKDKADKTIIT------ 1414
|
250
....*....|....*.
gi 488984360 465 apdcITHRLAFVPSGD 480
Cdd:PTZ00265 1415 ----IAHRIASIKRSD 1426
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-172 |
7.78e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 43.93 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAGdlpLLSGQRESHF---SRVTRLSFEQLQKLVS 80
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVAS---LISPTSGTLLfegEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 81 DEWQ---------RNNtdLLSPGEedtgrttaeiIQDEVKDPARCARLAEQFGI-SALLDRRFKYLSTGETRKTLLCQAL 150
Cdd:PRK10247 85 YCAQtptlfgdtvYDN--LIFPWQ----------IRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNL 152
|
170 180
....*....|....*....|..
gi 488984360 151 MTDPQLLILDEPFDGLDVNSRQ 172
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKH 174
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
263-433 |
8.20e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 44.39 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 263 LNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVtGDHPQGYSNDLTLFGRRRGSgetiWDIK---KHIG 339
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAQPLES----WSSKafaRKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 340 YVSSslHLDYRVSTNVRNVILSGYFDSIGIYQAVSDKQHKLVQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRALVKH 419
Cdd:PRK10575 89 YLPQ--QLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGL-KPLAHRLVDSLSGGERQRAWIAMLVAQD 165
|
170
....*....|....
gi 488984360 420 PTLLILDEPLQGLD 433
Cdd:PRK10575 166 SRCLLLDEPTSALD 179
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
100-191 |
8.38e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 44.94 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 100 RTTAEIIQDEVKDPARCARLaEQFGisallDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLA 179
Cdd:PRK09452 115 KTPAAEITPRVMEALRMVQL-EEFA-----QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELK 188
|
90
....*....|...
gi 488984360 180 DLH-SAGITLVLV 191
Cdd:PRK09452 189 ALQrKLGITFVFV 201
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
271-306 |
9.07e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 45.09 E-value: 9.07e-05
10 20 30
....*....|....*....|....*....|....*.
gi 488984360 271 NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLV 306
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI 361
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
271-433 |
9.63e-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: 43.41 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 271 NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYSndltlfgrrrgsgetiwdikkhigyVSSSLHLDyr 350
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS-------------------------VEGDIHYN-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 351 vstNVRNVILSGYFDSIGIYQAVSDKQHKL--VQQWLDILGidKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEP 428
Cdd:cd03233 71 ---GIPYKEFAEKYPGEIIYVSEEDVHFPTltVRETLDFAL--RCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNS 145
|
....*
gi 488984360 429 LQGLD 433
Cdd:cd03233 146 TRGLD 150
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
385-460 |
1.13e-04 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 43.64 E-value: 1.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 385 LDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDV---LIGEGATQLLfVSH 460
Cdd:COG4598 139 LAKVGLADKRDAYPAH-LSGGQQQRAAIARALAMEPEVMLFDEPTSALDP---ELVGEVLKVmrdLAEEGRTMLV-VTH 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
136-201 |
1.16e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.92 E-value: 1.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984360 136 LSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNRFDEIPEF 201
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEW 231
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
33-198 |
1.17e-04 |
|
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: 43.00 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 33 AFVGSNGSGKSALARALA---------GDLpLLSGQreshfsrvtrlsfeqlqklvsdewqrnntdllsPGEEDTGRTTA 103
Cdd:cd03232 37 ALMGESGAGKTTLLDVLAgrktagvitGEI-LINGR---------------------------------PLDKNFQRSTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 104 EIIQDEVKDPARCARLAEQFgiSALLdrrfKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHS 183
Cdd:cd03232 83 YVEQQDVHSPNLTVREALRF--SALL----RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLAD 156
|
170 180
....*....|....*....|...
gi 488984360 184 AGITLV--------LVLNRFDEI 198
Cdd:cd03232 157 SGQAILctihqpsaSIFEKFDRL 179
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
35-217 |
1.23e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.07 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 35 VGSNGSGKSALARALAG-----------------DLPLLSGQRESHFSRVTRlSFEQLQKLVSDEWQRNNTDLLSPG-EE 96
Cdd:PRK13631 58 IGNSGSGKSTLVTHFNGlikskygtiqvgdiyigDKKNNHELITNPYSKKIK-NFKELRRRVSMVFQFPEYQLFKDTiEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 97 DTGRTTAEIIQDEVKDPARCARLAEQFGI-SALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLA 175
Cdd:PRK13631 137 DIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM 216
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984360 176 ALLADLHSAGITLVLVLNRFDEIPEFVQFAGVLADCTLSETG 217
Cdd:PRK13631 217 QLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-191 |
1.38e-04 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 43.54 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 12 RLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARAL-------AGDLpLLSGQRESHFSRVTRLsFEQLQKLVsdeWQ 84
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDL-IVDGLKVNDPKVDERL-IRQEAGMV---FQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 85 RNNtdlLSP----------GEEDTGRTTAEiiqdEVKDPARcaRLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDP 154
Cdd:PRK09493 85 QFY---LFPhltalenvmfGPLRVRGASKE----EAEKQAR--ELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984360 155 QLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLV 191
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIV 192
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-175 |
1.38e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.48 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 4 LQISQGTFRLSDTKTLKIDHLSVAAGESWAFVGSNGSGKSALARALAG--DLPLLSGQRESHFSRVTRLSFEQLQKL--- 78
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLgif 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 79 -----------VSDE----------WQRNNTDLLSPGEedtgrtTAEIIQDEVK----DPARCAR-LAEQFgisalldrr 132
Cdd:CHL00131 88 lafqypieipgVSNAdflrlaynskRKFQGLPELDPLE------FLEIINEKLKlvgmDPSFLSRnVNEGF--------- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984360 133 fkylSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLA 175
Cdd:CHL00131 153 ----SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIA 191
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
24-170 |
1.68e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQ-------RESHFSRVTRLSFEQLQKLVsdEWQRNNTdllSPGEE 96
Cdd:PRK15064 340 LLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTvkwsenaNIGYYAQDHAYDFENDLTLF--DWMSQWR---QEGDD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 97 DT------GRTTaeIIQDEVKDPArcarlaeqfgisalldrrfKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNS 170
Cdd:PRK15064 415 EQavrgtlGRLL--FSQDDIKKSV-------------------KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES 473
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
115-191 |
1.72e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 43.05 E-value: 1.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984360 115 RCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADL-HSAGITLVLV 191
Cdd:PRK11300 133 RAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLI 210
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
282-428 |
1.74e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 282 TVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQG-YSNDLTLFGRRRGSGetiwDIK--KHIGYVssslhldyrvstnvrnV 358
Cdd:NF040905 23 SVREGEIHALCGENGAGKSTLMKVLSGVYPHGsYEGEILFDGEVCRFK----DIRdsEALGIV----------------I 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 359 I-----LSGYFdSIG--IY----QAVS-----DKQHKLVQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTL 422
Cdd:NF040905 83 IhqelaLIPYL-SIAenIFlgneRAKRgvidwNETNRRARELLAKVGLDES-PDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
....*.
gi 488984360 423 LILDEP 428
Cdd:NF040905 161 LILDEP 166
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-189 |
1.81e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.10 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 29 GESWAFVGSNGSGKSALARALAGDLP--LLSGQRESHFSRVTRLSFEQLQKLVSDewqrnntDLLSPgeEDTGRTT---- 102
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNRKPTKQILKRTGFVTQD-------DILYP--HLTVRETlvfc 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 103 -----AEIIQDEVKDPARCARLAEqFGIS----ALLDRRF-KYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQ 172
Cdd:PLN03211 165 sllrlPKSLTKQEKILVAESVISE-LGLTkcenTIIGNSFiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170
....*....|....*..
gi 488984360 173 QLAALLADLHSAGITLV 189
Cdd:PLN03211 244 RLVLTLGSLAQKGKTIV 260
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
114-238 |
1.97e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.57 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 114 ARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLN 193
Cdd:NF000106 123 ARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQ 202
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 488984360 194 RFDEIPEF------VQFAGVLADCTLSETgeKSSLLQQALVAQLAHSEKLD 238
Cdd:NF000106 203 YMEEAEQLaheltvIDRGRVIADGKVDEL--KTKVGGRTLQIRPAHAAELD 251
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
291-463 |
2.11e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 43.07 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 291 IVGPNGAGKSTLLSLVTG----DHPQGYSNDLTLFGRRRGSGEtIWDIKKHIGYVSSSLHLDYRVSTNVRNVilsgyfdS 366
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGliisETGQTIVGDYAIPANLKKIKE-VKRLRKEIGLVFQFPEYQLFQETIEKDI-------A 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 367 IGIYQAVSDKQ--HKLVQQWLDILGIDKRTAD-APFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRF 443
Cdd:PRK13645 114 FGPVNLGENKQeaYKKVPELLKLVQLPEDYVKrSPFE-LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINL 192
|
170 180
....*....|....*....|
gi 488984360 444 VDVLIGEGATQLLFVSHHAE 463
Cdd:PRK13645 193 FERLNKEYKKRIIMVTHNMD 212
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
388-488 |
2.72e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 388 LGIDKRTADAPFHSLSWGQ-QRLALIVRAL--VKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLfvshhaed 464
Cdd:PRK00635 796 LGLDYLPLGRPLSSLSGGEiQRLKLAYELLapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVI-------- 867
|
90 100
....*....|....*....|....
gi 488984360 465 apdcITHRLAFVPSGDgYTYQLGP 488
Cdd:PRK00635 868 ----IEHNMHVVKVAD-YVLELGP 886
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
381-460 |
2.87e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 42.75 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 381 VQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLFVSH 460
Cdd:PRK10419 131 ASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITH 210
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
387-460 |
3.17e-04 |
|
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: 42.76 E-value: 3.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984360 387 ILGIDKRTADAPFHSLSWGQQRLALIVRAL---VKHPTLLILDEPLQGLDPlnrQLVRRFVDVL--IGEGATQLLFVSH 460
Cdd:pfam13304 222 ILLENGGGGELPAFELSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHP---KLLRRLLELLkeLSRNGAQLILTTH 297
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-181 |
4.28e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 22 DHLS--VAAGESWAFVGSNGSGKSALARALAGDLP------LLSGQR-ESH--------------FSRVTRLSFEQlqkl 78
Cdd:NF033858 283 DHVSfrIRRGEIFGFLGSNGCGKSTTMKMLTGLLPasegeaWLFGQPvDAGdiatrrrvgymsqaFSLYGELTVRQ---- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 79 vsdewqrnNTDL------LSPgeedtgrttAEIiqdevkdPARCARLAEQFGISALLDRRFKYLSTGeTRKTL-LCQALM 151
Cdd:NF033858 359 --------NLELharlfhLPA---------AEI-------AARVAEMLERFDLADVADALPDSLPLG-IRQRLsLAVAVI 413
|
170 180 190
....*....|....*....|....*....|
gi 488984360 152 TDPQLLILDEPFDGLDVNSRQQLAALLADL 181
Cdd:NF033858 414 HKPELLILDEPTSGVDPVARDMFWRLLIEL 443
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
272-460 |
4.84e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.09 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 272 DRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVT-------GDHPQGYSN---DLTLFGRRRGSGETIWD-------I 334
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIErlydpteGDIIINDSHnlkDINLKWWRSKIGVVSQDpllfsnsI 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 335 KKHIGYVSSSLH-------------LDYRVSTNVRNV----------ILSGYFDSIGIYQAvsDKQHKLVQQwLDILGID 391
Cdd:PTZ00265 477 KNNIKYSLYSLKdlealsnyynedgNDSQENKNKRNScrakcagdlnDMSNTTDSNELIEM--RKNYQTIKD-SEVVDVS 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 392 KRTADAPFHS----------------LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQL 455
Cdd:PTZ00265 554 KKVLIHDFVSalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
....*
gi 488984360 456 LFVSH 460
Cdd:PTZ00265 634 IIIAH 638
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
403-479 |
4.91e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.41 E-value: 4.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984360 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIGEGATQLLfVSHHAEDApDCITHRLAFVPSG 479
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLL-TTQYMEEA-EQLAHELTVIDRG 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-59 |
5.22e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 41.61 E-value: 5.22e-04
10 20 30
....*....|....*....|....*....|....*....
gi 488984360 24 LSVAAGEswaFV---GSNGSGKSALARALAGDLPLLSGQ 59
Cdd:COG1101 27 LTIEEGD---FVtviGSNGAGKSTLLNAIAGSLPPDSGS 62
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
282-445 |
5.60e-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: 41.62 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 282 TVNPGEHWQIVGPNGAGKSTLLSLVTGD-HPQGysndltlfgrrrgsGETIWDIKKhIGYVSSSLHLDYrvSTNVRNvIL 360
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVlKPDE--------------GDIEIELDT-VSYKPQYIKADY--EGTVRD-LL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 361 SGYFDSIGiyqavSDKQHKlvQQWLDILGIDkRTADAPFHSLSWGQ-QRLALIVrALVKHPTLLILDEPLQGLDPLNRQL 439
Cdd:cd03237 83 SSITKDFY-----THPYFK--TEIAKPLQIE-QILDREVPELSGGElQRVAIAA-CLSKDADIYLLDEPSAYLDVEQRLM 153
|
170
....*....|
gi 488984360 440 V----RRFVD 445
Cdd:cd03237 154 AskviRRFAE 163
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-191 |
5.68e-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: 41.58 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 25 SVAAGESWAFVGSNGSGKSALARALAGDL-PLLSGQRE--------SHFsRVTRLSfEQLQKLVSDEW----QRNNTDLL 91
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLkPNLGKFDDppdwdeilDEF-RGSELQ-NYFTKLLEGDVkvivKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 92 sPGEEDTgrTTAEIIqDEVKDPARCARLAEQFGISALLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSR 171
Cdd:cd03236 100 -PKAVKG--KVGELL-KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180
....*....|....*....|
gi 488984360 172 QQLAALLADLHSAGITLVLV 191
Cdd:cd03236 176 LNAARLIRELAEDDNYVLVV 195
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
272-453 |
5.74e-04 |
|
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: 41.07 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 272 DRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGY-SNDLTLFGRRRGSgetiwDIKKHIGYVSS-SLHLDy 349
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGViTGEILINGRPLDK-----NFQRSTGYVEQqDVHSP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 350 rVSTnVRNVILsgyfdsigiYQAvsdkqhklvqqWLDILGIDKRtadapfhslswgqQRLALIVRaLVKHPTLLILDEPL 429
Cdd:cd03232 93 -NLT-VREALR---------FSA-----------LLRGLSVEQR-------------KRLTIGVE-LAAKPSILFLDEPT 136
|
170 180
....*....|....*....|....
gi 488984360 430 QGLDPLNRQLVRRFVDVLIGEGAT 453
Cdd:cd03232 137 SGLDSQAAYNIVRFLKKLADSGQA 160
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-191 |
7.19e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.21 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 24 LSVAAGESWAFVGSNGSGKSALARALAGDLPLLSGQRESHFSRVtrlsfeqlqklvsdewqrnntDLLSPGE-------- 95
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI---------------------DIRSPRDairagiml 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 96 --EDtgRTTAEIIQ-DEVKD-----------PARC-------ARLAEQFgISAL------LDRRFKYLSTGETRKTLLCQ 148
Cdd:PRK11288 333 cpED--RKAEGIIPvHSVADninisarrhhlRAGClinnrweAENADRF-IRSLniktpsREQLIMNLSGGNQQKAILGR 409
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984360 149 ALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLV 191
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFV 452
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
260-433 |
8.18e-04 |
|
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: 40.86 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 260 RIVLNDGVVSY--NDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLslvtgdhpqgysndLTLF-------GRRRGSGET 330
Cdd:cd03369 6 EIEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLI--------------LALFrfleaeeGKIEIDGID 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 331 IWDIKKHigyvssslhlDYRVSTNV---RNVILSGYFDS-IGIYQAVSDKQhklvqqwldILGIDKRTADApfHSLSWGQ 406
Cdd:cd03369 72 ISTIPLE----------DLRSSLTIipqDPTLFSGTIRSnLDPFDEYSDEE---------IYGALRVSEGG--LNLSQGQ 130
|
170 180
....*....|....*....|....*..
gi 488984360 407 QRLALIVRALVKHPTLLILDEPLQGLD 433
Cdd:cd03369 131 RQLLCLARALLKRPRVLVLDEATASID 157
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
129-180 |
9.52e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 38.37 E-value: 9.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984360 129 LDRRFKYLSTGETRKTL---LCQALM----------TDPQLLILDEPFDGLDVNSRQQLAALLAD 180
Cdd:pfam13558 26 TYRRSGGLSGGEKQLLAylpLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
136-176 |
9.87e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 9.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488984360 136 LSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSR-------QQLAA 176
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKyeiytiiNELAA 452
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
400-460 |
1.07e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.10 E-value: 1.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984360 400 HSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD-PLNRQLVRRFVDvLIGEGATQLLFVSH 460
Cdd:PRK11308 153 HMFSGGQrQRIA-IARALMLDPDVVVADEPVSALDvSVQAQVLNLMMD-LQQELGLSYVFISH 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
292-459 |
1.29e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.54 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 292 VGPNGAGKSTLLSLVTgdhpqgYSNDLTLFGRRRGS----GETIWD-------IKKHIGYV-------SSSLH------- 346
Cdd:PRK14243 42 IGPSGCGKSTILRCFN------RLNDLIPGFRVEGKvtfhGKNLYApdvdpveVRRRIGMVfqkpnpfPKSIYdniayga 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 347 --------LDYRVSTNVRNVILsgyfdsigiYQAVSDKqhkLVQQWLdilgidkrtadapfhSLSWGQQRLALIVRALVK 418
Cdd:PRK14243 116 ringykgdMDELVERSLRQAAL---------WDEVKDK---LKQSGL---------------SLSGGQQQRLCIARAIAV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984360 419 HPTLLILDEPLQGLDP--------LNRQLVRRFVDVLIGEGATQLLFVS 459
Cdd:PRK14243 169 QPEVILMDEPCSALDPistlrieeLMHELKEQYTIIIVTHNMQQAARVS 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
257-448 |
1.82e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 257 SAPRIVLNDGVVSYNDR--PVINHLSWTVNPGEHWQIVGPNGAGKSTLLS----LVTGDHPQ----GYsnDLTLFGrrrg 326
Cdd:PLN03130 1234 SSGSIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNalfrIVELERGRilidGC--DISKFG---- 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 327 sgetIWDIKKHIGYVSSSLHLdyrVSTNVR-NVILSGYFDSIGIYQAVSDKQHKLVQQwLDILGIDKRTADAPfHSLSWG 405
Cdd:PLN03130 1308 ----LMDLRKVLGIIPQAPVL---FSGTVRfNLDPFNEHNDADLWESLERAHLKDVIR-RNSLGLDAEVSEAG-ENFSVG 1378
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984360 406 QQRLALIVRALVKHPTLLILDEPLQGLDplnrqlVRrfVDVLI 448
Cdd:PLN03130 1379 QRQLLSLARALLRRSKILVLDEATAAVD------VR--TDALI 1413
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
268-323 |
2.18e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 39.81 E-value: 2.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984360 268 VSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGY-------SNDLTLFGR 323
Cdd:PRK13547 9 VARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvTGDVTLNGE 71
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-198 |
3.19e-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: 38.12 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 29 GESWAFVGSNGSGKSALARALAGDLPLLSGQreshfsrvtrlsfeqlQKLVSDEWQRNNTDLLSPGEedtgrttaeiiqd 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGG----------------VIYIDGEDILEEVLDQLLLI------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 109 evkdparcarlaeqfgisaLLDRRFKYLSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQL------AALLADLH 182
Cdd:smart00382 53 -------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleelRLLLLLKS 113
|
170
....*....|....*.
gi 488984360 183 SAGITLVLVLNRFDEI 198
Cdd:smart00382 114 EKNLTVILTTNDEKDL 129
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
129-303 |
3.42e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 129 LDRRFKYLSTGETRKTLLCQALMT---DPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVL------VLNRFDEI- 198
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIiehnmhVVKVADYVl 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 199 ---PEFVQFAG-VLADCTLSETGEKSSLLQQALVAQLAHSEKLDgitlPEPDVPPARHALADsaprIVLNDgvvSYNDRp 274
Cdd:PRK00635 883 elgPEGGNLGGyLLASCSPEELIHLHTPTAKALRPYLSSPQELP----YLPDPSPKPPVPAD----ITIKN---AYQHN- 950
|
170 180
....*....|....*....|....*....
gi 488984360 275 vINHLSWTVNPGEHWQIVGPNGAGKSTLL 303
Cdd:PRK00635 951 -LKHIDLSLPRNALTAVTGPSASGKHSLV 978
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
136-200 |
3.66e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 3.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984360 136 LSTGETRKTLLCQALMTDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVLVLNrfdEIPE 200
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISS---EMPE 453
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
129-206 |
5.89e-03 |
|
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: 37.69 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 129 LDRRFKYLSTGETRKTLLCQALM--TDPQLLILDEPFDGLDVNSRQQLAALLADLHSAGITLVL------VLNRFDEIPE 200
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILiehnldVLSSADWIID 160
|
....*.
gi 488984360 201 FVQFAG 206
Cdd:cd03238 161 FGPGSG 166
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
253-434 |
7.02e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 38.09 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 253 ALADSAPRIVLNDGVVSYNDRPVINHLSWTVNPGEHWQIVGPNGAGKSTLL-SL-----------VTGDhpqgysndLTL 320
Cdd:COG1117 4 PASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrCLnrmndlipgarVEGE--------ILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984360 321 FG-------------RRR------------GSgetIWD-----IKKHiGYVSSSlHLDYRVSTNVRNVilsgyfdsiGIY 370
Cdd:COG1117 76 DGediydpdvdvvelRRRvgmvfqkpnpfpKS---IYDnvaygLRLH-GIKSKS-ELDEIVEESLRKA---------ALW 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984360 371 QAVSDKQHKlvqqwldilgidkrtadaPFHSLSWGQQ-RLAlIVRALVKHPTLLILDEPLQGLDP 434
Cdd:COG1117 142 DEVKDRLKK------------------SALGLSGGQQqRLC-IARALAVEPEVLLMDEPTSALDP 187
|
|
| |
